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Database: UniProt
Entry: A0A229SQC3_9PSEU
LinkDB: A0A229SQC3_9PSEU
Original site: A0A229SQC3_9PSEU 
ID   A0A229SQC3_9PSEU        Unreviewed;       438 AA.
AC   A0A229SQC3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Pectate lyase {ECO:0000313|EMBL:OXM60849.1};
GN   ORFNames=CF165_40380 {ECO:0000313|EMBL:OXM60849.1};
OS   Amycolatopsis vastitatis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1905142 {ECO:0000313|EMBL:OXM60849.1, ECO:0000313|Proteomes:UP000215199};
RN   [1] {ECO:0000313|Proteomes:UP000215199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H5 {ECO:0000313|Proteomes:UP000215199};
RA   Adamek M., Alanjary M., Sales-Ortells H., Goodfellow M., Bull A.T.,
RA   Kalinowski J., Ziemert N.;
RT   "Comparative genome mining reveals phylogenetic distribution patterns of
RT   secondary metabolites in Amycolatopsis.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 9 family.
CC       {ECO:0000256|ARBA:ARBA00038263}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXM60849.1}.
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DR   EMBL; NMUL01000053; OXM60849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A229SQC3; -.
DR   OrthoDB; 9762467at2; -.
DR   Proteomes; UP000215199; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR40088; PECTATE LYASE (EUROFUNG); 1.
DR   PANTHER; PTHR40088:SF1; PECTATE LYASE PEL9; 1.
DR   Pfam; PF13229; Beta_helix; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:OXM60849.1};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..438
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038828725"
FT   DOMAIN          149..314
FT                   /note="Right handed beta helix"
FT                   /evidence="ECO:0000259|Pfam:PF13229"
SQ   SEQUENCE   438 AA;  46096 MW;  C114E949FAC885E5 CRC64;
     MKIFAFLVFS AVAVAVAGAP VAASSPAAGT TYYVAPAGSD SAAGTQTAPW ASVAHAQSVA
     QAGDTVYLRG GTYSYSRANK ACASQTDRVD AITLNKSGSA GNPIRYWAYP GETPVFDFSR
     VSDDCRIKGF DVTGNYIHLK GLEVKGVPQN NNLNHESWGI WISGSDNTFE LLNLHNNMGP
     GLFIQDGGGN LVVNSDSHDN YDPLTSNGAG ESADGFGAHI SANHPGNVFR GCRAWWNSDD
     GFDLINAFSS VTIENSWAWR NGYLPETTTS SGNGNGFKMG GYGGKYVSNG VKHAVRNSVA
     FNNKAAGFYA NHHTLANDYF DNTGYNNNPD FNMLGITSSG GATGLGNLRN NIAYKGSLTS
     NMSGTSTSYN SWNLSVTLSD AQFKSVSTSG WDAARQADGS LPVLPNLRLA ANSSLIDKGT
     NVGLPYNGKA PDLGAFES
//
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