CAZyme Information: OAX79997.1

Basic Information

• Species: Emergomyces africanus
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Emergomyces; Emergomyces africanus
• CAZyme ID: OAX79997.1
• CAZy Family: GH18
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2034		223324.93	6.0588

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EafricanusCBS136260	8860	N/A	91	8769

• Gene Location: location=LGUA01000826:2116-9746(+)

Full Sequence      

MNIFSLGVLSGLLALVGGQAGLLYDPASYPDIPSYGPQPNPDYMVDHQYNYFKTAPDKGK
QNGPVWLESGSFENYMSTVGNLTSENHTLSDSAAAGYWLPQLAPLGKQPLAGSNYKFFRD
VVKYGADNTGKKDATEAINAAIEDGNRCGLECGNTFVRGAIVYFPPGTYKICRPVIQLYY
TQFIGDALDPPTIKGCDTFQGIALFDTDPYIPNGNGQNWYINQNQFFRQIRNFIFDMTEM
PLSTSENDQPLVPTGIHWQVSQACSLQNLVFNMPKATDGNKATHVGIFMENGSGGFVSDL
EFNGGSIGWRAGSQQYTAINIKFNDCLTAVQMVWDWGFNWQRVEVDNAAIAFNISGRGGS
TGQGIGSISIIDSKISNCPIAVLTNSHKDKDSGSPNIVIDNLKMNNVETTVKSDNGDIIL
KGIDHVDLWAIGQRYDGYNGTYTSGEVKAPKKGSRLLDDHDQLFYRSRPQYEKLGIDKFR
IATEHDCKNDGTGDNTAAINTFLQDAIKADQIAYFPAGIYRVGGTVLIPTNSRVQGASWS
QIQGAGFYFNDIHNPRVIVQVGEKGDIGSMEIVDMMFTAQGATAGAIILEWNVHEIKQGS
AAMWDSHIRVGGAAGTDLDLDTCPKFEYSDACICASLLFHVTPQASGYFENIWIWLADHD
NDMSVYDSPDKLSNQISLYAARGTLIESEGPSWFYGTGSEHTVMYQYQLYGAKDIYLGHI
QTETPYYQPVPVAPYPFLTGKNFPGDPSYKQCKNNAACESAWGLRIINSKGVTLHGSGLY
SFFQEYYQDCVPTHNCQECLLEVRGSKDVVLFNIFTVGTEKIGTGINNGAIFQNDSNQSG
FTTEVSVWLPLPGDDDLNIVYVGPEVYEDPAVTCPHNCLLVFPTSSLETKTTIKPGKYTT
SLEYGHSGTTSIGDRVVSTFFTTITTITLNIDPITTDGMPYSNINITDGETSTILNVYPS
VDISPVPVPIPDGEGQITTRNVTVPPWPDITRGPPESWRNPTTSSADDHRNGVYHTPYVT
TVIATRPTVTTISFPSTVSPIVVKCPPSSEVPFNTPKTTATIYCSAPTTISVAFTCPAIK
IVTFIGSSAGVFTVDCTVSTTFSKPGATITRSTSKPTTSRPLPVWTTWPPKAIIPIEEEV
KDPEPGKTSCNLWFFSMCISIDDKKIGGLRWILPPGIYPPGPPPARAINPPPSWTIKPPL
PPWPKITVGRDNIVTYPKEEPTKCEKKSASMCATTVFKTTTTRGTTTSTISSTKSTCDTI
YGCSASDGGITTTTRTTVDNCPPQTITPKAFQTGAPSSTESEPRPQQAANGPPPPGCPAN
AVVYPSDIYNVGQIPQLLSKYKGKYVEIKSTVFHFTSYFWVPYLDQDTMDVLLESPDVAD
AYYYERWNLEHGPRPSDPVEGLKSSDVVGDRSRSNFSNVALGDNLQAAGRRGSILEDLSQ
ASLAKGKAWKAPDSNSVDDEGNFLFFFDAVAGAGQYVYIIDDGLWTNHHEFKQTDGSIEL
LIPPGESPRDNDPQVDHGSGVASKVLGEGLGICKSCNIVMVPQIWLTDPDVDYWARLPER
VLEAVIMILDDISTKGREGKAVLNISWGQDVLARSELLAQFRQFLHLLEQIVQTPTVCAA
GNSGKTVKEIDVYPALFADPVNPHGHLPNLIVVGATDVWGQQAEWSQYDNWMTTFARGDD
VWAPGYPTPNDNKKYRVVSGTSLSTPQVAGLVAYFRSLSSPWKDQLKQPANVKKMIKLFH
RRFTVHSPMAPNDPSLRKPVIWNGQMGVAQRLKKTLKMRPGKEKAWNLAALATRSRKLMV
APVLFFLTRVRVNRRILSTHDRRNRFRKHRKKTRTRAAGCRPTPDLVAQSPPVMTSASWT
REIRVSAMKMVVTQNHLSVVETKVVQCWSWTGGGGGDGSGEPPGPHIGKLLFALDEMVTS
RPGGDVWTRFWKVFGSELDGKIDLCWDTPLKLADASSDPEKRPLYPPSMEFIAEGHECKY
TGDENGAGILDCEGSRASFCKPRDPQDRSGCPPKQRFTWQWIVNSSLRVASDER

Enzyme Prediction     

No EC number prediction in OAX79997.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH55	87	848	1.2e-250	0.9932432432432432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
