ID   A0A0E0C6E0_9ORYZ        Unreviewed;      1463 AA.
AC   A0A0E0C6E0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=CHY-type domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI01G24940.3};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI01G24940.3}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI01G24940.3};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI01G24940.3}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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DR   EnsemblPlants; OMERI01G24940.3; OMERI01G24940.3; OMERI01G24940.
DR   Gramene; OMERI01G24940.3; OMERI01G24940.3; OMERI01G24940.
DR   Proteomes; UP000008021; Chromosome 1.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0098771; P:inorganic ion homeostasis; IEA:UniProt.
DR   GO; GO:0055080; P:monoatomic cation homeostasis; IEA:UniProt.
DR   CDD; cd12108; Hr-like; 3.
DR   CDD; cd16464; RING-H2_Pirh2-like; 1.
DR   Gene3D; 2.20.28.10; -; 1.
DR   Gene3D; 1.20.120.520; nmb1532 protein domain like; 3.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR012312; Hemerythrin-like.
DR   InterPro; IPR039512; RCHY1_zinc-ribbon.
DR   InterPro; IPR008913; Znf_CHY.
DR   InterPro; IPR037274; Znf_CHY_sf.
DR   InterPro; IPR017921; Znf_CTCHY.
DR   InterPro; IPR037275; Znf_CTCHY_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR21319:SF0; AND RING FINGER DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G08900)-RELATED; 1.
DR   PANTHER; PTHR21319; RING FINGER AND CHY ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF01814; Hemerythrin; 2.
DR   Pfam; PF05495; zf-CHY; 2.
DR   Pfam; PF14599; zinc_ribbon_6; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF161219; CHY zinc finger-like; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF161245; Zinc hairpin stack; 1.
DR   PROSITE; PS51266; ZF_CHY; 2.
DR   PROSITE; PS51270; ZF_CTCHY; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00601}.
FT   DOMAIN          954..1023
FT                   /note="CHY-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51266"
FT   DOMAIN          1210..1279
FT                   /note="CHY-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51266"
FT   DOMAIN          1282..1345
FT                   /note="CTCHY-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51270"
FT   DOMAIN          1346..1387
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          540..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..554
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1463 AA;  165469 MW;  0ECD14BCAA2952C0 CRC64;
     MATPTPMAGE GTLAAVMPRS PSPTASAAAG SAAEAPMLIF LYFHKAIRAE LEGLHAAAVR
     LATERAGDVG ALAERCRFFV NIYKHHCDAE DAVIFPALDI RVKNVAGTYS LEHKGENDLF
     SQLFALLQLD IQNDDSLRRE LASCTGAIQT CLSQHMSKEE EQVFPLLTKK FSYEEQADLV
     WQFLCNIPVN MMAEFLPWLS SSVSSDEHED IRCCLCKIVP EEKLLQQVVF AWIEGKTTRK
     VTENTTKPNS EATCDCKDAS SIDHADNHIS SHDDSKAGNK KYAESIDGQV ERHPIDEILY
     WHNAIRKELI DIAEETRRMQ QSGNFSDISS FNARLQFIAD VCIFHSIAED QVVFPAVDSE
     LSFVHEHAEE ERRFNNFRCL IQQIQIAGAK STALDFYSEL CSHADQIMET IEKHFCDEET
     KVLPQARMLF SPEKQRELLY KSLCVMPLKL LERVLPWLVS KLSDEEASSF LENMRLAAPS
     SETALVTLFS GWACKARSED KSNSGEYLCL TSGEMRCLLD EVDGLEKCRP FCPCASRSNT
     DASLHPQTEN GSRPGKRGND AESVPGTNGS DLSQTDDTEA RPCSKKPCCI PGLRVETGNL
     AISSSLASAK SFRSLSYNSS APSLYSSLFS WETDASLSCS DGISRPIDTI FKFHKAIRKD
     LEYLDVESGK LIDGDESCLR QFIGRFRLLW GLYRAHSNAE DEIVFPALES RETLHNVSHS
     YTLDHKQEEQ LFGDISDALA ELSQLHERLT HPHIEVSEAE KNDFNSSDEI DWTRKYNELA
     TKLQGMCKSI RAALSNHVHR EELELWPLFD EHFSVEEQDK LVGRIIGSTG AEVLQSMLPW
     VTSALTQEEQ NMMLDTWKQA TKNTIHLQDK IDQNDQMFKP GWKDIFRMNQ SELEAEVRKV
     SRDPTLDPRR KAYLIQNLMT SRWIAAQQKL PEPKSEECSE GAGIPGCAPS YRDQEKQIFG
     CEHYKRNCKL VAACCNKLFT CRFCHDKISD HTMERKATQE MMCMVCLKVQ PVGPNCQTPS
     CNGLSMAKYY CNICKFFDDE RHTLVVTTLV LSAANPWEIW RCTLACWTPC WLLKSFLRNT
     VIGVRIYFVM IVKEKGGLDF TGCTINAAPV VLIIPELSRP IQQIDKIDQN DQMFKPGWKD
     IFRMNQSELE AEVRKVSRDP TLDPRRKAYL IQNLMTSRWI AAQQKLPEPK SEECSEGAGI
     PGCAPSYRDQ EKQIFGCEHY KRNCKLVAAC CNKLFTCRFC HDKISDHTME RKATQEMMCM
     VCLKVQPVGP NCQTPSCNGL SMAKYYCNIC KFFDDERTVY HCPFCNLCRL GKGLGVDFFH
     CMKCNCCLGM KLTEHKCREK GLETNCPICC DFLFTSSAAV RALPCGHFMH SACFQAYTCS
     HYTCPICCKS LGDMAVYFGM LDALLAAEEL PEEYRDRCQD ILCNDCERKG RSRFHWLYHK
     CGSCGSYNTR VIKTDTADCS TPN
//