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Database: UniProt
Entry: A0A9W7HEJ7_HIBTR
LinkDB: A0A9W7HEJ7_HIBTR
Original site: A0A9W7HEJ7_HIBTR 
ID   A0A9W7HEJ7_HIBTR        Unreviewed;      1074 AA.
AC   A0A9W7HEJ7;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   28-JAN-2026, entry version 9.
DE   SubName: Full=NF-X-like 1 {ECO:0000313|EMBL:GMI75443.1};
GN   ORFNames=HRI_001213600 {ECO:0000313|EMBL:GMI75443.1};
OS   Hibiscus trionum (Flower of an hour).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Hibiscus.
OX   NCBI_TaxID=183268 {ECO:0000313|EMBL:GMI75443.1, ECO:0000313|Proteomes:UP001165190};
RN   [1] {ECO:0000313|EMBL:GMI75443.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hamamatsu line {ECO:0000313|EMBL:GMI75443.1};
RA   Koshimizu S., Masuda S., Ishii T., Shirasu K., Hoshino A., Arita M.;
RT   "Genome and transcriptome analyses reveal genes involved in the formation
RT   of fine ridges on petal epidermal cells in Hibiscus trionum.";
RL   Submitted (MAY-2023) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the NFX1 family.
CC       {ECO:0000256|ARBA:ARBA00007269}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GMI75443.1}.
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DR   EMBL; BSYR01000011; GMI75443.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9W7HEJ7; -.
DR   OrthoDB; 6512771at2759; -.
DR   Proteomes; UP001165190; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:TreeGrafter.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   CDD; cd06008; NF-X1-zinc-finger; 7.
DR   CDD; cd16492; RING-CH-C4HC3_NFX1-like; 1.
DR   InterPro; IPR034078; NFX1_fam.
DR   InterPro; IPR056234; RRM_NFXL1.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR000967; Znf_NFX1.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR12360; NUCLEAR TRANSCRIPTION FACTOR, X-BOX BINDING 1 NFX1; 1.
DR   PANTHER; PTHR12360:SF12; TRANSCRIPTIONAL REPRESSOR NF-X1; 1.
DR   Pfam; PF24435; RRM_NFXL1; 1.
DR   Pfam; PF01422; zf-NF-X1; 8.
DR   SMART; SM00438; ZnF_NFX; 9.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP001165190};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          104..165
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          107..163
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          972..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1013..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..43
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1026
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1050
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1074 AA;  116488 MW;  A142510855A084F2 CRC64;
     MSFQGRNRPR NPSQSTRREW VPRGSSSATT SVESSSPAAS NSTPDVNQAS TRSDNMHRQA
     GRPTNHRRDR QKERSENHVA VRKEIDPNLP QLVQEIQDKL ITSTVECMIC YDMVRRSGAI
     WSCSSCYSIF HLNCIKKWAR APTSVDLVAE KNQGFNWRCP GCQSVQFTSS KEIRYVCFCG
     KRTDPPTDLY LTPHSCGEPC GKQLEKELGL GSGVMKDELC PHVCVLQCHP GPCPPCKAFA
     PPRLCPCGKK VITTRCFDRK SVLTCGQRCD KLLECERHRC ERICHVGSCD PCKVPINAPC
     FCKKKVEVVI CGDMVVKGEV KAEGGIISCN STCGKKLRCG NHYCAEICHP GPCGDCEFMP
     SKIKSCYCGK TSLQDQRQSC LDPIPVCSEI CAKFLPCQVH QCDQVCHAGS CPPCLILVTQ
     KCLCGSTSRK VECYKTTLEN ERFTCDKPCG CKKNCGRHRC SERCCPLSNS NNLRSGNWDP
     HFCQMACGKK LRCGQHSCES LCHSGHCPPC LETIFTDLTC ACGRTSIPPP LPCGTPPPSC
     QLPCSVPQAC GHSSSHSCHF GDCPPCSVPV AKECIGGHVV LGNIPCGSKD IRCNKLCGKT
     RQCGLHACGR TCHPAPCDAS SGAEQSFRAS CGQTCGAPRR DCRHTCTAPC HPNAPCPDVR
     CDFRVTITCS CSRLSATVPC NAGGFNADTV FEASVIQKLP APLQPVDSTG KRIPLGQRKL
     MCDDECAKLE RKRVLANAFD ITPPNLDALH FGENSVTSEL IFDLYRRDPK WVLAVEERCK
     FLVLGKNRGA TGLKVHVFCP VLKDKRDAVR IIAERWKLAI SAAGWEPKRF IVVHDTPKSK
     PPARIIGGKG STGTGTVHPP VFDPLVDMDP RLVVSFLDLP READISALVL RFGGECELVW
     LNDKNALAVF SDPARAATAM RRLDHGSIYT GAATFVQSGG ASAANIAWGG TGPSAAVKAN
     PWKKAVVQEL GWGEHPRGGD EPLGGTSDPG SAWKDKVTPI PASINRWSVL DSETSVSSSS
     GAVPSEDPSK LADVQSMPTM DSNAANSNSA GFMGGGLNET EPSEVVDDWE KAYE
//
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