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CAZyme Information: MGYG000002900_01736

You are here: Home > Sequence: MGYG000002900_01736

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 Actinomyces urogenitalis
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Actinomyces; Actinomyces urogenitalis
CAZyme ID MGYG000002900_01736
CAZy Family GH125
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
423 MGYG000002900_61|CGC1 47282.69 4.3862
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002900 2460697 MAG United States North America
Gene Location Start: 5288;  End: 6559  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002900_01736.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH125 37 417 2.8e-132 0.9825870646766169

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam06824 Glyco_hydro_125 6.92e-179 38 417 8 416
Metal-independent alpha-mannosidase (GH125). This family, which contains bacterial and fungal glycoside hydrolases, is also known as GH125. They function as metal-independent alpha-mannosidases, with specificity for alpha-1,6-linked non-reducing terminal mannose residues. Structurally this family is part of the 6 hairpin glycosidase superfamily.
COG3538 COG3538 1.41e-169 16 423 7 426
Meiotically up-regulated gene 157 (Mug157) protein (function unknown) [Function unknown].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QPL06518.1 1.06e-239 5 423 8 426
QNP55313.1 5.12e-193 8 421 5 418
AOH45575.1 4.89e-190 7 417 13 419
BCY24077.1 4.89e-190 7 417 13 419
ALT41254.1 2.81e-189 5 419 11 421

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6RQK_A 4.29e-118 38 411 32 414
Crystalstructure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole [Clostridium perfringens str. 13],6RQK_B Crystal structure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole [Clostridium perfringens str. 13]
3QT3_A 6.66e-118 38 411 32 414
Analysisof a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Clostridium perfringens CPE0426 apo-structure [Clostridium perfringens],3QT9_A Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Clostridium perfringens CPE0426 complexed with alpha-1,6-linked 1-thio-alpha-mannobiose [Clostridium perfringens]
5M7I_A 2.43e-117 38 411 32 414
Crystalstructure of GH125 1,6-alpha-mannosidase mutant from Clostridium perfringens in complex with 1,6-alpha-mannobiose [Clostridium perfringens str. 13],5M7Y_A Crystal structure of GH125 1,6-alpha-mannosidase mutant from Clostridium perfringens in complex with 1,6-alpha-mannotriose [Clostridium perfringens str. 13]
2NVP_A 3.56e-114 38 411 32 414
X-RayCrystal Structure of Protein CPF_0428 from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR63. [Clostridium perfringens]
3QPF_A 3.91e-111 16 418 5 421
Analysisof a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Streptococcus pneumoniae SP_2144 apo-structure [Streptococcus pneumoniae],3QPF_B Analysis of a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Streptococcus pneumoniae SP_2144 apo-structure [Streptococcus pneumoniae],3QRY_A Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 1-deoxymannojirimycin complex [Streptococcus pneumoniae],3QRY_B Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 1-deoxymannojirimycin complex [Streptococcus pneumoniae],3QSP_A Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 non-productive substrate complex with alpha-1,6-mannobiose [Streptococcus pneumoniae],3QSP_B Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 non-productive substrate complex with alpha-1,6-mannobiose [Streptococcus pneumoniae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q10449 7.10e-61 15 422 64 499
Meiotically up-regulated gene 157 protein OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mug157 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000059 0.000003 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002900_01736.