CTF1_SCHPO
ID CTF1_SCHPO Reviewed; 363 AA.
AC O43040;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cleavage and termination factor 1;
DE AltName: Full=Transcription termination factor ctf1;
GN Name=ctf1; ORFNames=SPBC3B9.11c;
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 [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 [2]
RP CHARACTERIZATION.
RX PubMed=11389847; DOI=10.1016/s1097-2765(01)00235-0;
RA Aranda A., Proudfoot N.;
RT "Transcriptional termination factors for RNA polymerase II in yeast.";
RL Mol. Cell 7:1003-1011(2001).
CC -!- FUNCTION: Component of the cleavage factor I (CF I) involved in pre-
CC mRNA 3'-end processing.
CC -!- SUBUNIT: Interacts with res2.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; CU329671; CAA17791.1; -; Genomic_DNA.
DR PIR; T40350; T40350.
DR RefSeq; NP_596669.1; NM_001022591.2.
DR AlphaFoldDB; O43040; -.
DR SMR; O43040; -.
DR BioGRID; 277533; 14.
DR STRING; 4896.SPBC3B9.11c.1; -.
DR iPTMnet; O43040; -.
DR SwissPalm; O43040; -.
DR MaxQB; O43040; -.
DR PaxDb; O43040; -.
DR PRIDE; O43040; -.
DR EnsemblFungi; SPBC3B9.11c.1; SPBC3B9.11c.1:pep; SPBC3B9.11c.
DR GeneID; 2541018; -.
DR KEGG; spo:SPBC3B9.11c; -.
DR PomBase; SPBC3B9.11c; ctf1.
DR VEuPathDB; FungiDB:SPBC3B9.11c; -.
DR eggNOG; KOG0108; Eukaryota.
DR HOGENOM; CLU_028601_0_0_1; -.
DR InParanoid; O43040; -.
DR OMA; TKFRLMI; -.
DR PhylomeDB; O43040; -.
DR PRO; PR:O43040; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0033620; C:Mei2 nuclear dot complex; IDA:PomBase.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISM:PomBase.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; EXP:PomBase.
DR GO; GO:0031124; P:mRNA 3'-end processing; IPI:PomBase.
DR GO; GO:0006378; P:mRNA polyadenylation; IC:PomBase.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR Gene3D; 1.10.20.70; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR025742; CSTF2_hinge.
DR InterPro; IPR026896; CSTF_C.
DR InterPro; IPR038192; CSTF_C_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF14327; CSTF2_hinge; 1.
DR Pfam; PF14304; CSTF_C; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..363
FT /note="Cleavage and termination factor 1"
FT /id="PRO_0000081537"
FT DOMAIN 7..85
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 291..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 363 AA; 39963 MW; 66177BD3664E110C CRC64;
MSMTAGNVVF VGNIPYDVSE QQMTEIFNQV GPVKTFKLVL DPETGSGKGY GFCEFFDSET
TAMAVRKLNN SELGPRKIRV EFPSNDPRRN QSYEYTERTD RYMEQQNAHE SSYNSRFIPP
VLHSTSSLPA SQGGGMPSPA IYSSSMATNL NKNINSTSVP AYNFHNSMTS DFDSASQPHT
DAYNARTFQY NKSSQNKGDY TSGTSISNPT SIPLAPSVVQ VLSTFSAQEL LNMLSKLQTV
VHIAPEEARR LLIANPALPY AAFQAMLLMN LVDANVLQQV VVAVKNKNMH QPASATSSPP
SVPQKIPSSN HKSQQANGSD QGNEGKRMAL IQQLLALTPE QINALPPAQR DQILSIRRQH
FRQ
