dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000004892_00827

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Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1858;

CAZyme ID

MGYG000004892_00827

CAZy Family

GH141

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1119		122175.31	4.3533

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004892	1550618	MAG	China	Asia

Gene Location

Start: 1453; End: 4812 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000004892_00827.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH141	1	504	1.2e-46	0.905123339658444

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14256	Dockerin_I	7.62e-14	1052	1105	1	54	Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
pfam00404	Dockerin_1	2.37e-10	1053	1100	1	48	Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium.
cd00987	PDZ_serine_protease	1.50e-08	676	764	2	90	PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.
pfam13229	Beta_helix	2.19e-06	255	414	1	137	Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.
cd14253	Dockerin	1.30e-05	1053	1105	1	53	Dockerin repeat domain. Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWW32784.1	1.16e-107	1	739	77	772
AFZ35556.1	1.44e-25	4	647	106	709
BAU63437.1	8.93e-23	4	552	115	624
SDT08880.1	2.00e-20	4	422	80	526
QLQ40376.1	2.27e-19	4	508	78	588

PDB Hits help

has no PDB hit.

Swiss-Prot Hits help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000059	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000004892_00827.