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Database: UniProt
Entry: A0A482WZ48_LAOST
LinkDB: A0A482WZ48_LAOST
Original site: A0A482WZ48_LAOST 
ID   A0A482WZ48_LAOST        Unreviewed;      1015 AA.
AC   A0A482WZ48;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=RHD domain-containing protein {ECO:0000259|PROSITE:PS50254};
GN   ORFNames=LSTR_LSTR006131 {ECO:0000313|EMBL:RZF38536.1};
OS   Laodelphax striatellus (Small brown planthopper) (Delphax striatella).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Fulgoroidea;
OC   Delphacidae; Criomorphinae; Laodelphax.
OX   NCBI_TaxID=195883 {ECO:0000313|EMBL:RZF38536.1, ECO:0000313|Proteomes:UP000291343};
RN   [1] {ECO:0000313|EMBL:RZF38536.1, ECO:0000313|Proteomes:UP000291343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lst14 {ECO:0000313|EMBL:RZF38536.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:RZF38536.1};
RX   PubMed=29136191; DOI=.1093/gigascience/gix109;
RA   Zhu J., Jiang F., Wang X., Yang P., Bao Y., Zhao W., Wang W., Lu H.,
RA   Wang Q., Cui N., Li J., Chen X., Luo L., Yu J., Kang L., Cui F.;
RT   "Genome sequence of the small brown planthopper, Laodelphax striatellus.";
RL   Gigascience 6:1-12(2017).
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:RZF38536.1}.
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DR   EMBL; QKKF02022243; RZF38536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A482WZ48; -.
DR   STRING; 195883.A0A482WZ48; -.
DR   InParanoid; A0A482WZ48; -.
DR   Proteomes; UP000291343; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:UniProt.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0010604; P:positive regulation of macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0051173; P:positive regulation of nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProt.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.40.340; Rel homology domain (RHD), DNA-binding domain; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_dom.
DR   InterPro; IPR008366; NFAT.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR   InterPro; IPR032397; RHD_dimer.
DR   InterPro; IPR011539; RHD_DNA_bind_dom.
DR   InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR   PANTHER; PTHR12533; NFAT; 1.
DR   PANTHER; PTHR12533:SF7; NFAT NUCLEAR FACTOR, ISOFORM B; 1.
DR   Pfam; PF16179; RHD_dimer; 1.
DR   Pfam; PF00554; RHD_DNA_bind; 1.
DR   SMART; SM00429; IPT; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49417; p53-like transcription factors; 1.
DR   PROSITE; PS50254; REL_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000291343}.
FT   DOMAIN          188..354
FT                   /note="RHD"
FT                   /evidence="ECO:0000259|PROSITE:PS50254"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..813
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        88..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1015 AA;  110486 MW;  6135371A1F5CDDC9 CRC64;
     MLLKYSQTQK RAKLSASGKP QRVTGMKLTS NTNMGPRVHR KMMKNITNRK LNNTHHRGGI
     GLKREMKSSV TPVDPCDNSN DSGLGFDHHS DYPIRNRPSG RFPNREKSCC SEDALRFKKH
     RMDFKVESDE DANDYFSFYE TVQQKTQGIH NFPRCLSGSR RLDEAVQPPP PPLTSQLSAV
     SSDGRVSLEI MSEPESQHRA RYQTEGSRGA VKDRTGTSFP VVRLNGYNKP TVLQVFIGTD
     EGDVAPHMFY QACRVAGKNS TPSVESMIER TVVIEMDIHP VNNMITVCDC VGILKERNVD
     VEHRFPEGSP PSKNSRKKST SVRMVFRTTV RLPDGSYETL QATSDTIACT QPQGVPEVSL
     MSWTSSPATG GVDLFIIGKN FVKDTKVVFY EGEGDKAWKV SVQPNKDFLH QSHLVCKVPA
     YSRTNITSPA RVRVAVESCG KSSESQPFAY TPVLGYLPCS PTAPSAPTTA MPEVGLMEAR
     STSSNFQQNQ RGEFHPVMYW SSSPLMSAQP LDPAAGLRRP DQPLPLSKCV CHKECIQMQL
     MQQSALMQPA TESKPVVKKE QTELPASGAG IFAELSTTQQ PSLATIRQFV SNQTSEHPLP
     SINVENYLSR LENPPATFVV PKQEQPSQTP LEISATSAPI DLSNQLVSVQ GAIKTEPSFG
     ELISTAPIAA TPLPIGGKRK FSNDTDNGVN MKMACLTFPP QTTTDSLLVT SSSNSLLTPS
     MQEMIDTRNI SSELSQPLVD LVGSSLAPTE ATDRLDDLVN SAAEKHMSSS STASSPPSIL
     SPIISPEKSP SLLSPRIQTN MSPNSSPLNL LPTPLEELST AHGMMMSSQP QGSGSDMLSS
     SMNVVGLNGQ LVSPIEKPYT STSPLLLQNM LPERKEDTKT DGGHLGLMRE MEINRISAGD
     CTMVSDPVVS TYANVPVPVS NLLQSNVQQA LIPLTIPNAA DNILPAVPLN KVAQPVSLLP
     MATEQAVRPL SANQSESAVK RPQVTNPLTG GIQELTQMSE NDLLSYINPS CFDQV
//
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