dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000089_00864

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Basic Information help

Species

CAG-353 sp900066885

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; CAG-353; CAG-353 sp900066885

CAZyme ID

MGYG000000089_00864

CAZy Family

CBM2

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
673	MGYG000000089_1\|CGC8	74173.57	4.314

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000089	3052732	Isolate	United Kingdom	Europe

Gene Location

Start: 852719; End: 854740 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.4	3.2.1.91	3.2.1.73

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH5	289	627	6.6e-117	0.9967741935483871
CBM2	141	237	2.3e-17	0.900990099009901

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	1.88e-44	288	622	1	272	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	9.67e-37	283	640	33	383	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
smart00637	CBD_II	5.69e-14	147	226	2	77	CBD_II domain.
pfam00553	CBM_2	7.10e-12	139	228	1	86	Cellulose binding domain. Two tryptophan residues are involved in cellulose binding. Cellulose binding domain found in bacteria.
smart01063	CBM49	5.42e-05	147	226	8	83	Carbohydrate binding domain CBM49. This domain is found at the C terminal of cellulases and in vitro binding studies have shown it to binds to crystalline cellulose.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CUH91791.1	6.66e-240	138	673	38	577
QWT53501.1	2.93e-230	268	673	97	503
ADD61853.1	4.79e-229	268	673	97	503
QNL98527.1	2.74e-228	268	673	97	503
AGS52139.1	2.64e-224	142	673	124	661

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ECE_A	2.48e-67	284	640	10	343	AcidothermusCellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose [Acidothermus cellulolyticus],1ECE_B Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose [Acidothermus cellulolyticus]
1VRX_A	1.84e-66	284	640	10	343	ChainA, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus],1VRX_B Chain B, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus]
3VVG_A	4.83e-55	276	648	4	376	TheCrystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_B The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_C The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3W6L_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
3W6M_A	6.69e-55	276	648	4	376	Contributionof disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
2ZUM_A	3.36e-54	276	648	37	409	FunctionalAnalysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_A Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_B Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_C Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P10474	3.94e-178	271	671	621	1021	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
Q05332	2.24e-151	267	673	32	470	Endoglucanase G OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celG PE=3 SV=1
P50400	2.37e-144	275	672	41	438	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
P04956	2.36e-128	277	673	39	469	Endoglucanase B OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celB PE=3 SV=1
P23548	3.34e-78	274	648	27	382	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000009	1.000025	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000089_00864.