ID A0A0E0JMW7_ORYPU Unreviewed; 970 AA.
AC A0A0E0JMW7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:OPUNC01G27640.5};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC01G27640.5}
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:OPUNC01G27640.5}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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DR AlphaFoldDB; A0A0E0JMW7; -.
DR EnsemblPlants; OPUNC01G27640.5; OPUNC01G27640.5; OPUNC01G27640.
DR Gramene; OPUNC01G27640.5; OPUNC01G27640.5; 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; 2.
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; SSF50729; PH domain-like; 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 213..264
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 265..319
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 320..371
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 382..433
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 434..485
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 486..537
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 542..604
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 893..948
FT /note="BRX"
FT /evidence="ECO:0000259|PROSITE:PS51514"
FT REGION 612..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 106678 MW; B9030F2B370E9266 CRC64;
MFNILKALIT LKKGTKLIKY SWRGKPKIRA FRLSSISHKP QDETSLIWYS HKKEKFLRLS
SVTKIIPGQR TEVIYYQDHR SYDSTLDIAS NISRSFNSAG YCGTNSFSFR KSDVGFDRPN
MIRTSAADSS RVSISSALSS YSQGSGTDDI ESLGDVYVWG EVWTDVTPSD GHTSSSCSKV
DVLIPKPLES DVVLDVNQIA CGSRHVALTT RQGEVFTWGE EFGGRLGHGS DADISRPKLV
ESLSLTVVDF ISCGEFHTCA VTTSGDLFNW GDGSYNVGLL GCGTEASYWL PKKVSGPLEG
LQVLSVACGS WHSALTTSSG KLYTFGDGTF GVLGHGDRET LAYPKEVEAL SGFKTIKVAC
GIWHSAAIVE VTNQTGANVL SKKLYTWGDG DKNRLGHGDK EPRLVPKCVQ ALLEYNFHQL
ACGHNMTVAL ATSGRVFTMG SSSNGQLGNP KSDGKQPCLV QDRLAGELVE EISCGASHVT
VLTSRSEVYT WGMGANGRLG HGDLKDRKKP CLVEALKDRH VKSISCGSNF TTCICIHKWV
SGADQSVCTG CRQAFGFTRK RHDCYNCGLV HCHACSSRKV LKAALAPTPG KPHRVCDSCF
LKLKATEIGS NNSNRRNAVT RRSIDGREKL ERPEIRPSRT TAPAESIKYT EVKAARNDMR
ASQISSLLQF KDLSFSVLQP VAMSPALTAS PALSTPSPYT KKTKSPAPAI PQFPKTDIDN
LQKSNELLNQ EILKQKCEAQ HEQLQISDKK TKTVVSMATE ESTRCNTVVE FVKFLDNELN
GIVHELPSDA AESLKALQNQ VQALLREQRS HPSELLNPME HDGIQLSSGG NAIHDFSNHR
SGSTRYLFMS QDASSASGSA ISLTSEPPSH RVMEHHAKVH NNFVPKHDTQ GEVQLIEQFE
PGVYVTLIQL KDGSKVFKRV RFSKKRFAEN QAEEWWRENQ ERVFKKYNHP SVPQTTSANT
GSSNEEEHHS
//
