CCL1_YEAST
ID CCL1_YEAST Reviewed; 393 AA.
AC P37366; D6W435;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Cyclin CCL1;
GN Name=CCL1; OrderedLocusNames=YPR025C; ORFNames=YP9367.05C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8230216; DOI=10.1006/jmbi.1993.1587;
RA Valay J.G., Simon M., Faye G.;
RT "The kin28 protein kinase is associated with a cyclin in Saccharomyces
RT cerevisiae.";
RL J. Mol. Biol. 234:307-310(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH KIN28 AND TFB3.
RC STRAIN=DBY2019;
RX PubMed=9235928; DOI=10.1074/jbc.272.31.19319;
RA Feaver W.J., Henry N.L., Wang Z., Wu X., Svejstrup J.Q., Bushnell D.A.,
RA Friedberg E.C., Kornberg R.D.;
RT "Genes for Tfb2, Tfb3, and Tfb4 subunits of yeast transcription/repair
RT factor IIH. Homology to human cyclin-dependent kinase activating kinase and
RT IIH subunits.";
RL J. Biol. Chem. 272:19319-19327(1997).
RN [5]
RP SUBUNIT.
RX PubMed=11839796; DOI=10.1128/mcb.22.5.1288-1297.2002;
RA Keogh M.-C., Cho E.-J., Podolny V., Buratowski S.;
RT "Kin28 is found within TFIIH and a Kin28-Ccl1-Tfb3 trimer complex with
RT differential sensitivities to T-loop phosphorylation.";
RL Mol. Cell. Biol. 22:1288-1297(2002).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Regulatory component of the TFIIK complex (KIN28-CCL1 dimer)
CC which is the protein kinase component of transcription factor IIH
CC (TFIIH) and phosphorylates the C-terminal domain of RNA polymerase II
CC during transition from transcription to elongation after preinitiation
CC complex (PIC) formation, thereby positively regulating transcription.
CC TFIIH (or factor B) is essential for both basal and activated
CC transcription, and is involved in nucleotide excision repair (NER) of
CC damaged DNA. TFIIH has DNA-dependent ATPase activity and is essential
CC for polymerase II transcription in vitro.
CC -!- SUBUNIT: CCL1 and KIN28 form the TFIIK complex, a component of TFIIH
CC holo complex. Component of a complex consisting of KIN28, CCL1 and
CC TFB3. {ECO:0000269|PubMed:11839796, ECO:0000269|PubMed:9235928}.
CC -!- INTERACTION:
CC P37366; P06242: KIN28; NbExp=7; IntAct=EBI-4385, EBI-9691;
CC P37366; P17157: PHO85; NbExp=2; IntAct=EBI-4385, EBI-13327;
CC -!- MISCELLANEOUS: Present with 8700 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000305}.
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DR EMBL; X71902; CAA50721.1; -; Genomic_DNA.
DR EMBL; Z49274; CAA89279.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95021.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11451.1; -; Genomic_DNA.
DR PIR; S39383; S39383.
DR RefSeq; NP_015350.1; NM_001184122.1.
DR PDB; 6XI8; EM; 3.64 A; B=47-370.
DR PDB; 7KUE; EM; 3.50 A; B=1-393.
DR PDBsum; 6XI8; -.
DR PDBsum; 7KUE; -.
DR AlphaFoldDB; P37366; -.
DR SMR; P37366; -.
DR BioGRID; 36202; 154.
DR ComplexPortal; CPX-1659; General transcription factor complex TFIIH.
DR ComplexPortal; CPX-1660; General transcription factor complex TFIIK.
DR DIP; DIP-2258N; -.
DR IntAct; P37366; 58.
DR MINT; P37366; -.
DR STRING; 4932.YPR025C; -.
DR iPTMnet; P37366; -.
DR MaxQB; P37366; -.
DR PaxDb; P37366; -.
DR PRIDE; P37366; -.
DR EnsemblFungi; YPR025C_mRNA; YPR025C; YPR025C.
DR GeneID; 856136; -.
DR KEGG; sce:YPR025C; -.
DR SGD; S000006229; CCL1.
DR VEuPathDB; FungiDB:YPR025C; -.
DR eggNOG; KOG2496; Eukaryota.
DR GeneTree; ENSGT00940000168613; -.
DR HOGENOM; CLU_022620_4_2_1; -.
DR InParanoid; P37366; -.
DR OMA; FRVEQNT; -.
DR BioCyc; YEAST:G3O-34185-MON; -.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-SCE-69231; Cyclin D associated events in G1.
DR Reactome; R-SCE-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:P37366; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P37366; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:SGD.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IDA:SGD.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IGI:SGD.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:ComplexPortal.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
DR GO; GO:1905866; P:positive regulation of Atg1/ULK1 kinase complex assembly; IMP:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:SGD.
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:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR031658; Cyclin_C_2.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR027081; CyclinH/Ccl1.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR Pfam; PF16899; Cyclin_C_2; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR TIGRFAMs; TIGR00569; ccl1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cyclin; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..393
FT /note="Cyclin CCL1"
FT /id="PRO_0000080504"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 135..151
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 193..197
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 279..286
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 329..343
FT /evidence="ECO:0007829|PDB:7KUE"
SQ SEQUENCE 393 AA; 45210 MW; FE06E78FC38A8433 CRC64;
MTDIQLNGKS TLDTPSATMS AKEKEAKLKS ADENNKPPNY KRISDDDLYR HSSQYRMWSY
TKDQLQEKRV DTNARAIAYI EENLLKFREA HNLTEEEIKV LEAKAIPLTM EEELDLVNFY
AKKVQVIAQH LNLPTEVVAT AISFFRRFFL ENSVMQIDPK SIVHTTIFLA CKSENYFISV
DSFAQKAKST RDSVLKFEFK LLESLKFSLL NHHPYKPLHG FFLDIQNVLY GKVDLNYMGQ
IYDRCKKRIT AALLTDVVYF YTPPQITLAT LLIEDEALVT RYLETKFPSR EGSQESVPGN
EKEEPQNDAS TTEKNKEKST ESEEYSIDSA KLLTIIRECK SIIEDCKPPS TEEAKKIAAK
NYYCQNPSTL IQKLKRKLNG EDTSSTVEKK QKT
