ID   CPSF2_CAEBR             Reviewed;         842 AA.
AC   A8XUS3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Probable cleavage and polyadenylation specificity factor subunit 2 {ECO:0000250|UniProtKB:O17403};
DE   AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit;
DE            Short=CPSF 100 kDa subunit;
GN   Name=cpsf-2 {ECO:0000250|UniProtKB:O17403}; ORFNames=CBG19097;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [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. {ECO:0000250|UniProtKB:Q9P2I0}.
CC   -!- SUBUNIT: CPSF is a heterotetramer composed of four distinct subunits
CC       160, 100, 70 and 30 kDa. {ECO:0000250|UniProtKB:Q9P2I0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC       metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC       {ECO:0000255}.
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DR   EMBL; HE601047; CAP36398.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XUS3; -.
DR   SMR; A8XUS3; -.
DR   STRING; 6238.CBG19097; -.
DR   PRIDE; A8XUS3; -.
DR   WormBase; CBG19097a; CBP45280; WBGene00038369; Cbr-cpsf-2.
DR   eggNOG; KOG1135; Eukaryota.
DR   HOGENOM; CLU_002227_3_0_1; -.
DR   InParanoid; A8XUS3; -.
DR   OMA; MELVENC; -.
DR   OrthoDB; 1314980at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IBA:GO_Central.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
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   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   3: Inferred from homology;
KW   mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..842
FT                   /note="Probable cleavage and polyadenylation specificity
FT                   factor subunit 2"
FT                   /id="PRO_0000372682"
FT   REGION          414..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..736
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   842 AA;  96304 MW;  EA164313DE7218DC CRC64;
     MTSIIKLKVF SGAKDEGPLC YLLQVDNDYI LLDCGWDERF ELKYFEELRP YIPKISAVLI
     SHPDPLHLGG LPYLVAKCGL TAPVYCTVPV YKMGQMFIYD LVYSHLDVEE FQHYSLDDVD
     MAFEKVEQVK YNQTVVLKGD SGVNFTAMPA GHMIGGSMWR ICRITGEDII YCVDFNHRKD
     RHLSGCSFDN FNRPHLLITG AHHISLPQMK RKDRDEQLVT KILRTVRQKG DCMIVIDTAG
     RVLELAYLLD QLWANQDAGL STYNLVMMSH VASSVVQFAK SQLEWMDEKL FRYDSSSARY
     NPFTLKNVNL VHSHLELIKI RSPKVVLCSS QDMETGFSRE LFLDWCADQR NGVILTARPA
     SFTLAARLVE LAERANDGVL RNEDKHLSLL VRKRVPLEGE ELLEYKRRKA ERDAEETRIR
     MERARRQAQA NESDDSDDDD IAAPIVPRLS EKDHRSFDAI ENDSHCFDIM AKWDNQQKAS
     FFKSTKKSFP MYPYIEEKVK WDDYGEVIKP EDYTVISKID MRKGKNKDEP VVVHKREDEE
     EVYNPNDHDE EMPTKCVEFR NRIEISCRVE FIEYEGISDG ESTKKMLAGL MPRQIIIVHG
     SRDDTRDLYA YFTDNGFKKD QLNTPVANEL IDASVESFIY QVSLSDALLA EIQFKEVSEG
     NSLAWIDARI QEKESIDNML VAGASQLTIE DSLQEDAVEV VEEDVIPMET FQDDQNKQEA
     SEENVAEGEK SNGQSKENDE NASSIPIETQ PKIRGTLILT PLPKKQIPVH QAIFVNDPKL
     SEFKNLLVDK GYKAEFFSGT LLINGGKCSI LVERLDSKWR VLSQKTFTNF GSCSTTSLLF
     CK