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Database: UniProt
Entry: A0A453MA51_AEGTS
LinkDB: A0A453MA51_AEGTS
Original site: A0A453MA51_AEGTS 
ID   A0A453MA51_AEGTS        Unreviewed;      1048 AA.
AC   A0A453MA51;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
OS   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET5Gv21115200.7, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET5Gv21115200.7}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) 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; A0A453MA51; -.
DR   STRING; 200361.A0A453MA51; -.
DR   EnsemblPlants; AET5Gv21115200.7; AET5Gv21115200.7; AET5Gv21115200.
DR   Gramene; AET5Gv21115200.7; AET5Gv21115200.7; AET5Gv21115200.
DR   Proteomes; UP000015105; Chromosome 5D.
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   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
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   InterPro; IPR048534; Man2a1-like_dom.
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   Pfam; PF21260; Laman-like_dom; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000015105};
KW   Signal {ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT   CHAIN           22..1048
FT                   /note="Alpha-mannosidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT                   /id="PRO_5018809958"
FT   DOMAIN          362..436
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1048 AA;  117488 MW;  55D9B75B3089047C CRC64;
     MGPVRLALLL LLLAAAAVVL GPGGGGEAVY IPYNTSAGVV NGKLNVHVVP HTHDDVGWLK
     TVDQYYVGSN NSIQNACVQN VLDSLVPALL KDENRKFIYV EQAFFQRWWR QQSDMIKDTV
     KGLVSSGRLE FINGGMCMHD EATVHYIDMI DQTTLGHRFI KEEFGQIPRI GWQIDPFGHS
     AVQAYLLGAE VGFDALYFFR IDYQDRDTRN GTKELEVVWR GSKTFGSSAD IFAGIFPKNY
     EPPPGEFYFE VDDTSPVVQD DPLLFDYNVE QRVNDFVAAA LAQANVTRTN HIMFTMGTDF
     KYQYAESWFR QMDKLIHYVN KDGRVNALYS TPSIYTDAKF STNEPWPLKT NDFFPYADNP
     NAYWTGYFTS RPALKRYVRM MSGYYLAARQ LEFFIGRSKS GSTTDSLGDA LALAQHHDAV
     TGTEKQHVAN DYAKRLSIGY KKAEELVSTS LGCLSESGSN SRCSSPTTKF VQCPLLNITY
     CPPSEMNLSQ GKSLVVLVYN SLGWKREDVL RIPVMSDSIV VHDSEGREIE SQLLPIANAS
     SHLRDRHVKA YLGTSPAASP KFWVAFPASV APLGFSTYFI SIGKRSASIS STSTLNSQGS
     ESRNLQVGQG RLKLQYDAAG ALSQYSDSKT QVEANFEQKY KYYLGQDGSG DDPQASGAYI
     FRPKGVVPIK TDGQVPPTIL RGPILDEVHQ QINPWIYQIT RVYKGKDYVE TEFIVGPIPV
     DDENGKELST EIITSMATNK TFYTDSSGRD FIKRVRDYRS EWKIEVNQPV AGNYYPINLG
     IYVEDGSKEL SILVDRSVGG SSIKDGQIEL MLHRRLLNDD GRGVAEALDE KVCLDDQCEG
     LVIEGKYYLK IDPQGDGARW RRTFGQELYS PLLLAFAEKV QHKFCCTRDR SNSYSCRIEH
     APTCFSRMEA TGGIHMFHHS LEWIQLTAFL KMSRCLLLRE LEDGSVLLRL AHLYEAGEHK
     DLSAPASVDL KRVFPDKKIG KIIETSLSAN QERAAMEKKR LKWKVAGPPP KENVVRGGPL
     DPSKLVVELA PMEIRTFVIN FDHRLAAH
//
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