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CAZyme Information: CXQ85_003285-t46_1-p1

You are here: Home > Sequence: CXQ85_003285-t46_1-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 [Candida] haemuloni
Lineage Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; [Candida] haemuloni
CAZyme ID CXQ85_003285-t46_1-p1
CAZy Family GT22
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1229 PKFO01000002|CGC6 135000.18 7.0743
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_ChaemulonisB11899 5409 N/A 160 5249
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.113:99

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH47 44 501 3.4e-162 0.9955156950672646

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396217 Glyco_hydro_47 0.0 43 501 1 453
Glycosyl hydrolase family 47. Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).
240427 PTZ00470 1.08e-167 38 502 74 519
glycoside hydrolase family 47 protein; Provisional
269835 bZIP_ATF2 9.79e-23 980 1038 1 59
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar proteins: a DNA-binding and dimerization domain. ATF-2 is a sequence-specific DNA-binding protein that belongs to the Basic leucine zipper (bZIP) family of transcription factors. In response to stress, it activates a variety of genes including cyclin A, cyclin D, and c-Jun. ATF-2 also plays a role in the DNA damage response that is independent of its transcriptional activity. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.
197664 BRLZ 9.16e-14 976 1035 1 60
basic region leucin zipper.
269834 bZIP 4.12e-11 979 1035 2 48
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain. Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 585 44 627
0.0 1 585 44 628
0.0 1 585 44 628
0.0 1 585 44 628
0.0 1 585 44 628

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.20e-148 37 512 6 509
Crystal Structure Of Class I Alpha-1,2-mannosidase From Saccharomyces Cerevisiae At 1.54 Angstrom Resolution [Saccharomyces cerevisiae]
2.20e-147 37 512 40 543
Crystal structure of the yeast alpha-1,2-mannosidase with bound 1-deoxymannojirimycin at 1.59 A resolution [Saccharomyces cerevisiae]
2.00e-117 40 500 9 450
Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
2.43e-117 40 500 14 455
Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
2.59e-117 40 500 14 455
Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin [Homo sapiens],1FO3_A Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With Kifunensine [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.09e-257 1 564 1 558
Mannosyl-oligosaccharide 1,2-alpha-mannosidase OS=Candida albicans OX=5476 GN=MNS1 PE=3 SV=2
1.70e-147 20 512 28 547
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=MNS1 PE=1 SV=1
1.83e-135 15 503 25 513
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC2E1P5.01c PE=1 SV=2
7.14e-115 33 500 125 619
Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3 OS=Arabidopsis thaliana OX=3702 GN=MNS3 PE=1 SV=1
1.54e-113 40 500 253 694
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase OS=Homo sapiens OX=9606 GN=MAN1B1 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.808272 0.191734

TMHMM  Annotations      help

There is no transmembrane helices in CXQ85_003285-t46_1-p1.