CAZyme Information: PHYSODRAFT_310282-t26_1-p1

Basic Information

• Species: Phytophthora sojae
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
• CAZyme ID: PHYSODRAFT_310282-t26_1-p1
• CAZy Family: CE5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1116		123874.17	5.3259

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=JH159151:12028374-12031781(+)

Full Sequence      

MRGESCLRYHVTGAWWHYEWCFDRHVRQFHPQPAGPRGQQPKEQSILLGAYNAEKPQPLR
VLAVDNLARLADPDRMGYKAQQVYGSGDYCEEKRAKRTVKLQVKCCAFHDNETYVDSVEE
RAPCEYEMNVCSPVACGLMQRDQFVLTAPTHMEEEERQALTKTVRDMFYHAYNGYLTHAF
PQDDLLPLSCRGGEFELGRLPMLTLVDTLDTLAVLEDATEFRRAVALVVENADFALDTEV
SVFETTIRLLGGLLSAHLFAVNTDLKLYPEGGYDGSLLQLAVDLGDRLMPAFDTVTGIPY
GTVNLKHGVPKGETPIASTAGAGSLSIEFTMLSVLTGDPKYAAASRGAVRALFQRRSKLG
LLGKHINTKTGDWTETSSGPGSNSDSFYEYLLKMYELYGDRESLEMFAQVYPAVLAHNKH
GDWYTDVSMYTGCHHHSGSSAVVFESLAAFWPGMQIAAGDLKTAAESMNAFYRVWRDYGF
LSEQFNVGDWKPVKSRGGGGARYPLRPELIESTFYMHEATNDSSWLRAGAHVVHSLQKYA
KTPCGYASIADVESKKQEDYMPSFFLSETCKYLYLLFNTTHFFRQGNYVMTTEAHPLPIL
PTKVVEPILQEADAHVTKSEVAYENRYSPERVMRCKAPKFFDLINYSVHYEGKVVARTSR
CSPPAPSPAALIKASKSAAEKIAQSASERAKPTTTTTTTTTTTTTKTDNKPVDTESVASD
VLQEWLPALEEKLRKIGGKSVNDEWLEQLLEETSLGTTHQRRQPAKQQDAQGHVVQYLYG
GSQLGEFRVEQLPGRLRVTREETGDWIEASGIVDASHMIVGLGFNDGSNDDDAGADSYTF
EEPTSKKVDPSDDYHPPFMAWNHVYKVNEDLSLPVDQRCSLRVQLGYKPHPGEPQYNAKG
HPHVDGGGKGKPTVSLTVPCVGAGFGVTNTFKASRAFPNMELVIADPVDACSEVSDLPEE
SLRGKIVLAQRGECFFETKARNAAKWGAAGVIIANTEDDDLVMVMGGADENSAEATDEPL
DIPVVMVPERLGECIELTVRHHAHGVDHTRRRPRGISEASFPRIEGTADNIKVYGPVWGM
ELITMGSDREKDQEDDDENRQESFSIAIVGTPPWQH

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	167	599	6.3e-134	0.9977578475336323

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	1.12e-138	167	599	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	1.29e-85	138	602	54	521	glycoside hydrolase family 47 protein; Provisional
240122	PA_subtilisin_1	1.05e-17	921	1028	1	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.
239038	PA_C_RZF_like	3.63e-17	942	1033	44	131	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.
238300	PA	8.46e-16	922	1033	6	110	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
UIZ27914.1|GH47	0.0	80	1113	2	1042
AIG56334.1|GH47	3.57e-250	1	1087	43	934
AIG55397.1|GH47	2.56e-237	6	1088	33	932
QCE07576.1|GH47	1.35e-128	155	601	30	470
BAT94804.1|GH47	5.02e-128	155	601	30	470

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1FMI_A	3.98e-52	149	599	4	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	4.16e-52	149	599	4	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]
5KIJ_A	4.71e-52	162	599	7	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1X9D_A	2.11e-51	149	599	82	534	Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens]
5KK7_A	2.31e-51	162	599	7	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9FG93|MNS4_ARATH	5.42e-125	152	601	32	475	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q9SXC9|MNS5_ARATH	4.54e-117	136	600	13	479	Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1
sp|Q8BJT9|EDEM2_MOUSE	2.11e-112	147	597	28	480	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Mus musculus OX=10090 GN=Edem2 PE=1 SV=1
sp|Q9BV94|EDEM2_HUMAN	4.21e-112	164	597	39	480	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Homo sapiens OX=9606 GN=EDEM2 PE=1 SV=2
sp|Q925U4|EDEM1_MOUSE	9.46e-100	157	599	122	581	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 OTHER

Other	SP_Sec_SPI	CS Position
1.000040	0.000004

TMHMM  Annotations     

There is no transmembrane helices in PHYSODRAFT_310282-t26_1-p1.