dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: FUNGIDB

help

CAZyme Information: CXQ85_001914-t46_1-p1

You are here: Home > Sequence: CXQ85_001914-t46_1-p1

Basic Information help

Species

[Candida] haemuloni

Lineage

Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; [Candida] haemuloni

CAZyme ID

CXQ85_001914-t46_1-p1

CAZy Family

GH5

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1474	PKFO01000003\|CGC3	167106.20	5.1903

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	2.4.1.131:1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT4	336	472	1.9e-16	0.75625

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340835	GT4_ALG11-like	0.0	97	500	1	390	alpha-1,2-mannosyltransferase ALG11 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.
397941	Coatomer_WDAD	9.43e-153	902	1405	1	439	Coatomer WD associated region. This region is composed of WD40 repeats.
406369	ALG11_N	3.46e-98	97	306	1	208	ALG11 mannosyltransferase N-terminus.
215511	PLN02949	1.07e-89	93	468	30	393	transferase, transferring glycosyl groups
238121	WD40	2.04e-64	599	872	11	279	WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
6.48e-314	1	580	1	592
5.86e-312	1	580	1	592
1.66e-311	1	580	1	592
2.65e-310	1	580	1	592
3.96e-265	1	576	1	598

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.41e-235	585	1430	1	802	Crystal structure of yeast alpha/betaprime-COP subcomplex of the COPI vesicular coat [Saccharomyces cerevisiae YJM789],3MKQ_C Crystal structure of yeast alpha/betaprime-COP subcomplex of the COPI vesicular coat [Saccharomyces cerevisiae YJM789],3MKQ_E Crystal structure of yeast alpha/betaprime-COP subcomplex of the COPI vesicular coat [Saccharomyces cerevisiae YJM789]
7.70e-194	585	1421	3	777	The structure of the COPI coat triad [Mus musculus],5A1V_D The structure of the COPI coat linkage I [Mus musculus],5A1V_L The structure of the COPI coat linkage I [Mus musculus],5A1V_U The structure of the COPI coat linkage I [Mus musculus],5A1W_D The structure of the COPI coat linkage II [Mus musculus],5A1X_D The structure of the COPI coat linkage III [Mus musculus],5A1X_L The structure of the COPI coat linkage III [Mus musculus],5A1Y_D The structure of the COPI coat linkage IV [Mus musculus],5A1Y_L The structure of the COPI coat linkage IV [Mus musculus],5NZR_C The structure of the COPI coat leaf [Mus musculus],5NZS_C The structure of the COPI coat leaf in complex with the ArfGAP2 uncoating factor [Mus musculus],5NZT_C The structure of the COPI coat linkage I [Mus musculus],5NZT_H The structure of the COPI coat linkage I [Mus musculus],5NZU_C The structure of the COPI coat linkage II [Mus musculus],5NZV_C The structure of the COPI coat linkage IV [Mus musculus],5NZV_J The structure of the COPI coat linkage IV [Mus musculus]
1.66e-189	585	1201	1	604	yeast betaprime COP 1-604 with KTKTN motif [Saccharomyces cerevisiae]
1.48e-96	585	886	1	304	yeast betaprime COP 1-304 with KTKTN motif [Saccharomyces cerevisiae]
1.81e-96	585	886	1	304	yeast betaprime COP 1-304H6 [Saccharomyces cerevisiae],2YNO_B yeast betaprime COP 1-304H6 [Saccharomyces cerevisiae]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.35e-233	585	1430	1	802	Coatomer subunit beta' OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SEC27 PE=1 SV=1
3.98e-200	585	1441	3	793	Coatomer subunit beta'-1 OS=Arabidopsis thaliana OX=3702 GN=At1g79990 PE=2 SV=2
5.61e-197	8	580	8	602	GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALG11 PE=3 SV=2
1.52e-195	16	580	19	609	GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=ALG11 PE=3 SV=2
9.64e-195	585	1421	3	777	Coatomer subunit beta' OS=Rattus norvegicus OX=10116 GN=Copb2 PE=1 SV=3

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.037072	0.962911	CS pos: 20-21. Pr: 0.9094

TMHMM Annotations help

There is no transmembrane helices in CXQ85_001914-t46_1-p1.