dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002881_00330

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Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus;

CAZyme ID

MGYG000002881_00330

CAZy Family

GH48

CAZyme Description

Endoglucanase F

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
848	MGYG000002881_36\|CGC1	93022.44	4.1681

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002881	1270591	MAG	United States	North America

Gene Location

Start: 1615; End: 4161 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.-

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH48	44	752	2.8e-201	0.9950900163666121

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam02011	Glyco_hydro_48	0.0	44	755	1	620	Glycosyl hydrolase family 48. Members of this family are endoglucanase EC:3.2.1.4 and exoglucanase EC:3.2.1.91 enzymes that cleave cellulose or related substrate.
cd14256	Dockerin_I	1.63e-09	773	829	2	55	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	8.23e-05	773	829	1	54	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.
cd14256	Dockerin_I	0.002	719	793	3	56	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADX05724.1	0.0	1	795	1	805
CBL17316.1	1.72e-272	1	838	1	801
ADU23081.1	4.10e-240	1	758	1	779
BAJ05814.1	4.10e-240	1	758	1	779
CAS03459.1	1.87e-237	1	766	1	788

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1L1Y_A	6.08e-160	11	758	8	664	ChainA, cellobiohydrolase [Acetivibrio thermocellus],1L1Y_B Chain B, cellobiohydrolase [Acetivibrio thermocellus],1L1Y_C Chain C, cellobiohydrolase [Acetivibrio thermocellus],1L1Y_D Chain D, cellobiohydrolase [Acetivibrio thermocellus],1L1Y_E Chain E, cellobiohydrolase [Acetivibrio thermocellus],1L1Y_F Chain F, cellobiohydrolase [Acetivibrio thermocellus],1L2A_A Chain A, cellobiohydrolase [Acetivibrio thermocellus],1L2A_B Chain B, cellobiohydrolase [Acetivibrio thermocellus],1L2A_C Chain C, cellobiohydrolase [Acetivibrio thermocellus],1L2A_D Chain D, cellobiohydrolase [Acetivibrio thermocellus],1L2A_E Chain E, cellobiohydrolase [Acetivibrio thermocellus],1L2A_F Chain F, cellobiohydrolase [Acetivibrio thermocellus]
5YJ6_A	9.23e-159	43	757	12	636	ChainA, Dockerin type I repeat-containing protein [Acetivibrio thermocellus DSM 1313]
1F9O_A	8.99e-158	40	757	5	629	Crystalstructure of the cellulase Cel48F from C. Cellulolyticum with the thiooligosaccharide inhibitor PIPS-IG3 [Ruminiclostridium cellulolyticum],1FAE_A Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellobiose [Ruminiclostridium cellulolyticum],1FBO_A Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellobiitol [Ruminiclostridium cellulolyticum],1FCE_A PROCESSIVE ENDOCELLULASE CELF OF CLOSTRIDIUM CELLULOLYTICUM [Ruminiclostridium cellulolyticum],1G9G_A Xtal-Structure Of The Free Native Cellulase Cel48f [Ruminiclostridium cellulolyticum]
1F9D_A	2.52e-157	40	757	5	629	ChainA, ENDO-1,4-BETA-GLUCANASE F [Ruminiclostridium cellulolyticum],1FBW_A Chain A, ENDO-1,4-BETA-GLUCANASE F [Ruminiclostridium cellulolyticum],2QNO_A Chain A, Endoglucanase F [Ruminiclostridium cellulolyticum]
1G9J_A	2.52e-157	40	757	5	629	ChainA, CELLULASE CEL48F [Ruminiclostridium cellulolyticum]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A3DH67	1.94e-163	11	793	8	698	Cellulose 1,4-beta-cellobiosidase (reducing end) CelS OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celS PE=1 SV=1
P0C2S5	1.94e-163	11	793	8	698	Cellulose 1,4-beta-cellobiosidase (reducing end) CelS OS=Acetivibrio thermocellus OX=1515 GN=celS PE=1 SV=1
P37698	7.42e-161	2	796	1	689	Endoglucanase F OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=celCCF PE=1 SV=2
P50900	1.18e-151	41	796	37	690	Exoglucanase-2 OS=Thermoclostridium stercorarium (strain ATCC 35414 / DSM 8532 / NCIMB 11754) OX=1121335 GN=celY PE=1 SV=2
P22534	6.84e-142	73	755	1137	1739	Endoglucanase A OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celA PE=3 SV=2

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
0.000253	0.999001	0.000184	0.000211	0.000178	0.000148

TMHMM Annotations help

There is no transmembrane helices in MGYG000002881_00330.