ID   W9QPL1_9ROSA            Unreviewed;      1158 AA.
AC   W9QPL1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=L484_010511 {ECO:0000313|EMBL:EXB47725.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB47725.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-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; KE343933; EXB47725.1; -; Genomic_DNA.
DR   RefSeq; XP_010091945.1; XM_010093643.1.
DR   AlphaFoldDB; W9QPL1; -.
DR   STRING; 981085.W9QPL1; -.
DR   GeneID; 21393801; -.
DR   KEGG; mnt:21393801; -.
DR   eggNOG; KOG1958; Eukaryota.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000030645; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd10809; GH38N_AMII_GMII_SfManIII_like; 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; 1.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   TRANSMEM        44..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          491..576
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1158 AA;  132333 MW;  9C27EE55D9E1718D CRC64;
     MAFSTRRGGW ANSLLPSTSV SSPSSTSKSK FSRKSRRRLA LKDFLFKNFF AIGLFVSLFF
     FFLVVLRYGV PTPITSTFRS RNTARIAKPR KPSYRKPVSG GDAGAAVDIT TKGLYDKIEF
     LDVDGGAWKQ GWKVTYGGDE WDTEKLKIIV VPHSHNDPGW KLTVEEYYDR QSRHILDTIV
     DTLSKDSRRK FIWEEMSYLE RWWRDASDNR KESFVNLVKN GQLEIVGGGW VMNDEANSHY
     FAIIEQITEG NMWLNDNIGA IPKNSWAIDP FGYSPTMAYL LRRMGFDNML IQRTHYELKK
     ELSLHKNLEY IWRQSWDAEE TTDIFVHMMP FYSYDIPHTC GPEPAICCQF DFARMRSFTY
     ESCPWGDHPV ETNQENVKER AFKLLDQYRK KSTLYRTNTL LVPLGDDFRY INVDEAEAQF
     RNYQLLFDYI NSNPSLNAEA KFGTLEDYFR TLREESERIN YSRPGEVGSG QVGGFPSLSG
     DFFTYADRQQ DYWSGYYVSR PFFKAVDRVL EQTLRATDMM MALLLGYCQR AQCEKLPVGF
     SYKLTAARRN LALFQHHDGV TGTAKDHVVL DYGTRMHTSL QDLQIFLSKA IEVLLKIRHE
     KSDQNPSQFE PAQVRSKYDA QPVHKTIISR EGTYQSVVLF NPSEQAREEV VMVIVNKPDV
     TVVDSNWTCI QSQTAPELQH DKSNIFSGRH RVYFKASIPA LGLQTYYIAN GFAGCEKAKP
     SKLKFFSKSG SLPCPTPYAC SKAKDDTVQI RNRHQTLTFD VATGLLQKII HKDGSQNVVG
     EEISMYSSWG SGAYLFKPTG DAQPIVKSGG QIVISEGSLM QELFSYPHTE WVKSPISHST
     RLYNGENTVQ EFLIEKEYHV ELLGAEFDDK EIITRYKTDI DSKRVFFSDL NGFQMSRRET
     YDKIPVQGNY YPMPSLAFMQ GSNGQRFSVH SRQSLGVASV KDGWLEIMLD RRLVRDDGRG
     LGQGVMDNRA MNVIFHILVE SNISSTKNSV SNSLPLNPSL LSHRIGAHLN YPLHAFISKK
     PQDMSMRPPP RSFAPLAISL PCDLHIVSFK VPRPLKYSQQ QVGDPRFVLI LQRLSWDSSY
     CHKGRSQCTS IAKEPVNLFH MFRELAVLNA KATSLNLLHE DSEMLGYPEQ SGEVAQEGHV
     LVSPMEIQAY KLDLRPQQ
//