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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Cleavage and polyadenylation specificity factor subunit 2; AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit; Short=CPSF 100 kDa subunit;
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MyHits synonymsCPSF2_DICDI , Q55BS1 , B80C49B14F8926AE
match map segment
ismart:Lactamase_B ismart:Beta-Casp ipfam:RMMBL ipfam:CPSF100_C ipfam:Lactamase_B_6 ipfam:Beta-Casp  
Legends: 1, COMPBIAS Poly-Glu; 2, COMPBIAS Poly-Asn; 3, COMPBIAS Poly-Thr; 4, ismart:Beta-Casp [T]; 5, ipfam:RMMBL [T]; 6, ipfam:Beta-Casp [T].
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   02-NOV-2016, entry version 66.
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; Mycetozoa; Dictyosteliida; 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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
CC       specificity factor (CPSF) complex that play a key role in pre-mRNA
CC       3'-end formation, recognizing the AAUAAA signal sequence and
CC       interacting with poly(A) polymerase and other factors to bring
CC       about cleavage and poly(A) addition. {ECO:0000250}.
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}.
DR   EMBL; AAFI02000005; EAL72546.1; -; Genomic_DNA.
DR   RefSeq; XP_646760.1; XM_641668.1.
DR   ProteinModelPortal; 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   eggNOG; COG1236; LUCA.
DR   InParanoid; Q55BS1; -.
DR   KO; K14402; -.
DR   OMA; LMRNNIN; -.
DR   PhylomeDB; Q55BS1; -.
DR   Reactome; R-DDI-77595; Processing of Intronless Pre-mRNAs.
DR   PRO; PR:Q55BS1; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   Proteomes; UP000002195; Unassembled WGS sequence.
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:0006379; P:mRNA cleavage; ISS:dictyBase.
DR   GO; GO:0006378; P:mRNA polyadenylation; ISS:dictyBase.
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:SF5; PTHR11203:SF5; 2.
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    784       Cleavage and polyadenylation specificity
FT                                factor subunit 2.
FT                                /FTId=PRO_0000328361.
FT   COMPBIAS    434    439       Poly-Glu.
FT   COMPBIAS    676    695       Poly-Asn.
FT   COMPBIAS    700    706       Poly-Thr.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        17    227       ismart:Lactamase_B [T]
FT   MYHIT       247    372       ismart:Beta-Casp [T]
FT   MYHIT       551    603       ipfam:RMMBL [T]
FT   MYHIT       631    781       ipfam:CPSF100_C [T]
FT   MYHIT        22    198       ipfam:Lactamase_B_6 [T]
FT   MYHIT       247    372       ipfam:Beta-Casp [T]
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
//