403800	Pectate_lyase_3	1.24e-75	118	353	1	213	Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.
173787	Peptidases_S8_S53	1.55e-24	1475	1718	1	225	Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
173790	Peptidases_S8_PCSK9_ProteinaseK_like	3.07e-21	1462	1737	14	250	Peptidase S8 family domain in ProteinaseK-like proteins. The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K.
173799	Peptidases_S8_Subtilisin_like	3.29e-15	1579	1718	120	241	Peptidase S8 family domain in Subtilisin-like proteins. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
173794	Peptidases_S8_Autotransporter_serine_protease_like	1.29e-12	1472	1713	2	244	Peptidase S8 family domain in Autotransporter serine proteases. Autotransporter serine proteases belong to Peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Autotransporters are a superfamily of outer membrane/secreted proteins of gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters are may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS48832.1|GH55	0.0	92	2011	30	2025
QSS50317.1|GH55	0.0	44	1588	1	1549
QSS52973.1|GH55	0.0	5	1180	3	1190
VBB73332.1|GH55	0.0	44	1766	1	1808
CAP67893.1|GH55	0.0	44	1766	1	1804

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5M5Z_A	1.75e-183	93	846	2	751	Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
3EQN_A	3.91e-170	92	848	19	755	Chain A, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQN_B Chain B, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQO_A Chain A, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQO_B Chain B, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium]
1IC6_A	3.11e-10	1461	1718	19	240	STRUCTURE OF A SERINE PROTEASE PROTEINASE K FROM TRITIRACHIUM ALBUM LIMBER AT 0.98 A RESOLUTION [Parengyodontium album],1P7V_A Structure of a complex formed between Proteinase K and a designed heptapeptide inhibitor Pro-Ala-Pro-Phe-Ala-Ala-Ala at atomic resolution [Parengyodontium album],1P7W_A Crystal structure of the complex of Proteinase K with a designed heptapeptide inhibitor Pro-Ala-Pro-Phe-Ala-Ser-Ala at atomic resolution [Parengyodontium album],2DQK_A Crystal structure of the complex of proteinase K with a specific lactoferrin peptide Val-Leu-Leu-His at 1.93 A resolution [Parengyodontium album],2DUJ_A Crystal structure of the complex formed between proteinase K and a synthetic peptide Leu-Leu-Phe-Asn-Asp at 1.67 A resolution [Parengyodontium album],2G4V_A anomalous substructure of proteinase K [Parengyodontium album],2HD4_A Crystal structure of proteinase K inhibited by a lactoferrin octapeptide Gly-Asp-Glu-Gln-Gly-Glu-Asn-Lys at 2.15 A resolution [Parengyodontium album],2HPZ_A Crystal structure of proteinase K complex with a synthetic peptide KLKLLVVIRLK at 1.69 A resolution [Parengyodontium album],2ID8_A Crystal structure of Proteinase K [Parengyodontium album],2PQ2_A Chain A, Proteinase K [Parengyodontium album],2PWA_A Crystal Structure of the complex of Proteinase K with Alanine Boronic acid at 0.83A resolution [Parengyodontium album],2PWB_A Crystal structure of the complex of proteinase K with coumarin at 1.9 A resolution [Parengyodontium album],2PYZ_A Crystal structure of the complex of proteinase K with auramine at 1.8A resolution [Parengyodontium album],2V8B_A SAD Structure solution of Proteinase K grown in selenate solution [Parengyodontium album],3AJ8_A X-ray analysis of Crystal of Proteinase K Obtained from H2O Solution Using PEG 8000 [Parengyodontium album],3AJ9_A X-ray analysis of Crystal of Proteinase K Obtained from D2O Solution Using PEG 8000 [Parengyodontium