C3H65_ARATH
ID C3H65_ARATH Reviewed; 675 AA.
AC Q9LTS7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Zinc finger CCCH domain-containing protein 65;
DE Short=AtC3H65;
DE EC=3.1.-.-;
DE AltName: Full=Protein EMBRYO DEFECTIVE 1789;
GN Name=EMB1789; OrderedLocusNames=At5g56930; ORFNames=MHM17.4;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=18582464; DOI=10.1016/j.febslet.2008.06.029;
RA Addepalli B., Hunt A.G.;
RT "Ribonuclease activity is a common property of Arabidopsis CCCH-containing
RT zinc-finger proteins.";
RL FEBS Lett. 582:2577-2582(2008).
CC -!- FUNCTION: Possesses RNA-binding and ribonuclease activities in vitro.
CC {ECO:0000269|PubMed:18582464}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX832581; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AB024035; BAA97023.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96824.1; -; Genomic_DNA.
DR EMBL; BX832581; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_200503.1; NM_125075.3.
DR AlphaFoldDB; Q9LTS7; -.
DR STRING; 3702.AT5G56930.1; -.
DR PaxDb; Q9LTS7; -.
DR PRIDE; Q9LTS7; -.
DR EnsemblPlants; AT5G56930.1; AT5G56930.1; AT5G56930.
DR GeneID; 835795; -.
DR Gramene; AT5G56930.1; AT5G56930.1; AT5G56930.
DR KEGG; ath:AT5G56930; -.
DR Araport; AT5G56930; -.
DR TAIR; locus:2164660; AT5G56930.
DR eggNOG; KOG1040; Eukaryota.
DR HOGENOM; CLU_436393_0_0_1; -.
DR InParanoid; Q9LTS7; -.
DR OMA; TEIACEP; -.
DR OrthoDB; 392821at2759; -.
DR PhylomeDB; Q9LTS7; -.
DR PRO; PR:Q9LTS7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTS7; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR045124; Su(sable)-like.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR13119; PTHR13119; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 2: Evidence at transcript level;
KW Coiled coil; DNA-binding; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..675
FT /note="Zinc finger CCCH domain-containing protein 65"
FT /id="PRO_0000372015"
FT ZN_FING 350..377
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 384..406
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 409..432
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 294..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 314..342
FT /evidence="ECO:0000255"
FT COMPBIAS 487..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 675 AA; 73844 MW; 5E80C3904ACBF7F3 CRC64;
MESSVAPFPH RRTHLPNRNY RSLLYHFCSS FDREPQISLA TPAVLQELVL RTEIAQESPG
ETCEPPENLS ITESKLNGVS GDSSGEKVET ISQEKSLMLG DICDGIDLQD ASVVSRHTDF
FDSFELMINE TQDSVPESCV NLFEALDVND YDIVQNVLEK PNIATQVQVD PVESEKKAEE
VPKSVESNEV ISSGVLEACN GTVQREMELE KPVDNSPVLV DSVSRIVGGD DVEEGEISGD
DNDDMLVEDD ETVERHEEYQ VSQDGTGNSH LTSHKSFGVE VMNVDNQAKK IDQTFSNEAK
MDPGTSIKKR SAPSKDAKAR KRAKARIKRA QERIALGVKK LKLKPVAPKP KPIKYCRHYL
KGRCHEGDKC KFSHDTIPET KCSPCCYFAT QSCMKGDDCP FDHDLSKYPC NNFITKGFCY
RGDSCLFSHK GTPQSASDTP SANVTVSSTK ITAASFSPQK TKKQSVRDAI AKLPAIQARV
SSSVAFLKPS SHSNQRNSSD ASSSKINEHV TPPQVPPLRK PSVAPKGMSF LSLDKTSQED
TVKASSASKP NTDNSDSQTL KQSQQGSFLP LGPPKGISFL SFASEEQKTL NREPQKPASS
KNLKTTPSSH IQSSLLSAMK LAAEFESAKV ERGNNDPTEA VNKSNVTVDT AVTRNSGNIS
SKILEFLSSF SHGKN
