CPSF_ARATH
ID CPSF_ARATH Reviewed; 631 AA.
AC A9LNK9; Q9S9Q5; Q9S9Q6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=30-kDa cleavage and polyadenylation specificity factor 30 {ECO:0000303|PubMed:18479511};
DE EC=3.1.21.- {ECO:0000269|PubMed:17576667};
DE AltName: Full=Protein OXIDATIVE STRESS TOLERANT 6 {ECO:0000303|PubMed:18545667};
DE AltName: Full=Zinc finger CCCH domain-containing protein 11;
DE Short=AtC3H11;
GN Name=CPSF30 {ECO:0000303|PubMed:18479511};
GN Synonyms=OXT6 {ECO:0000303|PubMed:18545667};
GN OrderedLocusNames=At1g30460 {ECO:0000312|Araport:AT1G30460};
GN ORFNames=F26G16.5 {ECO:0000312|EMBL:AAF19746.1},
GN F26G16.6 {ECO:0000312|EMBL:AAF19747.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=16500995; DOI=10.1104/pp.105.070672;
RA Delaney K.J., Xu R., Zhang J., Li Q.Q., Yun K.-Y., Falcone D.L., Hunt A.G.;
RT "Calmodulin interacts with and regulates the RNA-binding activity of an
RT Arabidopsis polyadenylation factor subunit.";
RL Plant Physiol. 140:1507-1521(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=16897494; DOI=10.1007/s11103-006-0051-6;
RA Xu R., Zhao H., Dinkins R.D., Cheng X., Carberry G., Li Q.Q.;
RT "The 73 kD subunit of the cleavage and polyadenylation specificity factor
RT (CPSF) complex affects reproductive development in Arabidopsis.";
RL Plant Mol. Biol. 61:799-815(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP GENE FAMILY, AND INTERACTION WITH FIPS5.
RX PubMed=16282318; DOI=10.1074/jbc.m510964200;
RA Forbes K.P., Addepalli B., Hunt A.G.;
RT "An Arabidopsis Fip1 homolog interacts with RNA and provides conceptual
RT links with a number of other polyadenylation factor subunits.";
RL J. Biol. Chem. 281:176-186(2006).
RN [6]
RP FUNCTION, RNA-BINDING, MUTAGENESIS OF 80-CYS--PHE-86; 108-CYS--HIS-112 AND
RP 134-CYS--HIS-138, ACTIVITY REGULATION, AND INTERACTION WITH FIPS5.
RX PubMed=17576667; DOI=10.1093/nar/gkm457;
RA Addepalli B., Hunt A.G.;
RT "A novel endonuclease activity associated with the Arabidopsis ortholog of
RT the 30-kDa subunit of cleavage and polyadenylation specificity factor.";
RL Nucleic Acids Res. 35:4453-4463(2007).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=18331819; DOI=10.1016/j.abb.2008.02.027;
RA Addepalli B., Hunt A.G.;
RT "Redox and heavy metal effects on the biochemical activities of an
RT Arabidopsis polyadenylation factor subunit.";
RL Arch. Biochem. Biophys. 473:88-95(2008).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY METHYL
RP VIOLOGEN.
RX PubMed=18545667; DOI=10.1371/journal.pone.0002410;
RA Zhang J., Addepalli B., Yun K.Y., Hunt A.G., Xu R., Rao S., Li Q.Q.,
RA Falcone D.L.;
RT "A polyadenylation factor subunit implicated in regulating oxidative
RT signaling in Arabidopsis thaliana.";
RL PLoS ONE 3:E2410-E2410(2008).
RN [9]
RP NOMENCLATURE.
RX PubMed=18221561; DOI=10.1186/1471-2164-9-44;
RA Wang D., Guo Y., Wu C., Yang G., Li Y., Zheng C.;
RT "Genome-wide analysis of CCCH zinc finger family in Arabidopsis and rice.";
RL BMC Genomics 9:44-44(2008).
