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
//