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Database: UniProt
Entry: A0A0D2US84_GOSRA
LinkDB: A0A0D2US84_GOSRA
Original site: A0A0D2US84_GOSRA 
ID   A0A0D2US84_GOSRA        Unreviewed;       639 AA.
AC   A0A0D2US84;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE            EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN   ORFNames=B456_009G227800 {ECO:0000313|EMBL:KJB58820.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB58820.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB58820.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
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; CM001748; KJB58820.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2US84; -.
DR   STRING; 29730.A0A0D2US84; -.
DR   EnsemblPlants; KJB58820; KJB58820; B456_009G227800.
DR   Gramene; KJB58820; KJB58820; B456_009G227800.
DR   eggNOG; ENOG502QQ8E; Eukaryota.
DR   Proteomes; UP000032304; Chromosome 9.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   CDD; cd10317; RGL4_C; 1.
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   InterPro; IPR010325; Rhamnogal_lyase.
DR   PANTHER; PTHR32018:SF16; RHAMNOGALACTURONAN ENDOLYASE; 1.
DR   PANTHER; PTHR32018; RHAMNOGALACTURONATE LYASE FAMILY PROTEIN; 1.
DR   Pfam; PF14683; CBM-like; 1.
DR   Pfam; PF14686; fn3_3; 1.
DR   Pfam; PF06045; Rhamnogal_lyase; 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   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          357..429
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14686"
FT   DOMAIN          443..631
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14683"
SQ   SEQUENCE   639 AA;  73004 MW;  0FD3341CD8E6BB9C CRC64;
     MSSPGVQLYI QDHYVLMDNG IIQVTISSPD GIVTGIQYNG IDNLLEVEDE EVHRGYWDLV
     WSKTGSTGTT GTFDVFKGTS FKVVVETEDQ VEVSFTRTWD ISLEGDVVPL NLDKRFIMLR
     NSPGFYSYAV FEHLEEWPPF NLPQVRIVFK LRKDKFHYMA VADNRQRFMP LPEDRLLDRG
     QPLATPEAVL LVNPVEPEFK GEVDDKYQYS SENKDLKVHG WISLNPPVGF WQITPSSEFR
     SGGPIKQNLT SHVGPYCLAM FLSAHYAGED LVLKLNPGEP WKKVFGPVFL YLNSVSSEDN
     AFSLWEDAKD QMLRETQNWP YSFPASEDFP KPDQRGKVCG RLEVQDRYVS YEPIPANGAY
     IGMAPLGDVG SWQRECKGYQ FWTRADEDGN FTIDKIRTGE YNICAWVPGF IGDYKYDVVV
     NITEGCDISL GDLIYEPLRN GPTLWEIGIP DRTAAEFYIP DPDPKYINKL YVNHPDRYRQ
     YGLWERYADL YPDGDLVFTV GISDYKNDWF FAQVNRKRED GTYQGTTWQI KFLLRDVDHT
     GTYTLRLALA TAHLAELQVR VNDPKSDPPL FTTGEIGHDN TIARHGIHGL YRLYNIDVAG
     VELVEGENII FLTQAMNTDP LQGIMYDYIR LECPPTTSS
//
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