ID PCF11_YEAST Reviewed; 626 AA. AC P39081; D6VSL0; Q04932; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 185. DE RecName: Full=Protein PCF11; DE AltName: Full=protein 1 of CF I; GN Name=PCF11; OrderedLocusNames=YDR228C; ORFNames=YD9934.13C; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 286-626. RX PubMed=7885847; DOI=10.1093/nar/23.3.507; RA Davies C.J., Hutchison C.A. III; RT "Insertion site specificity of the transposon Tn3."; RL Nucleic Acids Res. 23:507-514(1995). RN [4] RP IDENTIFICATION IN THE CFIA COMPLEX, AND INTERACTION WITH RNA14 AND RNA15. RX PubMed=9032237; DOI=10.1128/mcb.17.3.1102; RA Amrani N., Minet M., Wyers F., Dufour M.-E., Aggerbeck L.P., Lacroute F.; RT "PCF11 encodes a third protein component of yeast cleavage and RT polyadenylation factor I."; RL Mol. Cell. Biol. 17:1102-1109(1997). RN [5] RP FUNCTION OF THE CFIA COMPLEX. RX PubMed=11344258; DOI=10.1073/pnas.101046598; RA Gross S., Moore C.; RT "Five subunits are required for reconstitution of the cleavage and RT polyadenylation activities of Saccharomyces cerevisiae cleavage factor I."; RL Proc. Natl. Acad. Sci. U.S.A. 98:6080-6085(2001). RN [6] RP INTERACTION WITH RBP1. RX PubMed=11149954; DOI=10.1073/pnas.98.2.445; RA Barilla D., Lee B.A., Proudfoot N.J.; RT "Cleavage/polyadenylation factor IA associates with the carboxyl-terminal RT domain of RNA polymerase II in Saccharomyces cerevisiae."; RL Proc. Natl. Acad. Sci. U.S.A. 98:445-450(2001). RN [7] RP INTERACTION WITH RBP1, AND MUTAGENESIS OF ALA-66 AND 68-ASP--ILE-70. RX PubMed=12727883; DOI=10.1093/emboj/cdg200; RA Sadowski M., Dichtl B., Huebner W., Keller W.; RT "Independent functions of yeast Pcf11p in pre-mRNA 3' end processing and in RT transcription termination."; RL EMBO J. 22:2167-2177(2003). RN [8] 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). RN [9] RP INTERACTION WITH RTT103. RX PubMed=15565157; DOI=10.1038/nature03041; RA Kim M., Krogan N.J., Vasiljeva L., Rando O.J., Nedea E., Greenblatt J.F., RA Buratowski S.; RT "The yeast Rat1 exonuclease promotes transcription termination by RNA RT polymerase II."; RL Nature 432:517-522(2004). RN [10] RP FUNCTION, AND RNA-BINDING. RX PubMed=15998810; DOI=10.1101/gad.1296305; RA Zhang Z., Fu J., Gilmour D.S.; RT "CTD-dependent dismantling of the RNA polymerase II elongation complex by RT the pre-mRNA 3'-end processing factor, Pcf11."; RL Genes Dev. 19:1572-1580(2005). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-140. RX PubMed=15241417; DOI=10.1038/nature02679; RA Meinhart A., Cramer P.; RT "Recognition of RNA polymerase II carboxy-terminal domain by 3'-RNA- RT processing factors."; RL Nature 430:223-226(2004). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-138. RX PubMed=15665873; DOI=10.1038/nsmb887; RA Noble C.G., Hollingworth D., Martin S.R., Ennis-Adeniran V., Smerdon S.J., RA Kelly G., Taylor I.A., Ramos A.; RT "Key features of the interaction between Pcf11 CID and RNA polymerase II RT CTD."; RL Nat. Struct. Mol. Biol. 12:144-151(2005). CC -!- FUNCTION: Component of the cleavage factor IA (CFIA) complex, which is CC involved in the endonucleolytic cleavage during polyadenylation- CC dependent pre-mRNA 3'-end formation and cooperates with cleavage factor CC NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. CC Independently involved in RNA polymerase II transcript termination. CC Binds RNA. Seems to bridge RNA polymerase II and the native transcript CC and may be involved in dismantling the RNA polymerase II elongation CC complex. {ECO:0000269|PubMed:11344258, ECO:0000269|PubMed:15998810}. CC -!