ID   W2L8Z6_PHYPR            Unreviewed;      1043 AA.
AC   W2L8Z6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
DE   Flags: Fragment;
GN   ORFNames=L917_08049 {ECO:0000313|EMBL:ETL93896.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL93896.1};
RN   [1] {ECO:0000313|EMBL:ETL93896.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL93896.1};
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 CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361199};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
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DR   EMBL; KI679504; ETL93896.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2L8Z6; -.
DR   EnsemblProtists; ETL93896; ETL93896; L917_08049.
DR   VEuPathDB; FungiDB:PPTG_11759; -.
DR   Proteomes; UP000054423; Unassembled WGS sequence.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR   CDD; cd10810; GH38N_AMII_LAM_like; 1.
DR   Gene3D; 2.60.40.1360; -; 1.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR011682; Glyco_hydro_38_C.
DR   InterPro; IPR015341; Glyco_hydro_38_cen.
DR   InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR   InterPro; IPR000602; Glyco_hydro_38_N.
DR   InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF3; LYSOSOMAL ALPHA-MANNOSIDASE; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF07748; Glyco_hydro_38C; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 1.
DR   SMART; SM00872; Alpha-mann_mid; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW   Hydrolase {ECO:0000256|RuleBase:RU361199};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   DOMAIN          370..443
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETL93896.1"
SQ   SEQUENCE   1043 AA;  117020 MW;  1614BE3D63461878 CRC64;
     SPLPHPRSST EKETDSPLMR VVGTLASALL AASASASCDP SKWTPPSDGV YNTTSRVDPN
     KLNVHLIAHS HDDPGWLISV DQYYTQRVQY ILDTAVEELV RNPDRQFMYV EQSFFQRWWH
     QQGSEVRGVV KQLVREGRLD LTVNGGWCMH DEATPHYIAM VDQTAYGHQL LMDEFGISPR
     IGWQIDPFGH SATQGSLLSQ GVGFDALYFA RIDYQDYGNR KKNKDLEFIW RPSKSRGKAS
     QVFTGEIIDH YCPPGKFDFG NNGNQIQDDA ELHDYDVCDE VEQFVSNAKM RGDHSKGNHV
     FIPMGCDFQF DNSLRWFKNM DKIIHYVNQD GRVNVLYSNL SYYTDLKREE GLSWSVKTDD
     FFPYGSAQDD YWSGFFTSRP TLKRFARVAN TLLQQVRQLD AVYQSHHSAP LDALQRAVGL
     VQHHDGLSGT EKQSVADDYS LRLNDGIIKA EKELNEVLFV IGEKEPYHLC LLANTSVCDV
     TTQNANFEVV VHNALARTSV QTLSIPITHK SAELSLLSGN AKVREQNVYV ALPVHPEVQV
     APYSFVFSAE LKPLSTTRFL VKQKDLVDEE PVTDSVDDND EVVVLENQLM RAEISKSTGS
     ITKLANKKKN IQIPLSLDVA YYQAFQADGP KSGAYVFRPD SNKTYPVTGK MSTPNSLPDV
     EMVELHATGS RTSVPRVAFK IGNWVTLEYR VNDNDEFLEI EWTVGPVPID DKKGKEVILR
     FDAGKSIASD ATLYTDSNGL EFMKRVRNHR DTWNLTLHDN QEAVAANYFP ITTGAYIKDA
     KHQLNVVTDR AQGAASLVDG QVEVMVHRRL LADDNKGVSE HLNETESVYD SATKKQVTKG
     LVVRGNFFIN VDSAEDGMRS IRSKMESQFF RPLTIYRKPV PSEVEAKVPW LTVGEFPENV
     GLTTLQELTK QCLMVRLSHL YAVDEHSTLS KPVTVDFSTL FSVKNSAVSE VTELVLTGTK
     ELAVEEEGVG MQWKTRDDTY GWTPRSLPVK GTSVTLQAIE VRAFRVCFAK TAGSVTVDEP
     EEDSYGESLG AALQDLAEII AYE
//