ID A0A0E0A7H5_9ORYZ Unreviewed; 1173 AA.
AC A0A0E0A7H5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM06G09820.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM06G09820.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM06G09820.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0E0A7H5; -.
DR STRING; 40148.A0A0E0A7H5; -.
DR EnsemblPlants; OGLUM06G09820.1; OGLUM06G09820.1; OGLUM06G09820.
DR Gramene; OGLUM06G09820.1; OGLUM06G09820.1; OGLUM06G09820.
DR eggNOG; KOG1958; Eukaryota.
DR HOGENOM; CLU_004690_1_0_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblPlants.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:EnsemblPlants.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042538; P:hyperosmotic salinity response; IEA:EnsemblPlants.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:EnsemblPlants.
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:UP000026961};
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 59..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 500..585
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1173 AA; 133059 MW; 5A181AED4E8673A6 CRC64;
MPFFSGGGGG RSGALLPTTS KPKGHHHLRS KGLSSPAASR RRGAHSASSS ASSSSRRRVL
YVAAAAFAAL FLLAFFRLGL PSSRPAATSP ARLRPRLTRR PAFRRDSAAA EAAAAAVAAR
IGREAHVDIT TKDLYDRIQF LDVDGGAWKQ GWEVSYKGDE WDGEKLKVFV APHSHNDPGW
RLTVEEYYEK QSRHILDTII ESLSKDSRRK FLWEEMSYLE RWWRDAPRKK QEAFTKLVRD
GQLEIVSGGW VMNDEMMEGN MWLNDTIGVV PKNSWSIDPF GYSATMAYLL RRMGFHNMLI
QRTHYELKKE LAMNKNLEYL WRQNWDIDET TDIFVHMMPF YSYDIPHTCG PEPAICCQFD
FARMRSFSYE SCPWRFDPVE TNANNVQERA MKLLDQYRKK STLYRTNTLL IPLGDDFRYV
STEEAEAQFR NYEKLFDYIN SNPHLKAEVK FGTLEDYFST LRDEAERINY TRPGELVSSE
LPGFPTLSGD FFTYADRNQD YWSGYYVSRP YFKAVDRVLE QTLRASEILS SFVLGYCQKL
QCVKLPISFS HKLTAARRNL ALFQHHDGVT GTAKDHVVVD YGTRMHTSLQ DLQLFMSRAV
EVLLGDIHDR SDPTLLSHFE PVQERSKYDV QPVYKVLNPH GGKAHSVVLF NPLEQTRDEI
VMVVVSNPDV SVLNSNGSCL RSQISPEWQY VSGEKVSTGQ HRLYWRASVP ALGLETYYVA
TGYDDCAKAT PAVVKAFTTA GQFPCPEPYV CSKLEGKTVE MKNSYHSLSF DVRHGLLQTV
TRNKDGEHTD VGEEIGMYRS HGSGAYLFKP IGEAQSIVEE GGYFILSEGP LVQEAHSLPK
TQWHKSPISH STRIYSCGDS IQDMLIEKEY HVELVGHVFN DKELIVKFKT DIDNQGVFYS
DLNGFQMSRR QTYDKIPLQG NYYPMPSLAF LQDSLGNRFS VHSKQSLGAA SLKNGWLEIM
LDRRLTQDDG RGLGQGVVDN RPMNVIFHLL RESNVSALPK THSLLTLQPS LLSHRVGAHL
NYPMHAFVSK KAQEKSFRLA QQTFAPLTSP LPCDVHVVNL KAPQPLKFHH AEAVEARFAL
LLQRRGWDAS FCRRGGLNCT TIGEEPVNLF YMFKDLAVLD VKATSLNLLH DDPEMLGYLE
QIGDVAQEGN VLISPMDIQA YKLDLQPPSS QEE
//