CAZyme Information: MGYG000004748_01094

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides
• CAZyme ID: MGYG000004748_01094
• CAZy Family: PL1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
812	MGYG000004748_4|CGC3	89875.64	4.8068

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004748	4696076	MAG	China	Asia

• Gene Location: Start: 89500; End: 91938 Strand: +

Full Sequence      

MRYFIFILLIGLLGACSSDSDLSGAVAAEKLELSKNELKLTNVEGSFTVAVTATGDWTAE
VIEADSEWLTLSKKNGTGNDEIRLFFTKNSDGAKRSGKVKVTMSGINSTLEQLISIEQLG
SDPDILFEYSSEPLPFSGGTFECKVVSNVEWDLQIDEKYNWVKQNKEAPMSRSFVTDNLS
FTIATNTTVEREALLVFKTVGEYVLERTVKIVQNGVSGVVSIEQDEYMIPYIYKTLIISA
PQGENPVEYDAVVSDSWITQDKKSSTVNDIVLKIEDNKDFLPRTATVKILDKMITIFQYG
KPDTSIGDDISASILAFPGAEGGGRFTAGGRGGEVYRVTNLLDYGKGEAIIEGSLRYGIE
KSTEPRTIVFDVSGIIELKRAIYLTDYPNLSIVGQTAPGDGITLKNYNFTFNLAKEPEKG
AGKKLNAIVRFLRFRPGDQYPDYGEDAVGGRYFTDAIIDHITAGWSVDETLTFYGVKNFT
AQWCIASESMNISNHAKGPHGYGAMFSGDNASYHHILLAHHGSRCPRISDMPAPQDRPAH
DYIGYFDVRNNVYYNWSEKGFGSYGGKYGEFNLVNCYYKPGPATGTGYKSWRVLSTDPTA
RAYIDGNFVVGKSNVSSDNWTEGVWGQFDKSIPELSTDEKQAMKMTSYQPFSKVTTHTAK
QAYDKVLEYAGASLRRDVIDQRIIREVSSGTNTYIGSKTFYMEDLKDDNGNVIGQKKVSV
TPQPGIIDTPSDAGGYIPVKSLKPWPDTDGDGIPDIWEQAYGLNPNDPSDAQQISTQVDP
NGRYPNLEVYFHNLVQHIIYYQNQGGQALEKK

Enzyme Prediction     

No EC number prediction in MGYG000004748_01094.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL1	373	578	8.8e-64	0.994535519125683

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14948	BACON	8.12e-16	31	118	2	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	1.71e-05	127	213	2	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.
pfam19190	BACON_2	1.87e-05	31	110	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.
cd14948	BACON	4.01e-05	247	298	26	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	8.23e-05	58	118	1	60	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDH54496.1	0.0	1	812	1	795
QUT78065.1	0.0	1	812	1	795
ALJ48967.1	0.0	1	812	1	795
SCV08385.1	0.0	1	812	1	795
QRQ55777.1	0.0	1	812	1	795

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A1DPF0	1.78e-35	313	795	20	415	Probable pectate lyase C OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=plyC PE=3 SV=1
Q4WL88	3.26e-35	313	795	20	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
Q5B297	3.32e-35	311	795	17	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
B0XMA2	5.97e-35	313	795	20	415	Probable pectate lyase C OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=plyC PE=3 SV=1
B8NQQ7	1.07e-34	311	795	17	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

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	1.000069	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004748_01094.