ID U5D4V2_AMBTC Unreviewed; 1093 AA.
AC U5D4V2;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=FYVE-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMTR_s00059p00031410 {ECO:0000313|EMBL:ERN17469.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN17469.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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DR EMBL; KI392312; ERN17469.1; -; Genomic_DNA.
DR RefSeq; XP_006856002.1; XM_006855940.1.
DR AlphaFoldDB; U5D4V2; -.
DR STRING; 13333.U5D4V2; -.
DR EnsemblPlants; ERN17469; ERN17469; AMTR_s00059p00031410.
DR GeneID; 18445808; -.
DR Gramene; ERN17469; ERN17469; AMTR_s00059p00031410.
DR KEGG; atr:18445808; -.
DR eggNOG; ENOG502QVGP; Eukaryota.
DR HOGENOM; CLU_005343_0_0_1; -.
DR OMA; YELICAD; -.
DR OrthoDB; 551430at2759; -.
DR Proteomes; UP000017836; 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; 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; 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:SF352; 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; 2.
DR PROSITE; PS50012; RCC1_3; 7.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836};
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 235..296
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 297..348
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 349..403
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 404..455
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 467..518
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 519..570
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 571..622
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 627..689
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1036..1091
FT /note="BRX"
FT /evidence="ECO:0000259|PROSITE:PS51514"
FT REGION 125..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 819..853
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 126..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1093 AA; 119136 MW; 744E1C6C9723C074 CRC64;
MADLASYGAE RDIEQAVTAL KKGTHLIKYG RKGKPKFCPF RLSADETSLV WYSHGEERHL
KLETVSKIIP GQRTAVFRRY LRPEKDYLSF SLLYNNGERT LDLICKDQVE TDVWVTGLKA
LISTGQRRRN KTDAHSEGLY SDEGGDLNQN SPIHRAFGAT LGINSSSTHR NLNTKAIIDF
YSREPSFTAA RSDVGTDRSN MLLRGGTGDN LRHSVSSAPS SSSQGSGPDD IESLGDVYVW
GEVWCDGSLK NGVDGAPNSG CSKADVLLPK PLECNVVLDV HHIACGVRHA ALVTRQGEVF
TWGEESGGRL GHGIDADSSQ PQLVESLALC NADFVACGEY HTCAVTVTGE LYTWGDGTHN
AGLLGHGNDV SHWIPKRVFG PLEGLQVTSV ACGPWHSALA TSTGQLFTFG DGTFGVLGHG
ERESVAYPRE VESLKGLKTS KVACGVWHTA AIVEVIVAQS GANVLSRKLF TWGDGDKNRL
GQGDKDPRLV PTCVPSLIEY NFHQLACGHD LTIGLTTSGH VFTMGSTVYG QLGNPQSDGK
LPCLVQDRLV GELVEEIACG SYHVAVLTSR SELFTWGKGA NGRLGHGDVE DRKTPTLVEA
LKDRHVKSIT CGSNFTATIC LHKWVSGTDQ SLCTGCRQAF GFTRKRHNCY NCGLVHCHAC
SSKKALRAAL APNPGKPHRV CDTCYSKLKK ASEASSSFSV DRKTNIFRRS IDQKDRTDRG
EVKSSKIILP RSFEPAKSLE VKSIKSGKKP DSLSLIRTSP IPSLLQLKDL SFSIGVNSPV
AKSTASPIQQ PVIIPRSASP LRRPSPPRSV TPFPTIGGLS ASKNTAEGLK KKNELLNQEV
SKLQAQVKTL KLQIEVRDEK MQKSVREAQA LAAEETTKCN AAKEVIKSLI SQLKDLAEKL
PPGIYDTSNL CTLMDLPNGD ILGGNHEPAT PDAIHGESSE GRPSVDSSSP MAVDSIELYQ
QNLIDNPMEN NEERNENQHL DDNQDQKMDE SSEIVTNDTD PIPPNGGEGE IASSATPADS
EDKETEAQGS KVKDSTQKTE QFEPGVYITF VLSEDGTKIF KRVRFSKKRF AERQAEVWWS
ANHNRVFEKY KTR
//
