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Database: UniProt
Entry: D9ZQD9_ARALL
LinkDB: D9ZQD9_ARALL
Original site: D9ZQD9_ARALL 
ID   D9ZQD9_ARALL            Unreviewed;       176 AA.
AC   D9ZQD9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=At1g23200-like protein {ECO:0000313|EMBL:ADL17275.1};
DE   Flags: Fragment;
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|EMBL:ADL17275.1};
RN   [1] {ECO:0000313|EMBL:ADL17275.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IOM_8 {ECO:0000313|EMBL:ADL17275.1};
RA   Foxe J.P., Stift M., Tedder A., Haudry A., Wright S.I., Mable B.K.;
RT   "Reconstructing origins of loss of self-incompatibility and selfing in
RT   North American Arabidopsis lyrata: a population genetic context.";
RL   Evolution 0:0-0(2010).
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; HM168528; ADL17275.1; -; Genomic_DNA.
DR   UniPathway; UPA00545; UER00823.
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:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
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   PANTHER; PTHR31707; PECTINESTERASE; 1.
DR   PANTHER; PTHR31707:SF152; PECTINESTERASE/PECTINESTERASE INHIBITOR 6-RELATED; 1.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   Pfam; PF04043; 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}.
FT   DOMAIN          9..61
FT                   /note="Pectinesterase inhibitor"
FT                   /evidence="ECO:0000259|Pfam:PF04043"
FT   DOMAIN          126..174
FT                   /note="Pectinesterase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01095"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADL17275.1"
FT   NON_TER         176
FT                   /evidence="ECO:0000313|EMBL:ADL17275.1"
SQ   SEQUENCE   176 AA;  19415 MW;  F58D1F2A3EF3D076 CRC64;
     RSYGQYSSPH DRQTALSAAI ANQDTCRNGF KDFKLTSSYS KYFPXQVHRN LTKSLSNSLA
     VTKAAAEAVA EKYPSTGFTK FSKQRSSGGG GGRRRLLMFS DDKFPSWFPL SDRKLLEDSE
     TTVKADLVVA KDGSGHYTSI QQAVNAAAKL PRXNTRLVIY VKAGVYKENV VIKKSI
//
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