album],3DYB_A Chain A, Proteinase K [Parengyodontium album],3GT3_A Structure of proteinase K with the mad triangle B3C [Parengyodontium album],3GT4_A Structure of proteinase K with the magic triangle I3C [Parengyodontium album],3L1K_A SAD structure solution of proteinase K grown in potassium tellurate solution [Parengyodontium album],3OSZ_A Crystal Structure of the complex of proteinase K with an antimicrobial nonapeptide, at 2.26 A resolution [Parengyodontium album],3Q40_A Sulphur SAD structure solution of proteinase K grown in SO4-less solution. [Parengyodontium album],3Q5G_A Sulphur SAD structure solution of proteinase K grown in SO4 solution [Parengyodontium album],3QMP_A Selenium SAD structure solution of proteinase K grown in SO4-less solution and soaked in selenate. [Parengyodontium album],4B5L_A The 1.6 A High Energy Room Temperature Structure of Proteinase K at 38.4 keV and 0.04 MGy [Parengyodontium album],4FON_A High Energy Remote SAD structure solution of Proteinase K from the 37.8 keV Tellurium K edge [Parengyodontium album],4WOB_A Proteinase-K Pre-Surface Acoustic Wave [Parengyodontium album],4WOC_A Proteinase-K Post-Surface Acoustic Waves [Parengyodontium album],4ZAR_A Crystal Structure of Proteinase K from Engyodontium albuminhibited by METHOXYSUCCINYL-ALA-ALA-PRO-PHE-CHLOROMETHYL KETONE at 1.15 A resolution [Parengyodontium album],5AVJ_A Crystal structure of proteinase K from Engyodontium album [Parengyodontium album],5AVK_A Crystal structure of proteinase K from Engyodontium album [Parengyodontium album],5B1D_A Crystal structure of proteinase K from Engyodontium album [Parengyodontium album],5B1E_A Crystal structure of proteinase K from Engyodontium album [Parengyodontium album],5CW1_A Proteinase K complexed with 4-iodopyrazole [Parengyodontium album],5I9S_A MicroED structure of proteinase K at 1.75 A resolution [Parengyodontium album],5KXU_A Chain A, Proteinase K [Parengyodontium album],5KXV_A Chain A, Proteinase K [Parengyodontium album],5MJL_A Chain A, Proteinase K [Parengyodontium album],5ROC_A Chain A, Proteinase K [Parengyodontium album],5ROD_A Chain A, Proteinase K [Parengyodontium album],5ROE_A Chain A, Proteinase K [Parengyodontium album],5ROF_A Chain A, Proteinase K [Parengyodontium album],5ROG_A Chain A, Proteinase K [Parengyodontium album],5ROH_A Chain A, Proteinase K [Parengyodontium album],5ROI_A Chain A, Proteinase K [Parengyodontium album],5ROJ_A Chain A, Proteinase K [Parengyodontium album],5ROK_A Chain A, Proteinase K [Parengyodontium album],5ROL_A Chain A, Proteinase K [Parengyodontium album],5ROM_A Chain A, Proteinase K [Parengyodontium album],5RON_A Chain A, Proteinase K [Parengyodontium album],5ROO_A Chain A, Proteinase K [Parengyodontium album],5ROP_A Chain A, Proteinase K [Parengyodontium album],5ROQ_A Chain A, Proteinase K [Parengyodontium album],5ROR_A Chain A, Proteinase K [Parengyodontium album],5ROS_A Chain A, Proteinase K [Parengyodontium album],5ROT_A Chain A, Proteinase K [Parengyodontium album],5ROU_A Chain A, Proteinase K [Parengyodontium album],5ROV_A Chain A, Proteinase K [Parengyodontium album],5ROW_A Chain A, Proteinase K [Parengyodontium album],5ROX_A Chain A, Proteinase K [Parengyodontium album],5ROY_A Chain A, Proteinase K [Parengyodontium album],5ROZ_A Chain A, Proteinase K [Parengyodontium album],5RP0_A Chain A, Proteinase K [Parengyodontium album],5RP1_A Chain A, Proteinase K [Parengyodontium album],5RP2_A Chain A, Proteinase K [Parengyodontium album],5RP3_A Chain A, Proteinase K [Parengyodontium album],5RP4_A Chain