ID   A0A316Z4R5_9BASI        Unreviewed;      1144 AA.
AC   A0A316Z4R5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE            EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN   ORFNames=FA09DRAFT_343870 {ECO:0000313|EMBL:PWN96740.1};
OS   Tilletiopsis washingtonensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Entylomatales; Entylomatales incertae sedis;
OC   Tilletiopsis.
OX   NCBI_TaxID=58919 {ECO:0000313|EMBL:PWN96740.1, ECO:0000313|Proteomes:UP000245946};
RN   [1] {ECO:0000313|EMBL:PWN96740.1, ECO:0000313|Proteomes:UP000245946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4186 {ECO:0000313|EMBL:PWN96740.1,
RC   ECO:0000313|Proteomes:UP000245946};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; KZ819298; PWN96740.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316Z4R5; -.
DR   STRING; 58919.A0A316Z4R5; -.
DR   OrthoDB; 2786490at2759; -.
DR   Proteomes; UP000245946; Unassembled WGS sequence.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
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; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR041147; GH38_C.
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   PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR   PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF17677; Glyco_hydro38C2; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245946}.
FT   DOMAIN          577..657
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1144 AA;  128421 MW;  C5058A91F201C827 CRC64;
     MPPAKPPYPV RADEARRPVH GVDVRSVQER RLGEFVGGQY SKYNLSSVLF EARTDKSDAI
     SIERWDPKAG EKPGFDEAVK QVYRPAKKGD QFGPSWTNHW VRLTINVPSA WHNKEWVELE
     FDPGCEALIF DTEGVTLQGI TGAYDSNRRV DFPITAKARK SELVLYIEVT CNGMFGVENS
     REGDPDPNRY FTLASCDLVV KNAEAWRLLW DFQLLRGLVD EMPRDGPLQN KALWVANKIQ
     DTFRQDDPAT IGECRRIAQE VLGKDWDKLE EGVYEQGNRK DRDDTALWSL GHCHIDTAWL
     WPFSATQQKV ARSWTTQLDL MERYPEFRFT ASTAQQYVWL EKLYPKTFTR LQKAVKRGTF
     QPIGGTWVEC DGNLPSGESF VRQFLYGQRY FESRFGQRSN IFWLPDSFGY NAQLPALARG
     AGCDYFFTQK LSWSNVNRFP HNTMVWVGLD GTQIITHLTP VDNYDSQCGV GDLVRGIKNN
     KNLNVQPSAL HLFGFGDGGG GPTAPELEAL RRARAVHNEG YTEMPKVCRL FPVSPRLIQR
     SRQVTVGKSA QDFFEHVTKI TDNGERLPRW SGDLYLEFHR GVQTSHGSIK RWNRKLEIMM
     TQIELAATLA SLREKGTYKY PKEQIDQLWE NIMLCQFHDV LPGSSIRLVY DDAERIYKET
     AKLGAKLLEE ANEAATGSRH VLKATNALNV RRRELVEVEA SRLASLPGVP TVQMLDGGAK
     ALVLMEDGHG TGEARPTSHN GPEHRAYATE SNGTFTLRNE LVSLSISKGH ISSLRTRHAD
     GHWLELLQRG QRAGLTICED YPPQFDAWET EIYSLNTTTD IAFSSVRIAE KGPWRSSLAL
     EASFGKSHAV VHISLDATSA SVEAQHPLAM LRFDAEVDWH EKHRFLRFEV PTVLSADLAS
     YETPFGVTKR PTARNTTWDA AKFEVCSHKF FDLSESGVGL SILNDCKYGA SVEGGRMRLS
     LLKAPTYPDA HTDEGKHQMA FALLPHQGPL TVATVHAARI FNAPLQPLTS RGPEYPRRMP
     VRLTQPRGGS VVLETIKRGE ADFDYHARSG AGTSIVLRMY EALGTHVRAT VHIKDLAVAS
     VSLTNLLEDD IDDEPATPSA EQQADEWVDV ASRGLRCGVG EDGETTVALA FRPFQIVTLK
     IVLA
//