CAZyme Information: PITG_09377-t26_1-p1

Basic Information

• Species: Phytophthora infestans
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora infestans
• CAZyme ID: PITG_09377-t26_1-p1
• CAZy Family: GH28
• CAZyme Description: ER degradation-enhancing alpha-mannosidase-like protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
719	DS028131|CGC6	79559.32	7.3735

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PinfestansT30-4	19344	403677	1547	17797

• Gene Location: location=DS028131:2716171-2718372(-)

Full Sequence      

MHVSERRHLQQQARDMFYHGYRNYMEHAYPWDELKPLSCSGRRWDRRERGDLDDVLGGFS
LTLVDSLDMLAVLGDRDEFARAVKLISSSVSFDRDVTVSVFESTIRVIGGLVSAHMLASP
EYFGMMDESEYNGELLDLAEELGRRLLPAFETPTGIPVHRINLRHGVLPRDRAANLTCPA
AAGSLLVEMAYLSRLTGDESFEERAKQAVVAIWDRRSDLDLLGSSIEVGSGKWIYSHGGI
GAGLDSFFEYLLKYHLISGDSEWLAMFNASYHAVETHVNHNNVYIEVDMNGGRNQVRARR
VSALQAFWPGLQVLAGDVSGAIRTHEHKFPLWDEYGAMPELLDLAPHGKSKPGNRGTVIS
WARTSPLRPELIESTYHLFQATKDHKYLKMGRQMLQDIRRVSEVPCGYAAVGDIHTLDVE
DRMDSYFLSETVKYLYLLFSDDPHVIVPGPARRRNTTVSTNRTCSATISDEKLTLGSAVS
CNNRSANASSTLEQFSCVRRNRKPLKASDVVFSTEGHILMLDSHLFRHTTKQKASSASPK
CENGKLQGHRRNVELEVARQVQLTPPVIPVGVAVRAGGVHVTTLVASPAKFGLQVTTPSA
VEAPLQLFVPDIGEACGSIDSERVRGKIVMVARGTCTFAEKAMRLQSAGAVGAVVINSKA
TSSRYPNRKYSLADDARGLGQFVTIPVLLVSREDASQLHRHASLNGGDVLIGSLSPWLY

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	16	519	3.2e-132	0.9932735426008968

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	1.41e-133	16	445	1	437	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	7.80e-76	5	446	71	502	glycoside hydrolase family 47 protein; Provisional
239041	PA_EDEM3_like	1.67e-18	586	698	2	112	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.
240122	PA_subtilisin_1	1.93e-15	588	714	2	118	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.
239045	PA_ScAPY_like	5.66e-11	596	698	17	108	PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae aminopeptidase Y (ScAPY). This group contains various PA domain-containing proteins similar to the S. cerevisiae APY, including Trichophyton rubrum leucine aminopeptidase 1(LAP1). Proteins in this group belong to the peptidase M28 family. ScAPY hydrolyzes amino acid-4-methylcoumaryl-7-amides (MCAs). ScAPY more rapidly hydrolyzes dipeptidyl-MCAs. Hydrolysis of amino acid-MCAs or dipeptides is stimulated by Co2+ while the hydrolysis of dipeptidyl-MCAs, tripeptides, and longer peptides is inhibited by Co2+. ScAPY is vacuolar and is activated by proteolytic processing. LAP1 is a secreted leucine aminopeptidase. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA23124.1|GH47	1.57e-248	2	719	23	727
AIG56058.1|GH47	1.86e-221	1	716	24	685
CAD7199021.1|GH47	2.54e-133	5	705	49	764
CAD7261104.1|GH47	2.93e-133	11	705	17	725
AGB92969.1|GH47	1.21e-132	1	690	42	738

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KIJ_A	5.01e-58	15	446	11	435	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
5KK7_A	5.38e-58	15	446	11	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	5.77e-58	15	446	16	440	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	6.05e-58	15	446	16	440	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]
1X9D_A	3.31e-57	15	446	94	518	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|Q92611|EDEM1_HUMAN	3.49e-120	13	442	134	565	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q9FG93|MNS4_ARATH	5.37e-120	4	450	35	459	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	1.67e-119	13	442	129	560	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|Q6GQB9|EDEM3_XENLA	1.05e-118	4	693	33	758	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2
sp|Q9BZQ6|EDEM3_HUMAN	3.14e-118	1	696	44	773	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Homo sapiens OX=9606 GN=EDEM3 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000025	0.000014

TMHMM  Annotations     

There is no transmembrane helices in PITG_09377-t26_1-p1.