A, Proteinase K [Parengyodontium album],5RP5_A Chain A, Proteinase K [Parengyodontium album],5RP6_A Chain A, Proteinase K [Parengyodontium album],5RP7_A Chain A, Proteinase K [Parengyodontium album],5RP8_A Chain A, Proteinase K [Parengyodontium album],5RP9_A Chain A, Proteinase K [Parengyodontium album],5RPA_A Chain A, Proteinase K [Parengyodontium album],5RPB_A Chain A, Proteinase K [Parengyodontium album],5RPC_A Chain A, Proteinase K [Parengyodontium album],5RPD_A Chain A, Proteinase K [Parengyodontium album],5RPE_A Chain A, Proteinase K [Parengyodontium album],5RPF_A Chain A, Proteinase K [Parengyodontium album],5RPG_A Chain A, Proteinase K [Parengyodontium album],5RPH_A Chain A, Proteinase K [Parengyodontium album],5RPI_A Chain A, Proteinase K [Parengyodontium album],5RPJ_A Chain A, Proteinase K [Parengyodontium album],5RPK_A Chain A, Proteinase K [Parengyodontium album],5RPL_A Chain A, Proteinase K [Parengyodontium album],5RPM_A Chain A, Proteinase K [Parengyodontium album],5RPN_A Chain A, Proteinase K [Parengyodontium album],5RPO_A Chain A, Proteinase K [Parengyodontium album],5RPP_A Chain A, Proteinase K [Parengyodontium album],5RPQ_A Chain A, Proteinase K [Parengyodontium album],5RPR_A Chain A, Proteinase K [Parengyodontium album],5RPS_A Chain A, Proteinase K [Parengyodontium album],5RPT_A Chain A, Proteinase K [Parengyodontium album],5RPU_A Chain A, Proteinase K [Parengyodontium album],5RPV_A Chain A, Proteinase K [Parengyodontium album],5RPW_A Chain A, Proteinase K [Parengyodontium album],5RPX_A Chain A, Proteinase K [Parengyodontium album],5RPY_A Chain A, Proteinase K [Parengyodontium album],5RPZ_A Chain A, Proteinase K [Parengyodontium album],5UVL_A Chain A, Proteinase K [Parengyodontium album],5WHW_A Using sound pulses to solve the crystal harvesting bottleneck [Parengyodontium album],5WJG_A Using sound pulses to solve the crystal harvesting bottleneck [Parengyodontium album],5WJH_A Using sound pulses to solve the crystal harvesting bottleneck [Parengyodontium album],5WRC_A Crystal structure of proteinase K from Engyodontium album [Parengyodontium album],6FJS_A Proteinase~K SIRAS phased structure of room-temperature, serially collected synchrotron data [Parengyodontium album],6J43_A Chain A, Proteinase K [Parengyodontium album],6K2P_A Crystal structure of proteinase K from Engyodontium album [Parengyodontium album],6K2R_A Crystal structure of proteinase K from Engyodontium album [Parengyodontium album],6K2S_A Crystal structure of proteinase K from Engyodontium album [Parengyodontium album],6K2T_A Crystal structure of proteinase K from Engyodontium album [Parengyodontium album],6K2V_A Crystal structure of proteinase K from Engyodontium album [Parengyodontium album],6K2W_A Crystal structure of proteinase K from Engyodontium album [Parengyodontium album],6K2X_A Crystal structure of proteinase K from Engyodontium album [Parengyodontium album],6LAW_A MicroED structure of proteinase K at 1.50A determained using crystal lamellas prepared by focused ion beam milling [Parengyodontium album],6MH6_A High-viscosity injector-based Pink Beam Serial Crystallography of Micro-crystals at a Synchrotron Radiation Source. [Parengyodontium album],6N4U_A MicroED structure of Proteinase K at 2.75A resolution from a single milled crystal. [Parengyodontium album],6QF1_A Chain A, Proteinase K [Parengyodontium album],6QXV_A Pink beam serial crystallography: Proteinase K, 1 us exposure, 1585 patterns merged (2 chips) [Parengyodontium album],6RUG_A Co-substituted alpha-Keggin bound to Proteinase K