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CAZyme Information: MGYG000000387_01515

You are here: Home > Sequence: MGYG000000387_01515

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; ;
CAZyme ID MGYG000000387_01515
CAZy Family GH95
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1088 MGYG000000387_27|CGC1 119609.8 4.2112
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000387 2488147 MAG Sweden Europe
Gene Location Start: 8711;  End: 11977  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.63

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH95 109 921 5.6e-224 0.9653739612188366

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam14498 Glyco_hyd_65N_2 1.19e-49 115 390 13 231
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 2.04e-13 1025 1081 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.
cd14253 Dockerin 2.76e-10 1026 1081 1 56
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 6.89e-10 1026 1079 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.
cd14252 Dockerin_like 2.18e-06 1026 1081 1 57
Dockerin repeat domains and domains resembling dockerin repeats. 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QPA42690.1 1.25e-170 111 944 58 789
QPA36938.1 1.25e-170 111 944 58 789
QHH85405.1 1.57e-170 111 944 58 789
QRH05335.1 1.57e-170 111 944 58 789
QHG35690.1 1.57e-170 111 944 58 789

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2EAB_A 1.04e-138 107 916 43 844
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]
2EAD_A 7.72e-138 107 916 43 844
ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum]
2EAE_A 1.47e-137 107 916 42 843
ChainA, Alpha-fucosidase [Bifidobacterium bifidum]
2RDY_A 6.40e-102 110 958 12 790
ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
4UFC_A 3.71e-99 110 919 32 739
Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8L7W8 8.14e-80 115 903 66 794
Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
A2R797 1.82e-72 102 903 25 758
Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1
Q5AU81 6.20e-60 100 918 24 793
Alpha-fucosidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afcA PE=1 SV=1
Q2USL3 1.06e-47 110 921 25 715
Probable alpha-fucosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=afcA 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
0.001154 0.997710 0.000474 0.000263 0.000189 0.000175

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000387_01515.