CAZyme Information: MGYG000003003_00582

Basic Information

• Species: CAG-1427 sp900539675
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; CAG-1427; CAG-1427 sp900539675
• CAZyme ID: MGYG000003003_00582
• CAZy Family: CBM13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1202	MGYG000003003_10|CGC1	129569.9	4.2405

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003003	1845572	MAG	United States	North America

• Gene Location: Start: 17782; End: 21390 Strand: -

Full Sequence      

MVGTKILKGFLSVVLAAGLCPSVAFAQPNEEATNGVSALTVVDTDSGDSVLGEDHEQSGS
NDNDIQSDVESSTDSGTKGNDASDDFTQDGNENFQGNESDKSGLTPDSSDGGLSINEPSE
NYDEAKVSQETESSNSDNDSNTDEISDGARALEKFGYVPADNIEDGQYLLQPSSNMDLTF
SPTALNLNSTETPRDEIFSIDVISEDSIQISNQQGKILTAGTNDVLFTDENGSDSQKWQF
FVQSQSDSNYAILNIATNKVLDISSGRITQGTKVGLYQPNGTVAQQWQLFDAGQVIEKLD
KQASGTKNLLSTDQIYWIETTIEPNMVIDVSGASSENDANVQLYRFNNTAAQQWTVSYDE
QGYVTFINVQSGKALDVQAGKGVSGANVRQYTPNGTYAQKWIVSQSSDGSYEIKSALWQG
LSLDLAGGSVVNKTNIRLYHSNDTAAQRFNIVTEDMLYSTLDEEAAANAGVLKDGTYLIN
SSLANDKVLDVANASLENAANVQLYTSNMTKAQQWTVSHDAMGYITFTNVGSEKVLDVAS
GNILPGTNVRQYASNESRAQKWIALPNEDGTFRIKSALGNDIVLDISKASASNKANVQTY
TSNGTIAQKFNFIDVNPVVDPCQDCELGGKYYKVVSALDGDYVLDVAKASLANGANIQLY
KANESYAQLYKFEFIPTPNDQSKGYYQIINARSGKALDVQDGNLVNKTNIQQWEPDSANP
NQLFSLVQNKDYTYTFINKGTGLVLDVSGAVAKNGSNIQGYNNNDSNAQRFVVEEVSDLM
PEGVVSLYSDLNSSKVVDVESGSLSSGANVQLYTENGSLAQKWNCSKVGNNVFTLQSLRS
GMNLAVDASGNVCQQTPSDSKAQQWIPTISNGLTVLKNAQTGKVLDVKNGSSADGTNIQT
YENNGTAAQRFNVVSVDILAGGTYFIQALKSPGFVMDVSGASSSDGANVQLYSNNDSGAQ
KWNVTKNGDGTYTFKNAANGKALDLKSANATSGSNIQQWTANGSAAQKWNLQYMNGGGIR
IVSAVNPDYSIGISGNAYINKANIELQSNATSDGQRFTFEPTKYVPPLPSDRQAMLDTIS
NYSSGTQWLIAVDRSTHKVGVFKGSMNNWSYQYYWSCVTGAPGTPTITGDYYTTGFKRTA
LTTDSRALWATQIWGGYFFHSILASTSELGNSLSHGCIRLDYSDALWIYNNIYAGTRVVI
YG

Enzyme Prediction     

No EC number prediction in MGYG000003003_00582.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM13	873	1027	1.3e-28	0.7606382978723404
CBM13	327	461	6.6e-23	0.6702127659574468
CBM13	732	866	5.3e-18	0.675531914893617
CBM13	473	564	8.7e-18	0.46808510638297873
CBM13	629	730	3.2e-16	0.4787234042553192

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam14200	RicinB_lectin_2	4.18e-20	907	999	1	89	Ricin-type beta-trefoil lectin domain-like.
pfam14200	RicinB_lectin_2	5.93e-20	350	439	1	89	Ricin-type beta-trefoil lectin domain-like.
pfam14200	RicinB_lectin_2	5.04e-19	671	761	4	89	Ricin-type beta-trefoil lectin domain-like.
cd16913	YkuD_like	1.60e-18	1089	1201	1	121	L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD. Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.
NF035929	lectin_1	2.64e-17	882	1011	721	836	lectin. Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRT49575.1	4.05e-111	297	1066	109	871
BAK44091.1	9.32e-72	299	1086	128	906
QRT49576.1	5.35e-55	461	981	414	928
AMK55176.1	2.30e-27	308	777	509	975
QOL34941.1	3.23e-21	297	530	753	985

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4XXT_A	1.13e-15	1086	1201	139	261	Crystalstructure of Fused Zn-dependent amidase/peptidase/peptodoglycan-binding domain-containing protein from Clostridium acetobutylicum ATCC 824 [Clostridium acetobutylicum ATCC 824]
4OUJ_A	5.09e-06	628	913	1	292	Crystalstructure of HA33B-Lac [Clostridium botulinum B1 str. Okra],4OUJ_B Crystal structure of HA33B-Lac [Clostridium botulinum B1 str. Okra]
4LO0_A	8.46e-06	630	913	1	289	ApoHA17-HA33 [Clostridium botulinum],4LO0_B Apo HA17-HA33 [Clostridium botulinum],4LO1_A HA17-HA33-Gal [Clostridium botulinum],4LO1_B HA17-HA33-Gal [Clostridium botulinum],4LO2_A HA17-HA33-Lac [Clostridium botulinum],4LO2_B HA17-HA33-Lac [Clostridium botulinum],4LO3_A HA17-HA33-LacNac [Clostridium botulinum],4LO3_B HA17-HA33-LacNac [Clostridium botulinum],4LO7_B HA70(D3)-HA17-HA33 [Clostridium botulinum],4LO7_D HA70(D3)-HA17-HA33 [Clostridium botulinum],4LO7_F HA70(D3)-HA17-HA33 [Clostridium botulinum],4LO7_H HA70(D3)-HA17-HA33 [Clostridium botulinum],4QD2_C Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex [Clostridium botulinum A str. Hall],4QD2_D Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex [Clostridium botulinum A str. Hall],4QD2_H Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex [Clostridium botulinum A str. Hall],4QD2_I Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex [Clostridium botulinum A str. Hall],5BP5_A Crystal structure of HA17-HA33-IPT [Clostridium botulinum],5BP5_B Crystal structure of HA17-HA33-IPT [Clostridium botulinum],5BQU_A Crystal structure of HA17-HA33-Lactulose [Clostridium botulinum],5BQU_B Crystal structure of HA17-HA33-Lactulose [Clostridium botulinum]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000298	0.998934	0.000253	0.000172	0.000172	0.000152

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003003_00582.