solved by MR [Parengyodontium album],6RUH_A Ni-substituted alpha-Keggin bound to Proteinase K solved by MR [Parengyodontium album],6RUK_A Cu-substituted alpha-Keggin bound to Proteinase K solved by MR [Parengyodontium album],6RUN_A Co-substituted alpha-Keggin bound to Proteinase K solved by EP [Parengyodontium album],6RUW_A Zn-substituted alpha-Keggin bound to Proteinase K solved by MR [Parengyodontium album],6RVE_A Co-substituted beta-Keggin bound to Proteinase K solved by MR [Parengyodontium album],6RVG_A Co-substituted beta-Keggin bound to Proteinase K solved by MR [Parengyodontium album],6RZP_A Multicrystal structure of Proteinase K at room temperature using a multilayer monochromator. [Parengyodontium album],6TXG_A Proteinase K in complex with a 'half sandwich'-type Ru(II) coordination compound [Parengyodontium album],6V8R_A Proteinase K Determined by MicroED Phased by ARCIMBOLDO_SHREDDER [Parengyodontium album],6ZET_AAA Chain AAA, Proteinase K [Parengyodontium album],6ZEU_AAA Chain AAA, Proteinase K [Parengyodontium album],6ZEV_AAA Chain AAA, Proteinase K [Parengyodontium album],7A68_A proteinase K crystallized from 0.5 M NaNO3 [Parengyodontium album],7A9F_A Chain A, Proteinase K [Parengyodontium album],7A9K_A Chain A, Proteinase K [Parengyodontium album],7A9M_A Chain A, Proteinase K [Parengyodontium album],7C0P_A Chain A, Proteinase K [Parengyodontium album],7LN7_A Chain A, Proteinase K [Parengyodontium album],7LPT_A Chain A, Proteinase K [Parengyodontium album],7LPU_A Chain A, Proteinase K [Parengyodontium album],7LPV_A Chain A, Proteinase K [Parengyodontium album],7LQ8_A Chain A, Proteinase K [Parengyodontium album],7LQ9_A Chain A, Proteinase K [Parengyodontium album],7LQA_A Chain A, Proteinase K [Parengyodontium album],7LQB_A Chain A, Proteinase K [Parengyodontium album],7LQC_A Chain A, Proteinase K [Parengyodontium album],7NJJ_A Chain A, Proteinase K [Parengyodontium album],7NUY_A Chain A, Proteinase K [Parengyodontium album],7NUZ_A Chain A, Proteinase K [Parengyodontium album],7S4Z_A Chain A, Proteinase K [Parengyodontium album]
1BJR_E	1.81e-09	1461	1718	19	240	Complex Formed Between Proteolytically Generated Lactoferrin Fragment And Proteinase K [Parengyodontium album],1CNM_A Enhancement Of Catalytic Efficiency Of Proteinase K Through Exposure To Anhydrous Organic Solvent At 70 Degrees Celsius [Parengyodontium album],1EGQ_A Enhancement Of Enzyme Activity Through Three-Phase Partitioning: Crystal Structure Of A Modified Serine Proteinase At 1.5 A Resolution [Parengyodontium album],1OYO_A Regulation of protease activity by melanin: Crystal structure of the complex formed between proteinase K and melanin monomers at 2.0 resolution [Parengyodontium album],1PJ8_A Structure of a ternary complex of proteinase K, mercury and a substrate-analogue hexapeptide at 2.2 A resolution [Parengyodontium album],1PTK_A Studies On The Inhibitory Action Of Mercury Upon Proteinase K [Parengyodontium album],2DP4_E Crystal structure of the complex formed between proteinase K and a human lactoferrin fragment at 2.9 A resolution [Parengyodontium album],2PKC_A CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION [Parengyodontium album],2PRK_A SYNCHROTRON X-RAY DATA COLLECTION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURE OF PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION [Parengyodontium album],3D9Q_X Proteinase K by LB nanotemplate method before high X-Ray dose on ESRF ID23-1 beamline [Parengyodontium album],3DDZ_X Proteinase K by LB nanotemplate method after the first step