CPSF2_DICDI
ID CPSF2_DICDI Reviewed; 784 AA.
AC Q55BS1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=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=cpsf2; ORFNames=DDB_G0270392;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex that play a key role in pre-mRNA 3'-end
CC formation, 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:0000250}.
CC -!- SUBUNIT: CPSF is a heterotetramer composed of four distinct subunits
CC 160, 100, 70 and 30 kDa. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72546.1; -; Genomic_DNA.
DR RefSeq; XP_646760.1; XM_641668.1.
DR AlphaFoldDB; Q55BS1; -.
DR SMR; Q55BS1; -.
DR STRING; 44689.DDB0233700; -.
DR PaxDb; Q55BS1; -.
DR EnsemblProtists; EAL72546; EAL72546; DDB_G0270392.
DR GeneID; 8617733; -.
DR KEGG; ddi:DDB_G0270392; -.
DR dictyBase; DDB_G0270392; cpsf2.
DR eggNOG; KOG1135; Eukaryota.
DR HOGENOM; CLU_002227_1_1_1; -.
DR InParanoid; Q55BS1; -.
DR OMA; MELVENC; -.
DR PhylomeDB; Q55BS1; -.
DR Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DDI-77595; Processing of Intronless Pre-mRNAs.
DR PRO; PR:Q55BS1; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:dictyBase.
DR GO; GO:0003723; F:RNA binding; ISS:dictyBase.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IBA:GO_Central.
DR GO; GO:0006379; P:mRNA cleavage; ISS:dictyBase.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS:dictyBase.
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..784
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 2"
FT /id="PRO_0000328361"
FT REGION 676..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 89448 MW; B80C49B14F8926AE CRC64;
MASIIKFTAL SGAKDESPPC YLLEIDDFCI LLDCGLSYNL DFSLLEPLEK VAKKIDAVLL
SHSDTTHIGG LPYVVGKYGL TGTIYGTTPV LKMGTMFLYD LYENKMSQEE FQQYSLDNID
SCFGEDRFKE LSFSQHYSLS GKGKGISITP YLAGHTIGAS VWKITKGTYS IVYAIDYNHR
NEGHLDSLQL TSDILKPSLL ITDSKGVDKT LAFKKTITRD QSLFEQINRN LRDGGNVLIP
VDTAGRVLEL LLCIENYWSK NKSLALYSVV FLGRFSFSVC QFARSQLEFM SSTASVKFEQ
NIENPFSFKH IKILSSLEEL QELPDTNKVI LTSSQDLETG FSRELFIQWC SDPKTLILFT
QKIPKDSLAD KLIKQYSTPN GRGKCIEIVQ GSRVPLTGDE LLQYEMEQAK QREEKRLEQL
RKEQEEREER ERLEEEEREQ LLNATNQDQL QQLLQLQQQK ERGIIDDSMV HMKNPFENDR
FDLLDSEFKK QSMITMFPYF EKHLKWGEYG EEDDDLILRN QDKKVEEVTM EEDEIQEQEI
PKKIITQTLR LPINCKIQTI DYEGCSDGRS IKAIIQQIAP TKLVLIRGSE QQSQSIENYV
KENIRTKGIY IPSIGEQLDL TSDTNVYELL LKDSLVNTLK TSKILDYEVS YIQGKVDILD
GSNVPVLDLI QSIPINNNNN NNNNNNNNNN NNNNNTTMMT TTTTTTNGHD ESFIGDIKLS
DLKQVLVNAG IQVQFDQGIL NCGGLVYIWR DEDHGGNSII NVDGIISDEY YLIKELLYKQ
FQIV