RN [10]
RP SUBUNIT, HOMODIMER, INTERACTION WITH CPSF100; CPSF160; CFIS2; CLPS3;
RP CSTF77; CSTF50; PAPS2; PAPS3; PCFS1; PCFS4; FIPS3 AND FIPS5, GENE FAMILY,
RP AND NOMENCLATURE.
RX PubMed=18479511; DOI=10.1186/1471-2164-9-220;
RA Hunt A.G., Xu R., Addepalli B., Rao S., Forbes K.P., Meeks L.R., Xing D.,
RA Mo M., Zhao H., Bandyopadhyay A., Dampanaboina L., Marion A.,
RA Von Lanken C., Li Q.Q.;
RT "Arabidopsis mRNA polyadenylation machinery: comprehensive analysis of
RT protein-protein interactions and gene expression profiling.";
RL BMC Genomics 9:220-220(2008).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CPSF73-I; CPSF73-II; CPSF100 AND
RP CPSF160.
RX PubMed=19573236; DOI=10.1186/1471-2121-10-51;
RA Rao S., Dinkins R.D., Hunt A.G.;
RT "Distinctive interactions of the Arabidopsis homolog of the 30 kD subunit
RT of the cleavage and polyadenylation specificity factor (AtCPSF30) with
RT other polyadenylation factor subunits.";
RL BMC Cell Biol. 10:51-51(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610 AND SER-612, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [13]
RP INTERACTION WITH CSTF77, AND RNA-BINDING.
RX PubMed=20214900; DOI=10.1016/j.febslet.2010.03.007;
RA Bell S.A., Hunt A.G.;
RT "The Arabidopsis ortholog of the 77 kDa subunit of the cleavage stimulatory
RT factor (AtCstF-77) involved in mRNA polyadenylation is an RNA-binding
RT protein.";
RL FEBS Lett. 584:1449-1454(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF 134-CYS--HIS-138.
RX PubMed=20888817; DOI=10.1016/j.febslet.2010.09.043;
RA Addepalli B., Limbach P.A., Hunt A.G.;
RT "A disulfide linkage in a CCCH zinc finger motif of an Arabidopsis CPSF30
RT ortholog.";
RL FEBS Lett. 584:4408-4412(2010).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23136375; DOI=10.1105/tpc.112.096107;
RA Thomas P.E., Wu X., Liu M., Gaffney B., Ji G., Li Q.Q., Hunt A.G.;
RT "Genome-wide control of polyadenylation site choice by CPSF30 in
RT Arabidopsis.";
RL Plant Cell 24:4376-4388(2012).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=24706550; DOI=10.1104/pp.114.236083;
RA Bruggeman Q., Garmier M., de Bont L., Soubigou-Taconnat L., Mazubert C.,
RA Benhamed M., Raynaud C., Bergounioux C., Delarue M.;
RT "The polyadenylation factor subunit CLEAVAGE AND POLYADENYLATION
RT SPECIFICITY FACTOR30: A key factor of programmed cell death and a regulator
RT of immunity in Arabidopsis.";
RL Plant Physiol. 165:732-746(2014).
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. May interact with poly(A) polymerase and other factors to
CC bring about cleavage and poly(A) addition (By similarity). Mediates
CC poly(A) site selection (PubMed:23136375). Binds RNA in a calcium-
CC dependent manner (PubMed:16500995, PubMed:17576667, PubMed:20214900).
CC Exhibits endonuclease activity with an ability to nick and degrade
CC linear as well as circular single-stranded RNA that leaves RNA 3' ends
CC with hydroxyl groups, thus mediating processing of the pre-mRNA as a
CC prelude to the polyadenylation (PubMed:17576667). Involved in the post-
CC transcriptional control, probably via poly(A) addition, of the
CC responses of plants to stress, especially genes mediating tolerance to
CC oxidative stress (PubMed:18545667). Plays a role in the regulation of
CC salicylic acid (SA) production via the control of messenger RNA 3' end
CC processing, thus being a key component of programmed cell death and
CC plant immune responses required for resistance to virulent Pseudomonas
CC syringae pv tomato DC3000 (Pst) (PubMed:24706550).
