ID B2B1C8_PODAN Unreviewed; 501 AA.
AC B2B1C8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=General transcription and DNA repair factor IIH {ECO:0000256|PIRNR:PIRNR015919};
GN ORFNames=PODANS_3_8890 {ECO:0000313|EMBL:CAP70830.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP70830.1};
RN [1] {ECO:0000313|EMBL:CAP70830.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP70830.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP70830.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP70830.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP27424.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|PIRNR:PIRNR015919}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR015919}.
CC -!- SIMILARITY: Belongs to the GTF2H2 family.
CC {ECO:0000256|ARBA:ARBA00006092, ECO:0000256|PIRNR:PIRNR015919}.
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DR EMBL; CU638743; CAP70830.1; -; Genomic_DNA.
DR EMBL; FO904938; CDP27424.1; -; Genomic_DNA.
DR RefSeq; XP_001909697.1; XM_001909662.1.
DR AlphaFoldDB; B2B1C8; -.
DR STRING; 515849.B2B1C8; -.
DR GeneID; 6193850; -.
DR KEGG; pan:PODANSg6733; -.
DR VEuPathDB; FungiDB:PODANS_3_8890; -.
DR eggNOG; KOG2807; Eukaryota.
DR HOGENOM; CLU_028556_2_0_1; -.
DR OrthoDB; 276422at2759; -.
DR Proteomes; UP000001197; Chromosome 3.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProtKB-UniRule.
DR CDD; cd01453; vWA_transcription_factor_IIH_type; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR007198; Ssl1-like.
DR InterPro; IPR004595; TFIIH_C1-like_dom.
DR InterPro; IPR012170; TFIIH_SSL1/p44.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR NCBIfam; TIGR00622; ssl1; 2.
DR PANTHER; PTHR12695; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 2; 1.
DR PANTHER; PTHR12695:SF2; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 2-RELATED; 1.
DR Pfam; PF07975; C1_4; 1.
DR Pfam; PF04056; Ssl1; 1.
DR PIRSF; PIRSF015919; TFIIH_SSL1; 1.
DR SMART; SM01047; C1_4; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50234; VWFA; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR015919};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR015919};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR015919};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR015919};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR015919};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 93..277
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 448..470
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT ZN_FING 320..337
FT /note="C4-type"
FT /evidence="ECO:0000256|PIRSR:PIRSR015919-1"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 54666 MW; 9149A32F6FAD621E CRC64;
MADSDDEYVG DLSGDDAGVD SVYGTRSKDG GKGKGGQKGK GTRKAAWEEV HRAWDEVAIA
EDGSITVAEL IEAEKRRRLM RDTTPIQRGI IRHMVLVLDM SIAMAEKDLL PNRFALTFSY
AMEFVNTFFQ QNPISQLGII GMRDGIAVRI SDMSGNPVEH IEKLRQWALK DPIGNPSLQN
ALEMCRGHLY HTPSHGTREV LIIYGALLSS DPGDISDTIT SLIADRIRVS IIGLAAQVAI
CAELCARTND NDDSQYRIAL HEQHFRELFL AATTPPVTHE AEQSNASLLM MGFPSRSLAS
KDFVSLCACH NKPTREGYTC TRCRIKVCRL PASCPVCGLT LILSIHLARS YHHLFPLKSW
VAVPWTEAKK SVACFSCQTP FPPVPKAAPP KIKLKVKESS GVGGQTAANI AKAKGRGEVP
AKTNTVTAPT PGLLPEAIKA GVSESGRYKC PECEEHFCID CDIYAHETIH NCPGCLARLV
KSQQQQQEEV VGAGEAMEVD S
//
