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CAZyme Information: MGYG000004876_01636

You are here: Home > Sequence: MGYG000004876_01636

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; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides;
CAZyme ID MGYG000004876_01636
CAZy Family CBM32
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
299 MGYG000004876_16|CGC1 33239.92 4.405
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004876 4781463 MAG China Asia
Gene Location Start: 42303;  End: 43202  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004876_01636.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM32 151 282 7.1e-18 0.9193548387096774

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00754 F5_F8_type_C 5.52e-15 148 281 1 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
cd00057 FA58C 7.53e-05 163 234 27 92
Substituted updates: Jan 31, 2002
pfam17132 Glyco_hydro_106 0.001 148 284 175 314
alpha-L-rhamnosidase.
cd08366 APC10 0.009 160 237 19 89
APC10 subunit of the anaphase-promoting complex (APC) that mediates substrate ubiquitination. This model represents the single domain protein APC10, a subunit of the anaphase-promoting complex (APC), which is a multi-subunit E3 ubiquitin ligase. E3 ubiquitin ligases mediate substrate ubiquitination (or ubiquitylation), a vital component of the ubiquitin-26S proteasome pathway for selective proteolytic degradation. The APC (also known as the cyclosome), is a cell cycle-regulated E3 ubiquitin ligase that controls important transitions in mitosis and the G1 phase by ubiquitinating regulatory proteins, thereby targeting them for degradation. In mitosis, the APC initiates sister chromatid separation by ubiquitinating the anaphase inhibitor securin and triggers exit from mitosis by ubiquitinating cyclin B. The C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats. APC10 domains are homologous to the DOC1 domains present in the HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase protein, and the Cullin-RING (Really Interesting New Gene) E3 ubiquitin ligase complex. The APC10/DOC1 domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain-like fold; their sequences are quite dissimilar, however, and are not included here.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT89968.1 2.47e-182 1 299 1 299
QRP56724.1 1.37e-120 1 299 1 297
QQT78032.1 1.37e-120 1 299 1 297
QUU07363.1 1.37e-120 1 299 1 297
ALK86788.1 1.18e-116 1 299 1 296

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2J7M_A 9.45e-07 151 236 14 99
Characterizationof a Family 32 CBM [Clostridium perfringens]
2J1A_A 9.61e-07 151 236 15 100
Structureof CBM32 from Clostridium perfringens beta-N- acetylhexosaminidase GH84C in complex with galactose [Clostridium perfringens ATCC 13124],2J1E_A High Resolution Crystal Structure of CBM32 from a N-acetyl-beta- hexosaminidase in complex with lacNAc [Clostridium perfringens ATCC 13124]
2V5D_A 6.06e-06 151 236 602 687
Structureof a Family 84 Glycoside Hydrolase and a Family 32 Carbohydrate-Binding Module in Tandem from Clostridium perfringens. [Clostridium perfringens]

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000068 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004876_01636.