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Database: UniProt
Entry: H3BEV9_LATCH
LinkDB: H3BEV9_LATCH
Original site: H3BEV9_LATCH 
ID   H3BEV9_LATCH            Unreviewed;      1452 AA.
AC   H3BEV9;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Nuclear receptor coactivator {ECO:0000256|PIRNR:PIRNR038181};
GN   Name=NCOA1 {ECO:0000313|Ensembl:ENSLACP00000020430.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000020430.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000020430.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR038181}.
CC   -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC       family. {ECO:0000256|ARBA:ARBA00009933, ECO:0000256|PIRNR:PIRNR038181}.
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DR   EMBL; AFYH01030894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01030895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01030896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01030897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01030898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01030899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01030900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01030901; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01030902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01030903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7897.ENSLACP00000020430; -.
DR   Ensembl; ENSLACT00000020570.1; ENSLACP00000020430.1; ENSLACG00000017956.1.
DR   eggNOG; KOG3561; Eukaryota.
DR   GeneTree; ENSGT00950000183021; -.
DR   HOGENOM; CLU_001988_0_0_1; -.
DR   InParanoid; H3BEV9; -.
DR   OMA; AQHVNIG; -.
DR   TreeFam; TF332652; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016922; F:nuclear receptor binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd18948; bHLH-PAS_NCoA1_SRC1; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 6.10.140.410; -; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR010011; NCO_DUF1518.
DR   InterPro; IPR028819; NCOA1_bHLH.
DR   InterPro; IPR009110; Nuc_rcpt_coact.
DR   InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
DR   InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf.
DR   InterPro; IPR017426; Nuclear_rcpt_coactivator.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR014935; SRC/p160_LXXLL.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR10684; NUCLEAR RECEPTOR COACTIVATOR; 1.
DR   PANTHER; PTHR10684:SF1; NUCLEAR RECEPTOR COACTIVATOR 1; 1.
DR   Pfam; PF07469; DUF1518; 2.
DR   Pfam; PF16665; NCOA_u2; 1.
DR   Pfam; PF08815; Nuc_rec_co-act; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF14598; PAS_11; 1.
DR   Pfam; PF08832; SRC-1; 1.
DR   PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 2.
DR   SMART; SM01151; DUF1518; 2.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|PIRNR:PIRNR038181};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR038181};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR038181};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PIRNR:PIRNR038181}.
FT   DOMAIN          23..80
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   DOMAIN          109..180
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          764..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          831..861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1250..1331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1424..1452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1261..1287
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1288..1314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1426..1452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1452 AA;  155769 MW;  83932C37C433279C CRC64;
     MSGLGDSLSD PTNPDLRKRK GSPCDALGQS MEKRRREQEN RYIEELAELL SANIGDIDSL
     SVKPDKCRIL KKTVDQIQQI KRLGQGKTTA DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL
     DGFFFVVNRE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHNEFVR NLLPKSLVNG
     VPWPKEAGRR NSHTFTCRML SRPPDEADTE NQEARNQYEV MQCFTVSQPK SIKEEGEDLQ
     SCLICIARRF PRQHPVMGTL SFVTKQDTTG KIISIETSNL RTSGRAGWED LVRKCIYAFF
     QPQGREPSYA KQLLQEVMLR GMAVSPTYRF AVNDGSVLTA QTKCKLYCPQ NPDTQPFIVG
     IHVIDREPST LSSPENTNPG LSFARGSPSG STCISSVHTT PTLPSATATC SAMPITDFSQ
     SPGPGTGMHF NGGAGQNNFG CSPVQRMGPG VSMSQGHVGV QSNTHPLNLN SSPMGSPAVT
     PPHFMSPRAR GSPGLVGSPR ISGNPFSPSM PGTHSPVAVP NSSISSASRP YSNNALNPVT
     GFGEGPSTPL GYSTPSPIQK QLSAQSSPGP LAMQTAKPEP RDSKEMSSAL GEMVPSDSCL
     SEAKPTASVS LHSGGEQLTE GESKAMQALG NTKLVQLLAT TAEQQLKHAD GDGTNAKEFL
     SCVGVSACST ASTVPGTPCP LSHSSLTERH KILHRLLQEG SPSDITTLSL EQEKKEAGLC
     SGVPAGGQLG SANSETSQEL ESPKKKETKD HQLLRYLLDK DEMGLGAPPS LSLDDVKVKS
     EKSGEESCPG TMPMGLPKSF LEETKPETLE QVSHLFPPVD LDQLLPTRCK AQRGDNGVPG
     ATLKSEVRSS PVPGTPTGMN DLMHQTIEAT DLKTLRDCGP PGLSGTSLIF LNFILSNYNR
     NESSFSLIST SVGFSSQLDD LLCPPTTPEG RNDEKALLDQ LVSFLSGKDE TELAELDRAL
     GIDKLVQGGN LEILTERFQP QQPAPALPHP PHPPQLMMDQ KPTLYPQAYL SPSTTSGLPH
     PYPGMARQAS PFAPMVTQVP SRGAFPTSMG MQQRPTLARP PLAPNQLRLQ LQQRLQGQQQ
     QLLQNRQAIL NQFGVAGPVS MAVRQGIQQQ PQQLPPPPLN AQMLAQRHRE LYSQQHRQRQ
     MMQQKALLMR QQSFGGTLPP SVVMPGPLGA SRVTQGPTQQ FSYPPNFGTN PGNPAASTSP
     FTQLGPNPEG GLPNRGAMGN RGMMGNVGGQ FAAGMNSQIQ QNVFQYSASG MGQQADPPFA
     PAMSPNSPMM SPRIPPSPSP MLQQTPPSPG YQSPDIKNWQ QGTLGNSSLL GQPGSGQPQP
     PPPPAGQQGM YNNMSITVSM AGGNAVSSVN QMGSMQMPSM NSMCSDQISD PALRPGSLYC
     NQLPSSDLLK NETEGAQVQQ VQVFADVQCT VNLVGGDPYL NQPGPMAAQK ATTGAQTPQS
     QQKSLLQQLL TE
//
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