CAZyme Information: MGYG000002403_04699

Basic Information

• Species: Robinsoniella peoriensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella peoriensis
• CAZyme ID: MGYG000002403_04699
• CAZy Family: GH95
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1963	MGYG000002403_123|CGC1	218379.75	4.2628

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002403	7202103	Isolate	not provided	not provided

• Gene Location: Start: 471; End: 6362 Strand: +

Full Sequence      

MEKKKWRHKIYRCIGAGMAAVLLTGSIPAPVLGAEVKNKEPLSAGKVFSDTYQDPQKGNL
NWREAMVSGNGENGVMESCHPVNDTFIFQNTTFNMPTDDYRETMDLTGELGDAREAVMNN
WNFWSQVQPELDYDYTLHPGHQLRMRLDDLEETDVSDYQRWTDYETAEIGVSFQADGETW
ERSTFTSREDNVTITWLRQPENGGRLNTTLSIDDLSDMAIDQGREIDEGLQYKKIAAQDG
SYLGLTAHYPVYDNSELKEAGFAGVTYVVNIGGTKERVRLGDIQDYLNAGTEDNFGIKVK
DAEGVVLITKSARDKEMGPASAFAGQNELPLVQRLIEETRAVAENEAYRTNGYFDYSKAL
APHEQLHGSEFNKIKFDLAGDEADDSLTNEELISKQRNSDRLNHAMLERAFYAGRYAQVC
TSGYSTSRLSGMWIGAWNGYWQADYTTDANVNLQISGVNIGNLQNASEGYINFLLRILPD
FEMNATQVYGMHDALLAPPRTDGDRGNLVHFNADYPFNYWNAGASWLLLPVYEYWQCFGN
SQIPLGKDIDLNALRSVLSIHDQDLSDAQISQIEERGYFDLEQDLLLPLLTKQANFWEQM
ADPRYYEGEDGYKHYDEGKTSLEGNEKYLILPGYSPENKPGNTGIAISANSTMDIAAARD
GLDMTIAMEEAVQRPGYEEAVEKWKSLKKLLPEYKYDTDGSLKEWALRDYSEQNNHRHVS
HMYGVWPAHDGADDSKLMEGAKKALENRKKYNTGDDNASHGWLHQALTEARLKNAQGVTD
SLLPLFTGSKLYYSSMMTNHDRNRDSAYCTDALITIPSIMLETLAYSDTGKIELLPALPD
DWGKGSITGMMARSRAQIERLDWDMEKGEVTARIRSDAAQEIDLSCGMDSSSAVILEGRG
EIITGEGVVRLTMEEGETAEVRFVRGQISQGTYQIIAEDKSLESVYTDESSDVVLGTPAD
SAAQKWNLTGRGIGQYLITSVDSGYALSADDGKVVQTLHGDIWQIEELEEGCRILTPDRT
KALTIKNGVPVIGDAGGAAVFQMVPQEYTEENLAVGSIEITGPKSIRSGESISLEALVET
AEGMQNDMELQWSVTETQGRAKINAQGVLTAQKAGAVTVQVSPKKAPRYVQEKVYEIKEG
LLDQDKLMGTVFGREEGEWEAGSPPALAFDGNTDTAYDGQNGGYAGLEMGGAFTLEGFRY
VVRGGFSDRWPGVRVQGSDDMTNWDTLYTIEESLDHPVYNSVWFADLPEEERPLKPYSYY
RVYSGDSEYCNVAELEFYGKAVNAFDGLENAIAYGKSIGTEGYEPGSVSRLLKALERAKQ
ITAESPEADIQEVYKALKKAIYNLKRPGLLYNDDRTVNLTGQWEEWADDRLFSEKEIYTS
DPGAAFSFRFDGIGFEMMGNKNPGLGYVKITVDGEDIPGGEKVSLYDSHSEGYQRQSIFK
YMDLKKGIHTVTVELLGNQNQEGKAPKMSVDAFYLFSVPEDETVDKTKLEQLLEELEQTE
ESDYTAESWEIYAAAYDQARIILDKADALQSEVDGAVSELKEAWNNLVSLTSVLEAGILE
YTVVESEADKYTKESWDSYREVYLMAQALLKQGVYTEAQVEQTIQELKAAREALCLKPET
TGWRELELAVAMAEKLEKVQSAYSCYTTESWQAVQEALDNARALMKTDADQDEIDHAFLE
LITACNLLKNGVQKSGLKAVIDGTEAILADTSAMAEYTPESVAAVREALKEARFAFAESS
ADQETINRVSRKLMDAVTNLLVKEADARLGILIQKAAELLKNADKYTTESVDKLKTELEA
ARAVNANSLATENEINEAYQSLAEAITALVRKANKEELRNALEKAEEILQESGRYLEESI
AGLETVDQEARAVYEDESADMDTVGTILKKLINEILKARLMGDVDLNGKVDTDDSANVLK
FSAELQELTDEQGKAADVNRDGVTDSDDAARILQYASEKIGEF

Enzyme Prediction     

No EC number prediction in MGYG000002403_04699.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH95	52	886	3.7e-118	0.9722991689750693
CBM62	1149	1279	2.5e-17	0.9694656488549618

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam14498	Glyco_hyd_65N_2	2.97e-11	61	308	9	224	Glycosyl hydrolase family 65, N-terminal domain. This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain.
cd14256	Dockerin_I	3.39e-10	1902	1955	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.
cd14253	Dockerin	3.33e-07	1902	1956	1	55	Dockerin repeat domain. Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit.
pfam00404	Dockerin_1	7.26e-07	1902	1955	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.
cd14255	Dockerin_III	3.07e-06	1902	1955	1	59	Type III 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. Two specific calcium-dependent interactions between cohesin and dockerin appear to be essential for cellulosome assembly, type I and type II. This subfamily represents the atypical type III dockerins and related domains.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACB76390.1	1.55e-265	26	923	25	927
QYR23103.1	6.11e-264	48	923	16	901
AFH60346.1	5.35e-263	60	924	30	900
AIQ45759.1	2.74e-260	48	895	16	872
AIQ51360.1	2.59e-253	48	876	16	852

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UFC_A	8.25e-21	42	863	16	721	Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus]
7KMQ_A	1.04e-20	41	885	34	758	ChainA, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306],7KMQ_B Chain B, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306]
2EAB_A	7.32e-17	102	919	117	867	Crystalstructure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAB_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAC_A Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum],2EAC_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum]
2EAE_A	1.65e-16	102	919	116	866	ChainA, Alpha-fucosidase [Bifidobacterium bifidum]
2EAD_A	3.74e-16	102	919	117	867	ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8L7W8	7.23e-19	158	863	163	792	Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 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
0.000335	0.998850	0.000257	0.000213	0.000173	0.000142

TMHMM  Annotations     

start	end
13	32