- SUBUNIT: Component of the CFIA complex, which is composed of RNA14, CC RNA15, PCF11 and CLP1. Interacts with RNA14, RNA15 and RTT103. CC Interacts directly with the phosphorylated CTD domain of RPB1/RNA CC polymerase II. {ECO:0000269|PubMed:11149954, CC ECO:0000269|PubMed:12727883, ECO:0000269|PubMed:15565157, CC ECO:0000269|PubMed:9032237}. CC -!- INTERACTION: CC P39081; Q08685: CLP1; NbExp=13; IntAct=EBI-12980, EBI-29732; CC P39081; P25298: RNA14; NbExp=10; IntAct=EBI-12980, EBI-15632; CC P39081; P25299: RNA15; NbExp=8; IntAct=EBI-12980, EBI-15640; CC P39081; P40073: SHO1; NbExp=2; IntAct=EBI-12980, EBI-18140; CC P39081; Q12159: YRA1; NbExp=2; IntAct=EBI-12980, EBI-29516; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- MISCELLANEOUS: Present with 2800 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; Z48612; CAA88508.1; -; Genomic_DNA. DR EMBL; U13239; AAC33145.1; -; Genomic_DNA. DR EMBL; BK006938; DAA12070.1; -; Genomic_DNA. DR PIR; S59435; S59435. DR RefSeq; NP_010514.3; NM_001180536.3. DR PDB; 1SZ9; X-ray; 2.10 A; A/B/C=1-140. DR PDB; 1SZA; X-ray; 2.20 A; A/B/C=1-140. DR PDB; 2BF0; X-ray; 2.30 A; X=1-138. DR PDB; 2NAX; NMR; -; A=538-608. DR PDB; 2NPI; X-ray; 2.95 A; C/D=454-563. DR PDB; 4C0B; X-ray; 2.77 A; C/D=454-563. DR PDB; 4C0H; X-ray; 2.70 A; C/D=454-563. DR PDB; 4OI4; X-ray; 2.40 A; B/D/U=454-563. DR PDB; 5M9Z; NMR; -; A=530-626. DR PDBsum; 1SZ9; -. DR PDBsum; 1SZA; -. DR PDBsum; 2BF0; -. DR PDBsum; 2NAX; -. DR PDBsum; 2NPI; -. DR PDBsum; 4C0B; -. DR PDBsum; 4C0H; -. DR PDBsum; 4OI4; -. DR PDBsum; 5M9Z; -. DR AlphaFoldDB; P39081; -. DR BMRB; P39081; -. DR SMR; P39081; -. DR BioGRID; 32280; 386. DR ComplexPortal; CPX-1895; mRNA cleavage factor complex CFIA. DR ComplexPortal; CPX-1896; mRNA cleavage factor complex CFI. DR DIP; DIP-944N; -. DR IntAct; P39081; 85. DR MINT; P39081; -. DR STRING; 4932.YDR228C; -. DR iPTMnet; P39081; -. DR MaxQB; P39081; -. DR PaxDb; 4932-YDR228C; -. DR PeptideAtlas; P39081; -. DR EnsemblFungi; YDR228C_mRNA; YDR228C; YDR228C. DR GeneID; 851814; -. DR KEGG; sce:YDR228C; -. DR AGR; SGD:S000002636; -. DR SGD; S000002636; PCF11. DR VEuPathDB; FungiDB:YDR228C; -. DR eggNOG; KOG2071; Eukaryota. DR GeneTree; ENSGT00440000034259; -. DR HOGENOM; CLU_015606_1_0_1; -. DR InParanoid; P39081; -. DR OMA; NIHADEN; -. DR OrthoDB; 12603at2759; -. DR BioCyc; YEAST:G3O-29807-MONOMER; -. DR BioGRID-ORCS; 851814; 1 hit in 10 CRISPR screens. DR EvolutionaryTrace; P39081; -. DR PRO; PR:P39081; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; P39081; Protein. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005849; C:mRNA cleavage factor complex; IPI:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0003729; F:mRNA binding; IDA:SGD. DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:SGD. DR GO; GO:0006378; P:mRNA polyadenylation; IDA:ComplexPortal. DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IDA:SGD. DR GO; GO:0030847; P:termination of RNA polymerase II transcription, exosome-dependent; IMP:SGD. DR GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IMP:SGD. DR CDD; cd16982; CID_Pcf11; 