RAD25_ENCCU
ID RAD25_ENCCU Reviewed; 672 AA.
AC Q8SSK1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 119.
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; OrderedLocusNames=ECU01_1060;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=GB-M1;
RX PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT "Identification of transcriptional signals in Encephalitozoon cuniculi
RT widespread among Microsporidia phylum: support for accurate structural
RT genome annotation.";
RL BMC Genomics 10:607-607(2009).
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; AL391737; CAD24977.2; -; Genomic_DNA.
DR RefSeq; XP_965942.1; XM_960849.1.
DR AlphaFoldDB; Q8SSK1; -.
DR SMR; Q8SSK1; -.
DR STRING; 284813.Q8SSK1; -.
DR GeneID; 860283; -.
DR KEGG; ecu:ECU01_1060; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_1060; -.
DR HOGENOM; CLU_008213_0_0_1; -.
DR InParanoid; Q8SSK1; -.
DR OrthoDB; 100698at2759; -.
DR Proteomes; UP000000819; Chromosome I.
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; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..672
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPB"
FT /id="PRO_0000388443"
FT DOMAIN 220..382
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 436..594
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 650..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 335..338
FT /note="DEAH box"
FT BINDING 233..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 672 AA; 76626 MW; 10F7344E4D02DBD9 CRC64;
MNEVVIPKKA TKHQFPYEEL VLKEDGESHP IWVNYDGLII LETFRESSRQ ASDFLIAIAE
PMSRPLQIHE FQITAYSLYA AVSVGLTTSD IIETLDRFSK NFLPRSVRVF ITECTLSYGK
VKLVMKESSF FLETANESVY KMLSSDAVIR SHTIGKSKEG GGLSIEVEEV ELVKKRCIEI
DYPLIEEYDF RNDKVLRSLQ IDLKPTTIIR SYQEICLNKM FGNGRARSGI IVLPCGSGKT
IVGITAISTI KKNCLVLCTS AVSVEQWKQQ TLQFTNMAPD GVGRFTSDHK EWPKDDSGIV
ITTYTMLAYT GKRSHEAQKI MDLIRRTEWG LLVLDEVHVV PAMMFRRVLS LVSHHCKLGL
TATLVREDDK IEDLNFLIGP KLYEADWQDL SAKGHIARVS CIEVWCGMTG DFYREYLSQP
TRRRRLLSIM NPTKFQVCEY LINKHESRGD KIIVFSDSVY ALKAYALKLG KPFIYGPTGQ
TERMRILKQF QTNPVINTIF LSKVGDTSID LPEATCLIQI SSHFGSRRQE AQRLGRILRA
KRRNDPDFKV YFYSLVSKDT DEMFYSSKRQ QFLIDQGYTF TILTDIPEVH ENEHCVYKTK
GQQRELLAGV LLASEKELES EESEDSEGIV YSTTKLKSLS GGDEMAYIER KAPQGRTLAK
GSKKSRKWNP RP
