ID   A0A1D6PTF4_MAIZE        Unreviewed;       711 AA.
AC   A0A1D6PTF4;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE            EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN   ORFNames=ZEAMMB73_Zm00001d049251 {ECO:0000313|EMBL:AQK49938.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK49938.1};
RN   [1] {ECO:0000313|EMBL:AQK49938.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK49938.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM000780; AQK49938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6PTF4; -.
DR   ExpressionAtlas; A0A1D6PTF4; baseline and differential.
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:SF32; 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; 2.
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:AQK49938.1};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          402..473
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14686"
FT   DOMAIN          488..680
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14683"
SQ   SEQUENCE   711 AA;  78585 MW;  8E511E9C1089DE6C CRC64;
     MDEVHRSALA AARRRRYVSW YPLASHSHMA AAAQARSSFL VLLVATWSLS PRLAGASTST
     EAAAAGRGVT LRLDASQVVV DNGAVQVALS APEGRITGVS YSGDGETTNL LGLDSTEFNV
     VSSSEDQVEL SFRSTYNPSH RNSLRLNIDK RCQNPSHGWF RLVMLRGSSG FYCYAIFEHD
     RAYPALNITE ARLVFKLNTA KFNYMAITDD IQRYMPSAAD REEPRAVPLA YKEAVLLVDP
     KEPQFRGEVD DKYQYSLDNK DNVVHGWISR GDPNAVGFWV ITPSNEFKSG GPLKRELTSH
     VGPTSLTMFM GTHYVGKYMV ANINDGEAWK KVLGPVFIYL NSGPSRGELW EDAKARARAE
     AASWPYSFLA SPEFPKAAER GSVVGRLLVR DSHEKHGMPA GSSAFVGLAS PGPPGSWATE
     SKGYQFWTRA APDGTFRIAN VREGVYGLYA FVPGFLGDYC YGSPLTVAPG RAIGVGDLVF
     EPPRSGPTVW EIGVPDRTAA EFYVPDPDPR YVNRLFVVRD RYRQYGLWER YADLYPDKDL
     VFTVGESDES KDWFFAHVTR KVGQVAVPTT WQIRFSLDRV VADDDTYTLR ISLAASQMCR
     LQVQVNGDAR RGRDFTTPDM GDDNAITRHG IHGSQWSLEC VVGGHLLRQG DNTIDIKLIA
     QQGPKGPAMV AGVMYDYIRL EGPPSRGVAS SRIPAFSLHR ILFLLAFLVM S
//