CPSF2_ORYSJ
ID CPSF2_ORYSJ Reviewed; 738 AA.
AC Q652P4; Q0IZH3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 OrderedLocusNames=Os09g0569400, LOC_Os09g39590; ORFNames=OJ1003_C09.22;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(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}.
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:0000250}.
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; AP005546; BAD46223.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF25892.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT09500.1; -; Genomic_DNA.
DR EMBL; AK063384; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK070608; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015611669.1; XM_015756183.1.
DR AlphaFoldDB; Q652P4; -.
DR SMR; Q652P4; -.
DR STRING; 4530.OS09T0569400-01; -.
DR PaxDb; Q652P4; -.
DR PRIDE; Q652P4; -.
DR EnsemblPlants; Os09t0569400-01; Os09t0569400-01; Os09g0569400.
DR GeneID; 4347905; -.
DR Gramene; Os09t0569400-01; Os09t0569400-01; Os09g0569400.
DR KEGG; osa:4347905; -.
DR eggNOG; KOG1135; Eukaryota.
DR HOGENOM; CLU_002227_3_0_1; -.
DR InParanoid; Q652P4; -.
DR OMA; MELVENC; -.
DR OrthoDB; 1314980at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; Q652P4; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblPlants.
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:0035194; P:post-transcriptional gene silencing by RNA; IEA:EnsemblPlants.
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 2: Evidence at transcript level;
KW mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..738
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 2"
FT /id="PRO_0000247467"
FT CONFLICT 244
FT /note="E -> G (in Ref. 4; AK070608)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="V -> M (in Ref. 4; AK063384)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="F -> Y (in Ref. 4; AK070608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 738 AA; 81376 MW; C1E73ED421902309 CRC64;
MGTSVQVTPL SGAYGEGPLC YLLAVDGFRF LLDCGWTDLC DPSHLQPLAK VAPTIDAVLL
SHADTMHLGA LPYAMKHLGL SAPVYATEPV FRLGILTLYD YFISRRQVSD FDLFTLDDID
AAFQNVVRLK YSQNHLLNDK GEGIVIAPHV AGHDLGGTVW KITKDGEDVV YAVDFNHRKE
RHLNGTALGS FVRPAVLITD AYNALNNHVY KRQQDQDFID ALVKVLTGGG SVLLPIDTAG
RVLEILLILE QYWAQRHLIY PIYFLTNVST STVDYVKSFL EWMNDSISKS FEHTRDNAFL
LKCVTQIINK DELEKLGDAP KVVLASMASL EVGFSHDIFV DMANEAKNLV LFTEKGQFGT
LARMLQVDPP PKAVKVTMSK RIPLVGDELK AYEEEQERIK KEEALKASLN KEEEKKASLG
SNAKASDPMV IDASTSRKPS NAGSKFGGNV DILIDGFVPP SSSVAPMFPF FENTSEWDDF
GEVINPEDYL MKQEEMDNTL MPGAGDGMDS MLDEGSARLL LDSTPSKVIS NEMTVQVKCS
LAYMDFEGRS DGRSVKSVIA HVAPLKLVLV HGSAEATEHL KMHCSKNSDL HVYAPQIEET
IDVTSDLCAY KVQLSEKLMS NVISKKLGEH EIAWVDAEVG KTDDKLTLLP PSSTPAAHKS
VLVGDLKLAD FKQFLANKGL QVEFAGGALR CGEYITLRKI GDAGQKGSTG SQQIVIEGPL
CEDYYKIREL LYSQFYLL
