ID C3XYB0_BRAFL Unreviewed; 1482 AA.
AC C3XYB0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS50157};
GN ORFNames=BRAFLDRAFT_126318 {ECO:0000313|EMBL:EEN66795.1};
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:EEN66795.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN66795.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN66795.1};
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).
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DR EMBL; GG666473; EEN66795.1; -; Genomic_DNA.
DR RefSeq; XP_002610785.1; XM_002610739.1.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG3912; Eukaryota.
DR InParanoid; C3XYB0; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 8.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR000620; EamA_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24393:SF15; IP01201P-RELATED; 1.
DR PANTHER; PTHR24393; ZINC FINGER PROTEIN; 1.
DR Pfam; PF00892; EamA; 1.
DR Pfam; PF21549; PRDM2_PR; 1.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR SUPFAM; SSF103481; Multidrug resistance efflux transporter EmrE; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT TRANSMEM 1158..1176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1196..1220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1226..1244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1251..1272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1284..1304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1324..1341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1371..1390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1402..1421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1427..1451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 105..125
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 155..183
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 185..212
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 213..241
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 242..269
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 270..297
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 299..326
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 789..816
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 817..845
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 846..873
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 406..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1482 AA; 164833 MW; 8D02A5AEA8385F11 CRC64;
MKTGGFSQGY SSSSVIEMIY QIVDEFGKVK FIVDASEPGT GNWMKYIRSA RNYNEQNMVA
LQINDQMYYK VVKDVEMGEE LMVYMKDAMY PDGTMPPNFE EEKRFRCGEC DDLFKSKVAL
RRHQKYACNN SLAIFNSINE DFKSRQTEEL TSQLFECTDC DRIFPNMPSL ERHVMTGHGS
ETREFKCDQC PKSFNWKSNL IRHQMSHDEQ KRFPCENCDK VFTDPSNLQR HIRSQHVGAR
SHACPECGKT FATSSGLKQH QHIHSSIKPF TCEVCLKSYT QFSNLCRHKR MHADCRQQIK
CRDCGQLFST MASLNKHRRF CEGRNNFGIS MPAMYRAASQ SQSGTPLPPS SRMPLRNMPP
ASLMDYFGTG GLHPPTTVPQ PASLSSVQSV PLSQTAAASL LSSRMQPPAV SYPSNTALRS
HHPSSASTVS ARSTFFPPTS TFSRPPFLNA VSMGPQKALL SSPMAHLLAQ PPASAGSTKD
TSTGQEEDMS RAKSGANTKE RANDLSEGSD VSDVSTPTGS DLETSGGSEL DSESEGDGAD
KKSSMHKEAR MAKHQKNDPS VKEEPEDESA FLKPNDQSAA IPTSGADTIK AIASIADKYF
GNDGEEMRSI RVQHQEGKPA GAYPTVAEAE KPFDLSVKKS ERMAAQATSS GEDQPLDLST
HPRKGDVDQA RNMAESRKSH AFGSLMATTY TSSQRGNPRL TYARPSPLAM DPIYRVEKRK
FTDRIYSGIQ EKYMRHANYP FSASEHLIQN GAAYEMGNRG GGMMPVSEFP PMASQLADPV
VRGKGKDRYT CRYCGKLFPR SANLTRHLRT HTGEQPYRCK YCDRSFSISS NLQRHVRNIH
NKEKPFKCPQ CERCFGQQTN LDRHLRKHEQ EDQDAASGKS PTSAEDLAEL ADKDESYFEQ
IQNFIESPTI TPRKENAEGN GNLEKKFSPS NGHVAEQMAA GSPPALINGN KQSPPPDNTP
CEEDDMMVDK EAETHKVNGH PKHAEEEEKK TAGVNGQHGP LGKLLNGDPL DYKPISETTM
DDISVDVVDY YGGVMGDAES DGDRSNRQRR SKTQAYSMML SLSDEEEMAM DDKHRGPRLR
SMRRSLRVGD YSVWKALTNT RKGSRDCQSS SNPQNNQQTE EALRRNQDVS GTRLDRVPVV
SGSHDVGNRI HQHAHNQASG MFIGEFSCLV VFKIWVLYHR CAKKSVDVGN QKFNPLVFLA
PALCDMTGTS LMYIGLTLTY ASSFQMLRGA VIIFTGLLSV AFLGRKLDWH HWCGIFFVLI
GLILVGVSDF IFKTPETGVS TNGVITGDLL ILMAQVIAAI QMVVEEKFVS GQNIPPMQGV
GWEGFFGFTV LTTLLFPFYF IKVGPPFGAN PRGVFEDALD GLWQISNNRN IALGVFGTII
SIAFFNFAGL SVTKEMSATT RMVLDSVRTL VIWVFSLAVG WEDFQYLQAI GFVILLSGTA
VYNDMLFVPL LRRYGILGPA HQVSLDEKRP LIQDNDVEPN YP
//