of high X-Ray dose on ESRF ID23-1 beamline [Parengyodontium album],3DE0_X Proteinase K by LB nanotemplate method after the second step of high X-Ray dose on ESRF ID23-1 beamline [Parengyodontium album],3DE1_X Proteinase K by LB nanotemplate method after the third step of high X-Ray dose on ESRF ID23-1 beamline [Parengyodontium album],3DE2_X Proteinase K by LB nanotemplate method after the fourth step of high X-Ray dose on ESRF ID23-1 beamline [Parengyodontium album],3DE3_X Proteinase K by Classical hanging drop method before high X-Ray dose on ESRF ID23-1 beamline [Parengyodontium album],3DE4_X Proteinase K by Classical hanging drop method after the first step of high X-Ray dose on ESRF ID23-1 beamline [Parengyodontium album],3DE5_X roteinase K by Classical hanging drop method after the second step of high X-Ray dose on ESRF ID23-1 beamline [Parengyodontium album],3DE6_X Proteinase K by Classical hanging drop method after the third step of high X-Ray dose on ESRF ID23-1 beamline [Parengyodontium album],3DE7_X Proteinase K by Classical hanging drop method after the fourth step of high X-Ray dose on ESRF ID23-1 beamline [Parengyodontium album],3DVQ_X Proteinase K by LB nanotemplate method before high X-Ray dose on ESRF ID14-2 beamline [Parengyodontium album],3DVR_X Proteinase K by LB nanotemplate method after the first step of high X-Ray dose on ESRF ID14-2 beamline [Parengyodontium album],3DVS_X Proteinase K by LB nanotmplate method after the second step of high dose on ESRF ID14-2 beamline [Parengyodontium album],3DW1_X Proteinase K by LB nanotemplate method after the third step high X-Ray dose on ESRF ID14-2 beamline [Parengyodontium album],3DW3_X Proteinase K by Classical hanging drop method before high X Ray dose on ESRF ID 14-2 beamline [Parengyodontium album],3DWE_X Proteinase K by Classical hanging drop method after high X-Ray dose on ESRF ID14-2 beamline [Parengyodontium album],3I2Y_X Proteinase K by Classical hanging drop Method before high X-Ray dose on ID14-2 Beamline at ESRF [Parengyodontium album],3I30_X Proteinase K by Classical hanging drop Method after high X-Ray dose on ID14-2 Beamline at ESRF [Parengyodontium album],3I34_X Proteinase K by LB Nanotemplate Method after high X-Ray dose on ID14-2 Beamline at ESRF [Parengyodontium album],3I37_X Proteinase K by LB Nanotemplate Method before high X-Ray dose on ID14-2 Beamline at ESRF [Parengyodontium album],3PRK_E INHIBITION OF PROTEINASE K BY METHOXYSUCCINYL-ALA-ALA-PRO-ALA-CHLOROMETHYL KETONE. AN X-RAY STUDY AT 2.2-ANGSTROMS RESOLUTION [Parengyodontium album],3PTL_A Crystal structure of proteinase K inhibited by a lactoferrin nonapeptide, Lys-Gly-Glu-Ala-Asp-Ala-Leu-Ser-Leu-Asp at 1.3 A resolution. [Parengyodontium album],4DJ5_X Proteinase K by Langmuir-Blodgett Hanging Drop Method at 1.8A resolution for Unique Water Distribution [Parengyodontium album],5AMX_A Crystal Structure of Proteinase K processed with the CrystalDirect automated mounting and cryo-cooling technology [Parengyodontium album],5K7S_A MicroED structure of proteinase K at 1.6 A resolution [Parengyodontium album],6CL7_A 1.71 A MicroED structure of proteinase K at 0.86 e- / A^2 [Parengyodontium album],6CL8_A 2.00 A MicroED structure of proteinase K at 2.6 e- / A^2 [Parengyodontium album],6CL9_A 2.20 A MicroED structure of proteinase K at 4.3 e- / A^2 [Parengyodontium album],6CLA_A 2.80 A MicroED structure of proteinase K at 6.0 e- / A^2 [Parengyodontium album],6CLB_A 3.20 A MicroED structure of proteinase K at 7.8 e- / A^2 [Parengyodontium album],6KKF_A Crystal