RAD25_ENTBH
ID RAD25_ENTBH Reviewed; 609 AA.
AC A9CRJ7;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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; ORFNames=EBI_23223;
OS Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Enterocytozoon.
OX NCBI_TaxID=481877;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348;
RX PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA Keeling P.J.;
RT "Patterns of genome evolution among the microsporidian parasites
RT Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT bieneusi.";
RL PLoS ONE 2:E1277-E1277(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348;
RX PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT Enterocytozoon bieneusi.";
RL PLoS Pathog. 5:E1000261-E1000261(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; ABGB01000001; EDQ31310.1; -; Genomic_DNA.
DR RefSeq; XP_001827839.1; XM_001827787.1.
DR AlphaFoldDB; A9CRJ7; -.
DR SMR; A9CRJ7; -.
DR STRING; 481877.A9CRJ7; -.
DR EnsemblFungi; EDQ31310; EDQ31310; EBI_23223.
DR VEuPathDB; MicrosporidiaDB:EBI_23223; -.
DR HOGENOM; CLU_008213_0_0_1; -.
DR InParanoid; A9CRJ7; -.
DR Proteomes; UP000001742; Unassembled WGS sequence.
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..609
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPB"
FT /id="PRO_0000388444"
FT DOMAIN 200..369
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 423..584
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 322..325
FT /note="DEAH box"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 609 AA; 70329 MW; 7CE90AB8B68B2D84 CRC64;
MKENSEDCPL WINYDGLIIL EMFRENSQQA TNFLIAIAEP ISRPENIHEY QITPYSLFAA
ASVGLTTDQI TNTLQKFSKN IIPRNVKNLI SDCTLSYGKL KLVRQSQKFF IEVYNDKIFN
FITSDEILKS FIVNSNIDEL KIEITNVEKI KKRCIEIDYP LIDEYDYTAY ESVNMIKNLH
IDLKPSCHIR SYQEISLNKM LGNGRARSGI IVLPCGSGKT LVGITAISTI KKSAIILCTS
AVSVEQWKQS ILLFTTINPY SVSRFTSDCK EWFENYNVEN TSQGGILITT YSMLSFSGKR
SYDVQRIINK IFAYNWGIMI LDEVHVVPAQ MFRKVVSSVL HQCKLGLTAT LVREDDKIED
LNFLIGPKLY EANWQDLSDK GHIAKVECSE VWCEMTAEFY REYLIQDTSK KRLLSIMNPV
KIQMCEYLIQ KHEAQGDKII VFSDSVFALK EYAIKMKKPF IYGPTSQTER MKILKQFQIN
SKINTLFLSK VGDTSIDLPE ATCLIQISSH FGSRRQEAQR LGRVLRAKKR NNPNFKAYFY
SLVSKDTEEM HYSAKRQQFL IDQGYSFKTI IGFNDMYYNE TRLYKTKQEQ KELLFNLLSK
NLSSDETDK
