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Database: UniProt
Entry: D0MVW7_PHYIT
LinkDB: D0MVW7_PHYIT
Original site: D0MVW7_PHYIT 
ID   D0MVW7_PHYIT            Unreviewed;      1039 AA.
AC   D0MVW7;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN   ORFNames=PITG_02266 {ECO:0000313|EMBL:EEY63780.1};
OS   Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY63780.1, ECO:0000313|Proteomes:UP000006643};
RN   [1] {ECO:0000313|Proteomes:UP000006643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX   PubMed=19741609; DOI=10.1038/nature08358;
RG   The Broad Institute Genome Sequencing Platform;
RA   Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA   Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA   Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA   Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA   Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA   Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA   Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA   Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA   Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA   Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA   Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA   Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA   Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA   Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA   Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA   Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA   Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA   Nusbaum C.;
RT   "Genome sequence and analysis of the Irish potato famine pathogen
RT   Phytophthora infestans.";
RL   Nature 461:393-398(2009).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601382-2};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family.
CC       {ECO:0000256|ARBA:ARBA00007658, ECO:0000256|RuleBase:RU361193}.
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DR   EMBL; DS028120; EEY63780.1; -; Genomic_DNA.
DR   RefSeq; XP_002907216.1; XM_002907170.1.
DR   AlphaFoldDB; D0MVW7; -.
DR   STRING; 403677.D0MVW7; -.
DR   EnsemblProtists; PITG_02266T0; PITG_02266T0; PITG_02266.
DR   GeneID; 9469654; -.
DR   KEGG; pif:PITG_02266; -.
DR   VEuPathDB; FungiDB:PITG_02266; -.
DR   eggNOG; KOG2429; Eukaryota.
DR   HOGENOM; CLU_281121_0_0_1; -.
DR   InParanoid; D0MVW7; -.
DR   OMA; WHYEWCF; -.
DR   OrthoDB; 942598at2759; -.
DR   Proteomes; UP000006643; Partially assembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd04818; PA_subtilisin_1; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 2.70.130.10; Mannose-6-phosphate receptor binding domain; 1.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR044674; EDEM1/2/3.
DR   InterPro; IPR001382; Glyco_hydro_47.
DR   InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR   InterPro; IPR012913; OS9-like_dom.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR036026; Seven-hairpin_glycosidases.
DR   PANTHER; PTHR45679; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 2; 1.
DR   PANTHER; PTHR45679:SF6; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 2; 1.
DR   Pfam; PF01532; Glyco_hydro_47; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF07915; PRKCSH; 1.
DR   PRINTS; PR00747; GLYHDRLASE47.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF48225; Seven-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR601382-2};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycosidase {ECO:0000256|RuleBase:RU361193};
KW   Hydrolase {ECO:0000256|RuleBase:RU361193};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601382-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006643}.
FT   DOMAIN          5..87
FT                   /note="Protein OS9-like"
FT                   /evidence="ECO:0000259|Pfam:PF07915"
FT   DOMAIN          928..1016
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   REGION          1018..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        241
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        382
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        480
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        505
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   BINDING         589
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
SQ   SEQUENCE   1039 AA;  115882 MW;  4F9C1240B82A5036 CRC64;
     MRGEKCLRYH VAGTWWHYEW CFDRHVRQFH PLPKGENTKE NSIMLGVFNP QKPEPLRVLA
     VDNLARLADP DRMGYMAHQR YNSGDFCEAR EARRSVKLQV KCCALHDNET YVDSVDEKAP
     CDYEMNVCSP VACGLMQRDQ FVLTAPTSME EDERKALTKT VRDMFYHAYN GYLTHAFPQD
     DLLPLSCKGG EFELGRLPML TLIDTLDTLA LLQDATEFRR AVGLVVENAD FDLDTEVSVF
     ETTIRMLGGL LSAHLFAVNT QLKLYPDGDY DDALLRLAVD LGDRLMPAFD TVTGIPYGTV
     NLKYGVPKGE TPIASTAGAG SLSVEFTMLS VLTGEPRYAT ASRGAVRALF QRRSKLGLLG
     KHINTKTGEW TETSSGPGSN SDSFYEYLMK MYELFGDREA LEMFAQVYPA VLVHNKHGDW
     YTDVSMYTGC HHHSGSSAII FESLASFWPG MQVAAGDLQV AAESMNAFYR VWRDYGFLSE
     QFNVGDWKPV KSRGGGGARY PLRPELIEST FYMHEATNDS SWLRAGAHVV HSLQKYTKTS
     CGYASIADVE SKKQEDLMPS FFLSETCKYL YLLFNTTHFF RQGNYVMTTE AHPLPILPTK
     LVEPILRASD ASSDVLNHNR YSPDRVMQCR VPKFYDLVDY SIHYEGKVVA RTSRCVPPAP
     SPAKLLKASK AVAEKLAAAS TETSSLSDIE KIAMAASDNA KPTTTKEKKS DTGSVTSDVL
     QEWLPSLQKK LQTIGGKNFD NMWLEKLLEE SSATSKKQPV SEQGGQAVQY LYGGNQLGEF
     RVEQLPGSVR VTREETGDWI EASGVHDANH MIVGLGFNDG SDGDAGADSY TFDEPKSDKI
     HVEQGDDYQP PFMAWNYVYK VNEDLTLPMD QRCSLRVQVG YTPYPGELQH NPHEAKGKPN
     VWLTVPCVGA GFGVTSTFKA SRAFPHSELV LADPFDACSD VSNLTEEHVR GKIVLVVRGE
     CFFEKKARNA AHWGAAGVIV VNTEDDDLVM VMGGLEENSE EAIDEPLDIP VVMVPQRLED
     HEESTETDRS LEWMAELTT
//
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