CAZyme Information: P174DRAFT_464602-t37_1-p1

Basic Information

• Species: Aspergillus novofumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus novofumigatus
• CAZyme ID: P174DRAFT_464602-t37_1-p1
• CAZy Family: GH78
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1329		143053.43	4.7258

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnovofumigatusIBT16806	11729	1392255	197	11532

• Gene Location: location=MSZS01000011:47858-53286(-)

Full Sequence      

MKLLAALTSALAWGVSLVEAKAVFAHYMVGNTKSLGLIDWRHKMQAAQAAGIDAFVLNMA
NKDPTNDIALPMAFTAADDIGFQLLFSFDYAGNGPWDKSVVIDMIKGYSTKDTYFKMAGK
PFVSTFEGPNNADDWKDIKKETNCFFMPDWSSVSAQPADAWPKGPANMTTYPNTLYYDFL
GSKPYMMPISPCNDMWFQCWQQAISLNRQPDFIKIISWNDYGESHYISPLDDCQYEAFDI
GRAPFNYIKDMPHNGWRETLPYYISMYKSGTATVTEERLVAWYQVNKNGACSDGGTTSNT
ANQLVFYDVLLTSNAQVQVSISGVVQAGGWDQEPHGALVFTTAAGQVVVMVKRGGATIAT
IMGASITSSCNGGLNNYSPWVGSARGPPITPVMTTGDLSKLDCVKGFGVLEFIGVCDFAC
ANGYCPSAACTCLKKGVANAPNDTGLVGYLLPRKSGSFAGLYSFDCNHGYCLDLVCGQTP
NDGGLCDFRCHLGFCPIHACTCTSTGILVQTPPKMNDKYPTVTLDPACAPPCVLVLPPSS
LASLTTISFDPWQTSLEFGWMTMDMVDGTVTTYYTAVTVSTEISILLVTTDLISFSEVIL
TTTVDGGVPSIIIPMASVSPPPFVITPTPVADITVAPVAQTICLPPWPWSGPSAMPDPSG
TSMTTSTSDPVVVPIVTGPFPATVFPMEIVSWVRDWLPEPTAIQVDGGDPVPVIPCWVWF
ICGIVLPGFKNLGIYPKGGPPPVGPNPPLGLTLKIPWPQIIIGPDRKPTYPDKPDPEEDS
CETATASVCTTTLSYGIVAKRAAEGAAPTWAPQIPFEDDITMMTVIATTATAIPCVVIPR
DPRNIDGIRTTLQQQLGGSVLDLFKSRMDQLGTMFFFVPAFTSDQTDAIWATRSEIVERN
SPDNMVSLSWPPDIGPVPVQGDYRFDSSAGEGTYVYHVDFGAQPSHPEFSNMFGWMENDP
KWHGSLCLSKEVGKTVGIVCKATVVATAWDFQKSINEHWLDALAKVHANISTGARGPRKM
ALLIQEIIKLGAVFVMGSGNSLGSPNGYLVLFRDPANPNHIPELIVIGSVLGQGILGQHA
NADWVTCYAPGYVTGLAAYFCGLNSTLTTAASVKERILRLTYCWQLQPNHPEGPYQRYIN
NVGRSIVPKCSDFSKAKRQSSGGSCPVLTCAGAGCGSSCAGFFCPGTLLKQNLDFLDPPN
LDSVQNLDSRYYKDWDGTITCTTTTPTKTIPTTTPTPPKSLSVPIGGPCRLTDECEDNCP
KPGAVQCESGVCTCLAPPPKTTPPHAAMCYDVQQCLNVYTCASGDTMVCEPTDYSNGNGL
CQCIKGNPS

Enzyme Prediction     

EC	3.2.1.59:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH71	23	361	2.6e-101	0.9946666666666667
CBM24	403	476	9.6e-19	0.9736842105263158

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397634	Glyco_hydro_71	4.05e-131	23	360	1	372	Glycosyl hydrolase family 71. Family of alpha-1,3-glucanases.
211418	GH71	3.20e-98	18	270	2	283	Glycoside hydrolase family 71. This family of glycoside hydrolases 71 (following the CAZY nomenclature) function as alpha-1,3-glucanases (mutanases, EC 3.2.1.59). They appear to have an endo-hydrolytic mode of enzymatic activity and bacterial members are investigated as candidates for the development of dental caries treatments.The member from fission yeast, endo-alpha-1,3-glucanase Agn1p, plays a vital role in daughter cell separation, while Agn2p has been associated with endolysis of the ascus wall.
211414	GH99_GH71_like	3.08e-31	23	264	1	283	Glycoside hydrolase families 71, 99, and related domains. This superfamily of glycoside hydrolases contains families GH71 and GH99 (following the CAZY nomenclature), as well as other members with undefined function and specificity.
173790	Peptidases_S8_PCSK9_ProteinaseK_like	2.32e-10	918	1120	12	252	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.
211416	GH99_GH71_like_3	0.001	104	229	148	309	Uncharacterized glycoside hydrolase family 99-like domain. This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAP83026.1|CBM24|GH71	2.49e-127	19	460	20	511
CAK48462.1|CBM24|GH71	1.36e-125	15	459	22	511
EAA33915.3|CBM24|GH71	6.76e-123	18	797	16	949
QKD62247.1|CBM24|GH71	1.95e-122	19	520	17	604
UPK95345.1|CBM24|GH71	2.71e-122	19	520	17	604

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z6O_A	8.65e-10	894	1114	1	255	Crystal structure of Penicillium cyclopium protease [Penicillium cyclopium]
1HT3_A	1.61e-06	918	1112	18	247	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]
3F7O_A	1.68e-06	923	1120	25	236	Crystal structure of Cuticle-Degrading Protease from Paecilomyces lilacinus (PL646) [Purpureocillium lilacinum],3F7O_B Crystal structure of Cuticle-Degrading Protease from Paecilomyces lilacinus (PL646) [Purpureocillium lilacinum]
1BJR_E	5.11e-06	918	1112	18	247	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]
1IC6_A	5.11e-06	918	1112	18	247	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B6GX22|MU71A_PENRW	2.02e-46	19	386	34	432	Mutanase Pc12g07500 OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=PCH_Pc12g07500 PE=1 SV=1
sp|O13716|AGN1_SCHPO	7.54e-28	21	382	22	420	Glucan endo-1,3-alpha-glucosidase agn1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=agn1 PE=1 SV=2
sp|O94510|AGN2_SCHPO	6.65e-20	21	325	11	365	Ascus wall endo-1,3-alpha-glucanase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=agn2 PE=1 SV=2
sp|C5NZ70|SUB2C_COCP7	1.10e-09	922	1121	145	383	Subtilisin-like protease CPC735_013710 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CPC735_013710 PE=3 SV=1
sp|G3FNQ9|SPAZ_ORBOL	1.58e-09	923	1142	147	408	Cuticle-degrading serine protease OS=Orbilia oligospora OX=2813651 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000668	0.999294	CS pos: 20-21. Pr: 0.9639

TMHMM  Annotations     

There is no transmembrane helices in P174DRAFT_464602-t37_1-p1.