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
//