ID K1XZV5_MARBU Unreviewed; 392 AA.
AC K1XZV5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Pectate lyase {ECO:0000313|EMBL:EKD18389.1};
GN ORFNames=MBM_03382 {ECO:0000313|EMBL:EKD18389.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD18389.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD18389.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD18389.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH921433; EKD18389.1; -; Genomic_DNA.
DR RefSeq; XP_007291271.1; XM_007291209.1.
DR AlphaFoldDB; K1XZV5; -.
DR STRING; 1072389.K1XZV5; -.
DR GeneID; 18759317; -.
DR KEGG; mbe:MBM_03382; -.
DR eggNOG; ENOG502QSUT; Eukaryota.
DR HOGENOM; CLU_030634_1_0_1; -.
DR InParanoid; K1XZV5; -.
DR OrthoDB; 2292519at2759; -.
DR Proteomes; UP000006753; 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:EKD18389.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..392
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003853586"
FT DOMAIN 118..291
FT /note="Right handed beta helix"
FT /evidence="ECO:0000259|Pfam:PF13229"
SQ SEQUENCE 392 AA; 42350 MW; D0FFDE974E38C314 CRC64;
MRYNIFLVVV AAAHSAYAAT YYVSPTGSDT AAGTLAAPYR SIQLAVDKVV PGDTIFMRGG
TYSLTTNIKI TRKDGTSSAR ITLSAYNNEK VILDGEALPG TPSELNSSLP LVNRGVLQVL
ASSYWTFINF ELINGPYGVF HANSSYNRYE RLVTRENYES GFHMQGICER NTVLYLDSYK
NRDPRRLGEN ADGFALKEGE GEGNLIKGVR VWGNSDDGLD LWEFRSGVTI EDSVSWGNGN
NTWGFSPFNG DGNGFKLGGG DDGAVRPANH VVRNCISFQN VQKGFVDNGQ TGVFNISRNS
AWNNGNVGFF MESSTATLVD NLAVRNGRSE FSFTGGSQVT AGNTWQIAGT WNDAALMSTD
SAVIKGPRDA DGKIRSSNFL RPKNGAAVGA VI
//