CC {ECO:0000250|UniProtKB:O95639, ECO:0000269|PubMed:16500995,
CC ECO:0000269|PubMed:17576667, ECO:0000269|PubMed:18545667,
CC ECO:0000269|PubMed:20214900, ECO:0000269|PubMed:23136375,
CC ECO:0000269|PubMed:24706550}.
CC -!- ACTIVITY REGULATION: Endonuclease activity is repressed by the N-
CC terminal domain of FIPS5 (PubMed:17576667). Nuclease activity is
CC inhibited by zinc (>100 uM), cadmium in a progressive manner (50
CC percent activity at 1 mM Cd(2+)), and high salt levels (e.g. KCl or
CC NaCl >600 mM). Stimulated by ATP in the presence of Zn(2+), even at
CC inhibitory zinc concentrations. Elevated temperatures prevent RNA-
CC binding at 55 degrees Celsius, but endonuclease activity at 70 degrees
CC Celsius. The sulfhydryl reagent dithiothreitol (DTT) inhibits both RNA-
CC binding and nuclease activities (PubMed:18331819).
CC {ECO:0000269|PubMed:17576667, ECO:0000269|PubMed:18331819}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex (Probable). Can form homodimers
CC (PubMed:18479511). Binds to calmodulin (PubMed:16500995,
CC PubMed:16897494). Forms a complex with cleavage and polyadenylation
CC specificity factor (CPSF) subunits CPSF73-I, CPSF73-II, CPSF100,
CC CPSF160, CFIS2, FIPS3, FIPS5, PAPS2, PAPS3, CLPS3, PCFS1, PCFS4, CSTF50
CC and CSTF77 (PubMed:16282318, PubMed:18479511, PubMed:20214900,
CC PubMed:17576667, PubMed:19573236). {ECO:0000269|PubMed:16282318,
CC ECO:0000269|PubMed:16500995, ECO:0000269|PubMed:16897494,
CC ECO:0000269|PubMed:17576667, ECO:0000269|PubMed:18479511,
CC ECO:0000269|PubMed:19573236, ECO:0000269|PubMed:20214900, ECO:0000305}.
CC -!- INTERACTION:
CC A9LNK9; Q9LKF9: CPSF100; NbExp=3; IntAct=EBI-962511, EBI-1775444;
CC A9LNK9; Q8GUP1: CSTF77; NbExp=2; IntAct=EBI-962511, EBI-1775543;
CC A9LNK9; F4KDH9: FIPS5; NbExp=3; IntAct=EBI-962511, EBI-962489;
CC A9LNK9; O80438: MAK3; NbExp=3; IntAct=EBI-962511, EBI-15205450;
CC A9LNK9; Q8VY64: NFYA4; NbExp=4; IntAct=EBI-962511, EBI-4461713;
CC A9LNK9; O82312: PAPS2; NbExp=3; IntAct=EBI-962511, EBI-1775513;
CC A9LNK9; O82239: RFI2; NbExp=3; IntAct=EBI-962511, EBI-4425094;
CC A9LNK9; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-962511, EBI-4424877;
CC A9LNK9; Q93Z00: TCP14; NbExp=3; IntAct=EBI-962511, EBI-4424563;
CC A9LNK9; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-962511, EBI-4426144;
CC A9LNK9; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-962511, EBI-15192297;
CC A9LNK9; Q8LPR5: TCP4; NbExp=4; IntAct=EBI-962511, EBI-15192325;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16500995,
CC ECO:0000269|PubMed:19573236}. Cytoplasm {ECO:0000269|PubMed:19573236}.
