dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000517_01108

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Basic Information help

Species

UMGS1889 sp900556055

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UMGS1889; UMGS1889 sp900556055

CAZyme ID

MGYG000000517_01108

CAZy Family

CBM2

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
693		75619.26	4.5188

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000517	2612851	MAG	Fiji	Oceania

Gene Location

Start: 102899; End: 104980 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	307	645	3.2e-118	0.9967741935483871
CBM2	154	250	1.5e-16	0.900990099009901

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	5.88e-46	306	640	1	272	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	1.20e-37	315	658	47	383	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
smart00637	CBD_II	1.28e-10	160	251	1	88	CBD_II domain.
pfam00553	CBM_2	2.57e-09	153	249	1	93	Cellulose binding domain. Two tryptophan residues are involved in cellulose binding. Cellulose binding domain found in bacteria.
smart01063	CBM49	7.01e-05	154	240	1	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	2.07e-241	152	691	38	577
ADD61853.1	4.47e-237	286	691	97	503
QNL98527.1	6.34e-237	286	691	97	503
QWT53501.1	1.47e-235	286	691	97	503
AGS51642.1	4.70e-234	161	691	83	611

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ECE_A	3.85e-64	304	665	12	350	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	2.81e-63	304	665	12	350	ChainA, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus],1VRX_B Chain B, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus]
3VVG_A	3.48e-61	308	666	21	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	4.84e-61	308	666	21	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	2.73e-60	308	666	54	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	7.31e-175	289	690	621	1022	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
Q05332	2.97e-145	293	691	40	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	9.54e-136	286	692	34	440	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
P04956	8.12e-135	291	691	35	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	2.91e-76	291	666	32	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
0.000001	0.000028	0.998470	0.000000	0.001541	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000517_01108.