CAZyme Information: MGYG000001151_01318

Basic Information

• Species: Ruminococcus_C sp000433635
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp000433635
• CAZyme ID: MGYG000001151_01318
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
770	MGYG000001151_158|CGC1	85334.85	4.0764

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001151	2508735	MAG	China	Asia

• Gene Location: Start: 14592; End: 16904 Strand: -

Full Sequence      

MKGLQKFAALCTSVVLGVCGMGSVLAQPLTADAATESTVPEGFVYVDGTHFMCDGEPFYF
AGCNSYDMFTLGDGSSNDSTEAIETKFMNKEAIDARMQQMEDNGVRVLRTWGFSNETWHG
FELAPGEYNEAEFMLFDYIMYSAQQHNIRVIITLENYWEAYGGIDKKLSWAGAGSGGNHK
SRAAYFTNETCKQWYKDYAKHFAERTNYFTGVQYKDDPTVFAWDLMNEPRYQDAGEDSTG
LTLRAWVDEMGAYIKEVDPNHMVYAGLEGHGVDYGFGGDEGNPFVYIQQSPYIDFCSAHP
YPDEHWANMTPEDTKNTMVQWIEDAHQEVGKPFVVTEFNVHSSLPEAEYEDYWKAVFDTI
EEYDAAGGLFWEFNDRKLSEFTGMDGDPILTYFQQHAARMEDKTPMNSLYTKNTVVDKDN
PMDVLLSYEMQSGTVTGLQLDDTTLTAGTDYKQTEDTITVSASVFSDVATGEHTIQLLTS
EGNQPKVKIRVYSAAEEAQKRSVIDDFESYGEDTALAAAYTTNVNGDTLKISLDAEHTKN
GSYAMKYDYSVADGGAGYCGATKKLSNADWTGFDGVRFWILSDGSNRETTFQFVDGAGAY
WESIQKVTAETGWQEVKIPFSDFHVQQWGTAAETPTLQGVSEFSIYTGQNGNPGTGVWYF
DDIGLYRAGSTTTTTTTTTGTTTTTTTTTTTAETTTDADTDTNYGDVNLDGKVDLVDAIM
INKYLAGQITLSEQATKNADVNADGSLGDGDSTILMRFILMVIPNLPYVE

Enzyme Prediction     

No EC number prediction in MGYG000001151_01318.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	91	373	2.3e-80	0.9930795847750865
CBM23	503	666	3.7e-47	0.9938271604938271

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3934	COG3934	1.52e-21	89	388	24	289	Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism].
cd14256	Dockerin_I	2.18e-18	704	760	1	57	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.
pfam03425	CBM_11	2.94e-16	504	666	7	173	Carbohydrate binding domain (family 11).
pfam00404	Dockerin_1	4.43e-11	705	760	1	56	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.
pfam00150	Cellulase	5.97e-10	87	375	23	270	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADL52789.1	2.03e-199	27	665	604	1332
BAV13033.1	2.03e-199	27	665	604	1332
ADZ85047.1	4.08e-185	41	529	636	1129
QEH70547.1	1.29e-182	41	529	636	1129
AEY66038.1	4.99e-143	37	406	30	395

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1RH9_A	6.28e-51	43	381	6	344	ChainA, endo-beta-mannanase [Solanum lycopersicum]
4QP0_A	1.42e-42	43	372	4	325	CrystalStructure Analysis of the Endo-1,4-beta-mannanase from Rhizomucor miehei [Rhizomucor miehei]
3PZ9_A	6.46e-40	48	371	18	340	Nativestructure of endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3PZG_A I222 crystal form of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3PZI_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 in complex with beta-D-glucose [Thermotoga petrophila RKU-1],3PZM_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with three glycerol molecules [Thermotoga petrophila RKU-1],3PZN_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with citrate and glycerol [Thermotoga petrophila RKU-1],3PZO_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 in complex with three maltose molecules [Thermotoga petrophila RKU-1],3PZQ_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with maltose and glycerol [Thermotoga petrophila RKU-1]
6TN6_A	5.50e-38	48	371	1	326	X-raystructure of the endo-beta-1,4-mannanase from Thermotoga petrophila [Thermotoga petrophila RKU-1]
3WH9_A	3.78e-32	43	389	2	324	Theligand-free structure of ManBK from Aspergillus niger BK01 [Aspergillus niger],3WH9_B The ligand-free structure of ManBK from Aspergillus niger BK01 [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9FZ29	3.28e-55	39	394	25	380	Mannan endo-1,4-beta-mannosidase 1 OS=Arabidopsis thaliana OX=3702 GN=MAN1 PE=2 SV=1
Q9SG94	4.63e-54	23	381	11	375	Mannan endo-1,4-beta-mannosidase 3 OS=Arabidopsis thaliana OX=3702 GN=MAN3 PE=2 SV=1
Q6Z310	1.94e-53	25	382	20	377	Putative mannan endo-1,4-beta-mannosidase 9 OS=Oryza sativa subsp. japonica OX=39947 GN=MAN9 PE=2 SV=2
Q7Y223	9.43e-53	43	381	42	387	Mannan endo-1,4-beta-mannosidase 2 OS=Arabidopsis thaliana OX=3702 GN=MAN2 PE=2 SV=1
Q9FJZ3	1.24e-52	32	381	20	372	Mannan endo-1,4-beta-mannosidase 7 OS=Arabidopsis thaliana OX=3702 GN=MAN7 PE=2 SV=1

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
0.000282	0.999027	0.000225	0.000164	0.000146	0.000127

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001151_01318.