CC Note=Localized in the cytoplasm when not in complex or when associated
CC with CPSF100, but move to the nucleus when associated with the cleavage
CC and polyadenylation specificity factor (CPSF) subunits CPSF160 or
CC CPSF73s. {ECO:0000269|PubMed:19573236}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AtCPSF30-YT521B;
CC IsoId=A9LNK9-1; Sequence=Displayed;
CC Name=2; Synonyms=AtCPSF30;
CC IsoId=A9LNK9-2; Sequence=VSP_037127, VSP_037128;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, siliques,
CC stems and flowers. {ECO:0000269|PubMed:16897494,
CC ECO:0000269|PubMed:18545667}.
CC -!- INDUCTION: Isoform 2 is up-regulated by exposure to the oxidative agent
CC methyl viologen (MV). {ECO:0000269|PubMed:18545667}.
CC -!- DISRUPTION PHENOTYPE: In oxt6, small plants, especially at temperatures
CC above 22 degrees Celsius. Enhanced tolerance to oxidative stress
CC associated with elevated constitutive expression of genes that encode
CC proteins containing thioredoxin- and glutaredoxin- related domains
CC (PubMed:18545667). Altered poly(A) site choice (PubMed:18545667,
CC PubMed:23136375). Suppresses cell death in lesion-mimic mutants (e.g.
CC mips1, lsd1, mkk4, cpr5, and cat2). Enhanced sensitivity to virulent
CC Pseudomonas syringae pv tomato DC3000 (Pst) (PubMed:24706550).
CC {ECO:0000269|PubMed:18545667, ECO:0000269|PubMed:23136375,
CC ECO:0000269|PubMed:24706550}.
CC -!- SIMILARITY: Belongs to the CPSF4/YTH1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19746.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EU250988; ABX26048.1; -; mRNA.
DR EMBL; AY140901; AAN41459.1; -; mRNA.
DR EMBL; AC009917; AAF19746.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC009917; AAF19747.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31221.1; -; Genomic_DNA.
DR PIR; B86429; B86429.
DR PIR; C86429; C86429.
DR RefSeq; NP_174334.2; NM_102782.4. [A9LNK9-1]
DR PDB; 5ZUU; X-ray; 1.95 A; A/B/C/D=221-400.
DR PDBsum; 5ZUU; -.
DR AlphaFoldDB; A9LNK9; -.
DR SMR; A9LNK9; -.
DR BioGRID; 25160; 50.
DR IntAct; A9LNK9; 49.
DR MINT; A9LNK9; -.
DR STRING; 3702.AT1G30460.1; -.
DR iPTMnet; A9LNK9; -.
DR PaxDb; A9LNK9; -.
DR PRIDE; A9LNK9; -.
DR ProteomicsDB; 220550; -. [A9LNK9-1]
DR EnsemblPlants; AT1G30460.1; AT1G30460.1; AT1G30460. [A9LNK9-1]
DR GeneID; 839925; -.
DR Gramene; AT1G30460.1; AT1G30460.1; AT1G30460. [A9LNK9-1]
DR KEGG; ath:AT1G30460; -.
DR Araport; AT1G30460; -.
DR TAIR; locus:2028175; AT1G30460.
DR eggNOG; KOG1040; Eukaryota.
DR eggNOG; KOG1902; Eukaryota.
DR HOGENOM; CLU_413563_0_0_1; -.
DR InParanoid; A9LNK9; -.
DR OMA; VGMAPFM; -.
DR OrthoDB; 688490at2759; -.
DR PhylomeDB; A9LNK9; -.
DR PRO; PR:A9LNK9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A9LNK9; baseline and differential.
DR Genevisible; A9LNK9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IDA:TAIR.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IMP:TAIR.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0034052; P:positive regulation of plant-type hypersensitive response; IMP:UniProtKB.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IMP:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:1900363; P:regulation of mRNA polyadenylation; IMP:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:0006396; P:RNA processing; IDA:TAIR.
