CAZyme Information: H257_01053-t26_1-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_01053-t26_1-p1
• CAZy Family: AA15
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
671	KI913115|CGC3	74076.38	7.1526

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AastaciAPO3	19584	N/A	465	19119

• Gene Location: location=KI913115:443346-446523(-)

Full Sequence      

MRSWGAIIAAAAVAIGGVVTNALHWTEKQHLQEKAKEMFFHGYNSYMTHAYPWDELKPLS
CEGRRWDRKERGDLDDALGGFALTLIDSLSMLALVDAVEFEAAVTRVIHTVSFDRDVTVS
VFESTIRVIGGLLSAHMLATSGAVGSMHLAYQGELLDLAVDLGTRLLPAFNTKTGLPVHR
VNLMHGMMRNAPALTCPAAAGSLLLEFSVLSRLSNIPDFEEVARDAVLGLWDRRSDLNLL
GSTINVNTGDWVHTHTGIGAGLDSFYEYLLKYYILSGDSDFLDMFNKSYVSIETHLLHRD
GYHREVDMSLGHIYSNRVSALQAFWPGLQVLAGDLSAAVRSHHQLFDLWNEFGALPELYD
RSGKGSVIHWAQHYPLRPELAESTYHLYAATKDEKYLKIGRKLLQDIEDTSRVSCGYAAV
GNVHDKRLEDRMDSFFLSETVKYLYLLFSNDTSVLIPKHATNQNSLSASHVLFTTEGHLF
PIVPSLYQDATSKRRKFVRQAHQHRTCAAPQHSALTSKNAHLDAAVTIRLGDVHLKTLSA
SPAQFGYKLSNGRVDGALYAALDDVQTACRDLSALEGSIRGKIVLVKRGKCSFTRKAMHI
QQMGGIGMIAVNSKPTTAANAHRLYSLSDDGAGHHVTIPVVMISKPDGQHLQHNVAHRDG
DLVVSLSMLLA

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	38	482	4.3e-131	0.9977578475336323

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	2.08e-137	38	482	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	1.19e-78	33	484	74	520	glycoside hydrolase family 47 protein; Provisional
239041	PA_EDEM3_like	3.07e-17	540	666	2	126	PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This group contains various PA domain-containing proteins similar to mouse EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein). EDEM3 contains a region, similar to Class I alpha-mannosidases (gylcosyl hydrolase family 47), N-terminal to the PA domain. EDEM3 accelerates glycoprotein ERAD (ER-associated degradation). In transfected mammalian cells, overexpression of EDEM3 enhances the mannose trimming from the N-glycans, of a model misfolded protein [alpha1-antitrypsin null (Hong Kong)] as well as, from total glycoproteins. Mannose trimming appears to be involved in the selection of ERAD substrates. EDEM3 has a different specificity of trimming than ER alpha-mannosidase 1. The significance of the PA domain to EDEM3 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.
239038	PA_C_RZF_like	4.71e-17	523	664	9	146	PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA domain-containing proteins similar to C-RZF (chicken embryo RING zinc finger) protein. These proteins contain a C3H2C3 RING finger. C-RZF is expressed in embryo cells and is restricted mainly to brain and heart, it is localized to both the nucleus and endosomes. Additional C3H2C3 RING finger proteins belonging to this group, include Arabidopsis ReMembR-H2 protein and mouse sperizin. ReMembR-H2 is likely to be an integral membrane protein, and to traffic through the endosomal pathway. Sperizin is expressed in haploid germ cells and localized in the cytoplasm, it may participate in spermatogenesis. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.
240122	PA_subtilisin_1	3.26e-13	542	651	2	104	PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG56058.1|GH47	5.65e-303	13	670	14	696
CCA23124.1|GH47	1.82e-216	24	647	23	681
CDS05465.1|GH47	1.12e-141	38	510	1	461
QCE07576.1|GH47	7.70e-131	27	486	31	472
CAY09791.1|GH47	1.63e-130	6	486	19	481

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KIJ_A	9.85e-51	30	482	1	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1FMI_A	1.12e-50	30	482	6	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	1.17e-50	30	482	6	456	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]
5KK7_A	5.24e-50	30	482	1	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens],5KK7_B Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens]
1X9D_A	5.35e-50	30	482	84	534	Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9FG93|MNS4_ARATH	2.75e-127	17	486	26	477	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q6GQB9|EDEM3_XENLA	2.55e-125	2	648	9	759	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2
sp|Q92611|EDEM1_HUMAN	2.41e-124	31	482	130	586	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	5.84e-124	31	482	125	581	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|Q2HXL6|EDEM3_MOUSE	8.09e-124	3	648	19	773	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Mus musculus OX=10090 GN=Edem3 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.853819	0.146193

TMHMM  Annotations     

Start	End
7	26