RAD25_ANTLO
ID RAD25_ANTLO Reviewed; 687 AA.
AC Q6E6J3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPB;
DE Short=TFIIH subunit XPB;
DE EC=3.6.4.12;
DE AltName: Full=DNA repair helicase RAD25;
DE AltName: Full=RNA polymerase II transcription factor B subunit SSL2;
DE Short=TFB subunit SSL2;
DE AltName: Full=Suppressor of stem-loop mutation 2;
GN Name=SSL2; Synonyms=RAD25;
OS Antonospora locustae (Microsporidian parasite) (Nosema locustae).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Antonospora.
OX NCBI_TaxID=278021;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15186746; DOI=10.1016/j.cub.2004.04.041;
RA Slamovits C.H., Fast N.M., Law J.S., Keeling P.J.;
RT "Genome compaction and stability in microsporidian intracellular
RT parasites.";
RL Curr. Biol. 14:891-896(2004).
CC -!- FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the general
CC transcription and DNA repair factor IIH (TFIIH) core complex, which is
CC involved in general and transcription-coupled nucleotide excision
CC repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA
CC transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA
CC around the lesion to allow the excision of the damaged oligonucleotide
CC and its replacement by a new DNA fragment. The ATPase activity of
CC XPB/SSL2, but not its helicase activity, is required for DNA opening.
CC In transcription, TFIIH has an essential role in transcription
CC initiation. When the pre-initiation complex (PIC) has been established,
CC TFIIH is required for promoter opening and promoter escape. The ATP-
CC dependent helicase activity of XPB/SSL2 is required for promoter
CC opening and promoter escape. Phosphorylation of the C-terminal tail
CC (CTD) of the largest subunit of RNA polymerase II by the kinase module
CC TFIIK controls the initiation of transcription.
CC {ECO:0000250|UniProtKB:Q00578}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in
CC NER. The core complex associates with the 3-subunit CTD-kinase module
CC TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit
CC holoenzyme (holo-TFIIH) active in transcription.
CC {ECO:0000250|UniProtKB:Q00578}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00578}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000305}.
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DR EMBL; AY548884; AAT12293.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6E6J3; -.
DR SMR; Q6E6J3; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR032438; ERCC3_RAD25_C.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001161; XPB/Ssl2.
DR InterPro; IPR032830; XPB/Ssl2_N.
DR Pfam; PF16203; ERCC3_RAD25_C; 1.
DR Pfam; PF13625; Helicase_C_3; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00603; rad25; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Transcription; Transcription regulation.
FT CHAIN 1..687
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPB"
FT /id="PRO_0000388442"
FT DOMAIN 239..401
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 455..609
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 636..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 354..357
FT /note="DEAH box"
FT COMPBIAS 646..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 252..259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 687 AA; 78771 MW; E2624BDC3A8769C0 CRC64;
MTRCGWHTCT RVRPRMGETL LPRKASQHEF EPEEIRMKQE HTECPLLVSH NGIIILETFT
ANAKQATDFL IAIAEPVSRP AHVHEYRITP YSLYAAVSVG LTTEDILSTL DRFAKNTVPD
TIVRFVRECT LSYGKTRLVF KGGRFLVEAA TREVFDVLTG DAEISRLRAA GTVRDADARY
VFEVRVDCIE QVRRRCIEID YPMIEEYDFR DDVALRSLDM DLRDTVSIRT YQEVSLNKMF
GNRRARSGVI VLPCGAGKTL VGITAMCTIK KPCIVLCTSG VSVEQWRQQV LAFSTVSADA
VSRFTSERKE MFEADAGILI TTYTMLAFSG RRSAEAQRVM EWLRGTEWGL MILDEVHVVP
AAMFRKVVSA VSHHCKLGLT ATLVREDDKI EDLNFLIGPK LYEADWQDLS MQGHIARVEC
VEVWCDMTAE FYREYLGQDP RRRRVLSIMN PAKFQTCEFL IRKHEALGEK IIVFSDNVLA
LRTYALKLGK PFIYGPTGQT ERMRILRQFQ TNPAINTLFL SKVGDTSIDL PEASCLIQIS
SHFGSRRQEA QRLGRILRAK RRNDPGFRVY FYTLVSKDTE EMYYSRKRQQ FLVDQGYTFR
TVTALEGFRD TDVRVFRGKA EQRELLATVL LASEEDLESE ESEDGDEAAA DRRHLRTRGG
AEDTVPASRT RTERHLLFRK MHKRHRR