DR InterPro; IPR007275; YTH_domain.
DR InterPro; IPR045168; YTH_prot.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12357; PTHR12357; 1.
DR Pfam; PF04146; YTH; 2.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50882; YTH; 1.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm; DNA-binding;
KW Endonuclease; Hydrolase; Hypersensitive response; Metal-binding;
KW mRNA processing; Nuclease; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..631
FT /note="30-kDa cleavage and polyadenylation specificity
FT factor 30"
FT /id="PRO_0000371970"
FT DOMAIN 237..372
FT /note="YTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT ZN_FING 60..87
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 88..112
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 114..141
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 12..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..432
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 239..250
FT /note="YFVVKSNNRENF -> CVQSPKVFNWVL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16897494"
FT /id="VSP_037127"
FT VAR_SEQ 251..631
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16897494"
FT /id="VSP_037128"
FT MUTAGEN 80..86
FT /note="CGFLHQF->STFLYQ: Loss of RNA-binding, but normal
FT endonuclease activity."
FT /evidence="ECO:0000269|PubMed:17576667"
FT MUTAGEN 108..112
FT /note="CVYKH->QDSTYKY: Reduced endonuclease activity, but
FT slightly increased RNA-binding."
FT /evidence="ECO:0000269|PubMed:17576667"
FT MUTAGEN 134..138
FT /note="CRYRH->STYRY: Loss of endonuclease activity, slighty
FT reduced RNA-binding, and loss of interaction with FIPS5."
FT /evidence="ECO:0000269|PubMed:17576667,
FT ECO:0000269|PubMed:20888817"
FT STRAND 234..245
FT /evidence="ECO:0007829|PDB:5ZUU"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:5ZUU"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:5ZUU"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:5ZUU"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:5ZUU"
FT STRAND 288..297
FT /evidence="ECO:0007829|PDB:5ZUU"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:5ZUU"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:5ZUU"
FT STRAND 323..334
FT /evidence="ECO:0007829|PDB:5ZUU"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:5ZUU"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:5ZUU"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:5ZUU"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:5ZUU"
FT HELIX 380..392
FT /evidence="ECO:0007829|PDB:5ZUU"
SQ SEQUENCE 631 AA; 70015 MW; 120272CD4142355F CRC64;
MEDADGLSFD FEGGLDSGPV QNTASVPVAP PENSSSAAVN VAPTYDHSSA TVAGAGRGRS
FRQTVCRHWL RGLCMKGDAC GFLHQFDKAR MPICRFFRLY GECREQDCVY KHTNEDIKEC
NMYKLGFCPN GPDCRYRHAK LPGPPPPVEE VLQKIQQLTT YNYGTNRLYQ ARNVAPQLQD
RPQGQVPMQG QPQESGNLQQ QQQQQPQQSQ HQVSQTLIPN PADQTNRTSH PLPQGVNRYF
VVKSNNRENF ELSVQQGVWA TQRSNEAKLN EAFDSVENVI LIFSVNRTRH FQGCAKMTSR
IGGYIGGGNW KHEHGTAQYG RNFSVKWLKL CELSFHKTRN LRNPYNENLP VKISRDCQEL
EPSVGEQLAS LLYLEPDSEL MAISIAAEAK REEEKAKGVN PESRAENPDI VPFEDNEEEE
EEEDESEEEE ESMAGGPQGR GRGRGIMWPP QMPLGRGIRP MPGMGGFPLG VMGPGDAFPY
GPGGYNGMPD PFGMGPRPFG PYGPRFGGDF RGPVPGMMFP GRPPQQFPHG GYGMMGGGRG
PHMGGMGNAP RGGRPMYYPP ATSSARPGPS NRKTPERSDE RGVSGDQQNQ DASHDMEQFE
VGNSLRNEES ESEDEDEAPR RSRHGEGKKR R
