ID   CPSF1_CAEBR             Reviewed;        1454 AA.
AC   A8XPU7;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Probable cleavage and polyadenylation specificity factor subunit 1 {ECO:0000250|UniProtKB:Q9N4C2};
DE   AltName: Full=Cleavage and polyadenylation specificity factor 160 kDa subunit {ECO:0000250|UniProtKB:Q9N4C2};
DE            Short=CPSF 160 kDa subunit {ECO:0000250|UniProtKB:Q9N4C2};
GN   Name=cpsf-1 {ECO:0000312|EMBL:CAP34673.1}; ORFNames=CBG16808;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP34673.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: CPSF plays a key role in pre-mRNA 3'-end formation,
CC       recognizing the AAUAAA signal sequence and interacting with
CC       poly(A)polymerase and other factors to bring about cleavage and poly(A)
CC       addition. This subunit is involved in the RNA recognition step of the
CC       polyadenylation reaction (By similarity).
CC       {ECO:0000250|UniProtKB:Q9V726}.
CC   -!- SUBUNIT: CPSF is a heterotetramer composed of four distinct subunits
CC       160 (cpsf-1), 100 (cpsf-2), 70 (cpsf-3), and 30 kDa (cpsf-4).
CC       {ECO:0000250|UniProtKB:Q9V726}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9V726}.
CC   -!- SIMILARITY: Belongs to the CPSF1 family. {ECO:0000255}.
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DR   EMBL; HE600944; CAP34673.1; -; Genomic_DNA.
DR   RefSeq; XP_002645115.1; XM_002645069.1.
DR   AlphaFoldDB; A8XPU7; -.
DR   SMR; A8XPU7; -.
DR   STRING; 6238.CBG16808; -.
DR   EnsemblMetazoa; CBG16808.1; CBG16808.1; WBGene00036642.
DR   GeneID; 8587113; -.
DR   KEGG; cbr:CBG_16808; -.
DR   CTD; 8587113; -.
DR   WormBase; CBG16808; CBP04005; WBGene00036642; Cbr-cpsf-1.
DR   eggNOG; KOG1896; Eukaryota.
DR   HOGENOM; CLU_002414_0_0_1; -.
DR   InParanoid; A8XPU7; -.
DR   OMA; PMTKFKL; -.
DR   OrthoDB; 360328at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 3.
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   mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..1454
FT                   /note="Probable cleavage and polyadenylation specificity
FT                   factor subunit 1"
FT                   /id="PRO_0000394292"
FT   REGION          810..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1454 AA;  163390 MW;  417AE5BBFF4D2913 CRC64;
     MYGYLRETDD STAINYSAYG KFLPGENTGF QLLTIGAKFL RIFRVNPYVL KEPGEDNEEW
     QQKTKLECMF SCRLLNKCQS VAVARVPQLP DQDSILMTFD DAKLSIVAVN EKERNMQTIS
     LHAFENEYLR DGFTTYFNPP IVRTDPANRC AASLVYGKHI AILPFHENSK RILSYIIPLK
     QIDPRLDNVA DMVFLEGYYE PTILFLYEPL QTTPGRACVR YDTMCIMGVS VNIVDRQFAV
     VWQTANLPMD CNSLLSIPKP LGGAVVFGSN TIVYLNQAVP PCGIVLNSCY DGFTKFPLKD
     MKHLKMTLDC STSVYMEDGR IAVGSREGDL YLLRLVTSSG GATVKSLEFS KVCDTSIAFT
     LTVCAPGHLF VGSRLGDSQL LEYTLLKVTK ESAKKQRLEQ QNPSEIELDE DDIELYGGAI
     EMQQNDDDEQ ISESLQFREL DRLLNVGPVK SMCFGRPNYM SNDLIDAKRK DPVFDLVTAS
     GHGKNGALCV HQRSMRPEII TSSLLEGAEQ LWAVGRKENE SHKYLIVSRV RSTLILELGE
     ELVELEEQLF VTNEPTVAAG ELLQGALAVQ VTSTCIALVT DGQQMQEVHI DSNFPVVQAS
     IVDPYVAVLT QNGRPLLYEL AMEPYVHLRE VNVNETSFAT FSEQISTQLT SVSIYSDASQ
     IMKKNTVDGR DEKPENAAEN GHHVAVPKIK KEIPDDDAML YGEDDDFLYG DAEEDEPMVA
     AESGESSTRL QNTRKRKRLG HDAIMSSRGG EQSDAIDPTR TYSSITHWLV VAHDNGRITI
     HSLPDLELVY QIGRFSNVPE LLVDMTVEEE EKEKKAKQTA AQEKEKETEK KKDDAKNEED
     QVNSEMKKLC EKVVEAQIVG MGINQAHPVL IAIIDEEVVL YEMFASYNPQ PGHLGVAFRK
     LPHLIGLRTS PYVNIDGKRA PFEMEMEHGK RYTLIHPFER ISSINNGVMI GGAVPTLLVY
     GAWGGMQTHQ MTIDGSIKAF TPFNNENVLH GFVYMTQQKS ELRIARMHPD FDYDMPYPVK
     KIEVGKTVHN VRYLMNSDIY AVVSSVPKPS NKIWVVMNDD KQEEIHEKDE NFVLPAPPKY
     TLNLFSSQDW AAVPNTEFEF EDMEAVTAME DVPLKSESRY GGLDTYLALA TVNNYGEEVL
     VRGRIILCEV IEVVPEPGQP TSNRKIKVLY DKEQKGPVTG LCAINGLLLS GMGQKVFIWQ
     FKDNDLMGIS FLDMHYYVYQ LHSIRTIALA LDARESMSLI RFQEENKAMS IASRDDRKCA
     QAPMASEFLV DGMHIGFLLS DEHGNITLFS YSPEAPESNG GERLTVKAAI NIGTNINAFL
     RVKGHTSLLD SSSPEERENI EQRMNTIFGS LDGSFGYIRP LTEKSYRRLH FLQTFIGSVT
     PQIAGLHIKG ARSSKPSQPI VNGRNARNLI DGDVVEQYLH LSVYDKTDLA RRLGVGRYHI
     LDDLMQLRRM AYYY