CAZyme Information: PPTG_03696-t26_1-p1

Basic Information

• Species: Phytophthora parasitica
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica
• CAZyme ID: PPTG_03696-t26_1-p1
• CAZy Family: AA6
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
752	KI669564|CGC10	83154.70	7.3835

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PparasiticaINRA-310	23240	761204	119	23121

• Gene Location: location=KI669564:2588268-2590526(-)

Full Sequence      

MTPRQVYPMCLRLAFLLVSVALVGTLCSAHMHVSERRHLQQQARDMFYHGYRNYMKHAYP
WDELKPLSCSGRRWDRRERGDLDDVLGGFSLTLVDSLDMLAVLGDCDEFARAVKLISSSV
SFDRDVTVSVFESTIRVIGGLVSAHMLASPEYFGLMDEHEYNGELLELAEDLGRRILPAF
ETPTGIPVHRINLQRGVLPKDRAANLTCPAAAGSLLVEMAYLSRLTGDESFEERAKQAVV
AIWDRRSDLDLLGSSIDVGSGQWIYSHGGIGAGLDSFFEYLLKYHLISGDSGWLEMFNAS
YHAVETHVNHNDVYIEVDMNGGRNQVRARRVSALQAFWPGLQVLAGDVSGAIRTHEHMFP
LWDEYGAMPELLDLAPHGKSKPGNRGTVISWARTSPLRPELIESTYHLYQATKDHKYLKM
GRQMLQDIRRVSEVPCGYAAVGDIHTLDVEDRMDSYFLSETAKYLFLLFSDDNVIVPAPI
RQRNATATNRTCSATVSDDKITLGSSLSCNNRTINGNSTLEHSSYVRRNRKPLKASDVVF
STEGHILMLDSHLFRHTTKQKASSASPKCENGKLQVHRRNVELEVARRGQLTPPVIPVGV
AVRIGGVHVTTLVASPAKFGLQVTTPSAVEAPLLLFTPDIGEACGSIDSDRVHGKIVMVA
RGKCTFAEKALRLQSAGAVGIVVINSKASSSRYPNRKYSLADDARGLGQYVTIPVVLVAR
EDATQLHRHASLNNVQSDSGAVLIGSLSPWLY

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	46	547	1.6e-132	0.9932735426008968

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	9.60e-134	46	475	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	6.11e-77	35	475	71	502	glycoside hydrolase family 47 protein; Provisional
239041	PA_EDEM3_like	4.20e-18	614	729	2	121	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	1.97e-15	616	726	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.
238300	PA	3.94e-11	619	728	9	114	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA23124.1|GH47	2.73e-250	14	752	5	727
AIG56058.1|GH47	5.56e-224	17	735	11	683
AGB92969.1|GH47	2.26e-132	25	718	36	738
CAD7086284.1|GH47	1.49e-130	13	728	12	742
AAM50976.1|GH47	2.59e-129	25	718	36	747

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KIJ_A	7.91e-58	40	472	6	431	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
5KK7_A	8.49e-58	40	472	6	431	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	9.11e-58	40	472	11	436	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	9.55e-58	40	472	11	436	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	5.22e-57	40	472	89	514	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|Q6GQB9|EDEM3_XENLA	2.13e-122	15	718	15	754	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2
sp|Q92611|EDEM1_HUMAN	7.37e-122	36	475	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	2.50e-121	36	475	122	563	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|Q9BZQ6|EDEM3_HUMAN	3.46e-121	14	724	27	773	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Homo sapiens OX=9606 GN=EDEM3 PE=1 SV=2
sp|Q2HXL6|EDEM3_MOUSE	2.67e-119	14	724	28	774	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 SP

Other	SP_Sec_SPI	CS Position
0.000230	0.999748	CS pos: 29-30. Pr: 0.9660

TMHMM  Annotations     

Start	End
13	32