CAZyme Information: EPrPVT00000016978-p1

Basic Information

• Species: Phytopythium vexans
• Lineage: Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans
• CAZyme ID: EPrPVT00000016978-p1
• CAZy Family: GH16
• CAZyme Description: ER degradation-enhancing alpha-mannosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1208	PvexDAOMBR484_SC0178|CGC1	133648.63	5.4028

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PvexansDAOMBR484	11991	1223560	34	11957

• Gene Location: location=PvexDAOMBR484_SC0178:1557-5183(+)

Full Sequence      

MLPRDDAAELGAKGPARRRRPRGSWRRRTAVPALALPFLLLTTWCVAFGVAGATEAASQT
GEDSLPLSRDNGLRELSGKSLRAFKNRVKRQLRGSECVQHHEAGDWWRYEWCVDRFVRQF
HRPVPNVVHGRKASPPATNAEEQTVLLGVHNVDKARPLHIERVDRFDRVKDPDVAGFVAI
EQYQVPGEFCAAANRSRSVEIQYQCCAFRANETYIERVEEPAVCSYRVRVCSPAACGLMQ
RDAYVLGAAPQMAQDEQRALAQTVKDMFYHAYSGYMTHAFPQDDLAPLSCRGAEFELGKL
PMLTLIDTLDMLAILEDGPEFRRAVSLVLENASFDLDEEVSVFETTIRVLGGLLSAHMFA
ADATRELYVSEDYHGGLLKLAVDLGDRLLPAFDTATGIPYGTVNLRRGVPKDETPIASTA
GAGSLSLEFTMLSVLTGDVKYAVAARRSVRALFDRRSALGLLGKHIDTRSGDWTETGSGP
GSNSDSFYEYLLKMYMLFDDREALEMFATVYPAVLEHNLHGDWYADVSMWTGCSHTNSIL
FESLASFWPGMQAGAGHLLSAAKSMNAFFRVWREYGFLPEQFNVLEWRPVKGRGARYPLR
PELLESTFYMHEATNDSSWLRAGAHAVHSLQKYARTDCGYASIGNVETKAQEDYMPSFFL
SETCKYLYLLFNDTHFFRRGGYVMTTEAHPFPVLPTKLVAPILQAGNKHEPLNRTHFPDD
RGLQCLPPSFSDHVEYSIEFEGEVVSRTPRCSKAKAAKEQQKTSTTSTTAAKGAVTTGLE
QWLPKIEEKLRRQFDFLYRKEDDEPELTVKSFIMGDVQHGGVAVPTPAGTKQDWLRELLH
GEVPAADSNLMDGPGALGQFDVSQSDGVMRFTRQATGDWLEVSGVSDALHMLVTVGRRKL
PEIPTARRDTTKKTEEEEEEWNPALQPTHHVHKLSTAGDVLPLSTRCTFKLVATALDIDD
PRQARSPELPFACVPAAFGIADELSNSLLFGQAPVVTAMPRDGCGELINPPEELRGAIVL
IARGTCYFETKVRNAAAHGAAGVVIINTEDDAYRVMVMGGSGVIDDESGEDENGSGSDRQ
AADPAQATEDPSQTSTEQAGDDGGVKIPVIMISRGMGEWLERSYLSNGRFTIQATIDLAV
WNRDQRPPVDDILHRGGRAFPYVDGLTSDNLRLYGPEWGVQMVATTTGNTGYHSYAIGIV
ETPQYESS

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	267	693	2.7e-132	0.9977578475336323

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	3.51e-139	267	693	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	6.03e-84	211	696	23	521	glycoside hydrolase family 47 protein; Provisional
239038	PA_C_RZF_like	6.06e-11	971	1127	24	139	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.
240122	PA_subtilisin_1	1.77e-07	974	1136	1	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.
239041	PA_EDEM3_like	4.74e-06	975	1034	4	59	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ27914.1|GH47	0.0	178	1203	1	1041
AIG56334.1|GH47	7.98e-243	88	1202	39	949
AIG55397.1|GH47	4.99e-234	97	1201	33	945
BAD52943.1|GH47	2.04e-124	235	721	27	528
CAY33089.1|GH47	2.04e-124	235	721	27	528

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KIJ_A	3.71e-55	264	693	9	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1FMI_A	4.27e-55	264	693	14	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	4.47e-55	264	693	14	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]
5KK7_A	1.82e-54	264	693	9	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]
1X9D_A	2.44e-54	264	693	92	534	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|Q9FG93|MNS4_ARATH	1.82e-118	249	695	29	475	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q9SXC9|MNS5_ARATH	8.39e-117	236	717	13	491	Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1
sp|Q8BJT9|EDEM2_MOUSE	1.35e-106	247	690	27	479	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Mus musculus OX=10090 GN=Edem2 PE=1 SV=1
sp|Q9BV94|EDEM2_HUMAN	1.92e-106	247	690	27	479	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Homo sapiens OX=9606 GN=EDEM2 PE=1 SV=2
sp|Q925U4|EDEM1_MOUSE	1.07e-104	166	738	43	635	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
0.993195	0.006806

TMHMM  Annotations     

Start	End
29	51