ID A0A0K6FYF3_9AGAM Unreviewed; 460 AA.
AC A0A0K6FYF3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN ORFNames=RSOLAG22IIIB_09294 {ECO:0000313|EMBL:CUA71007.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA71007.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA71007.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA71007.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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}.
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DR EMBL; CYGV01001211; CUA71007.1; -; Genomic_DNA.
DR Proteomes; UP000044841; 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; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
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 InterPro; IPR016590; Rhamnogalacturonase_B.
DR InterPro; IPR015364; RhgB_N.
DR PANTHER; PTHR36574; RHAMNOGALACTURONATE LYASE-RELATED; 1.
DR PANTHER; PTHR36574:SF1; RHAMNOGALACTURONATE LYASE-RELATED; 1.
DR Pfam; PF14683; CBM-like; 2.
DR Pfam; PF14686; fn3_3; 1.
DR Pfam; PF09284; RhgB_N; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000044841};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..460
FT /note="rhamnogalacturonan endolyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005502313"
FT DOMAIN 24..269
FT /note="Rhamnogalacturonase B N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09284"
FT DOMAIN 276..351
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 364..391
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
FT DOMAIN 406..459
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 460 AA; 49378 MW; 32179615AC790987 CRC64;
MLRHTLLSAS LLLTSFIAPA FAGFGVKENG NLFEVDTDAG LIFSVDKRNG DITSMLFNGI
QAQDQSKRSH IASGLGTAPC SWTKIGNYIK ITCTTSTLTQ YYVAQYKNPG IHMATYITAE
PSVGELRFIA RLNAKTIPNG YTAATVAGSS STVEGSDVFV VSGQTRSKFY SSRQFIDDQV
HGATGPGIGA YMIIPGTGYE SASGGPFFRD INNQNGGQQE VYYYMNSGHA QTEAYRMGLH
GPYLLQFTTG GVPSANINLA FWDGLGIQGY VPVSKRGYVK GKASGVPSNY AGLVVVGWSN
SAAQYWARAD ASTGNYYSPA MKPGTYTMTM YKGELAVATS SVTISAGQTG TANIQSAEAN
PTAIWQIGDF DGTPRGFLNA DMIETMHPSD KRMHEWLXXX XXXXXXSGTW RGNNTRYTVN
IPSGVLKSNE VNVMTINVIS GSSGDVYLSP NVVIDAVRLY
//
