CAZyme Information: PHYSODRAFT_288737-t26_1-p1

Basic Information

• Species: Phytophthora sojae
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
• CAZyme ID: PHYSODRAFT_288737-t26_1-p1
• CAZy Family: AA7
• CAZyme Description: family 47 glycoside hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
714	JH159160|CGC9	78343.13	6.5976

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsojaeP6497	28142	1094619	1653	26489

• Gene Location: location=JH159160:2267715-2269859(-)

Full Sequence      

MEHAYPWDELKPLSCSGRRWDRRERGDLDDVLGGFSLTLVDSLDMLAVLGDRDEFARAVK
LVAGSVTFDRDVTVSVFESTIRVIGGLVSAHMLASPEYFGMMEEDEYNGELLSLAEDLGR
RLLPAFDTPTGIPVHRVNLRRGVLPKDRAAKLTCPAAAGSLLVEMAYLSRLSGDQRFEQR
AKEAVVAIWDRRSDIDLLGSAIDVGSGEWVHSHGGIGAGLDSFFEYLLKYHLVSGDSQWL
AMFNASYQAVETHVNHDDVYIEVDMNGGKDQVRTRRVSALQAFWPGLQVLAGDVSGAIRT
HEHMFPLWDEFGAMPELLDLAPRGMSKPGNRGTVISWARTSPLRPELIESTYHLYQATRD
HKYLKMGRQMLQDIRRVSEVPCGYAAVGNIHTLDIEDRMDSYFLSETAKYLYLLFSDEPD
VIVPVPPVRQRKNASSPSNRTCATTTPSKLQTVGTSLECKTASANASSSLGETSLRRNKK
SLKASDVVFSTEGHILMIDSHLFRQPQQKSSLVAPKCENGKLQVRQRNVELQAAREILTT
PPVIPVGLAVRLGDVHVMTLVASPAKFGLQVTTPSAVEAPLLLFTPEIGEACGAIDANQV
RGKIVMVARGTCTFAEKALRLQKAGAAGVVVVNSKAAYSRNPNRKYSLADDKRGLGRYVT
IPVVLVSREDATELHRHASLKRLLSDDDGDSEGDQGAQGDGIGTLVGSLSPWLY

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	1	497	9.6e-128	0.9753363228699552

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	5.37e-130	1	418	10	434	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	1.11e-68	2	417	89	498	glycoside hydrolase family 47 protein; Provisional
240122	PA_subtilisin_1	5.05e-19	564	674	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.
239041	PA_EDEM3_like	8.46e-18	562	677	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.
396691	PA	7.84e-14	578	674	1	89	PA domain. The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor and members of the RZF family. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA23124.1|GH47	1.02e-237	1	714	46	727
AIG56058.1|GH47	1.21e-215	1	687	48	687
AGB92969.1|GH47	1.32e-125	1	666	66	738
AAM50976.1|GH47	2.52e-124	1	666	66	747
NP_609611.1|GH47	2.52e-124	1	666	66	747

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KIJ_A	2.21e-55	4	422	24	435	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
5KK7_A	2.36e-55	4	422	24	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	2.53e-55	4	422	29	440	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	2.65e-55	4	422	29	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	1.37e-54	4	422	107	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|Q925U4|EDEM1_MOUSE	1.86e-116	1	421	141	563	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|Q92611|EDEM1_HUMAN	1.17e-115	1	421	146	568	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q9FG93|MNS4_ARATH	1.30e-115	1	415	56	445	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q6GQB9|EDEM3_XENLA	1.49e-115	1	698	54	792	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2
sp|Q2HXL6|EDEM3_MOUSE	4.91e-112	1	686	69	792	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
1.000065	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PHYSODRAFT_288737-t26_1-p1.