Entry euk:CPSF2_CAEEL

ID   CPSF2_CAEEL             Reviewed;         843 AA.
AC   O17403;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   15-MAR-2017, entry version 109.
DE   RecName: Full=Probable cleavage and polyadenylation specificity factor subunit 2;
DE   AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit;
DE            Short=CPSF 100 kDa subunit;
GN   Name=cpsf-2; ORFNames=F09G2.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION.
RX   PubMed=15790806; DOI=10.1126/science.1109267;
RA   Kim J.K., Gabel H.W., Kamath R.S., Tewari M., Pasquinelli A.,
RA   Rual J.F., Kennedy S., Dybbs M., Bertin N., Kaplan J.M., Vidal M.,
RA   Ruvkun G.;
RT   "Functional genomic analysis of RNA interference in C. elegans.";
RL   Science 308:1164-1167(2005).
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
CC       poly(A) addition. {ECO:0000269|PubMed:15790806}.
CC   -!- SUBUNIT: CPSF is a heterotetramer composed of four distinct
CC       subunits 160, 100, 70 and 30 kDa. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       RNA-metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; FO080529; CCD64424.1; -; Genomic_DNA.
DR   PIR; T32487; T32487.
DR   RefSeq; NP_504822.1; NM_072421.4.
DR   UniGene; Cel.6876; -.
DR   ProteinModelPortal; O17403; -.
DR   STRING; 6239.F09G2.4; -.
DR   iPTMnet; O17403; -.
DR   EPD; O17403; -.
DR   PaxDb; O17403; -.
DR   PeptideAtlas; O17403; -.
DR   PRIDE; O17403; -.
DR   EnsemblMetazoa; F09G2.4; F09G2.4; WBGene00017313.
DR   GeneID; 179103; -.
DR   KEGG; cel:CELE_F09G2.4; -.
DR   CTD; 179103; -.
DR   WormBase; F09G2.4; CE09299; WBGene00017313; cpsf-2.
DR   eggNOG; KOG1135; Eukaryota.
DR   eggNOG; COG1236; LUCA.
DR   GeneTree; ENSGT00870000136523; -.
DR   HOGENOM; HOG000264343; -.
DR   InParanoid; O17403; -.
DR   KO; K14402; -.
DR   OMA; LMRNNIN; -.
DR   OrthoDB; EOG091G03GG; -.
DR   PhylomeDB; O17403; -.
DR   Reactome; R-CEL-109688; Cleavage of Growing Transcript in the Termination Region.
DR   Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-CEL-72187; mRNA 3'-end processing.
DR   Reactome; R-CEL-77595; Processing of Intronless Pre-mRNAs.
DR   PRO; PR:O17403; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00017313; -.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:WormBase.
DR   GO; GO:0003723; F:RNA binding; ISS:WormBase.
DR   GO; GO:0031124; P:mRNA 3'-end processing; ISS:WormBase.
DR   GO; GO:0006379; P:mRNA cleavage; IEA:InterPro.
DR   GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR022712; Beta_Casp.
DR   InterPro; IPR027075; CPSF2.
DR   InterPro; IPR025069; Cpsf2_C.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR011108; RMMBL.
DR   PANTHER; PTHR11203:SF41; PTHR11203:SF41; 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   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 2.
PE   3: Inferred from homology;
KW   Complete proteome; mRNA processing; Nucleus; Reference proteome;
KW   RNA-binding.
FT   CHAIN         1    843       Probable cleavage and polyadenylation
FT                                specificity factor subunit 2.
FT                                /FTId=PRO_0000074396.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       642    840       ipfam:CPSF100_C [T]
FT   MYHIT       242    368       ismart:Beta-Casp [T]
FT   MYHIT       563    618       ipfam:RMMBL [T]
FT   MYHIT        22    191       ipfam:Lactamase_B_6 [T]
FT   MYHIT        17    222       ismart:Lactamase_B [T]
FT   MYHIT       242    368       ipfam:Beta-Casp [T]
SQ   SEQUENCE   843 AA;  95616 MW;  BEFBC3928DEC0976 CRC64;
     MTSIIKLKVF SGAKDEGPLC YLLQVDGDYI LLDCGWDERF GLQYFEELKP FIPKISAVLI
     SHPDPLHLGG LPYLVSKCGL TAPVYATVPV YKMGQMFIYD MVYSHLDVEE FEHYTLDDVD
     TAFEKVEQVK YNQTVVLKGD SGVHFTALPA GHMLGGSIWR ICRVTGEDIV YCVDFNHKKE
     RHLNGCSFDN FNRPHLLITG AHHISLPQMR RKDRDEQLVT KILRTVRQKG DCMIVIDTAG
     RVLELAHLLD QLWSNADAGL STYNLVMMSH VASSVVQFAK SQLEWMNEKL FKYDSSSARY
     NPFTLKHVTL CHSHQELMRV RSPKVVLCSS QDMESGFSRE LFLDWCSDPR NGVILTARPA
     SFTLAAKLVN MAERANDGVL KHEDRLISLV VKKRVALEGE ELLEYKRRKA ERDAEETRLR
     MERARRQAQA NESDDSDDDD IAAPIVPRHS EKDFRSFDGS ENDAHTFDIM AKWDNQQKAS
     FFKTTKKSFP MFPYIEEKVK WDDYGEVIKP EDYTVISKID LRKGQNKDEP VVVKKREEEE
     EVYNPNDHVE EMPTKCVEFK NRVEVSCRIE FIEYEGISDG ESTKKLLAGL LPRQIIVVHG
     SRDDTRDLVA YFADSGFDTT MLKAPEAGAL VDASVESFIY QVALSDALLA DIQFKEVSEG
     NSLAWIDARV MEKEAIDNML AVGTSNLMID DKNREEDVND QEENGATEGE GNAEPMEIGE
     NGSQESLAIS ESGKEVENGH TNDSRTKKGT KGKIRGNLIL DPLPKRLIPI HQAVFVNDPK
     LSDFKNLLTD KGYKAEFLSG TLLINGGNCS IRRNDTGVFQ MEGAFTKDYY KLRRLFYDQF
     AVL
//