ID W2HVA2_PHYPR Unreviewed; 1211 AA.
AC W2HVA2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN ORFNames=L916_20417 {ECO:0000313|EMBL:ETL25766.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL25766.1};
RN [1] {ECO:0000313|EMBL:ETL25766.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ05E6 {ECO:0000313|EMBL:ETL25766.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ05E6.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KI676421; ETL25766.1; -; Genomic_DNA.
DR AlphaFoldDB; W2HVA2; -.
DR EnsemblProtists; ETL25766; ETL25766; L916_20417.
DR VEuPathDB; FungiDB:PPTG_18414; -.
DR Proteomes; UP000053864; Unassembled 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 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; IPR044865; MRH_dom.
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.
DR PROSITE; PS51914; MRH; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR601382-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 91..222
FT /note="MRH"
FT /evidence="ECO:0000259|PROSITE:PS51914"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 469
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 567
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 592
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT BINDING 676
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
SQ SEQUENCE 1211 AA; 134735 MW; 001921E07FC0A358 CRC64;
MLPRQPRSRP GKLDASPRAP RRSSTAAIKH AYSCVFLLSI ALLLVSSSAA QAENQAQDVS
NKLSHFNGLH TLSGASYRAF KNRLKRQMRG ESCLRYHVGS TWWHYEWCFD RHVRQFHPFP
KGENSEEKSI MLGVFDPQKP QPLRVLAVDN LARLTDPDRM GYMAQQRYSA GDFCEARGAR
RSVKLQVKCC ALHDNETYVD SVDEKAPCDY EMNVCSPVAC GLMQRDQFVL TAPTYMKEDE
RKALTKTVRE MFYHAYNGYL THAFPQDDLL PVSCKGGEFE LGRLPMLTLI DTLDTLALLE
DATEFRRAVG LVVENADFDL DTEVSVFETT IRMLGGLLSA HLFAVNTDLK LFPEGGYDGS
LLRLAVDLGD RLMPAFDTVT GIPYGTVNLK HGVPKGETPI ASTAGAGSLS VEFTMLSVLT
GEPKYAAASR GAVRALFQRR SKLGLLGKHI NTKTGEWTET SSGPGSNSDS FYEYLMKMYE
LFGDREALEM FAQVYPAVLV HNKHGDWYTD VSMYTGCHHH SGSSAIIFES LASFWPGMQV
AAGDLKVAAE SMNSFYRVWR DYGFLSEQFN VGDWKPVKSR GGGGARYPLR PELIESTFYM
HEATNDSSWL RAGAHVIHSL QKYTKTSCGY ASIADVESKK QEDDMPSFFL SETCKYLYLL
FNTTHFFRQG NYVMTTEAHP LPILPTKLVE PVLQASSASN DVVYDNRYSP HRVMQCEVPK
FYDFIDYSVH YEGKVVARTS RCLPPAPSPA ALLKASKSMA KKLATTTADT DAMSAIEKIA
QAASENAKPT TNEKKKSIDT ESVASNVLQE WLPALEEKLR KIGGKNIDDK WLEKLLEENS
LKSKQPTTDQ NSQGQVVQYL YGGNQLGEFR VEQLPGRVRV TREETGDWIE ASGVLDASFM
IIGLGLNDGS DGDAGADSYT FDEPTSDKIE QGDDYHPPYL SWNYVYKINE DFTLPMDQRC
SLRVQVGYTS YPGELQHSAK GSPHDKGKPN VWLTVPCVGA GFGVTSTFQA SRAFPSSELV
LADPIDACSE VTNLSEENVR GKTLIVLRGE CFFEKKARNA AKWGAAGVIV VNTEDDDLVM
VMGGMEENSE QDTDEPLGIP VVMVPQRLGE WFEARLAESK ASSLSPVKVS VELTVRHHDG
NADIRRRPRG IHGDGSFPRV DGKADNMKIY GPLWGIELIT INSSKEKSQE QEEYHQDSFT
IAIVGTPPWQ H
//
