ID D7MRW1_ARALL Unreviewed; 602 AA.
AC D7MRW1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Pectinesterase family protein {ECO:0000313|EMBL:EFH41171.1};
GN ORFNames=ARALYDRAFT_919784 {ECO:0000313|EMBL:EFH41171.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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; GL348720; EFH41171.1; -; Genomic_DNA.
DR RefSeq; XP_002864912.1; XM_002864866.1.
DR AlphaFoldDB; D7MRW1; -.
DR STRING; 81972.D7MRW1; -.
DR EnsemblPlants; scaffold_803184.1; scaffold_803184.1; scaffold_803184.1.
DR GeneID; 9300987; -.
DR Gramene; scaffold_803184.1; scaffold_803184.1; scaffold_803184.1.
DR KEGG; aly:9300987; -.
DR eggNOG; ENOG502QW0X; Eukaryota.
DR HOGENOM; CLU_012243_9_3_1; -.
DR OrthoDB; 668039at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:InterPro.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0052542; P:defense response by callose deposition; IEA:EnsemblPlants.
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:SF389; PECTINESTERASE_PECTINESTERASE INHIBITOR 64-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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..237
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT REGION 62..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 65463 MW; 963C303C086EF300 CRC64;
MDSPKLPYSL SASSSTPFAS AAVKPHRNKL LSRNGILIII AVSCILLLLI SLLIYATVSK
SSRSHRNPSH QTPTSDDQPP PETPPSPPPI AQIRLACNAT RFPDHCVASL SKPGQVPPDP
KPVQIIHSAI SVSFENLKSG QSKIKSILDS SAGNQNRTNI ATICLEILSY SQHRTESTDI
AVTSGEIKDA RAWMSAALAY QFDCWSGLKT VNDTKQVVDT ITFFEDLVNL TGNALSMMLS
FDNFGDDVVS WIRPATERDG FWEKAGPSLG SGTGTEANLG FPSGLTEDVT VCENGGKACN
YKTVQEAVDA APDTNGTVKF VIRIKEGVYE ETVRVPFEKK NVVFIGDGMG KTVITGSLNV
GQPGMTTFNS ATVGVLGDGF MARDLTIENT AGADAHQAVA FRSDSDFSIL ENCEFLGNQD
TVYAHSLRQF YKQCRIQGNV DFIFGNSAAV FQDCDILIAS KHSKLEQGGA NNAITAHGRI
DASQSTGFVF LNCSINGTEE YMKEFQANPK AHKNFLGRPW KEFSRTVFVN CNLESLISPD
GWMPWSGDFA LKTLYYGEYK NKGPGSVRTN RVPWSSEIPE KHVDVYSVAN FIQADEWAST
TA
//
