ID C3Y5N9_BRAFL Unreviewed; 2907 AA.
AC C3Y5N9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS50157};
GN ORFNames=BRAFLDRAFT_87954 {ECO:0000313|EMBL:EEN64286.1};
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:EEN64286.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN64286.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN64286.1};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GG666487; EEN64286.1; -; Genomic_DNA.
DR RefSeq; XP_002608276.1; XM_002608230.1.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; C3Y5N9; -.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription 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; 27.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24392:SF31; C2H2-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24392; ZINC FINGER PROTEIN; 1.
DR SMART; SM00355; ZnF_C2H2; 64.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 22.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 30.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 13..40
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 41..68
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 348..370
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 374..401
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 402..427
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 478..505
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 506..533
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 656..683
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 684..714
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 715..742
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 836..863
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 864..891
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 894..921
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1026..1053
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1054..1081
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1276..1303
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1304..1331
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1495..1522
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1523..1550
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1696..1718
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1724..1751
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1752..1779
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1834..1861
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2354..2382
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2398..2425
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2466..2493
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2494..2521
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2543..2570
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2827..2849
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 2875..2902
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 79..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..2070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2281..2344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1189
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1959..1980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1981..1996
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2002..2022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2055..2070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2283..2304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2313..2327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2907 AA; 334623 MW; 8A54D5B6F5D07080 CRC64;
MMESPVESNK PQLKCGECDR TFSSKDQLDS HYSTHTWKQC FQCNFCSYTT TSINQIKQHA
ETHRGQKSAN TTVEQELIGG NSDHEETKET SDECAAQSPN AEGDKEAVIV IDSDDDHEDE
DRQNRHDVQN TSNLLAIQRY IEGATGKEAQ NEESIANSKS STLSCANAAP LEAALTLDAK
SDQNLPQETV ERNIATGYKD SSQQSRNIFA QLMGDFPVAT LQPSSPMVDC STSTGTERQQ
SQTSSSTSHG GTNPVASGSR EETTADPGAD IQCEVVSSSN SARKKKRNKK AKKLWTCECG
LSTYYLDNLR RHLRKGSCSQ QKHNVYRARP TMATTGAVVK KTARQVRFEC SRCSFWSATR
SELVKHQKTH VRTHFCSECP FQTNHTAKLR RHMQMHEGDH LFTCTECSFS SDHRNILTRH
KKLHEAEICN PGVSQKTFKS LPNEPDLELV CSMCPFTTRE GKYYLLEHEA EHYEDKRMRC
DQCDLTTLDK RNFQSHLWSH DGQKPFECAH CPYRTAHAKS LDRHQRNHNA DLPFQCHLCS
FSAKGQSALS AHMNVHGMNS RFDQKKSGES ESSRRKQGES EEGEEDCLST SETNDSFEAT
ELEIPPEQLD SRKGAVEEKE SHVDGEYFNC KHCAFSAKDR YVLLLHAAKH YSDMTYRCDQ
CDFRSRHSVS LKEHLFIHLG QKPYVCTKDP KCPFVSAHQG NMRSHMKSHS ANLPFKCRFC
TFSTVRQSVL TKHQRLHWLA RQKSGQETKS RPPKRTVYKC KHCEHTAQSQ HALMCHQAEH
KNLRVFQCNR CQFFTNSRFI FRTHRSKHLS RDKVGMKHGD RGKKVQVEPS VQQKPFNCST
CSYTTDKKHL LLVHQAKHSG DKAFHCDECD FSTLTVENLI QHLRTHERRK VQKYKCDECP
YIAERQRALI NHKNNHKADL PFKCKYCSYT ATRGYYIRVH MLLHIHSKTD RSETEDGRGH
SESIPNTSTD VSDPAILHHD ANSDGKVTSE KASKSVPGIR LVMTGSGQYR TTEPASQPPK
PASKMIYCEY CDHSTTRPRD MKVHVRLHTG ERPYACPDCP FRAIQSHHLQ KHQKYHQANL
AQKCRLCTFS CRSASLLRSH VQLHNDKRKW HRCPHCNFVT SSYRVVHTHI KKQHVLSSSL
TGAASVLPVK EKSPSPQPGE VSEVSVEGSE SAEEEYQGAE EEDVDVVGLE EEAGQTQDLD
RSLEKHEEDG DSADNSEDQA EVLCVPHEKD TDRQPPGTIR NTGGLEEVKC NHCEFLSASH
VDHLIHLSTH NNNKKICCDQ CDYTTSNESL FKHHWQTHTS ENLFKCDLCP YRGTGRANLL
QHQSFHSAKQ SLKCRWCSFS CSERLHLDNH SRLHGQGRFK YKCQYCHFNT DKVFLHLVHK
AKHSSTGIIK CNMCKSFQTK DTDALKEHLK KHTHQEYPSK NLSFLQRYKS KVYAEDDLYG
CKLCPYKTLQ PKSMIVHLSW HGANEVYKCP FCNFSHTRLY IIDDHKKLHG YMGSFKCNQC
SYATDEKYRL LKHKAMHSGR KSFKCDQCDY TTDNSHRLMI HTTRHSGQKT HMCPLCPFET
MSKTDLKVHK QKHGAKHSQK CKYCTYSCEN KKHLSKHLKL HEDKTDLRCL KCDFVATSEC
SLSWHEANHH KDDDVQPDES VVTKEAVNDA PVSSVKSKLL STWRYQRKKC PQCPFIAQDL
NRLQDHVQKH GAALPFKCTQ CSYTCERETD LTQHSRCHGV KGAFVCQECS YSTEKKLGLL
LHQVTHTSDG MYSCDQCDLK TPDKEALLSH MKEHDGTQVF RCSVCPYSTV IESYYVLHQR
RHHVRLPLSC KYCSYSAGKK KDIEQHTRMH KRKFHCRECT YTTDSRYHFL VHRGLHTEQK
IFSCDKCPFH TKAMVALRNH LLNQCNNKKL KCSECPFVVD RREVLMNHMK YHNVNLRYKC
DHCSFSTALG WHFNRHAKLH KKSTGQRQKP SASSTEQQDS SRDNEERKKK PSLVESDHDS
DVEVVDSDEN DSTDQVETPE QDMMNDDGHE ADNSRSTDET GDVTEDVDVT EDVTGDVTGD
VTGDGNCESS KEKVMDVSGP STSVTTSTHQ PTAKQQTVFN LVKSYASYHL SCRFCPYKTS
KRIHLVSHEA KHGADLPFKC SKCSYSDRFE GKMAIHMRVH GCPGRYQCSQ CYYSTNNEGF
LQVHMSSRHR TSKVFHCSKC DFSTERPKYL KEHIYKQHLC KSPPTKVKAL QYKCIRCSFQ
AATLADLWEH HKVQHKEEEK HFYKDASVYK CRHCSFVAPK QHRMARHIRI HLRDLAYTRQ
PTDKVAKASS SGTNKVTWTD GQKVGSDEDS QEVPPVGYQS SAPNCDVSDE KSVKKSKNTA
RKSVPLWNKE RPAYQCPDCD YTATREHQVL AHAQNIHRKE PEVERQKVAH YPRRFKLFKC
HSCPYTSYRH VHVSIHEKYH SANYPFKCDQ CTYTCQFLYK LLQHKELHER GDSVSPPPMP
RNITVYKCPL CPYTSYKRTV VQEHKTYHKA DYPHKCSDCS YSCKTDAKLQ DHMKLHTQDG
SADQAQEEPA MSQVSHRGQA SLFKCSMCPY RSYQRTHIYC HERLHYANLP NKCCYCSYSS
LFEYKVQQHQ KLHEVEDGSA RLSDNDASQD AIFSIMESST HEYDEDLTAA AHNADEELQT
EGILSRKRGL NAVFDNSDRY PLRAEGRLSI RLFRCAKCHF YSKSWRLLQL HKAQHELKMI
RSDSRKRSLP AAQPDREAEG GMYRCRYCPY GSTHISHVWR HEERHNAGLP FKCRYCSYSS
LLEFWTDRHE AVHKEERQVE AMQDIRDLQI QPEERSPVFA YGDDKLFAGI DTEEELATNS
DGSDDAYSCR LCGRTFEEWR TYQQHARQHR QAGGEHVSHA VALGDPFTGR VFYVFTCKLC
GRRFTGQVDW IQHMQHHRRN NRVPDRR
//