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CAZyme Information: MGYG000000587_00513

You are here: Home > Sequence: MGYG000000587_00513

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; Monoglobales_A; UBA1381; ;
CAZyme ID MGYG000000587_00513
CAZy Family GH141
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1183 131385.02 4.5485
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000587 1865333 MAG Madagascar Africa
Gene Location Start: 1611;  End: 5162  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000587_00513.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH141 36 549 9.9e-134 0.9620493358633776

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10238 HSPA14-like_NBD 7.42e-04 688 816 1 128
Nucleotide-binding domain of human HSPA14 and similar proteins. Human HSPA14 (also known as 70-kDa heat shock protein 14, HSP70L1, HSP70-4; the gene encoding HSPA14 maps to 10p13), is ribosome-associated and belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HSPA14 interacts with the J-protein MPP11 to form the mammalian ribosome-associated complex (mRAC). HSPA14 participates in a pathway along with Nijmegen breakage syndrome 1 (NBS1, also known as p85 or nibrin), heat shock transcription factor 4b (HSF4b), and HSPA4 (belonging to a different subfamily), that induces tumor migration, invasion, and transformation. HSPA14 is a potent T helper cell (Th1) polarizing adjuvant that contributes to antitumor immune responses.
pfam00395 SLH 0.001 1130 1172 1 42
S-layer homology domain.
pfam06439 DUF1080 0.006 824 991 4 167
Domain of Unknown Function (DUF1080). This family has structural similarity to an endo-1,3-1,4-beta glucanase belonging to glycoside hydrolase family 16. However, the structure surrounding the active site differs from that of the endo-1,3-1,4-beta glucanase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUL54275.1 3.40e-141 24 992 395 1348
AIQ43746.1 4.64e-140 24 992 395 1348
QYR21751.1 2.33e-138 39 1018 426 1384
ANE49726.1 4.36e-102 3 623 11 628
SDS22682.1 2.57e-92 28 623 41 606

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5MQP_A 5.33e-47 19 539 29 574
Glycosidehydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_B Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_C Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_D Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_E Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_F Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_G Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_H Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron]

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.000306 0.998975 0.000233 0.000166 0.000158 0.000152

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000587_00513.