CAZyme Information: MGYG000001599_01413

Basic Information

• Species: Phocaeicola sp900544075
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900544075
• CAZyme ID: MGYG000001599_01413
• CAZy Family: PL1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
806	MGYG000001599_11|CGC1	89962.47	4.4357

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001599	4213385	MAG	China	Asia

• Gene Location: Start: 10551; End: 12971 Strand: +

Full Sequence      

MRNYLFALVIGLFAACSSENEMSADMVQDKLELSKKDLKINNVEGSFTIEVTASGEWTAA
VEETAAEWIRLSKDKGTGNDELRLFFSDNTKGERRAGKVFVSLTGSSTTIEHELTVEQLG
AEPDILFEYDGNPVSFRGGELPLNVVSNVEWSMVKDEACTWLSLKEEQLETRSFESDELI
LKVERNTGDVRSTELKFVATGDYVLQKTLEITQEAVSGVATLEFDEFSVPYKCKSLVIPF
TQYEDDEFDAIPSESWITYDKNNSTSNEIVLSLEDNMDKLPRTATVKILDKTVTIFQYGK
PDTNIGDDKSVTALAFPGAEGGGRMTTGGRGGAVYKVTSLDDYNEGDTPIEGTLRYGIEE
VKGPRNIIFETSGYIDLKRPIYLNDYPHLSIWGQTAPGDGITIRGYNFSFNLNRGDVQVG
DNGSLNVILRFLRFRPGDTHQDYGEDAIGGRYFKDAIIDHITAGWSVDETLTFYGVKNFT
AQWCIASESLNISNHAKGAHGYGAMFSGDNATFHHILLAHHGSRCPRISDLSAPEDRGPY
DYCGYFDVRNNVYYNWSDKGFGSYGGKLAYFNLTNCYYKPGPATGTGYKSYRILSTDPTA
RAYIEDNYVEGNPKVSADNWTDGVWAQFDKSIVAEGVTEEEKLAMRMSDYHPYSKVTTHT
SQNAYESVLEYAGASLRRDAVDERIVHEVRTGTAPHTGSKEFYYDEDYNLVTVDEHKPGI
IDTPNDAGGYPELKKGYVWPDTDKDGIPDIWEIAYGLNPNNPDDAKSINTDVDSNGRYNN
LEVYLHNLVQHIVYLQNQGGTQMEKN

Enzyme Prediction     

No EC number prediction in MGYG000001599_01413.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL1	372	578	1.1e-63	0.994535519125683

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14948	BACON	1.07e-14	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	2.70e-06	138	214	15	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	1.97e-05	221	297	3	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.
smart00656	Amb_all	0.002	423	563	38	173	Amb_all domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT78065.1	0.0	1	805	1	794
ALJ48967.1	0.0	1	805	1	794
SCV08385.1	0.0	1	805	1	794
QRQ55777.1	0.0	1	805	1	794
QDM11683.1	0.0	1	805	1	794

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q5B297	6.37e-37	309	789	15	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
B8NQQ7	3.78e-36	314	789	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
Q4WL88	1.75e-35	309	789	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
B0XMA2	2.37e-35	309	789	16	415	Probable pectate lyase C OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=plyC PE=3 SV=1
Q2UB83	5.76e-35	314	789	21	414	Probable pectate lyase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 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	1.000077	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001599_01413.