CPSF3_DICDI
ID CPSF3_DICDI Reviewed; 774 AA.
AC Q86A79; Q555Y4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 3;
DE Short=Cleavage and polyadenylation specificity factor 3;
DE EC=3.1.27.- {ECO:0000250|UniProtKB:Q9UKF6};
GN Name=cpsf3; ORFNames=DDB_G0274799;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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. Has endonuclease activity, and functions as mRNA 3'-
CC end-processing endonuclease (By similarity).
CC {ECO:0000250|UniProtKB:Q9UKF6}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UKF6};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9UKF6};
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex. {ECO:0000250|UniProtKB:Q9UKF6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UKF6}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF3 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000012; EAL70292.1; -; Genomic_DNA.
DR RefSeq; XP_643926.1; XM_638834.1.
DR AlphaFoldDB; Q86A79; -.
DR SMR; Q86A79; -.
DR STRING; 44689.DDB0233696; -.
DR PaxDb; Q86A79; -.
DR EnsemblProtists; EAL70292; EAL70292; DDB_G0274799.
DR GeneID; 8619353; -.
DR KEGG; ddi:DDB_G0274799; -.
DR dictyBase; DDB_G0274799; cpsf3.
DR eggNOG; KOG1137; Eukaryota.
DR HOGENOM; CLU_009673_2_3_1; -.
DR InParanoid; Q86A79; -.
DR OMA; VMIPRRC; -.
DR PhylomeDB; Q86A79; -.
DR Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DDI-77595; Processing of Intronless Pre-mRNAs.
DR PRO; PR:Q86A79; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:UniProtKB.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; ISS:UniProtKB.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR021718; CPSF73-100_C.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF11718; CPSF73-100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM01098; CPSF73-100_C; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Metal-binding; mRNA processing; Nuclease; Nucleus;
KW Reference proteome; RNA-binding; Zinc.
FT CHAIN 1..774
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 3"
FT /id="PRO_0000327796"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 423
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
SQ SEQUENCE 774 AA; 88040 MW; 6172D3A227429CC1 CRC64;
MHHNNHHHGH HGRYQHHHNQ HLKRPLKGGT EDDDILEITP IGSGSEVGRS CVLLKYKGKK
VMFDCGVHPA YSGLVSLPFF DSIESDIPDI DLLLVSHFHL DHAAAVPYFV GKTKFKGRVF
MTHPTKAIYG MLLSDYVKVS NITRDDDMLF DKSDLDRSLE KIEKVRYRQK VEHNGIKVTC
FNAGHVLGAA MFMIEIAGVK ILYTGDFSRQ EDRHLMGAET PPVKVDVLII ESTYGVQVHE
PRLEREKRFT SSVHQVVERN GKCLIPVFAL GRAQELLLIL DEYWIANPQL HHVPIYYASA
LAKKCMGVYR TYINMMNDRV RAQFDVSNPF EFKHIKNIKG IESFDDRGPC VFMASPGMLQ
SGLSRQLFER WCSDKRNGIV IPGYSVEGTL AKHIMSEPAE ITRLDNVNVP LNLTVSYVSF
SAHSDFLQTS EFIQEIQPPH VVLVHGDANE MSRLRQSLVA KFKTINVLTP KNAMSVALEF
RPEKVAKTLG SIITNPPKQN DIIQGILVTK DFTHHILSAS DIHNYTNLKT NIIKQKLTLP
FAQTYHILIS TLEQIYEQII ESTESTGGGG NEKPTITIYN EIKLIYNIGV SIILEWNSNT
VNDMICDSII ALISQIELNP LSIKVRNPNF NNIDEKEEIT KDDIEKEKEK EKEQQDGDDD
DDDEIQIKVV SRKSRKLSNK LNTITEVKLL LEQQYGNFKV DENDPLILHF NLDNQKAIIH
LETLTVESLD QILKQKIENS IKRIILSVSP IGNNLNQINN QDNENNIKME TDFK
