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CAZyme Information: MGYG000000924_01383

You are here: Home > Sequence: MGYG000000924_01383

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 An172 sp002160515
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; An172; An172 sp002160515
CAZyme ID MGYG000000924_01383
CAZy Family GH95
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1628 178578.72 4.1237
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000924 2081481 MAG China Asia
Gene Location Start: 223;  End: 5109  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.63

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH95 45 804 1.5e-255 0.9847645429362881

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam14498 Glyco_hyd_65N_2 4.82e-66 51 302 1 233
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 1.96e-13 1569 1622 1 53
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.
pfam00404 Dockerin_1 4.27e-08 1570 1621 1 51
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 6.38e-06 1570 1621 1 56
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.
cd00063 FN3 3.10e-05 1392 1470 9 93
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QHB24557.1 0.0 9 1586 10 1586
QEI32060.1 0.0 9 1586 10 1586
QRT30709.1 0.0 9 1586 10 1586
ASM69030.1 0.0 7 1562 5 1558
QNM13266.1 0.0 65 1389 70 1376

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2EAB_A 3.78e-241 36 842 2 895
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 2.92e-240 36 842 2 895
ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum]
2EAE_A 5.58e-240 36 842 1 894
ChainA, Alpha-fucosidase [Bifidobacterium bifidum]
2RDY_A 4.62e-132 48 842 2 790
ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
4UFC_A 1.29e-118 49 796 22 736
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 9.99e-96 74 781 67 792
Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
A2R797 1.72e-90 48 786 20 761
Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1
Q5AU81 2.91e-77 43 786 16 780
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 1.26e-68 76 795 35 711
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
0.000533 0.998615 0.000208 0.000251 0.000181 0.000161

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000924_01383.