structure of proteinase K complexed with a triglycine [Parengyodontium album],6PKJ_A MicroED structure of proteinase K from an uncoated, single lamella at 2.17A resolution (#2) [Parengyodontium album],6PKK_A MicroED structure of proteinase K from an uncoated, single lamella at 2.18A resolution (#5) [Parengyodontium album],6PKL_A MicroED structure of proteinase K from an uncoated, single lamella at 2.59A resolution (#7) [Parengyodontium album],6PKM_A MicroED structure of proteinase K from an uncoated, single lamella at 2.17A resolution (#8) [Parengyodontium album],6PKN_A MicroED structure of proteinase K from an unpolished, platinum-coated, single lamella at 2.08A resolution (#9) [Parengyodontium album],6PKO_A MicroED structure of proteinase K from a platinum coated, unpolished, single lamella at 2.07A resolution (#12) [Parengyodontium album],6PKP_A MicroED structure of proteinase K from a platinum-coated, polished, single lamella at 1.91A resolution (#10) [Parengyodontium album],6PKQ_A MicroED structure of proteinase K from a platinum-coated, polished, single lamella at 1.85A resolution (#11) [Parengyodontium album],6PKR_A MicroED structure of proteinase K from a platinum-coated, polished, single lamella at 1.79A resolution (#13) [Parengyodontium album],6PKS_A MicroED structure of proteinase K from low-dose merged lamellae that were not pre-coated with platinum 2.16A resolution (LD) [Parengyodontium album],6PKT_A MicroED structure of proteinase K from merging low-dose, platinum pre-coated lamellae at 1.85A resolution (LDPT) [Parengyodontium album],6PQ0_A LCP-embedded Proteinase K treated with MPD [Parengyodontium album],6PQ4_A LCP-embedded Proteinase K treated with lipase [Parengyodontium album],6PU4_A MicroED structure of proteinase K recorded on Falcon III [Parengyodontium album],6PU5_A MicroED structure of proteinase K recorded on CetaD [Parengyodontium album],7JSY_A Chain A, Proteinase K [Parengyodontium album]
1HT3_A	2.42e-09	1461	1718	19	240	MERCURY INDUCED MODIFICATIONS IN THE STEREOCHEMISTRY OF THE ACTIVE SITE THROUGH CYS-73 IN A SERINE PROTEASE: CRYSTAL STRUCTURE OF THE COMPLEX OF A PARTIALLY MODIFIED PROTEINASE K WITH MERCURY AT 1.8 A RESOLUTION [Parengyodontium album],1PEK_E STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH A SUBSTRATE-ANALOGUE HEXA-PEPTIDE INHIBITOR AT 2.2 ANGSTROMS RESOLUTION [Parengyodontium album],1PFG_A Strategy to design inhibitors: Structure of a complex of Proteinase K with a designed octapeptide inhibitor N-Ac-Pro-Ala-Pro-Phe-DAla-Ala-Ala-Ala-NH2 at 2.5A resolution [Parengyodontium album],6K8M_E High resolution crystal structure of proteinase K with thiourea [Parengyodontium album]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B0V1|E13B_ARTBC	1.24e-173	76	848	22	873	Probable glucan endo-1,3-beta-glucosidase ARB_02077 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02077 PE=1 SV=1
sp|P49426|EXG1_COCCA	2.85e-150	63	820	11	757	Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
sp|Q9Y778|SMP1_MAGPO	3.67e-17	1437	1718	110	363	Subtilisin-like proteinase Mp1 OS=Magnaporthiopsis poae OX=148304 PE=1 SV=1
sp|Q03420|ALP_HYPAT	9.17e-17	1378	1737	71	383	Alkaline proteinase OS=Hypocrea atroviridis OX=63577 GN=prb1 PE=1 SV=1
sp|E4UZP9|SUB2_ARTGP	1.84e-16	1465	1721	154	380	Subtilisin-like protease 2 OS=Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) OX=535722 GN=SUB2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000220	0.999751	CS pos: 20-21. Pr: 0.6733

TMHMM  Annotations     

There is no transmembrane helices in OAX79997.1.