ID   A0A3M6VNC6_9STRA        Unreviewed;       906 AA.
AC   A0A3M6VNC6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=DD238_000539 {ECO:0000313|EMBL:RMX67927.1};
OS   Peronospora effusa.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Peronospora.
OX   NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX67927.1, ECO:0000313|Proteomes:UP000282087};
RN   [1] {ECO:0000313|EMBL:RMX67927.1, ECO:0000313|Proteomes:UP000282087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R14 {ECO:0000313|EMBL:RMX67927.1,
RC   ECO:0000313|Proteomes:UP000282087};
RA   Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA   Reyes Chin-Wo S., Mou B., Michelmore R.;
RT   "Comparative genomics of downy mildews reveals potential adaptations to
RT   biotrophy.";
RL   Submitted (JUN-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RMX67927.1}.
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DR   EMBL; QLLG01000155; RMX67927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M6VNC6; -.
DR   STRING; 542832.A0A3M6VNC6; -.
DR   Proteomes; UP000282087; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000282087};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   DOMAIN          211..284
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   906 AA;  101961 MW;  635E545BE34D23CF CRC64;
     MMDQTAYGHQ LLMDEFGISP RIGWQIDPFG HSATQGSLLS QGIGFDALYF ARIDYQDYEN
     RKRNKELEFI WRPSKSRGKR SQVFTGEIID HYCPPEKFDF GKNKNQIQDD TELHDYDVCD
     EVEQFVNNAK MRGGLSKGNH VFIPMGCDFQ YDNSRRWFKN MDKIIHYVNQ DARVNVLYSN
     LSYYTDMKRA EGLTWSVKTD DFFPYGSAQD DYWSGFFTSR PTLKRFARVA NTLLQQVRQL
     DAIYQSHHSS TLAALQRAVG LVQHHDGLSG TEKQSVADDY ALRLNDGIIQ AEKEMNEVLF
     VIGEKELYHL CLLANTSVCD VSTQNTEFEV LVHNALARTT VQTVSIPITH KSAEVKVLSG
     NASVRAQSVF VALPVHPETQ VAPYSLVFSA ELKPLSTTRF FVKQKGVDYS TAMNENIDEH
     KERHENAGAD GLDEYTENDD VVVLENQMMR AEISKMTGSI TKLANKKKNI QIPLSLEVRY
     YQAFQDHGPK SGAYVFRPDS NKTYPVTVKS EAMPTLVSGV TMIELQTTSL AADGGLASVP
     RVAFKIGNWV TLEYRMNDDD EFLEIEWTVG PVPIDDKKGK EVIVRFDAGN SIASASTLYT
     DSNGLEFMKR VRNHRDTWNL TLHDNQEEVA ANYFPITTGA YIKDSERQLN VVTDRAQGAA
     SLADGQVEVM VHRRLLVDDN KGVDEPLNEK ESVYNTATKK YATKGLAVRG NFFINVDSAE
     DGMRSIRSKM ESQFFRPLTA YRKLVSSKEK AKVPWLTVGE FPLNVGLTTV QELSKQCLMV
     RLSHLYAVDE HSSLSQPVTV DFSSLFSVKN SVVSEVTELV LTGTKELSLE NKGRAMEWKT
     TDDAHGWSPR SLPVKGTSVT LQAIEVRAFR VCFAKDAGMI EDTAIDNDDD LFGTALQDLA
     EIIAIE
//