ID   A0A0E0M9E7_ORYPU        Unreviewed;       787 AA.
AC   A0A0E0M9E7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=LIM zinc-binding domain-containing protein {ECO:0000259|PROSITE:PS50023};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC10G13430.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC10G13430.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC10G13430.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00008276}.
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DR   AlphaFoldDB; A0A0E0M9E7; -.
DR   EnsemblPlants; OPUNC10G13430.1; OPUNC10G13430.1; OPUNC10G13430.
DR   Gramene; OPUNC10G13430.1; OPUNC10G13430.1; OPUNC10G13430.
DR   HOGENOM; CLU_015869_0_2_1; -.
DR   Proteomes; UP000026962; Chromosome 10.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd09440; LIM1_SF3; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   InterPro; IPR001645; Folylpolyglutamate_synth.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR001781; Znf_LIM.
DR   NCBIfam; TIGR01499; folC; 1.
DR   PANTHER; PTHR11136:SF6; FOLYLPOLYGLUTAMATE SYNTHASE; 1.
DR   PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 1.
DR   Pfam; PF00412; LIM; 2.
DR   SMART; SM00132; LIM; 2.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 4.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE   3: Inferred from homology;
KW   LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          572..632
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          666..726
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   REGION          755..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..787
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   787 AA;  86587 MW;  FB168B597DA2ABBC CRC64;
     MRASGGASPP PSAFTTTTLL VPSSSTVAMP PPRLAHLRRS SLLLLHHHRG GGGGSAPPLP
     LGRHPLLRPP PPPFQLLTPR FAMASVAQPG VAAGSAEYEE VLGCISSLIT QKVRADTGNR
     GNQWELMAKY LQILELEEPI ARLKVVHVAG TKGKGSTCTF AESILRSCGF RTGLFTSPHL
     MDVRERFRLN GLDISEEKFI RYFWWCWNKL KDRTGGDIPM PAYFRFLALL AFKIFSDEQV
     DVAVLEVGLG GKYDATNVVK APVVCGISSL GYDHMEILGN TLGEIAGEKA GILKKGVPAY
     TVPQPEEAMS VLKHRASELG VPLQVVQPLD PQQLDDQPLG LHGEHQYMNA GLAVALVNTW
     LQKQGHFNIL HKKHSVTLPD QFIKGLSSAC LLGRAQIVPD PEVLSKDSSS LIFYLDGAHS
     PESMEICARW FSCVTRKDEK QPGSLDQPHI GTYSRKILLF NCMSVRDPQR LLPCLLVTCA
     QNGFQFDHAL FVPNQSQYNK LGSHASPPSE RVQIDLSWQL SLQRVWEGLL HSNKGLNGSK
     SSTASSVFES LPLAIKWLRE TAQQNQSTSY QDKCNACDKT VHFIDLLTAD SIPYHKSCFR
     CSHCKGTLSM CSYSSMDGVL YCKTHFEQLF KETGTFKKNF PSGAKANSEQ PKIPSKLSSL
     FCGTQDKCTA CKKTVYPLEK MTLEGEAYHR TCFKCAHGGC LLTNASYAAH NGILYCQNHF
     WQLFKKTGSY DNLLKPASAA ENTVESEVAV AVAEPAKEEP EMEEVAKEEE ASPEQVAEAV
     VEDQEHS
//