CAZyme Information: EPrPRT00000015523-p1

Basic Information

• Species: Pythium arrhenomanes
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium arrhenomanes
• CAZyme ID: EPrPRT00000015523-p1
• CAZy Family: CE2
• CAZyme Description: ER degradation-enhancing alpha-mannosidase.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
658	ParrATCC12531_SC00230|CGC1	72926.71	6.2265

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ParrhenomanesATCC12531	13857	1223556	52	13805

• Gene Location: location=ParrATCC12531_SC00230:2210-4585(+)

Full Sequence      

MTRWLSLLVVLFTATLCGHGTHATMHASERRHLRDRARAMFYHGYNSYMDHAFPWDELKP
LSCEGRRWDQRERGDLDDVLGGFALTLVDSLDMLAVLGDRDEFRRAVHLVIDTVSFDRDV
TVSYNGELLDLAVDLGQRLLPAFDTPTQIPVHRINLRHGLAANAPAITCPAAAGSLLVEF
AYLSRLSGLSVFEDKARDAWTSSHVGIGAGLDSFFEYLLKYHLVSGNTVWRDMFNLSYSA
VETHMNHQDFHLEAFWPGLQVLAGDVSSAIRSHDNLFLLWNKYGAMPELFDLASVDGGVI
PWARTSPLRPELIESTYHLYQATRDHKYLKIGRKLLEDMERVSRVDCGYAAVGNIHTLAV
EDRMDSYFLSETVKYLYLLFSDDPDVIVPAMPLNGGSLNGSIETEPRLVNGSFIDNTTTG
ELYSRVLKSSEVVFSTEGHVLHVDAAIFERKDLSQPGGSSSTSPAFWCENGHALIHKEKQ
RQATPTAAATKPSITFVPIGVSVRVGDVHFGRFGHVEAPLLLFSHRVGNACEPFSSDLQA
EMTGRIVVVARGQCSFADKALHVQQAGGKGMIIINTKRRDNAAEPPRYMITDDSNGAGAR
VRIPLVLMSRPVALELHRAVRLKLQLMDREAGGTDELPSSSSTTGEDDVVVSLSAWLY

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	199	442	5.7e-51	0.5493273542600897

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	2.75e-108	40	441	1	451	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	2.03e-56	34	383	73	499	glycoside hydrolase family 47 protein; Provisional
239041	PA_EDEM3_like	6.92e-13	529	626	28	122	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.
238300	PA	9.71e-13	508	626	4	122	PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of 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: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.
240122	PA_subtilisin_1	6.35e-12	529	609	28	97	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
CCA23124.1|GH47	2.03e-209	26	658	23	727
AIG56058.1|GH47	2.41e-192	25	620	24	678
CAD7199021.1|GH47	6.22e-102	24	622	44	763
CAD7261104.1|GH47	5.43e-101	34	622	16	724
BAN20892.1|GH47	1.15e-100	29	388	36	468

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KKB_A	1.94e-38	31	383	20	448	Structure of mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus],5KKB_B Structure of mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus]
1NXC_A	2.24e-38	31	383	18	446	Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases) [Mus musculus]
5KIJ_A	5.98e-37	32	387	1	435	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
5KK7_A	6.28e-37	32	387	1	435	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]
1FMI_A	6.60e-37	32	387	6	440	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6GQB9|EDEM3_XENLA	6.42e-96	3	608	10	754	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2
sp|Q2HXL6|EDEM3_MOUSE	3.41e-93	8	648	29	812	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Mus musculus OX=10090 GN=Edem3 PE=1 SV=2
sp|Q9BZQ6|EDEM3_HUMAN	9.34e-93	25	648	44	811	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Homo sapiens OX=9606 GN=EDEM3 PE=1 SV=2
sp|Q92611|EDEM1_HUMAN	4.83e-92	30	386	127	568	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	2.30e-91	30	386	122	563	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000229	0.999742	CS pos: 23-24. Pr: 0.9684

TMHMM  Annotations     

There is no transmembrane helices in EPrPRT00000015523-p1.