ID F6HV68_VITVI Unreviewed; 1149 AA.
AC F6HV68;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN OrderedLocusNames=VIT_14s0066g02390 {ECO:0000313|EMBL:CCB58586.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB58586.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN596252; CCB58586.1; -; Genomic_DNA.
DR RefSeq; XP_002276468.1; XM_002276432.4.
DR RefSeq; XP_010661000.1; XM_010662698.2.
DR RefSeq; XP_019080600.1; XM_019225055.1.
DR AlphaFoldDB; F6HV68; -.
DR STRING; 29760.F6HV68; -.
DR PaxDb; 29760-VIT_14s0066g02390-t01; -.
DR EnsemblPlants; Vitvi14g01872_t001; Vitvi14g01872_P001; Vitvi14g01872.
DR EnsemblPlants; Vitvi14g01872_t002; Vitvi14g01872_P002; Vitvi14g01872.
DR EnsemblPlants; Vitvi14g01872_t003; Vitvi14g01872_P003; Vitvi14g01872.
DR GeneID; 100243903; -.
DR Gramene; Vitvi14g01872_t001; Vitvi14g01872_P001; Vitvi14g01872.
DR Gramene; Vitvi14g01872_t002; Vitvi14g01872_P002; Vitvi14g01872.
DR Gramene; Vitvi14g01872_t003; Vitvi14g01872_P003; Vitvi14g01872.
DR KEGG; vvi:100243903; -.
DR eggNOG; KOG1958; Eukaryota.
DR HOGENOM; CLU_004690_1_0_1; -.
DR InParanoid; F6HV68; -.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000009183; Chromosome 14.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
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:0006491; P:N-glycan processing; IBA:GO_Central.
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; ALPHA-MANNOSIDASE 2-RELATED; 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183};
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 37..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 483..568
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1149 AA; 131469 MW; 529C5548B1F44E29 CRC64;
MAFSSRRGGW AHSLLPSSNS KSKLPRKARK RTFLKDFFLA NFFTIGLSLS LIFLLFITFR
YGVPKPLAFK SSNSRLPKLR KQGPRKPISP EVAGSGAAVD ITTKDLYDKI EFLDKDGGPW
KQGWVVNYKG NEWDSEKLKI FVVPHSHNDP GWKLTVEEYY DRQSRHILDT IVETLSKDAR
RKFIWEEMSY LERWWRDASD TRKEAFTNLV KNGQLEIVGG GWVMNDEANS HYFAIIEQIT
EGNMWLNDTI GVVPKNSWAI DPFGYSPTMA YLLRRMGFEN MLIQRTHYEL KKELSWHKNL
EYIWRQSWDA EESTDIFVHM MPFYSYDVPH TCGPEPAICC QFDFARMRGF MYELCPWGQH
PVETNQENVQ ERALKLLDQY KKKSTLYRTN TLLVPLGDDF RYISIDEAEA QFRNYQLLFD
YINSNPSLNA EAKFGTLEDY FHTLREEADR INYSRPGEIG SGQVGGFPSL SGDFFTYADR
QHDYWSGYYV SRPFFKAVDR VLEQTLRATE MLIALLLGHC HRAQCERLPT GFAYKLTAAR
RNLALFQHHD GVTGTAKDHV VEDYGTRMHT SLQDLQIFMS KAIEVLLGIR HEKSDQTTAQ
FEPAQLRSKY DIQPTHRAIS PPEGSAQSVV FFNPLEQTRN EVVMVVVNRP DVTVLASNWT
CVKSQVSPEW QHDKSKIFTG RHRVHWKASV PAMGLETYYI AVGYVGCEKA KQAKLKFATK
SNHLPCPAPY ACSKLEGDTA EIQNRHQTLT FDVKLGLLQK ISHKDGSQSV VGEDISMYSS
WGSGAYLFKP TGDAQPIIKS GGQMVISEGP LMQEVFSYPK TTVEKTPISH STRIYNGEKN
SIQEFVVEKE YHVELIGQDF NDKELIVRYK TDIDNKRIFY SDLNGFQMSR RETYDKIPLQ
GNYYPMPSLA FMQGSNGQRF SVHTRQSLGA ASLKNGWLEI MLDRRLLRDD ERGLGQGVMD
NRPMNVVFHI LVESNISSTS NPVSNPLPLD PSLLSHSVGA HLNYPLHAFI AKKPQETAVQ
QPSRSFSPLT ASLPCDLHVV TFKVPRPSKY PLQPPEDPRF VLMLQRRKWD SSYCRKGRSQ
CTRIADEPVN LFSMFKGLTV LNARATSLNL LHEDTEMLGY SEKVGEAAQE GPVLISPMEI
QAYKLELRP
//