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Database: UniProt
Entry: F6HV68_VITVI
LinkDB: F6HV68_VITVI
Original site: F6HV68_VITVI 
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
//
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