ID C3ZTM2_BRAFL Unreviewed; 1232 AA.
AC C3ZTM2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Cilia- and flagella-associated protein 45 {ECO:0000256|ARBA:ARBA00034142};
GN ORFNames=BRAFLDRAFT_124948 {ECO:0000313|EMBL:EEN44129.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN44129.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN44129.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN44129.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- SIMILARITY: Belongs to the CFAP45 family.
CC {ECO:0000256|ARBA:ARBA00034116}.
CC -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000256|ARBA:ARBA00008573}.
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DR EMBL; GG666678; EEN44129.1; -; Genomic_DNA.
DR RefSeq; XP_002588118.1; XM_002588072.1.
DR AlphaFoldDB; C3ZTM2; -.
DR STRING; 7739.C3ZTM2; -.
DR eggNOG; KOG1726; Eukaryota.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; C3ZTM2; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd06959; NR_DBD_EcR_like; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.565.10; Retinoid X Receptor; 2.
DR InterPro; IPR033253; CFAP45.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR004345; TB2_DP1_HVA22.
DR InterPro; IPR043597; TPH_dom.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR15504:SF0; CILIA- AND FLAGELLA-ASSOCIATED PROTEIN 45; 1.
DR PANTHER; PTHR15504; NASOPHARYNGEAL EPITHELIUM SPECIFIC PROTEIN 1; 1.
DR Pfam; PF03134; TB2_DP1_HVA22; 1.
DR Pfam; PF13868; TPH; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
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}.
FT DOMAIN 644..719
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT REGION 106..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 308..395
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 492..617
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 126..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..219
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1232 AA; 140791 MW; 426DE9025D90BA7D CRC64;
METFADVFIS WVPFYYEVKI VFVVWLLSPY TKGSSFIYRK FVHPALSKRE KEIDEYIAQA
SERSYETMVK MGKSGLNMAA TAVAKTAIKG QQTITERLIR GLSTQDLSTV GRDSSSERDV
PSSRMSVSDD EALTMRTSPV DSNRLTEEME RQRDRKGGEE IVETKYSHIR GPRSMLEEQA
GGEPGPPPTG TWPRQRKLYD SVEIDDDGDD DDDDDDTDEQ IPIKSAPTKS KKKEITGKVR
TSSQAYQTPV ANLRLSSGNN KSKKAGRETI QVITKDLIRN LIVPMEDPSG QSIILHQGEF
ARIKSAARVL TKEERERLEE MRKREKEEAI DACAQRKTFM KVKDLDRKQN EKLNDLEEEA
QEQAQYLLEK AKKQQEEQED EIKALNELIL NAKCHAIRDA QILEKGVIQK ELTEEEKRLD
LMMEVDRVND LKLQEEITLR RKQERLIGKQ QIIDQIQQNE EDRLLDQEKK DQEARQMLQY
LEKLQMEDLK ELERKRLQQL DIQVEIQRAN QEADDMRAKK AEQERLADQK VIEYQKQRAQ
REAEYEAEQE RIKKEKEKEV ARLRALQERA KDLQAEKDAL RAKRNQEQAE REWRKKEREE
ARLKAEMEEL LKRAREDQVS VATIFEDMPA QDASSFPEAA GTEGGDCVVC GDKGSGFHYG
VYSCEGCKGF FRRTVTKGYV KACKSGSKCN MDMYTRRKCP ECRLRSCRAA GMRSDCLLTQ
AQCRSKFLYR KNQAPKSDHP LSPTSQEVPV QSPINQSSPT GAQQQQNQVS NSANQSETSG
SPSSSAQLCE TVSEEMSLPQ ENDNRSSSTN LLDEIMSSFM DFSSNNPVLT RTDSTGSDDM
LSFLALLAND TQSIDEYDLD TGIGLFDEAT TPNQSNSILE HAENLLSLHK GEASLEANVS
APTKGQDAED RSGSSTSDIH APTESVNQTP TTSGLKATLQ LSQNSQPTDE EQETSSSSSS
CQETDECARN LEEGPWKIKR FARPNAVQNL SPVYRAIISD IAAFRKKIFE RDHKMMCRLM
KETLQCNSKK EKQARFVAHM GRVVEKTVEF VKTIRCFQDL CIEDQIEVVK LFVMWLLLIT
VHTEVFNATL MKWYEGMLDL KIDITTLDLL QCVIVVSPDR PNIKGRNILE QSYAEYIECL
RAYCKVAYPE NRMMFARLLM LSILAEARKL HWDKGEEYAI EELMRDVDQG VDPEKEVRAM
IASRYGEEQA RRIFDTAETI EMEEEDKNQA NQ
//
