ID A0A135U4C0_9PEZI Unreviewed; 593 AA.
AC A0A135U4C0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN ORFNames=CSAL01_07796 {ECO:0000313|EMBL:KXH55231.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH55231.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH55231.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH55231.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-
CC (1->4)-alpha-D-galactopyranosyluronic acid bonds of
CC rhamnogalacturonan I domains in ramified hairy regions of pectin
CC leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-
CC unsaturated D-galactopyranosyluronic acid at the non-reducing end.;
CC EC=4.2.2.23; Evidence={ECO:0000256|ARBA:ARBA00001324};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000256|ARBA:ARBA00010418}.
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:KXH55231.1}.
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DR EMBL; JFFI01001735; KXH55231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135U4C0; -.
DR STRING; 1209931.A0A135U4C0; -.
DR OrthoDB; 2715696at2759; -.
DR Proteomes; UP000070121; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10316; RGL4_M; 1.
DR CDD; cd10320; RGL4_N; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR029413; RG-lyase_II.
DR InterPro; IPR029411; RG-lyase_III.
DR PANTHER; PTHR32018:SF1; RHAMNOGALACTURONAN ENDOLYASE; 1.
DR PANTHER; PTHR32018; RHAMNOGALACTURONATE LYASE FAMILY PROTEIN; 1.
DR Pfam; PF14683; CBM-like; 1.
DR Pfam; PF14686; fn3_3; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KXH55231.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..593
FT /note="rhamnogalacturonan endolyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007804581"
FT DOMAIN 315..397
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 412..591
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 593 AA; 65036 MW; E6D276F84AD53ECA CRC64;
MRTNLFAAAL GGLISNAFAA PTQAEPFLRQ VDNQTWIIGN DMWNMTQGLK YGVKLYYKDR
DLVGNAVGHY VSYNGAANDI AWSSATIAKK GTHEGTPFID VKFTANDGDF HWVIFQGLAG
AYQYFVNRNL PTLGEFRTLW RLDNTTFPNG KTDLHDKPLP KLADYLPENK VQDETWRTPD
GTGYITKYDF SDFIRTQKYY GVYGDEVGSW YINAGKDYYN GNHLKQELMV HRESATGDAV
QLNMVHGTHF QVSAVDVFPV GKMWGPWLWY LNDGSKSDAE SRAASEFASW PYPWLDDAPY
QSRGTVKGKL LLSDGRPAAG AAVFLGDNHP NKTALDMGSD YYYTTYADAS GAFSIPHVRT
TAAGYALQAW SAGAALADVT THILFNDVHV TEADQTTDLG TLNWAVSKRT KLFQVGDFDR
TSLGFAHGGD PYFGHAIIAS CPENIVFRAS ASGSSSSNSS CSASKTSDWC YGQTYKGNYT
ISFRIPTLPN PVPTSANLIV SLAGYSTGAS SVVLANGQQI GNLTSGAVGV DSTSGLLNDP
SVYRSATAAG EWRLFEFPVP GALLKQGENE VTFQLTRNTT WRGFIWDSIV LEW
//
