ID   TFB3_SCHPO              Reviewed;         318 AA.
AC   O94684;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=RNA polymerase II transcription factor B subunit 3;
DE   AltName: Full=CDK-activating kinase assembly factor MAT1 homolog;
DE   AltName: Full=RING finger protein pmh1;
DE   AltName: Full=RNA polymerase II transcription factor B 38 kDa subunit;
DE   AltName: Full=RNA polymerase II transcription factor B p38 subunit;
GN   Name=pmh1; Synonyms=mcr1, tfb3; ORFNames=SPBC776.18c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTERACTION WITH SKP1; MCS2 AND
RP   MCS6.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=15555586; DOI=10.1016/j.bbrc.2004.10.190;
RA   Bamps S., Westerling T., Pihlak A., Tafforeau L., Vandenhaute J.,
RA   Maekelae T.P., Hermand D.;
RT   "Mcs2 and a novel CAK subunit Pmh1 associate with Skp1 in fission yeast.";
RL   Biochem. Biophys. Res. Commun. 325:1424-1432(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   SUBUNIT.
RX   PubMed=14534314; DOI=10.1074/jbc.m306750200;
RA   Spaehr H., Khorosjutina O., Baraznenok V., Linder T., Samuelsen C.O.,
RA   Hermand D., Maekelae T.P., Holmberg S., Gustafsson C.M.;
RT   "Mediator influences Schizosaccharomyces pombe RNA polymerase II-dependent
RT   transcription in vitro.";
RL   J. Biol. Chem. 278:51301-51306(2003).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Acts as component of the general transcription and DNA repair
CC       factor IIH (TFIIH or factor B), which is essential for both basal and
CC       activated transcription, and is involved in nucleotide excision repair
CC       (NER) of damaged DNA. TFIIH has CTD kinase activity and DNA-dependent
CC       ATPase activity, and is essential for polymerase II transcription (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: One of the nine subunits forming the core-TFIIH basal
CC       transcription factor. Interacts also with skp1 and with the mcs2-mcs6
CC       complex. {ECO:0000269|PubMed:14534314, ECO:0000269|PubMed:15555586}.
CC   -!- INTERACTION:
CC       O94684; Q9Y709: skp1; NbExp=3; IntAct=EBI-1168961, EBI-1172248;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF191500; AAF05735.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA22891.1; -; Genomic_DNA.
DR   PIR; T40689; T40689.
DR   RefSeq; NP_596334.1; NM_001022255.2.
DR   AlphaFoldDB; O94684; -.
DR   SMR; O94684; -.
DR   BioGRID; 277209; 6.
DR   IntAct; O94684; 4.
DR   MINT; O94684; -.
DR   STRING; 4896.SPBC776.18c.1; -.
DR   iPTMnet; O94684; -.
DR   MaxQB; O94684; -.
DR   PaxDb; O94684; -.
DR   PRIDE; O94684; -.
DR   EnsemblFungi; SPBC776.18c.1; SPBC776.18c.1:pep; SPBC776.18c.
DR   GeneID; 2540684; -.
DR   KEGG; spo:SPBC776.18c; -.
DR   PomBase; SPBC776.18c; pmh1.
DR   VEuPathDB; FungiDB:SPBC776.18c; -.
DR   eggNOG; KOG3800; Eukaryota.
DR   HOGENOM; CLU_048466_1_0_1; -.
DR   InParanoid; O94684; -.
DR   OMA; PANCPVA; -.
DR   PhylomeDB; O94684; -.
DR   Reactome; R-SPO-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR   Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-SPO-69202; Cyclin E associated events during G1/S transition.
DR   Reactome; R-SPO-69231; Cyclin D associated events in G1.
DR   Reactome; R-SPO-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR   Reactome; R-SPO-72086; mRNA Capping.
DR   Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-SPO-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-SPO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-SPO-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-SPO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-SPO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   PRO; PR:O94684; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; IBA:GO_Central.
DR   GO; GO:0070985; C:transcription factor TFIIK complex; IDA:PomBase.
DR   GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IDA:PomBase.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:PomBase.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006289; P:nucleotide-excision repair; ISO:PomBase.
DR   GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IC:PomBase.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR015877; Cdk-activating_kinase_MAT1_cen.
DR   InterPro; IPR004575; MAT1/Tfb3.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12683:SF13; PTHR12683:SF13; 1.
DR   Pfam; PF06391; MAT1; 1.
DR   Pfam; PF17121; zf-C3HC4_5; 1.
DR   PIRSF; PIRSF003338; MAT1_metazoa; 1.
DR   TIGRFAMs; TIGR00570; cdk7; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA damage; DNA repair; Metal-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..318
FT                   /note="RNA polymerase II transcription factor B subunit 3"
FT                   /id="PRO_0000055940"
FT   ZN_FING         13..54
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   318 AA;  36674 MW;  FF8472C61268565B CRC64;
     MDDEGARKVD EKCPLCQADR YLNPNMKLLI NPECYHKMCE SCVDRIFTTG PAQCPTPGCN
     KILRKAKFRE QTFEDAQIER EVDVRKRISR IFNKGQQEFD SLQAYNDYLE EVEILTFNLI
     YKIDVEETEE KVKQYEKQNR DSIAANSARA AAEARILAQN EILLKRQKQE AREAAIREHQ
     KEKERREQVE QQIIFDLATS GKDPNKIIQL SDSLKKQQEN IASSVSNISR SSSILLSDVQ
     QVAEDTTPFS PLAGEKDGSK YFSYSKNTYQ DLYLEKVSHE PGRKCGFRIE DCHLRCLYEA
     FSGIDYDLES LKKLEVAS