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Database: UniProt
Entry: M5BPZ3_THACB
LinkDB: M5BPZ3_THACB
Original site: M5BPZ3_THACB 
ID   M5BPZ3_THACB            Unreviewed;       514 AA.
AC   M5BPZ3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE            EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN   ORFNames=BN14_03160 {ECO:0000313|EMBL:CCO29156.1}, RSOLAG1IB_04888
GN   {ECO:0000313|EMBL:CEL62532.1};
OS   Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS   rot fungus) (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO29156.1, ECO:0000313|Proteomes:UP000012065};
RN   [1] {ECO:0000313|EMBL:CCO29156.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Isolate 7/3/14 {ECO:0000313|EMBL:CCO29156.1};
RA   Jelonek L.;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCO29156.1, ECO:0000313|Proteomes:UP000012065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065},
RC   and Isolate 7/3/14 {ECO:0000313|EMBL:CCO29156.1};
RX   PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA   Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA   Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA   Schlueter A.S.;
RT   "Establishment and interpretation of the genome sequence of the
RT   phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL   J. Biotechnol. 0:0-0(2013).
RN   [3] {ECO:0000313|EMBL:CEL62532.1, ECO:0000313|Proteomes:UP000059188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL62532.1};
RA   Wibberg Daniel;
RL   Submitted (NOV-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}.
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DR   EMBL; CAOJ01004361; CCO29156.1; -; Genomic_DNA.
DR   EMBL; LN679106; CEL62532.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5BPZ3; -.
DR   STRING; 1108050.M5BPZ3; -.
DR   HOGENOM; CLU_016624_0_0_1; -.
DR   Proteomes; UP000012065; Unassembled WGS sequence.
DR   Proteomes; UP000059188; 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; 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:SF9; RHAMNOGALACTURONATE LYASE B; 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:CCO29156.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059188};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          312..386
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14686"
FT   DOMAIN          399..512
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14683"
SQ   SEQUENCE   514 AA;  57161 MW;  689B04C2595FC71C CRC64;
     MLKSSGNIVS LSLDGRNLLG TGKGLYLDCY CTPAGFYTPG SSNAKVKSLN GTDATGTSWG
     GLVLQDTYPT TGQLFEQYWF LRDGEAGLHS FSRVAYYNET TPFLRDLGEL RTLFRPTSNL
     WTHISTNRQH WAPLPSAEAT GKQVVVQDAT WYLGNTPNDT YVQQEADYFT KYTFADTWRD
     HKAHGLYADG STSNGTTYGA WLVMNTRDTY FGGPIHSDLT VDGITYNYIV SNHHGDTAPN
     ITHGFDRTFG PFFYYFNSGK NASLDALRDD AEKYADPEWN AAFYDSIASS VPNYVTTSRR
     GTFSLSVSIP AEAERTIAIL SVDGLDPQDN AQDTTAYQYW GDVSNSGSLT IPRVKEGTYR
     LTIYADGIFG QYEEDGIVIA AGKDTKHEVK WIPESAGKEL WRIGTPDKTA GEFRHGFARD
     PSRPLHPQEY RIYWGQWDFP TDFPNGINYT IGKSDASKDW NYVHWSVFGP SYTRAEAVST
     NMNNWTINFE HANATGADST GTLTIQLAGA KSSR
//
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