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Database: UniProt
Entry: F6I0G4_VITVI
LinkDB: F6I0G4_VITVI
Original site: F6I0G4_VITVI 
ID   F6I0G4_VITVI            Unreviewed;       555 AA.
AC   F6I0G4;
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=Pectinesterase inhibitor domain-containing protein {ECO:0000259|SMART:SM00856};
GN   OrderedLocusNames=VIT_04s0044g01000 {ECO:0000313|EMBL:CCB60430.1};
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:CCB60430.1, 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   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC       family. {ECO:0000256|ARBA:ARBA00007786}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC       {ECO:0000256|ARBA:ARBA00006027}.
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DR   EMBL; FN596506; CCB60430.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6I0G4; -.
DR   STRING; 29760.F6I0G4; -.
DR   PaxDb; 29760-VIT_04s0044g01000-t01; -.
DR   EnsemblPlants; Vitvi04g02246_t001; Vitvi04g02246_P001; Vitvi04g02246.
DR   Gramene; Vitvi04g02246_t001; Vitvi04g02246_P001; Vitvi04g02246.
DR   eggNOG; ENOG502QW0X; Eukaryota.
DR   HOGENOM; CLU_012243_9_3_1; -.
DR   InParanoid; F6I0G4; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000009183; Chromosome 4.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR   GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd15798; PMEI-like_3; 1.
DR   Gene3D; 1.20.140.40; Invertase/pectin methylesterase inhibitor family protein; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR035513; Invertase/methylesterase_inhib.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR000070; Pectinesterase_cat.
DR   InterPro; IPR006501; Pectinesterase_inhib_dom.
DR   NCBIfam; TIGR01614; PME_inhib; 1.
DR   PANTHER; PTHR31707; PECTINESTERASE; 1.
DR   PANTHER; PTHR31707:SF271; PECTINESTERASE/PECTINESTERASE INHIBITOR 51-RELATED; 1.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   Pfam; PF04043; PMEI; 1.
DR   SMART; SM00856; PMEI; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   SUPFAM; SSF101148; Plant invertase/pectin methylesterase inhibitor; 1.
PE   3: Inferred from homology;
KW   Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..555
FT                   /note="Pectinesterase inhibitor domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011110000"
FT   DOMAIN          46..195
FT                   /note="Pectinesterase inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00856"
FT   REGION          27..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  60690 MW;  4240B0F0BFC0473E CRC64;
     MASLFLLALL SLFLFFSLSS ASHHHSPRHS LPHFPQPITP QPSTASVPPQ IHQACAATRY
     PETCEASLIA SDRVPPDPKP IDVIQSALWV SLENLKTAQS MVKDILDASA RNLNRTTAAK
     NCLEVLHNSE YRISSTMEAL PHGKIKDARA WVSAALLYQY DCWSALKYAN DTQQVNKTMS
     FLDSLLGLSS NGLSMMASYD IFGNDIGSWR PPKTERDGFW EPSGLGEESG LGVKGGVPTG
     LPPDATVCKD GNGCYKTVQE AVDAAPANAG DRKFVIRIRE GVYEETVRVP LEKKNVVFLG
     DGMGKTVITG SLNVGQPGIS TYNTATVGVS GDGFMASGLT FQNTAGPDAH QAVAFRSGSD
     LSVIENCEFL GNQDTLYAHS LRQFYKSCNI QGNVDFIFGN SASIFQDCLI LIRPRQLKPE
     KGENNAVTAH GRTDPAQTTG FVFQNCVVNG TDDYMKLYYS NPKVHKNFLG RPWKEFSRTV
     FIRCFLEPLV TPQGWLPWSG DFALKTLYYG EFNNSGLGAS LSARVTWSSQ IPAQHLNTYS
     VQNFIQGNGW IPTTS
//
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