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Database: UniProt
Entry: A0A0D3E2R2_BRAOL
LinkDB: A0A0D3E2R2_BRAOL
Original site: A0A0D3E2R2_BRAOL 
ID   A0A0D3E2R2_BRAOL        Unreviewed;      1028 AA.
AC   A0A0D3E2R2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   Name=106317815 {ECO:0000313|EnsemblPlants:Bo9g022110.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo9g022110.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo9g022110.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo9g022110.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-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   RefSeq; XP_013611040.1; XM_013755586.1.
DR   AlphaFoldDB; A0A0D3E2R2; -.
DR   STRING; 109376.A0A0D3E2R2; -.
DR   EnsemblPlants; Bo9g022110.1; Bo9g022110.1; Bo9g022110.
DR   GeneID; 106317815; -.
DR   Gramene; Bo9g022110.1; Bo9g022110.1; Bo9g022110.
DR   KEGG; boe:106317815; -.
DR   eggNOG; KOG1959; Eukaryota.
DR   HOGENOM; CLU_004690_2_0_1; -.
DR   OMA; HCNDDPI; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000032141; Chromosome C9.
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   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:SF61; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361199};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW   Signal {ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT   CHAIN           24..1028
FT                   /note="Alpha-mannosidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT                   /id="PRO_5017853805"
FT   DOMAIN          357..431
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
FT   REGION          967..990
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        973..987
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1028 AA;  115780 MW;  9A6D55AA12A73E13 CRC64;
     MVIPGLSVLI CVTSWLSLES VNGVYVKYGT EARVVPDKLN VHLVPHSHDD VGWLKTVDQY
     FIGSNNSIQK ACVRNVMDSV MDSLRRDPNR KFVFAEMAFF TRWWGEQNPE THEHVKKLVN
     SGQLEFVNGG WSMNDEATCH YIDMIDQMTL GHRFIMQTFN ITPRAAWQID PFGHSSVQAY
     LMGAELGFDS LHFARIDYQD REKRKDEKSL EFVWRGSETF ASSSQIFTNT FPVHYSPPSG
     FHYEITDDYA PLQDDPLLDA FNVKEAVDNF VNASLFYANV TRGNHVMWTM GDDFQYQFAE
     SWFRQMDRLI HYVNKDGRVN AVYSTPSLYV DAKNAAKNIT WPLKTHDFFP YADRDSAYWT
     GYFTSRPALK RYVRSLSGYY LAARQLEFLV GKKSGGPNTC RLGDSLAIAQ HHDGVTGTAK
     QHVTNDYAKR LAHGASEAEA VVNSALAHLM NKARTKPDIS LTQCSSMNMS YCPVTEETIS
     GQKSLILVAY NSLAWNRTEV IRIPVNDVGL NVEDSSGNTL DAQYIPMDNV TSNLRSNYSK
     AYLGVSSQQI PKYWLVFKAT VPPLGWNTFF ISKATGEGSD KNKHSPGTFS PMKGITEIGP
     GNLKLVFSPD SGLLKQMHNS RTGAKILVDQ NYLWYASNVG DSKNSQVSGA YIFRPNASLA
     YSVSSKPELQ IVKGPLVDEV HQQFSPWVSQ VIRVYKDKEH AEFEYTIGPI PVGKDYVGKE
     VITRMVANMS TEKTFYTDSN GRDFLKRVRD NRTDWTLKVN EPIAGNYYPL NLGMYTKDKK
     VELSVLVDRA TGGGSIKDGE LELMLHRRTC MDDSRGVEES LEETVCINGT CTGLTVRGNY
     YVSINPVGGE GARWRRGTGQ EIYTPLVMAF THENKEKWKG SNSVKGNAMD PHYAFPPNVA
     LITLEELDLG NVLLRLAHLY EAGEESEYSK VAKVELKKLF PGKTIKGVKE MSLVATQEKA
     KMKEKMKWKV EGEAEQSQSS SHPQKGGPID SSALVVELSP MEIRTFLLQF SQKQPAKQQR
     RRKFILGF
//
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