CAZyme Information: MGYG000000151_01000

Basic Information

• Species: Clostridium paraputrificum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium paraputrificum
• CAZyme ID: MGYG000000151_01000
• CAZy Family: CBM2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
964		107300.95	4.8319

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000151	3486414	Isolate	United Kingdom	Europe

• Gene Location: Start: 386783; End: 389677 Strand: -

Full Sequence      

MHIKKRIKRMAAFVVFLGILFTLMPCKLTSASASGVPGKPTLSSDQYGVDYDGDYNITMN
MYYGNNATSYKLYERYGINGEYKVISEGELTDGTPAVQSKVIEVRGRQNIGIYSYYAEFI
NSYGSACSDVLEVRVGKDGDAKIIIDKVDNEGIQYQTTIAQCKESYKITNRKNTSSKFSV
ISSNTSVVKASIKDGNTLVVEGVSAGRSGIKIVDESTGDIRQIGFRVKNSDGSLPGMPDY
LSIGQVSEDTDNDLNFWKDTSNNDTNKRCDIRYIYVNGGPFGGWRSWTTEDGDRVKSYIR
ESLKLGMIPFFVYYNIPDSGESYELDLKHINDKAYMEGYYKDLKFFLDICNEYAGDETVG
MIFEPDFLGYMMQQNKKDPSTISALVDTAYTSGVLEKGKDPTFENSVKGLVESINYTVRK
EYKNSYFGWQFNIWSYDSTEIPNQGLLHKTEFIGWDNGRQFIKQVAQETADYYKSAGITS
YDADFISIDKYGLDGAYEDNAATNPEGSKWLWNADIWNNYLLYTKTLHEVTEKPVILWQI
PVGHLNSSEEPNPYNGGKFDDLTNAVGNYEDSAPTYFFGDTFNASSDARKEYFSKNLAND
SKIKVEGNKITWGGHMEETKDAGVVSILFGAGVNASTDAVGSPAPDNYWWITKAQRYLKN
PLSLDITINPPAPSDEKPLSPEISSSSLESNGNYTLKIKIPSNSKAKEYKLYENGKVIKN
GSVATSETTVRHEILNKPTGTYMYQVELINGSASSTSQIITVKVSNNVVPPIDVPLKATL
TVDKSSNDGNYNLAISIPEKSNAISYNLYEDDKIIKTGDVSILPQVINVNFTNKIKGTYV
YRVDLINKDATTKSDTITVSCNPTVVENGIKVEYATTADWGTGANFQITIFNNTDMDLVN
WTLCFDFDKKINSLPDVNFTQNGSTYTITPKSWNNVIPKGGKLVLFGGCEGNVNNLNIYN
VKVN

Enzyme Prediction     

No EC number prediction in MGYG000000151_01000.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM2	871	949	2.6e-17	0.7821782178217822

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00553	CBM_2	1.61e-13	871	941	2	74	Cellulose binding domain. Two tryptophan residues are involved in cellulose binding. Cellulose binding domain found in bacteria.
smart00637	CBD_II	2.44e-12	877	941	1	67	CBD_II domain.
cd02848	E_set_Chitinase_N	2.85e-05	702	757	46	99	N-terminal Early set domain associated with the catalytic domain of chitinase. E or "early" set domains are associated with the catalytic domain of chitinase at the N-terminal end. Chitinases hydrolyze the abundant natural biopolymer chitin, producing smaller chito-oligosaccharides. Chitin consists of multiple N-acetyl-D-glucosamine (NAG) residues connected via beta-1,4-glycosidic linkages and is an important structural element of fungal cell wall and arthropod exoskeletons. On the basis of the mode of chitin hydrolysis, chitinases are classified as random, endo-, and exo-chitinases and belong to families 18 and 19 of glycosyl hydrolases based on sequence criteria. The N-terminal domain of chitinase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSW17965.1	0.0	1	953	1	957
QDT41727.1	6.17e-198	36	693	160	805
QDV49819.1	2.58e-197	35	671	166	790
QDU09854.1	1.46e-192	35	678	158	786
QDT98581.1	1.47e-191	35	678	158	784

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6BT9_A	4.75e-09	770	952	482	660	ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
3NDY_E	8.52e-07	868	947	1	82	Thestructure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_F The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_G The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_H The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDZ_E The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_F The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_G The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_H The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000633	0.596145	0.402557	0.000262	0.000199	0.000172

TMHMM  Annotations     

start	end
12	34