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TFB1_NEUCR
ID   TFB1_NEUCR              Reviewed;         663 AA.
AC   Q9P5N7; Q7SC31;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=General transcription and DNA repair factor IIH subunit tcf-29;
DE            Short=TFIIH subunit tcf-29;
DE   AltName: Full=RNA polymerase II transcription factor B 73 kDa subunit;
DE   AltName: Full=RNA polymerase II transcription factor B p73 subunit;
DE   AltName: Full=RNA polymerase II transcription factor B subunit 1;
DE   AltName: Full=Transcription factor-29;
GN   Name=tcf-29; ORFNames=B8B20.390, NCU05423;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Component of the general transcription and DNA repair factor
CC       IIH (TFIIH) core complex, which is involved in general and
CC       transcription-coupled nucleotide excision repair (NER) of damaged DNA
CC       and, when complexed to TFIIK, in RNA transcription by RNA polymerase
CC       II. In NER, TFIIH acts by opening DNA around the lesion to allow the
CC       excision of the damaged oligonucleotide and its replacement by a new
CC       DNA fragment. In transcription, TFIIH has an essential role in
CC       transcription initiation. When the pre-initiation complex (PIC) has
CC       been established, TFIIH is required for promoter opening and promoter
CC       escape. Phosphorylation of the C-terminal tail (CTD) of the largest
CC       subunit of RNA polymerase II by the kinase module TFIIK controls the
CC       initiation of transcription. {ECO:0000250|UniProtKB:P32776}.
CC   -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC       XPB/rad25, XPD/dnr-10, tcf-30/SSL1, tcf-29/TFB1, tcf-11/TFB2, tcf-
CC       14/TFB4 and rtf-1/TFB5, which is active in NER. The core complex
CC       associates with the 3-subunit CTD-kinase module TFIIK composed of div-
CC       66/cyclin H, prk-3/KIN28 and rtf-2/TFB3 to form the 10-subunit
CC       holoenzyme (holo-TFIIH) active in transcription.
CC       {ECO:0000250|UniProtKB:P32776}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TFB1 family. {ECO:0000305}.
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DR   EMBL; AL355933; CAB91486.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA34010.1; -; Genomic_DNA.
DR   PIR; T49685; T49685.
DR   RefSeq; XP_963246.1; XM_958153.2.
DR   AlphaFoldDB; Q9P5N7; -.
DR   SMR; Q9P5N7; -.
DR   STRING; 5141.EFNCRP00000006580; -.
DR   EnsemblFungi; EAA34010; EAA34010; NCU05423.
DR   GeneID; 3879394; -.
DR   KEGG; ncr:NCU05423; -.
DR   VEuPathDB; FungiDB:NCU05423; -.
DR   HOGENOM; CLU_019188_1_0_1; -.
DR   InParanoid; Q9P5N7; -.
DR   OMA; IYNENVP; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; IBA:GO_Central.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; IBA:GO_Central.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.3970.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR005607; BSD_dom.
DR   InterPro; IPR035925; BSD_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR027079; Tfb1/GTF2H1.
DR   InterPro; IPR013876; TFIIH_BTF_p62_N.
DR   PANTHER; PTHR12856; PTHR12856; 1.
DR   Pfam; PF03909; BSD; 2.
DR   Pfam; PF08567; PH_TFIIH; 1.
DR   SMART; SM00751; BSD; 2.
DR   PROSITE; PS50858; BSD; 2.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..663
FT                   /note="General transcription and DNA repair factor IIH
FT                   subunit tcf-29"
FT                   /id="PRO_0000119259"
FT   DOMAIN          147..206
FT                   /note="BSD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00036"
FT   DOMAIN          227..278
FT                   /note="BSD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00036"
FT   REGION          452..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..479
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   663 AA;  73030 MW;  1148B5E17A5D2800 CRC64;
     MAPIEIPRGQ ASYKKREGII TLTPDKTALI WSPLPGTGPP VISLSVSNIT NLQQTPKTNP
     KVVLRVVEKP KAPGADPAAY PFQFTHATEA RNEADAIKDL LSQIIAELRG DDPSLPKPAK
     SGPNGAGASA AMAMASAVNS KHLPFRWFED DMLKADVELQ QSLMKKDKAL AHIYNDAKLS
     KPDSLSDASF NSQFWATRIS LLRAYAIELN QKKGSYNVLS TIKPRTENGE LKLNINHEQV
     QLIFQQHPLV KRIYNENVPK LTESEFWSRF FLSRLSKKLR GERITDNDNT DPLFDKYLEA
     DNTMAVPAKI TATSVPPIIN IEGNEENQGG FRGGNLKDVE MRPRANIPII KTLNSLSEKI
     MANVAPTDVD PSAASYSKDG IADALSKQLA LQDLRGDAEA QLIRLSVKDT STFFTGNQPS
     LTDQEAADAR LYATQVPSDV LFEVQADMDT LDSDGRGGID LHRSIGVDPD SDDEGNNSLD
     SKSGPKPQHV GSRAALRFAQ NQILESMKSA RSHLTTTTTH GGSHTTTTNA SEERPMSLPT
     DIAHRATLTC ATTAEFLKQF WTVFNNSSNS SPEKQQELAY LADSLVRSKQ RIEALADEAE
     KRRQEIMEKR KREIREYYQK TGRKAKWVPV GGGRDAVWAA FEGVVGGLER AVAVWEMVKS
     GRI
 
 
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