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
//