C3H24_ARATH
ID C3H24_ARATH Reviewed; 809 AA.
AC Q8L7S3; Q9SKM5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Zinc finger CCCH domain-containing protein 24;
DE Short=AtC3H24;
DE EC=2.1.1.-;
GN OrderedLocusNames=At2g28450; ORFNames=T1B3.3;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8L7S3-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01024}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20681.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006283; AAD20681.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08124.1; -; Genomic_DNA.
DR EMBL; AY128289; AAM91097.1; -; mRNA.
DR EMBL; BT002293; AAN72304.1; -; mRNA.
DR PIR; A84685; A84685.
DR RefSeq; NP_180412.2; NM_128405.3. [Q8L7S3-1]
DR AlphaFoldDB; Q8L7S3; -.
DR SMR; Q8L7S3; -.
DR BioGRID; 2743; 3.
DR IntAct; Q8L7S3; 3.
DR STRING; 3702.AT2G28450.1; -.
DR iPTMnet; Q8L7S3; -.
DR PaxDb; Q8L7S3; -.
DR PRIDE; Q8L7S3; -.
DR ProteomicsDB; 240383; -. [Q8L7S3-1]
DR EnsemblPlants; AT2G28450.1; AT2G28450.1; AT2G28450. [Q8L7S3-1]
DR GeneID; 817393; -.
DR Gramene; AT2G28450.1; AT2G28450.1; AT2G28450. [Q8L7S3-1]
DR KEGG; ath:AT2G28450; -.
DR Araport; AT2G28450; -.
DR TAIR; locus:2056553; AT2G28450.
DR eggNOG; KOG1677; Eukaryota.
DR eggNOG; KOG2187; Eukaryota.
DR HOGENOM; CLU_014689_4_1_1; -.
DR InParanoid; Q8L7S3; -.
DR OMA; EGSHDEY; -.
DR OrthoDB; 248059at2759; -.
DR PhylomeDB; Q8L7S3; -.
DR PRO; PR:Q8L7S3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L7S3; baseline and differential.
DR Genevisible; Q8L7S3; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR045850; TRM2_euk.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR45904; PTHR45904; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Metal-binding;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..809
FT /note="Zinc finger CCCH domain-containing protein 24"
FT /id="PRO_0000371983"
FT ZN_FING 79..107
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 732
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 536
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 586
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 704
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 809 AA; 89023 MW; 0F2B9D7E720778C1 CRC64;
METSSIEINE LPLATKTQTP PASVEPIPME TSSIDELPSS DSNATDNIEA VGEKRKRADE
DEKTNLESSD TKITTPSPWW KTSLCSYFRR EASCSHGNEC KYAHGEAELR MKPDNTWDPT
SERGKKAKAM KMSEHEEKEE DEVLFTEQMM ESIDGDEGGG GSVSVVDLSL SKCLVHLPNK
WQSDELKKFL GEQGVLYKSA KKRRGMIVGF VTFENAEQLQ SGVEILDGKT VNSSNLKIAD
VLPRTFDKND ARKSVKSARD AVTPLAYLSY ADQLEQKKTS IGQMLKKLAR NARKACPNGN
SLPQWVLTSR DRGGLACNLE GIIESPITNG YRNKCEFSVG LSLQGKPTVG FSLGSFCAGV
TAVEEPVDCP NVSKIASQYA SIFQKFIENS KFQVWNRFQH SGFWRQLTVR EGRKPGVFSN
DEDAITRIAE VMLMVQVCLT GSDEAEVATE FEELAKAFAE GARASSPTLP LTVLVVQNHS
GISNVAPPDA PLQVLAIPIS DNGTDQEQTT NVLTEARIHD HINNLRFSIS PTAFFQVNTV
TAEKLYSIAG DWADLGPDTL LFDVCCGTGT IGLTLAHRVG MVIGIEMNAS AVADAERNAT
INGISNCKFI CSKAEDVMSS LLKQYLDVTQ MEEAKPLSNA NDDLNKQIPS TEEMTNSEHV
ADQNLPPSNT QVEELQDNEQ KDSSSLEPEK TTKPQFKNVV AIVDPPRSGL HPAVIKALRT
HPRLKRLVYI SCNPETLVAN AIELCTPSFD EPDRGNKNYR GRKKIGIAAL ARHRAKSMPT
SEAFRPVKAM AVDLFPHTDH CEMVMLLER
