dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000004633_01157

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Basic Information help

Species

Erysipelatoclostridium sp002160495

Lineage

Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium sp002160495

CAZyme ID

MGYG000004633_01157

CAZy Family

CBM32

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
510	MGYG000004633_33\|CGC1	57015.27	3.9149

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004633	2814686	MAG	Germany	Europe

Gene Location

Start: 20193; End: 21725 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000004633_01157.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CBM32	106	232	3.6e-24	0.9516129032258065
CBM32	1	80	1.7e-16	0.6693548387096774

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00754	F5_F8_type_C	6.32e-17	103	230	3	125	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam00754	F5_F8_type_C	3.00e-09	2	78	40	125	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
cd00057	FA58C	1.21e-07	103	235	15	143	Substituted updates: Jan 31, 2002
pfam07554	FIVAR	5.74e-07	307	369	1	69	FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
TIGR01612	235kDa-fam	9.23e-05	236	447	989	1240	reticulocyte binding/rhoptry protein. This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQY28197.1	2.79e-207	1	505	1337	1834
QMW73769.1	2.79e-207	1	505	1337	1834
QPS12968.1	2.79e-207	1	505	1337	1834
QQV04833.1	3.91e-207	1	505	1337	1834
QUN12787.1	1.34e-170	1	510	1343	1892

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2RV9_A	3.52e-26	95	235	7	136	Solutionstructure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis]
4ZXE_A	3.63e-26	95	235	8	137	X-raycrystal structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5. [Paenibacillus fukuinensis],4ZXE_B X-ray crystal structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5. [Paenibacillus fukuinensis],4ZXE_C X-ray crystal structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5. [Paenibacillus fukuinensis]
4ZY9_A	6.85e-26	95	235	8	137	X-raycrystal structure of selenomethionine-labelled V110M mutant of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis],4ZY9_B X-ray crystal structure of selenomethionine-labelled V110M mutant of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis]
2RVA_A	4.41e-16	1	83	51	137	Solutionstructure of chitosan-binding module 2 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis]
4ZZ5_A	4.52e-16	1	83	52	138	X-raycrystal structure of chitosan-binding module 2 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis],4ZZ5_B X-ray crystal structure of chitosan-binding module 2 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis],4ZZ8_A X-ray crystal structure of chitosan-binding module 2 in complex with chitotriose derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis],4ZZ8_B X-ray crystal structure of chitosan-binding module 2 in complex with chitotriose derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
E8MGH9	9.08e-11	239	431	1668	1871	Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 PE=1 SV=1
P26831	4.21e-09	6	453	1112	1589	Hyaluronoglucosaminidase OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagH PE=1 SV=2

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
1.000040	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations download full data without filtering help

start	end
483	502