CFT2_SCHPO
ID CFT2_SCHPO Reviewed; 797 AA.
AC O74740;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cleavage factor two protein 2;
GN Name=cft2; ORFNames=SPBC1709.15c;
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 IDENTIFICATION IN THE CPF COMPLEX.
RX PubMed=14617822; DOI=10.1074/mcp.m300081-mcp200;
RA Roguev A., Shevchenko A., Schaft D., Thomas H., Stewart A.F.,
RA Shevchenko A.;
RT "A comparative analysis of an orthologous proteomic environment in the
RT yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.";
RL Mol. Cell. Proteomics 3:125-132(2004).
RN [3]
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. May be involved in
CC poly(A)-site recognition. May be involved in the association of the
CC CPF, CPFIA and RNA polymerase II complexes (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation factor (CPF)
CC complex, which is composed of cft1, cft2, ysh1, pta1, swd2, pfs2, dis2,
CC yth1, ssu72, and fip1. {ECO:0000269|PubMed:14617822}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAA21254.1; -; Genomic_DNA.
DR PIR; T39643; T39643.
DR RefSeq; NP_595448.1; NM_001021357.2.
DR AlphaFoldDB; O74740; -.
DR SMR; O74740; -.
DR BioGRID; 276498; 7.
DR STRING; 4896.SPBC1709.15c.1; -.
DR iPTMnet; O74740; -.
DR MaxQB; O74740; -.
DR PaxDb; O74740; -.
DR PRIDE; O74740; -.
DR EnsemblFungi; SPBC1709.15c.1; SPBC1709.15c.1:pep; SPBC1709.15c.
DR GeneID; 2539954; -.
DR KEGG; spo:SPBC1709.15c; -.
DR PomBase; SPBC1709.15c; cft2.
DR VEuPathDB; FungiDB:SPBC1709.15c; -.
DR eggNOG; KOG1135; Eukaryota.
DR HOGENOM; CLU_002227_3_0_1; -.
DR InParanoid; O74740; -.
DR OMA; MELVENC; -.
DR PhylomeDB; O74740; -.
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:O74740; -.
DR Proteomes; UP000002485; Chromosome II.
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; IBA:GO_Central.
DR GO; GO:0006379; P:mRNA cleavage; ISO:PomBase.
DR GO; GO:0006378; P:mRNA polyadenylation; ISO:PomBase.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR CDD; cd16293; CPSF2-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
DR InterPro; IPR035639; CPSF2_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR PANTHER; PTHR45922; PTHR45922; 1.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF13299; CPSF100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Reference proteome.
FT CHAIN 1..797
FT /note="Cleavage factor two protein 2"
FT /id="PRO_0000339461"
FT REGION 519..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 89451 MW; 33B3F9F4F415B47C CRC64;
MLNYQCLETD SYCGTSHIEL DGIHIYIDPG SDDSLKHPEV PEQPDLILLS HSDLAHIGGL
VYAYYKYDWK NAYIYATLPT INMGRMTMLD AIKSNYISDM SKADVDAVFD SIIPLRYQQP
TLLLGKCSGL TITAYNAGHT LGGTLWSLIK ESESVLYAVD WNHSKDKHLN GAALYSNGHI
LEALNRPNTL ITDANNSLVS IPSRKKRDEA FIESVMSSLL KGGTVLLPVD AASRVLELCC
ILDNHWSASQ PPLPFPILFL SPTSTKTIDY AKSMIEWMGD NIVRDFGINE NLLEFRNINT
ITDFSQISHI GPGPKVILAT ALTLECGFSQ RILLDLMSEN SNDLILFTQR SRCPQNSLAN
QFIRYWERAS KKKRDIPHPV GLYAEQAVKI KTKEPLEGEE LRSYQELEFS KRNKDAEDTA
LEFRNRTILD EDLSSSSSSE DDDLDLNTEV PHVALGSSAF LMGKSFDLNL RDPAVQALHT
KYKMFPYIEK RRRIDEYGEI IKHQDFSMIN EPANTLELEN DSDDNALSNS NGKRKWSEIN
DGLQQKKEEE DEDEVPSKII TDEKTIRVSC QVQFIDIEGL HDGRSLKTII PQVNPRRLVL
IHASTEEKED MKKTCASLSA FTKDVYIPNY GEIINVSIDV NAFSLKLADD LIKNLIWTKV
GNCEVSHMLA KVEISKPSEE EDKKEEVEKK DGDKERNEEK KEEKETLPVL NALTLRSDLA
RAPRAAPLLV GNIRLAYLRK ALLDQGISAE LKGEGVLLCG GAVAVRKLSG GKISVEGSLS
NRFFEIRKLV YDALAVV
