CAZyme Information: PABG_03998-t30_1-p1

Basic Information

• Species: Paracoccidioides brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; NA; Paracoccidioides; Paracoccidioides brasiliensis
• CAZyme ID: PABG_03998-t30_1-p1
• CAZy Family: GH36
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1886		206335.40	5.3834

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PbrasiliensisPb03	8548	482561	121	8427

• Gene Location: location=KN305535:1611110-1617978(-)

Full Sequence      

MGMSDHAHQPNHGLASFWTGPRWAQLFGGITAWCGMSLTVLFPPRSMEAINTTRDDCQII
ADMQAQPCQLQNLVFNMPKATDSNKVTHVGIFMENGSGGFVSDLVFNGGNIGWRAGSQQY
TAMNLKFNGCLTAVQMIWDWGFNWQRIEVDGGAIAFNISGRGGDTGQGVGSVSIIADSVI
SNCPIAILTNSRKDGINGPPSIVIDNLKMNSVGTTVKSEDGDVILDGTNHVGLWAMGRRY
DGYNGTYISGEVDAPQKAKRLLDKDGKLFYRPRPQYKDLKVDEFLIATEHDCKNDGTGDN
TGDINAFLEKAKKERKIAYFPAGVYRVGGTVFIPTGSRVQGASWSQIQGAGFYFNDIHNP
RVVVQVGEKGDVGDMEIVDMMFTAQGATAGAVLVEWNVHEDSQGSAAMWDSHIRVGGASG
TDLDIQTCPKFEFSDACICASLLFHITPQASGYFENIWIWLADHDNDKSVYDSPDKIANQ
ISLYAARGTLIESEGPSWFYGTGSEHTVMYQYQVYGAKDIYLGHIQTETPYYQPVPIAPL
PFSSAKEFPGDPSFEKCKTTGCSTAWGLRIINSEGITLHSSGLYSFFQEYYQDCVPTHNC
QERVLEVKGSKDVALFNTFTVGIVEIGTGINHGAIFQNDSNQSGFTTEVSVWIPLEGDDE
YDIVYVGPEVYDKPSLMCPADCILVFPTSSLSSKTTIDPGKYTTSVEYGRRSTTTIGGRE
VPTFYTTVTTITLTIDPITTDGMPYSNINITEGQTSTPLTVLPSVDIPPIPVPIPDGEGK
TTTRNITVPPWPAITRGPPESWNNPNASPTDGTKEGVYHTPFVTTVVATKPTVSTLSFPS
TVSPIVVKCPPHSKVPFNTPKTTPTINCGVPTTVSVAFTCPATKVVTFIGSSTGVFTVDC
TVSTTFTKPDQTITSGPTNKPTTTQPLPVWSTWPPRVVTPIEEEVKKPEPGKTSCKLWFF
SFCLNGGNKGLRWNLPPGIYPPGPPPPGAIDPPPSWTIKPPLPPWPPITVGRDNILTYPK
EEPTKCEKRSASICATTVFKTTTSRGTITSTATSTSSTCDTIYGCSASDWDRTTTQTKPD
NCPLPTTQPLQAAAAPPKPPPPGCPANAIVYPSNMKNVGQIPQLLEKYKGKYVEIKSDVL
HLTSFFWVPFLDQETMDALLKSPDVSDAYYYESWYAAVEKDRRTPSESIDVQGQSNLNRL
NDSRAVSENGKVIQSETLAAHTRAHAFIWDLSQVSMPRYAIWREPTGSTINDDGNMLFQY
DEVEGTGQVIFLMGEDDIWRTHLVRCHHYVAQVLLPKDDWGWLPPGPADREHGSGVASKA
VGFNLGTCEGCSIYVVSLYGAEKGSDETDGQLYWERYIQQLLNIVEVVQTLGLQGKAVIN
LSSTYNFFMREEHTKSMYELFTMLDNYGVAIVAASGNYAPLLREIMHYPAKYGDPHDKYY
IPNMIVVGATDEKGHQTGFSQYSDWMTTFAPGQDVWVPRFDHGGYITNLGTSFSAPLVSG
LIGYYRSLPSPWKQQLQFPANVKKMIKIFHRRIVVHDEPIVDEVMKPIIWNAQVGDFSCL
SHYETVDQWDHKGACPRIKPNLADETNDGETVRPCRYDPGLRNSSKEFDGSYCPLLPRAG
PGGHTVSFTSNGGAKASPTCVSGTGCGGHLCTGFFCSPMPTGVPPDRHDPKDPNASSRVP
TKTGPNDPEPTCDDKCKLDNGHRCSCGENGCDDKSPSCCANASCPYCECDENGCSPSSPR
CCGNRSCEWSRTGGGGGNNPRPKPKTGFVMITVSTVDNPAPPYLHHYWEVWLRTNPNKID
YCKDKSLVKEKTDDISGALPPSLGPFSADGITCKYIGDKKKAGKLECDTNVAKTSCMVLN
PIPKWECTLENPVYYPTVQCDWEAVE

Enzyme Prediction     

No EC number prediction in PABG_03998-t30_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH55	63	652	5.7e-182	0.768918918918919

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
403800	Pectate_lyase_3	2.14e-24	65	157	124	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	2.07e-21	1298	1517	32	235	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.
173799	Peptidases_S8_Subtilisin_like	7.04e-13	1309	1510	62	243	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.
173797	Peptidases_S8_4	9.78e-13	1303	1516	29	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.
173810	Peptidases_S8_Thermitase_like	2.97e-12	1374	1527	124	253	Peptidase S8 family domain in Thermitase-like proteins. Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan 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 the 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS48832.1|GH55	0.0	65	1880	199	2043
QSS62360.1|GH55	0.0	209	1880	1	1567
QSS50317.1|GH55	0.0	65	1382	231	1547
QSS52973.1|GH55	0.0	65	982	272	1190
VBB73332.1|GH55	0.0	65	1762	261	2030

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3EQN_A	7.26e-119	65	652	181	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]
5M5Z_A	1.07e-114	65	650	161	751	Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
1DBI_A	7.60e-06	1361	1501	113	235	Crystal Structure Of A Thermostable Serine Protease [Bacillus sp. Ak1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B0V1|E13B_ARTBC	1.98e-116	65	652	199	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	8.03e-107	65	623	206	756	Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
sp|P53626|E13B_TRIHA	2.52e-44	200	658	306	756	Glucan endo-1,3-beta-glucosidase BGN13.1 OS=Trichoderma harzianum OX=5544 GN=bgn13.1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.998166	0.001856

TMHMM  Annotations     

There is no transmembrane helices in PABG_03998-t30_1-p1.