1. DR Gene3D; 1.25.40.90; -; 1. DR InterPro; IPR006569; CID_dom. DR InterPro; IPR008942; ENTH_VHS. DR InterPro; IPR045154; PCF11-like. DR InterPro; IPR047415; Pcf11_CID. DR InterPro; IPR021605; Pcf11_Clp1-ID. DR PANTHER; PTHR15921:SF3; PRE-MRNA CLEAVAGE COMPLEX 2 PROTEIN PCF11; 1. DR PANTHER; PTHR15921; PRE-MRNA CLEAVAGE COMPLEX II; 1. DR Pfam; PF11526; CFIA_Pcf11; 1. DR Pfam; PF04818; CID; 1. DR SMART; SM00582; RPR; 1. DR SUPFAM; SSF48464; ENTH/VHS domain; 1. DR PROSITE; PS51391; CID; 1. PE 1: Evidence at protein level; KW 3D-structure; mRNA processing; Nucleus; Reference proteome; RNA-binding; KW Transcription; Transcription regulation; Transcription termination. FT CHAIN 1..626 FT /note="Protein PCF11" FT /id="PRO_0000058247" FT DOMAIN 4..139 FT /note="CID" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724" FT REGION 1..130 FT /note="Interaction with RBP1 CTD (CID)" FT REGION 263..286 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MUTAGEN 66 FT /note="A->D: Loss of interaction with RBP1 CTD." FT /evidence="ECO:0000269|PubMed:12727883" FT MUTAGEN 68..70 FT /note="DSI->AAA: Loss of interaction with RBP1 CTD." FT /evidence="ECO:0000269|PubMed:12727883" FT CONFLICT 286..288 FT /note="NSL -> ILS (in Ref. 3; AAC33145)" FT /evidence="ECO:0000305" FT CONFLICT 515 FT /note="I -> V (in Ref. 3; AAC33145)" FT /evidence="ECO:0000305" FT HELIX 3..16 FT /evidence="ECO:0007829|PDB:1SZ9" FT HELIX 24..36 FT /evidence="ECO:0007829|PDB:1SZ9" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:1SZ9" FT HELIX 41..54 FT /evidence="ECO:0007829|PDB:1SZ9" FT HELIX 57..73 FT /evidence="ECO:0007829|PDB:1SZ9" FT HELIX 78..83 FT /evidence="ECO:0007829|PDB:1SZ9" FT HELIX 86..95 FT /evidence="ECO:0007829|PDB:1SZ9" FT HELIX 99..112 FT /evidence="ECO:0007829|PDB:1SZ9" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:1SZ9" FT HELIX 125..137 FT /evidence="ECO:0007829|PDB:1SZ9" FT HELIX 486..490 FT /evidence="ECO:0007829|PDB:4OI4" FT HELIX 495..498 FT /evidence="ECO:0007829|PDB:4OI4" FT HELIX 543..547 FT /evidence="ECO:0007829|PDB:2NAX" FT STRAND 550..553 FT /evidence="ECO:0007829|PDB:2NAX" FT TURN 555..557 FT /evidence="ECO:0007829|PDB:5M9Z" FT STRAND 561..564 FT /evidence="ECO:0007829|PDB:2NAX" FT TURN 565..568 FT /evidence="ECO:0007829|PDB:2NAX" FT STRAND 569..576 FT /evidence="ECO:0007829|PDB:2NAX" FT TURN 577..580 FT /evidence="ECO:0007829|PDB:2NAX" FT STRAND 581..585 FT /evidence="ECO:0007829|PDB:2NAX" FT STRAND 587..590 FT /evidence="ECO:0007829|PDB:2NAX" FT STRAND 593..596 FT /evidence="ECO:0007829|PDB:2NAX" FT HELIX 597..603 FT /evidence="ECO:0007829|PDB:2NAX" SQ SEQUENCE 626 AA; 71898 MW; 66F91BA9577E82F1 CRC64; MDHDTEVIVK DFNSILEELT FNSRPIITTL TKLAEENISC AQYFVDAIES RIEKCMPKQK LYAFYALDSI CKNVGSPYTI YFSRNLFNLY KRTYLLVDNT TRTKLINMFK LWLNPNDTGL PLFEGSALEK IEQFLIKASA LHQKNLQAML PTPTVPLLLR DIDKLTCLTS ERLKNQPNDE KLKMKLLVLS QLKQELKREK LTLNALKQVQ MQLRQVFSQD QQVLQERMRY HELQQQQQQQ QQQQQQQQQQ QQQYHETKDM VGSYTQNSNS AIPLFGNNSD TTNQQNSLSS SLFGNISGVE SFQEIEKKKS LNKINNLYAS LKAEGLIYTP PKESIVTLYK KLNGHSNYSL DSHEKQLMKN LPKIPLLNDI LSDCKAYFAT VNIDVLNNPS LQLSEQTLLQ ENPIVQNNLI HLLYRSKPNK CSVCGKRFGN SESEKLLQNE HLDWHFRINT RIKGSQNTAN TGISNSNLNT TTTRKNIQSR NWYLSDSQWA AFKDDEITST KHKNDYTDPH ANKNIDKSAL NIHADENDEG SVDNTLGSDR SNELEIRGKY VVVPETSQDM AFKCPICKET VTGVYDEESG EWVWKNTIEV NGKYFHSTCY HETSQNSSKS NSGKVGLDDL KKLVTK //