CAZyme Information: MGYG000000224_00246

Basic Information

• Species: Bacteroides sp003545565
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp003545565
• CAZyme ID: MGYG000000224_00246
• CAZy Family: PL1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
795	MGYG000000224_1|CGC5	87467.12	4.6943

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000224	3747034	Isolate	China	Asia

• Gene Location: Start: 310669; End: 313056 Strand: -

Full Sequence      

MDKSKWILLLCFLFTWGCSSDSEGKDSTDVTTGKIEKLIEPVTSISADGKEAVSVTFTAN
KAWTAKAEKTWCTVTPASGETGGDIILTITAGENGSYDERNSKVTITCGDAVEYVTVTQK
QKDAILLTSGKVEVKREGEEFTVEVKANVSFTSEVSEEDRDWLRLVTQTRALSTSVLKFA
ASENMSDEKREGAITFKSGDLLETVTVYQAGSIPTIVLNETNYKIPAEGQDITIELQSNV
EYTIQLPAGVDWIREKPATKGMSTYTHHFTVDANDEDTSRRAEIVFTSKKGVSDSVRIVQ
YSSHPSMEQVEFAAFPGAEGHGKNTVGGREGKVYHVTSLEDDGTEGTLRWALGQDGPKTI
VFDVAGTIHLKSDIKTQKDYLTIAGQTSPGGICIADYQFWINSNDVIIRFLRFRPGDIGG
AEPDGLGGMDKKNIIVDHCSMSWSVDECLSVYGMENSTVQWCLAAQALHNSTHGKGSHGY
GGNWGGNRASYHHNMIAHCKSRVPRLGPRSTTQESEYVDIRNNVYYNWSGEGCYGGENQH
MNIVNNYYKPGPATNSAGTSKRTRYRIAKIGVRTTAYCQDKDGNWNSWQPSLHKWGTFYI
DGNTVEGYADVTADNWEKGVYEQQDNNEKVDYLWTDDVKKDIRKETLVVETGGVTTHSAT
DAYVKVMEYVGACNYRDAIDKLILGDVKNGLATCTATDNSAGLGYINTPKDILSALPELN
GNPYPALKTDTSIDVTDTDGDGMPDDFEIEFGLNPNDANDGNSKTLDPDMNYTNLEMYLH
YLVKDIMKKQVEGGL

Enzyme Prediction     

No EC number prediction in MGYG000000224_00246.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL1	365	548	1.8e-76	0.994535519125683

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14948	BACON	3.33e-18	44	120	10	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.
cd14948	BACON	6.14e-14	124	210	1	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.
cd14948	BACON	1.74e-11	215	300	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.
pfam13004	BACON	2.42e-11	63	120	3	61	Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.
pfam19190	BACON_2	3.10e-11	39	119	4	88	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
QGT73510.1	2.88e-216	314	790	40	507
ALJ48964.1	4.08e-216	314	790	40	507
QRQ55774.1	4.08e-216	314	790	40	507
QDM11680.1	4.08e-216	314	790	40	507
QUT78068.1	4.08e-216	314	790	40	507

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B8NQQ7	6.29e-46	314	783	22	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	3.62e-44	314	783	22	414	Probable pectate lyase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyC PE=3 SV=1
Q0CLG7	3.28e-41	314	783	22	414	Probable pectate lyase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyC PE=3 SV=1
Q5B297	1.59e-40	314	785	22	413	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
B0XMA2	4.43e-37	314	783	23	415	Probable pectate lyase C OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 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	1.000089	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000224_00246.