CAZyme Information: MGYG000000105_01150

Basic Information

• Species: Bacteroides clarus
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides clarus
• CAZyme ID: MGYG000000105_01150
• CAZy Family: PL1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
816	MGYG000000105_2|CGC4	89868.02	4.4515

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000105	3966085	Isolate	Canada	North America

• Gene Location: Start: 286463; End: 288913 Strand: -

Full Sequence      

MRYFLFILLAGLLGACSDEGELNGAVGTDSLELSKKELKLSNVATSSTVDITATGEWLAT
IVEPATNDAEQAWLTLSKSSGTGNDELRLFVAENTAGAKRMGKVKVTMAGAGSTLEQEIA
IEQLGSEPDILFEFTSEPISFRGAEVELKVVANMEWKMDIDEQCDWIEVVEETPVTRNFS
EQILKLKVALNTGNARTTELVFSTVGEYKLQRVLKVMQEAVNGVAAIEQDEYTIPYKCRT
LVIPFTQEGDEPVDNFDAIPSEAWITHNKRESTSNEIVLTIADNEDFLPRTSTVRILDKT
ITIFQYGKPDTGIGDDKSVEALAFPGAEGGGRFTTGGRGGVLYKVTNLDDYGLGETPIEG
SLRYGIEQIQGPRTIVFDVDGTIELKRGIYLVDYPDLSIIGQTAPGEGITLKNYNFSFNL
SKDPEKGAGNSINAIVRFLRIRPGDACSDYAEDAIGGRYFKNGIIDHVTAGWSVDETLTF
YGVQNFTAQWCIASESLNLSNHAKGAHGYGAMFSGDNTTFHHILLAHHGSRCPRISDLSE
PGTQGSYDYCGYFDVRNNVYYNWSESGFGSYGGKYATFNLTNCYYKPGPATGTGYKSYRV
LSTDPTARAYISDNYIEGNSKVSSDNWTDGVWAQFDKSLVEQGVSDEEKQAMKMADYQPF
SKVTSHTAQVAYERVLDYAGASLRRDEIDRRIIGEVRAGSAPYKGSKMSYWDEKGNLVTL
KDSDKKPGIIDTPSDAAGGYVEMKKGYLWPDSDNDGIPDIWELAYGLNPEDPSDANVISS
SVDPNGRYSNLEVYFHNLVQHIVYYQNQGGQPMERK

Enzyme Prediction     

No EC number prediction in MGYG000000105_01150.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL1	381	585	6.1e-62	0.9890710382513661

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14948	BACON	5.29e-14	30	123	1	82	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
cd14948	BACON	9.20e-06	227	305	4	82	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
cd14948	BACON	3.48e-05	132	219	2	83	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
smart00656	Amb_all	1.42e-04	396	570	17	173	Amb_all domain.
pfam19190	BACON_2	5.32e-04	31	115	2	84	Viral BACON domain. This family represents a distinct class of BACON domains found in crAss-like phages, the most common viral family in the human gut, in which they are found in tail fiber genes. This suggests they may play a role in phage-host interactions.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT78065.1	0.0	1	816	1	795
ALJ48967.1	0.0	1	816	1	795
SCV08385.1	0.0	1	816	1	795
QRQ55777.1	0.0	1	816	1	795
QDM11683.1	0.0	1	816	1	795

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B8NQQ7	3.46e-37	322	799	21	414	Probable pectate lyase C OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=plyC PE=3 SV=1
Q2UB83	1.16e-36	322	799	21	414	Probable pectate lyase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyC PE=3 SV=1
Q0CLG7	3.91e-36	313	799	11	414	Probable pectate lyase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyC PE=3 SV=1
Q5B297	1.00e-35	322	799	21	411	Probable pectate lyase C OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyC PE=3 SV=1
Q4WL88	6.04e-35	317	799	16	415	Probable pectate lyase C OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=plyC PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000019	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000105_01150.