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CAZyme Information: QYA_127793T0-p1

You are here: Home > Sequence: QYA_127793T0-p1

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 Mucor lusitanicus
Lineage Mucoromycota; Mucoromycetes; ; Mucoraceae; Mucor; Mucor lusitanicus
CAZyme ID QYA_127793T0-p1
CAZy Family GH125
CAZyme Description Dolichyl-phosphate-mannose--protein mannosyltransferase [Source:UniProtKB/TrEMBL;Acc:A0A168HU83]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
448 50453.02 9.1334
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_MlusitanicusCBS277-49 11852 747725 0 11852
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.109:12

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT39 4 243 1.2e-42 0.9820627802690582

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
224839 PMT1 2.05e-67 5 448 33 464
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones].
396786 PMT 1.33e-37 5 246 6 244
Dolichyl-phosphate-mannose-protein mannosyltransferase. This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.
397103 MIR 9.16e-16 290 448 6 172
MIR domain. The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.
197746 MIR 6.85e-07 277 329 3 57
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases.
224720 ArnT 1.81e-04 37 210 58 206
4-amino-4-deoxy-L-arabinose transferase or related glycosyltransferase of PMT family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
9.53e-128 6 431 53 452
1.00e-81 6 448 121 558
4.02e-78 2 448 47 497
5.98e-75 10 448 79 515
5.98e-75 10 448 79 515

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.10e-56 9 448 63 498
Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor and a peptide acceptor [Saccharomyces cerevisiae W303],6P2R_A Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor [Saccharomyces cerevisiae W303]
1.99e-54 1 448 70 511
Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor and a peptide acceptor [Saccharomyces cerevisiae W303],6P2R_B Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor [Saccharomyces cerevisiae W303]
2.38e-18 274 448 19 192
Structure of the Pmt2-MIR domain with bound ligands [Saccharomyces cerevisiae]
5.64e-18 273 448 1 175
Crystal structure of the MIR domain (aa 337-532) of the S. cerevisiae mannosyltransferase Pmt2 [Saccharomyces cerevisiae]
8.10e-16 278 448 15 185
Structure of the Pmt3-MIR domain with bound ligands [Saccharomyces cerevisiae],6ZQQ_B Structure of the Pmt3-MIR domain with bound ligands [Saccharomyces cerevisiae],6ZQQ_C Structure of the Pmt3-MIR domain with bound ligands [Saccharomyces cerevisiae],6ZQQ_D Structure of the Pmt3-MIR domain with bound ligands [Saccharomyces cerevisiae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.88e-68 1 448 133 574
Protein O-mannosyl-transferase 2 OS=Mus musculus OX=10090 GN=Pomt2 PE=1 SV=1
1.84e-67 5 448 67 504
Protein O-mannosyl-transferase 2 OS=Homo sapiens OX=9606 GN=POMT2 PE=1 SV=2
5.79e-62 10 448 54 485
Protein O-mannosyl-transferase 2 OS=Drosophila melanogaster OX=7227 GN=tw PE=2 SV=1
1.25e-61 10 448 52 483
Protein O-mannosyl-transferase 2 OS=Drosophila pseudoobscura pseudoobscura OX=46245 GN=tw PE=3 SV=1
2.62e-61 5 448 77 511
Protein O-mannosyl-transferase 2 OS=Danio rerio OX=7955 GN=pomt2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.998079 0.001908

TMHMM  Annotations      download full data without filtering help

Start End
39 61
81 100
135 152
177 199
219 241