RAD25_NOSCE
ID RAD25_NOSCE Reviewed; 659 AA.
AC C4V922;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=NCER_101030;
OS Nosema ceranae (strain BRL01) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX NCBI_TaxID=578460;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRL01;
RX PubMed=19503607; DOI=10.1371/journal.ppat.1000466;
RA Cornman R.S., Chen Y.P., Schatz M.C., Street C., Zhao Y., Desany B.,
RA Egholm M., Hutchison S., Pettis J.S., Lipkin W.I., Evans J.D.;
RT "Genomic analyses of the microsporidian Nosema ceranae, an emergent
RT pathogen of honey bees.";
RL PLoS Pathog. 5:E1000466-E1000466(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; ACOL01000080; EEQ82285.1; -; Genomic_DNA.
DR RefSeq; XP_002995956.1; XM_002995910.1.
DR AlphaFoldDB; C4V922; -.
DR SMR; C4V922; -.
DR STRING; 578460.C4V922; -.
DR EnsemblFungi; EEQ82285; EEQ82285; NCER_101030.
DR KEGG; nce:NCER_101030; -.
DR VEuPathDB; MicrosporidiaDB:NCER_101030; -.
DR HOGENOM; CLU_008213_0_0_1; -.
DR InParanoid; C4V922; -.
DR Proteomes; UP000009082; 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..659
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPB"
FT /id="PRO_0000388445"
FT DOMAIN 215..377
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 431..589
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 330..333
FT /note="DEAH box"
FT BINDING 228..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 659 AA; 75649 MW; 70C110630D9BE4AA CRC64;
MNNVMLPKKA QKHQFPVEEI ILKDDHENFS LWINYDALII LETFKQNSKQ ASDFLIAIAE
PVSRPKYIHE YQITAYSLYA AVSVGLSTDD ILSTLSYFSK NIMPRSVKNF IVECTLSYGK
IKLVIQFNKY FIEAANNDIL KKLIDDKIIR SNLFVTDNSV EVINVELVKK RCIEIDYPLI
EEYDFKNDTV LESFFIDLKP STMIRSYQET CLNKMFCNGR ARSGIIVLPC GSGKTLVGIT
ALTTIKKSCL ILCTSAVSVE QWRQQTMLFT NISGDNICRF TSEYKEWYKD KCGIIITTYT
MLAYNGKRSP EAQKIMDLIQ STEWGLLLLD EVHVVPAMMF RKVISLVTHH CKLGLTATLV
REDDKIEDLN FLIGPKLYEA DWQDLSAKGH IAKVECFEVW CGMTGEFYKE YLIQTSRKKR
LLSIMNPTKF QACEYLISRH EAKGDKIIVF SDSVAALKSY ALKLGKPFIY GPTGQTERMR
ILKQFQTNPL INTIFLSKVG DTSIDLPEAT CLIQISSHFG SRRQEAQRLG RILRAKRRND
PDFKVFFYSL VSKDTDEMFY SSKRQQFLVD QGYSFNIITE IPEIYKNENR VYKSKSQQKE
LLVSVLLSSD KELESDTEAD NEEIGVYSGI LKGSTGVDGM AYMETNERND LGKNKRRRK
