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Database: UniProt
Entry: A0A061FEM7_THECC
LinkDB: A0A061FEM7_THECC
Original site: A0A061FEM7_THECC 
ID   A0A061FEM7_THECC        Unreviewed;       645 AA.
AC   A0A061FEM7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE            EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN   ORFNames=TCM_046891 {ECO:0000313|EMBL:EOY15516.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY15516.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY15516.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
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; CM001886; EOY15516.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061FEM7; -.
DR   STRING; 3641.A0A061FEM7; -.
DR   EnsemblPlants; EOY15516; EOY15516; TCM_046891.
DR   Gramene; EOY15516; EOY15516; TCM_046891.
DR   eggNOG; ENOG502QQM5; Eukaryota.
DR   HOGENOM; CLU_015099_1_0_1; -.
DR   InParanoid; A0A061FEM7; -.
DR   OMA; DCAANET; -.
DR   Proteomes; UP000026915; Chromosome 8.
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: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   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, ECO:0000313|EMBL:EOY15516.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          359..424
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14686"
FT   DOMAIN          445..633
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14683"
SQ   SEQUENCE   645 AA;  73878 MW;  AD8605350017E584 CRC64;
     MSSRGVQLDV QDKYVVMDND ILQVTISNPG GIVTGLQYNG IDNLLAVEND ETDRGYWDLV
     WNLAGRKGTK GKFDRIEATS FNVIVENEEQ VELSFTRMWD SSLEGRVVPL NIDKRFVMLR
     NSSGFYTYAI YEHLEEWPAF ILDRFRVAFK LRKDKFHYMA MADNRQRCMP LPDDRLPYRS
     QTLAYPEAVL LVDPLEPEFR GEVDDKYQYS CENKDNRVHG WICTDPPVPV GFWQITPSDE
     FRSAGPLKQN LTSHVGPTTL AVMHSVHYSG EDLLLKFGTN EPWKKVFGPI FIYLNSLSNG
     GDPLSLWEDA KEQMTIEVQG WPYTFPVSED FPQSDQRGNV SGRLLVKDRY VHDDNIPANG
     AYVGLAPPGD VGSWQREVKG YQFWTKTDED GYFCINNIRT GDYNLYAWVP GFIGDYRYNV
     IITPTAGYDI YMGDLVYEPP RDGPTLWEIG IPDRTAAEFY VPDPSPVYIN KLYVNHQDRF
     RQYGLWERYA ELYPDGDLVY TVGVSDYTKD WFFAQVTRKK DDNTYQGTTW QIKFKLDCVD
     ESGTYKLRLA LASAHASELQ VRVNDPDAIS PLFSSGQIGK DNTIARHGIH GLYWLYNVDI
     PGNLLHEGDN TIFLTQSKST SPFQGIMYDY IRLEGPPSSD ANKRP
//
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