ID M7BIU0_CHEMY Unreviewed; 1014 AA.
AC M7BIU0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Transcription initiation factor TFIID subunit 7 {ECO:0000313|EMBL:EMP31968.1};
GN ORFNames=UY3_10891 {ECO:0000313|EMBL:EMP31968.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP31968.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB543129; EMP31968.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BIU0; -.
DR STRING; 8469.M7BIU0; -.
DR eggNOG; KOG0545; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR CDD; cd08047; TAF7; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR039663; AIP/AIPL1/TTC9.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR006751; TAFII55_prot_cons_reg.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11242; ARYL HYDROCARBON RECEPTOR INTERACTING PROTEIN RELATED; 1.
DR PANTHER; PTHR11242:SF1; PPIASE FKBP-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF04658; TAFII55_N; 1.
DR SMART; SM01370; TAFII55_N; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Initiation factor {ECO:0000313|EMBL:EMP31968.1};
KW Protein biosynthesis {ECO:0000313|EMBL:EMP31968.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 12..178
FT /note="TAFII55 protein conserved region"
FT /evidence="ECO:0000259|SMART:SM01370"
FT REGION 107..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 254..339
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 198..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 111585 MW; DC2AECC45A7584FC CRC64;
MSKNKDDAPH ELESQFILRL PPEYASTVRR AVQSGSVNLK DRLTIELHPD GRHGIVRVDR
VPLAAKLVDL PCITESLKTI DKKTFYKTAD ICQMLVCTVD GDLYPPLEEP TVSTDPKANK
KKDKDREKKF IWNHGITLPL KNVRKRRFRK TAKKKYIESP DVEKEVKRLL STDAEAVSVR
WEVIAEDETK EADNHGSLTG LDISSPGMSG HKQGHGSSEH DELREIFNDI SSSSEDEDER
DHHDDEDLNI MDTEEDLERQ LQDKLNESDG QQQENEGTNQ IAMGIQKQID NLKGKLQETQ
ERRKRQEDLI MKVENLALKT RLQAVLDEFK QQEDREKQQL TFHFQTLKDD FERTVIDDSR
QAGIPMEIIV GKLFKIEVWE TLLTSMRIGE VAEFWCDAIH TGMYALVSKG MRRIAEGKDP
LEGQKHRCGM GNMFDYHSTG YADLDELQRD PQPLIFIMEL FKVDDPSSYK RDTWAMNKEE
KLSAVPVLHS EGNRLVLLKR YQEAAAKYQE AVICLRNVQA KEKPWAEDWL SLEKLITPLV
LNYCQCQLEL GEYYEVLEHT TDLLQKNNEN VKAYFKRAKA HAAVWNEEAA REDFLRVAQL
DPSLAAAVKK ELRLLGERMR EKHVEDRQRY QGLFQQPQLK GATEGKGQWG GDGNAGVGRQ
EGGDSGENRE ETGLGTESST AREEEQDQRI SGAEAGTRES GLGEENTQAK REQALGESGA
ETGLGEESAR AEREEPGKGP DQGNSGVDGG MEETGSGEGN IEAEREEPGE GTDQGNSGVD
GGMEETGSGE GNIEAEKEEP GEGTDQGNSG VDGGMEETGL GEGNIEAEKE EPGEGTDQGN
SGVDGGMEET GSGEGNIEAE REEPGEGTDQ GNSRVDGGME ETGSGEGNIE AEREELGEGT
DQGNSGVDGA GRGQGNLGTE ETGLGEGFSR AEMERTSQGD CAAGSHSIQG QKGPLERGLG
EENARESHGA GARERSSEAD EEWGGRAEGC SSMKAAGQSS GEGVGPGAEN SRLL
//