dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000002295_00782

You are here: Home > Sequence: MGYG000002295_00782

Basic Information help

Species

Ruminococcus_C callidus

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C callidus

CAZyme ID

MGYG000002295_00782

CAZy Family

GH5

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
925	MGYG000002295_3\|CGC1	101592.41	4.0932

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002295	2957494	Isolate	China	Asia

Gene Location

Start: 49589; End: 52366 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.151	3.2.1.78

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH5	69	390	3.1e-94	0.9896193771626297
CBM23	533	696	1e-45	0.9938271604938271

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3934	COG3934	9.13e-38	46	420	4	313	Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism].
pfam03425	CBM_11	1.55e-14	526	696	2	173	Carbohydrate binding domain (family 11).
cd14256	Dockerin_I	4.60e-14	858	914	1	57	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.
pfam03442	CBM_X2	1.21e-13	709	788	2	83	Carbohydrate binding domain X2. This domain binds to cellulose and to bacterial cell walls. It is found in glycosyl hydrolases and in scaffolding proteins of cellulosomes (multiprotein glycosyl hydrolase complexes). In the cellulosome it may aid cellulose degradation by anchoring the cellulosome to the bacterial cell wall and by binding it to its substrate. This domain has an Ig-like fold.
pfam03442	CBM_X2	1.36e-10	439	516	1	80	Carbohydrate binding domain X2. This domain binds to cellulose and to bacterial cell walls. It is found in glycosyl hydrolases and in scaffolding proteins of cellulosomes (multiprotein glycosyl hydrolase complexes). In the cellulosome it may aid cellulose degradation by anchoring the cellulosome to the bacterial cell wall and by binding it to its substrate. This domain has an Ig-like fold.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL33682.1	1.20e-209	36	801	40	894
CBK97477.1	1.61e-204	36	788	40	883
QEH70547.1	5.65e-198	3	800	2	635
ADZ85047.1	6.07e-197	3	535	2	544
CCO04515.1	5.27e-188	3	779	6	876

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3PZ9_A	3.48e-82	47	421	21	378	Nativestructure of endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3PZG_A I222 crystal form of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3PZI_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 in complex with beta-D-glucose [Thermotoga petrophila RKU-1],3PZM_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with three glycerol molecules [Thermotoga petrophila RKU-1],3PZN_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with citrate and glycerol [Thermotoga petrophila RKU-1],3PZO_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 in complex with three maltose molecules [Thermotoga petrophila RKU-1],3PZQ_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with maltose and glycerol [Thermotoga petrophila RKU-1]
6TN6_A	3.35e-79	47	421	7	364	X-raystructure of the endo-beta-1,4-mannanase from Thermotoga petrophila [Thermotoga petrophila RKU-1]
4QP0_A	6.32e-77	36	430	2	356	CrystalStructure Analysis of the Endo-1,4-beta-mannanase from Rhizomucor miehei [Rhizomucor miehei]
4AWE_A	2.95e-61	37	434	5	385	TheCrystal Structure of Chrysonilia sitophila endo-beta-D-1,4- mannanase [Neurospora sitophila]
3ZIZ_A	3.29e-60	42	410	19	338	ChainA, Gh5 Endo-beta-1,4-mannanase [Podospora anserina]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B8NVK8	1.00e-71	21	434	22	386	Probable mannan endo-1,4-beta-mannosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=manA PE=3 SV=2
Q2TXJ2	2.66e-71	21	433	22	385	Probable mannan endo-1,4-beta-mannosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=manA PE=3 SV=1
A1D8Y6	5.35e-65	31	413	19	362	Probable mannan endo-1,4-beta-mannosidase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=manA PE=3 SV=1
Q0JKM9	2.66e-64	37	430	36	406	Mannan endo-1,4-beta-mannosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=MAN1 PE=2 SV=2
A1C8U0	2.77e-63	34	358	89	375	Mannan endo-1,4-beta-mannosidase F OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=manF PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.001040	0.790082	0.207573	0.000632	0.000360	0.000278

TMHMM Annotations download full data without filtering help

start	end
7	29