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Database: UniProt
Entry: A0A0E0JMX1_ORYPU
LinkDB: A0A0E0JMX1_ORYPU
Original site: A0A0E0JMX1_ORYPU 
ID   A0A0E0JMX1_ORYPU        Unreviewed;       963 AA.
AC   A0A0E0JMX1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=FYVE-type domain-containing protein {ECO:0008006|Google:ProtNLM};
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:OPUNC01G27640.9};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC01G27640.9}
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:OPUNC01G27640.9}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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DR   AlphaFoldDB; A0A0E0JMX1; -.
DR   EnsemblPlants; OPUNC01G27640.9; OPUNC01G27640.9; OPUNC01G27640.
DR   Gramene; OPUNC01G27640.9; OPUNC01G27640.9; OPUNC01G27640.
DR   Proteomes; UP000026962; Chromosome 1.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 3.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR013591; Brevis_radix_dom.
DR   InterPro; IPR027988; BRX_N.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22870:SF456; OS01G0700200 PROTEIN; 1.
DR   PANTHER; PTHR22870; REGULATOR OF CHROMOSOME CONDENSATION; 1.
DR   Pfam; PF08381; BRX; 1.
DR   Pfam; PF13713; BRX_N; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00415; RCC1; 6.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   PROSITE; PS51514; BRX; 1.
DR   PROSITE; PS00626; RCC1_2; 1.
DR   PROSITE; PS50012; RCC1_3; 6.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   REPEAT          206..257
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          258..312
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          313..364
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          375..426
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          427..478
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          479..530
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   DOMAIN          535..597
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          886..941
FT                   /note="BRX"
FT                   /evidence="ECO:0000259|PROSITE:PS51514"
FT   REGION          605..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          939..963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..631
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        942..956
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   963 AA;  105853 MW;  747D27ECD33AD57F CRC64;
     MESKSPSTKL IKYSWRGKPK IRAFRLSSIS HKPQDETSLI WYSHKKEKFL RLSSVTKIIP
     GQRTEVIYYQ DHRSYDSTLD IASNISRSFN SAGYCGTNSF SFRKSDVGFD RPNMIRTSAA
     DSSRVSISSA LSSYSQGSGT DDIESLGDVY VWGEVWTDVT PSDGHTSSSC SKVDVLIPKP
     LESDVVLDVN QIACGSRHVA LTTRQGEVFT WGEEFGGRLG HGSDADISRP KLVESLSLTV
     VDFISCGEFH TCAVTTSGDL FNWGDGSYNV GLLGCGTEAS YWLPKKVSGP LEGLQVLSVA
     CGSWHSALTT SSGKLYTFGD GTFGVLGHGD RETLAYPKEV EALSGFKTIK VACGIWHSAA
     IVEVTNQTGA NVLSKKLYTW GDGDKNRLGH GDKEPRLVPK CVQALLEYNF HQLACGHNMT
     VALATSGRVF TMGSSSNGQL GNPKSDGKQP CLVQDRLAGE LVEEISCGAS HVTVLTSRSE
     VYTWGMGANG RLGHGDLKDR KKPCLVEALK DRHVKSISCG SNFTTCICIH KWVSGADQSV
     CTGCRQAFGF TRKRHDCYNC GLVHCHACSS RKVLKAALAP TPGKPHRVCD SCFLKLKATE
     IGSNNSNRRN AVTRRSIDGR EKLERPEIRP SRTTAPAESI KYTEVKAARN DMRASQISSL
     LQFKDLSFSV LQPVAMSPAL TASPALSTPS PYTKKTKSPA PAIPQFPKTD IDNLQKSNEL
     LNQEILKQKC EAQHEQLQIS DKKTKTVVSM ATEESTRCNT VVEFVKFLDN ELNGIVHELP
     SDAAESLKAL QNQVQALLRE QRSHPSELLN PMEHDGIQLS SGGNAIHDFS NHRSGSTRYL
     FMSQDASSAS GSAISLTSEP PSHRVMEHHA KVHNNFVPKH DTQGEVQLIE QFEPGVYVTL
     IQLKDGSKVF KRVRFSKKRF AENQAEEWWR ENQERVFKKY NHPSVPQTTS ANTGSSNEEE
     HHS
//
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