ID A0A0E0H7Z9_ORYNI Unreviewed; 1057 AA.
AC A0A0E0H7Z9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=FYVE-type domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA04G29540.1};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA04G29540.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA04G29540.1};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA04G29540.1}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA04G29540.1};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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DR AlphaFoldDB; A0A0E0H7Z9; -.
DR SMR; A0A0E0H7Z9; -.
DR STRING; 4536.A0A0E0H7Z9; -.
DR EnsemblPlants; ONIVA04G29540.1; ONIVA04G29540.1; ONIVA04G29540.
DR Gramene; ONIVA04G29540.1; ONIVA04G29540.1; ONIVA04G29540.
DR eggNOG; ENOG502QT6C; Eukaryota.
DR HOGENOM; CLU_005343_0_0_1; -.
DR OMA; FECGRDS; -.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00065; FYVE_like_SF; 1.
DR CDD; cd13365; PH_PLC_plant-like; 1.
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; IPR001849; PH_domain.
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; REGULATOR OF CHROMOSOME CONDENSATION; 1.
DR PANTHER; PTHR22870:SF91; REGULATOR OF CHROMOSOME CONDENSATION (RCC1) FAMILY WITH FYVE ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08381; BRX; 1.
DR Pfam; PF13713; BRX_N; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF16457; PH_12; 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; 3.
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:UP000006591};
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 280..331
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 332..386
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 387..438
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 448..499
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 500..551
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 552..603
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 608..670
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 989..1044
FT /note="BRX"
FT /evidence="ECO:0000259|PROSITE:PS51514"
FT REGION 679..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1057 AA; 115592 MW; 903E40F95FD23C48 CRC64;
MADPVDIDKA LIALKKGTQL LKYGRKGKPK FTPFRLSNDE STLIWVSNNK EKSLKLSSVS
RVLSGQRTLV FQRFLLPEKD HLSFSLIYND GKRSLDLICK DKVEAEVWFA GLNVLISPGQ
HGSQHQHIDG IRNGALSFEC GRDSSLSSSS AYTTDSFENK LSSANSAKDR SSGEFTYSER
TDVSDMQVKG ASSDIRISVS SALSTSSHGS GDDSESFGDV YVWGEVMCDT TCRQGSDSNA
YSATAATDIL VPKPLESNVM LDVSYVACGV KHAALVTRQA EVFTWGEECS GRLGHGAGTS
IFQPRLVESL SICNVETIAC GEFHTCAITA TGDLYTWGDG THNAGLLGHG SNVSHWIPKR
VSGPLEGLQV SAVSCGTWHT ALITSSGKLY TFGDGTFGVL GHGNRETISY PKEVESLKGL
RTISVSCGVW HTAAVVEVIM AQSNTSSGKL FTWGDGDKYR LGHGDRSSKL KPTCVPSLID
YNFHKAVCGH TLTIGLTTSG HIFTAGSSVY GQLGNPNNDG RYPRLVEEKL GGGGVVEVVC
GAYHVAVLTQ SGEVYTWGKG ANGRLGHGDI ADRKTPTFVE ALRDRSVKRI ACGSGFTAAI
CQHKSVSGME QSQCSSCRQP FGFTRKRHNC YNCGLVHCHS CSSKKALRAA LSPNPGKPYR
VCDSCYLKLS KVLDSGIGHN KNNTPRIPGD SKADKMDSKG NRVASANSSD MIKNLDVKAA
KQTKKYDYPP QFPAILQLKD IPFIGAADQQ PNDSTYSSPL LRLPNLNSSS SLSSESFDIL
RDANELLKQE VQKLKEEVNS LRQQREQQDA DLQKSEAKAH EAMTLASEEA SKSKAAKDVI
KSLTAQLKEM AERLPPASCD MKQTRQPYLP GGAVSPDTGR ENQKRYEPGS FQYPQTPTSV
ASARFNGFLA QAHQISEPNG NTMVPHDSRH ENNGNTKEFP VAQQMTNGGM TGYRPRTEDH
DRRETERFQI NLHGFNMRGS SSPSNQVEAE WIEQYEPGVY LTLVSLRDGT KELKRVRFSR
RRFGEHQAES WWNDNREKVY DKYNVRGTDR ISSVMTA
//
