ID   CFT1_SCHPO              Reviewed;        1441 AA.
AC   O74733;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Protein cft1;
DE   AltName: Full=Cleavage factor two protein 1;
GN   Name=cft1; ORFNames=SPBC1709.08;
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   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: RNA-binding component of the cleavage and polyadenylation
CC       factor (CPF) complex, which plays a key role in polyadenylation-
CC       dependent pre-mRNA 3'-end formation and cooperates with cleavage
CC       factors including the CFIA complex and NAB4/CFIB. Involved in poly(A)
CC       site recognition. May be involved in coupling transcription termination
CC       and mRNA 3'-end formation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the CFT1 family. {ECO:0000305}.
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; CU329671; CAA21247.1; -; Genomic_DNA.
DR   PIR; T39636; T39636.
DR   RefSeq; NP_595441.1; NM_001021350.2.
DR   AlphaFoldDB; O74733; -.
DR   SMR; O74733; -.
DR   BioGRID; 276248; 20.
DR   IntAct; O74733; 1.
DR   STRING; 4896.SPBC1709.08.1; -.
DR   iPTMnet; O74733; -.
DR   MaxQB; O74733; -.
DR   PaxDb; O74733; -.
DR   PRIDE; O74733; -.
DR   EnsemblFungi; SPBC1709.08.1; SPBC1709.08.1:pep; SPBC1709.08.
DR   GeneID; 2539694; -.
DR   KEGG; spo:SPBC1709.08; -.
DR   PomBase; SPBC1709.08; cft1.
DR   VEuPathDB; FungiDB:SPBC1709.08; -.
DR   eggNOG; KOG1896; Eukaryota.
DR   HOGENOM; CLU_002414_0_0_1; -.
DR   InParanoid; O74733; -.
DR   OMA; PMTKFKL; -.
DR   PhylomeDB; O74733; -.
DR   Reactome; R-SPO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR   Reactome; R-SPO-72187; mRNA 3'-end processing.
DR   Reactome; R-SPO-77595; Processing of Intronless Pre-mRNAs.
DR   PRO; PR:O74733; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006379; P:mRNA cleavage; ISO:PomBase.
DR   GO; GO:0006378; P:mRNA polyadenylation; ISO:PomBase.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR   InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..1441
FT                   /note="Protein cft1"
FT                   /id="PRO_0000290635"
FT   REGION          741..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1441 AA;  160301 MW;  C89EE516A10C686B CRC64;
     MSTIFQDLVD STVIKNAVQG QFTSLVSNNL VVSKVNSLHL FEIEKIQKDE SSFPLDDSLQ
     NEFSTSIIDE SQAFMETNMH LIRTNEQTTY VLRLVSQVKV FGTITEISAL KGKGSNGCDL
     LIMLTDYAKV STLEWDMQSQ SFVTNSLHYY EDVKSSNICS SHTPTQLLVD PDSDCCLLRF
     LTDMMAIIPY PANEDLDMEE AAIENSKISS SYAYKPSFVL ASSQLDASIS RILDVKFLYG
     YREPTLAILY SPEQTSTVTL PLRKDTVLFS LVTLDLEQRA SAVITTIQSL PYDIYASVSI
     PTPLGGSLLL GGNELIYVDS AGRTVGIGVN SYYSKCTDFP LQDQSDFNLE LEGTIAIPLT
     SSKTETPFVV LVHTSGQFFY LDFLLDGKSV KGLSLQALDL EINDDFLKSG ITCAVPAGEN
     LVFLGSQTTD SYLLRWSRRT TNEEVRLDEG DDTLYGTNDA EMDDMLDIYE TDESVGSKRK
     IAYENGPLRL EICDVLTNIG PITDFAVGKA GSYSYFPQDN HGPLELVGTA GADGAGGLVV
     FRRNIFPLIA GEFQFDGCEA LWTVSISGKL RNMKSRIQAQ YSNPELETYL VLSKEKESFI
     FLAGETFDEV QHSDFSKDSK TLNVGSLLSG MRMVQICPTS LRVYDSNLRL TQLFNFSKKQ
     IVVSTSICDP CIIVVFLGGG IALYKMDLKS QRLIKTDLQN RLSDVKTASL VSPDSSALFA
     KLFTYNETLN AKGQIANGMN DSASETDLDI QPNHKTSNND QMGYDQSVSA DDVPEVDNTI
     VTEKNVSNLD QESLEKHPIL FALTDEGKLK VYNLADFSLL MECDVFDLPP TLFNGMESER
     TYFNKESSQE LVELLVADLG DDFKEPHLFL RSRLNEITVY KAFLYSNTDK HKNLLAFAKV
     PQETMTREFQ ANVGTPRDAE STMEKKASSS VDHLKMTALE VVGNHSAVFV TGRKPFLILS
     TLHSNAKFFP ISSNIPILSV APFHAHHAPQ GYIYVDENSF IRICKFQEDF EYDNKWPYKK
     VSLGKQINGI AYHPTKMVYA VGSAVPIEFK VTDEDGNEPY AITDDNDYLP MANTGSLDLV
     SPLTWTVIDS YEFQQFEIPL SVALVNLEVS ETTKLRKPYI AVGTSITKGE DIAVRGSTYL
     FEIIDVVPQP GRPETRHKLK LVTREEIKGT VAVVCEVDGY LLSGQGQKVI VRALEDEDHL
     VGVSFIDLGS YTLSAKCLRN LLLFGDVRQN VTFVGFAEEP YRMTLFSKGQ EALNVSAADF
     LVQGENLYFV VADTSGNLRL LAYDPENPES HSGERLVTRG DFHIGNVITA MTILPKEKKH
     QNAEYGYDTG DDFSCVMVNS DGGLQMLVPI SDRVYRRLNI IQNYLANRVN TIGGLNPKSY
     RLITSPSNLT NPTRRILDGM LIDYFTYMSV AHRHEMAHKC GVPVSTIMND LVELDEALSY
     M