CAZyme Information: PADG_08053-t30_1-p1

Basic Information

• Species: Paracoccidioides brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; NA; Paracoccidioides; Paracoccidioides brasiliensis
• CAZyme ID: PADG_08053-t30_1-p1
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2108	KN275969|CGC3	230913.66	5.1490

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PbrasiliensisPb18	8522	502780	132	8390

• Gene Location: location=KN275969:740348-748065(-)

Full Sequence      

MIYPKNMSSLGLFLQFLSLVAAQASLLYDPARFPNIPSYGPQPNPPYMVDNQYNYFKVAP
DRGEQNGPVWLESGSFETYMLNSGHSKQHNDTSVDAPGNLKKIVGSASNTTAASSYWLPK
LAPLGQPLAGAGYKFYRDVVEYGADNTGETDATEAINAAIGDGKRCGLECGNTFVQGAII
YFPPGTYKICRPVIQLYYTQFIGDALNPPTIKGCDTFQGIALFDTDPYIPGGNGQNWYIN
QNQFFRQIRNFIFDLTEMPLTTDDHDQPLVPTGIHWQVSQACSLQNLVFNMPEATDDNKV
THVGIFMENGSGGFVSDLEFNGGNIGWRAGSQQYTAMNLKFNGCLTAVQMIWSWGFNWQR
IEVDGGAIAFNISGRGGSTGQGIGSVSIIDSRISNCPIAILTNTRKDGVNGSPNIVIDNL
AMYNVETTVQSDNGDVILKGTDFVKLWAIGRRYNGYNGTYTAGEVDAPRKGSGLLNINGK
LFYQPRPQYEDLRLDQFLIATEHGCMNDGTGDNTADINSFLEKANRGGKVAYFPAGIYRV
GGTVLIPTGSRVQGASWSQIQGAGVYFNDLHNPRVVVQVGERGDVGSMEIVDMMFTTQGA
TAGAIVLEWNVHQDRQGSAAMWDSHVRVGGSLGTDLDVKTCPKFEFRDACICASLLFHVT
PQASGYFENVWIWLADHDNDMSVYDSPDKLSNQISLYAARGTLIESEGPSWFYGTGSEHT
VMYQYQLYGAKNIYLGHIQTETPYYQPVPIAPLPFVPGKEFPGDPSFEKCKTIGCQAAWG
LRIINSKSITLHSSGLYSFFQEYYQDCVPTHNCQERSLEVRGSKGVALFNIFTVGMVEIG
TGINHGAVLQNDSNQSGFTTEVSVWLPLSGDDEYDIVYVGPEVYEKPSVTCPADCILVFP
TSSLSSRTTIDPGNYTTSLEYGHRGTTIISGREVPTFYTTVTTITLAIDPIITDGMPYSN
INITKGQTSAVLTVLPSVDIPPVPVPMPDGEGKTTTRNVTVPPWPDITRGPPESWSDPNA
SPTEGTREGVYHTPFVTTVVATRPTVSTISFSSTVSPIVVECPPNSKVPFNTPKTTPTIN
CRKPTTVSIGFTCPATKVVTFIGSSTGVFTVDCTVSTTFTKSEETITPSPTNKPTTTQPL
PVWSTWPPRVITPIEEEVKKPEPGKTPCKLWFFSFCLNREKGETRGLRWILPPGIYPPGP
PPPRAINLPSWTIKSPLPPWPPITVGRDNIITYPQKEPTKCEKKSASICATTVFKATTTR
GTITSTSSSTSSTCDTIYGCSASDWDTTTTRTKPDNCPSPTAKPGQAAARPPIPPWGCPA
NALVYPSDMDDVRHIRELLAKYKDKYVEVKSEALHFTVFFWVPYLDQETMNTLVESPDVA
DAFYYEHRPDNDGILTDLRGRVRDISYNVDAIKSHGQGGVNHSNDSVVAQGNGNVDQLMP
SALIARESNYIWDLSQISMPRGMIWKDPYSATLSANGQFMFHYDRISGDDQYIYIMDEDE
ISETHPEMTHHNDIEYLRPDDRYSDPGPARPDVEHGTGVASKVIGRNLGSCQRCTLIVSS
LFEGVDEQDESVTLARYLDQVRGVIDDVLLKNRMGKAVINISANFDPTVGVVFIRELHKL
LVELDGLNVAIVVSASNRADESPEIDRYPALFAKPGSDLYIPNLIVVGATDAHGHITDFS
QYADWMTTFAPGDNIWIPLGDMDYMTSSGTSYSAPFVSGLIGYFRSLPSPWVNQLKDPGS
VKKMIKLFHRRIVVSNEPINVHKMKPIIWNGQFGEYSCLSDYRTVEQWDPRGYCPRIKLD
LHEETNDGETVAPCRYDSVVLDNSLKRFDGSYCPRLPKTGPSGHTVSFTSNGRVKPSPTC
ASGTGCGGRLCTGFFCSTMPTGVPPDRHDPKDPNASSRVPTTTKPSDPEPTCGDKCKLDK
GNRCSCGENGCDDQSPSCCANASCPYCECGENGCTPSSPWCCGNDSCEWSRTGGGGGNNP
RPKPRTGFVLISVSNVENPAPPHIHHYWELWSATPSKNVDMCKDDPLVKEKTDDIAGAFP
PSLGPFTANGVTCKYIGNKKNAGKLECDTNVSKTSCKAVDPIKKYECTLENPIKYLTVSC
EWEAQELP

Enzyme Prediction     

No EC number prediction in PADG_08053-t30_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH55	108	865	3.6e-246	0.9905405405405405

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
403800	Pectate_lyase_3	2.24e-75	136	371	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	4.59e-22	1491	1737	1	236	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	1.44e-17	1481	1737	17	247	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.
173797	Peptidases_S8_4	6.32e-16	1501	1735	10	216	Peptidase S8 family domain, uncharacterized subfamily 4. 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.
173799	Peptidases_S8_Subtilisin_like	8.10e-13	1521	1737	51	252	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS48832.1|GH55	0.0	83	2102	2	2045
QSS50317.1|GH55	0.0	48	1620	1	1565
QSS52973.1|GH55	0.0	7	1198	1	1190
QSS62360.1|GH55	0.0	422	2102	1	1569
VBB73332.1|GH55	0.0	48	2017	1	2071

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5M5Z_A	3.02e-179	112	863	2	751	Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
3EQN_A	1.92e-173	132	865	45	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B0V1|E13B_ARTBC	6.05e-175	111	865	38	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	2.67e-150	116	836	48	756	Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
sp|P53626|E13B_TRIHA	1.16e-51	110	815	31	706	Glucan endo-1,3-beta-glucosidase BGN13.1 OS=Trichoderma harzianum OX=5544 GN=bgn13.1 PE=1 SV=1
sp|D4D1U5|SUB12_TRIVH	3.72e-07	1535	1722	188	354	Subtilisin-like protease 12 OS=Trichophyton verrucosum (strain HKI 0517) OX=663202 GN=SUB12 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000373	0.999594	CS pos: 22-23. Pr: 0.9776

TMHMM  Annotations     

There is no transmembrane helices in PADG_08053-t30_1-p1.