ATX5_ARATH
ID ATX5_ARATH Reviewed; 1043 AA.
AC Q8GZ42; Q941G9; Q9LV06;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Histone-lysine N-methyltransferase ATX5;
DE EC=2.1.1.-;
DE AltName: Full=Protein SET DOMAIN GROUP 29;
DE AltName: Full=Trithorax-homolog protein 5;
DE Short=TRX-homolog protein 5;
GN Name=ATX5; Synonyms=SDG29, SET29; OrderedLocusNames=At5g53430;
GN ORFNames=MYN8.4;
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 637-865, AND NOMENCLATURE.
RX PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT "The Arabidopsis thaliana genome contains at least 29 active genes encoding
RT SET domain proteins that can be assigned to four evolutionarily conserved
RT classes.";
RL Nucleic Acids Res. 29:4319-4333(2001).
CC -!- FUNCTION: Histone methyltransferase. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. TRX/MLL
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97320.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB020754; BAA97320.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96353.1; -; Genomic_DNA.
DR EMBL; AK117221; BAC41897.1; -; mRNA.
DR EMBL; BT005981; AAO64916.1; -; mRNA.
DR EMBL; AY049755; AAL12216.1; -; mRNA.
DR RefSeq; NP_200155.2; NM_124722.3.
DR AlphaFoldDB; Q8GZ42; -.
DR SMR; Q8GZ42; -.
DR STRING; 3702.AT5G53430.1; -.
DR iPTMnet; Q8GZ42; -.
DR PaxDb; Q8GZ42; -.
DR PRIDE; Q8GZ42; -.
DR ProteomicsDB; 240922; -.
DR EnsemblPlants; AT5G53430.1; AT5G53430.1; AT5G53430.
DR GeneID; 835424; -.
DR Gramene; AT5G53430.1; AT5G53430.1; AT5G53430.
DR KEGG; ath:AT5G53430; -.
DR Araport; AT5G53430; -.
DR TAIR; locus:2178446; AT5G53430.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_006335_0_0_1; -.
DR InParanoid; Q8GZ42; -.
DR OMA; CKKIWNH; -.
DR OrthoDB; 112057at2759; -.
DR PhylomeDB; Q8GZ42; -.
DR PRO; PR:Q8GZ42; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GZ42; baseline and differential.
DR Genevisible; Q8GZ42; AT.
DR GO; GO:0031011; C:Ino80 complex; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:TAIR.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0009294; P:DNA-mediated transformation; IMP:TAIR.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IGI:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd15663; ePHD_ATX3_4_5_like; 1.
DR CDD; cd15495; PHD_ATX3_4_5_like; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 3.
DR InterPro; IPR041955; ATX3/4/5_ePHD.
DR InterPro; IPR042011; ATX3/4/5_PHD.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR025780; Hist-Lys_N-MeTrfase_ATX.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00249; PHD; 3.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS51566; SAM_MT43_TRX_MLL; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1043
FT /note="Histone-lysine N-methyltransferase ATX5"
FT /id="PRO_0000233358"
FT DOMAIN 223..292
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT DOMAIN 901..1018
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1027..1043
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT ZN_FING 661..695
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 719..776
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT BINDING 911
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 955
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 978..979
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 981
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1031
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1033
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1038
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1043 AA; 119122 MW; 0871B150AA379250 CRC64;
MIIKRKLKTL KRCNSTNEED DIVRKKRKVN LNGGGSGGDY YYPLNLLGEI GAGIVPGKNG
FSVSLCKQVS CSPKVEVVEE EEEEEEIKST RLVSRPPLVK TSRGRVQVLP SRFNDSVIEN
WRKDNKSSGE EREEEIEEEA CRKEKVKVSS NHSLKIKQQE TKFTPRNYKY SSSSALCGEI
DDEDKCEEIV RYGNSFEMKK QRYVDDEPRP KKEGVYGPED FYSGDLVWGK SGRNEPFWPA
IVIDPMTQAP ELVLRSCIPD AACVMFFGHS GTENERDYAW VRRGMIFPFV DYVERLQEQS
ELRGCNPRDF QMALEEALLA DQGFTEKLMQ DIHMAAGNQT FDDSVYRWVE EAAGSSQYLD
HVAPSQDMKK YRNPRACVGC GMVLSFKMAQ KMKALIPGDQ LLCQPCSKLT KPKHVCGICK
RIWNHLDSQS WVRCDGCKVW IHSACDQISH KHFKDLGETD YYCPTCRTKF DFELSDSEKP
DSKSKLGKNN APMVLPDKVI VVCSGVEGIY FPSLHLVVCK CGSCGPERKA LSEWERHTGS
KAKNWRTSVK VKSSKLPLEE WMMKLAEFHA NATAAKPPKR PSIKQRKQRL LSFLREKYEP
VNVKWTTERC AVCRWVEDWD YNKIIICNRC QIAVHQECYG TRNVRDFTSW VCKACETPEI
KRECCLCPVK GGALKPTDVE TLWVHVTCAW FQPEVCFASE EKMEPALGIL SIPSSNFVKI
CVICKQIHGS CTQCCKCSTY YHAMCASRAG YRMELHCLEK NGRQITKMVS YCSYHRAPNP
DTVLIIQTPS GVFSAKSLVQ NKKKSGTRLI LANREEIEES AAEDTIPIDP FSSARCRLYK
RTVNSKKRTK EEGIPHYTGG LRHHPSAAIQ TLNAFRHVAE EPKSFSSFRE RLHHLQRTEM
ERVCFGRSGI HGWGLFARRN IQEGEMVLEY RGEQVRGIIA DLREARYRRE GKDCYLFKIS
EEVVVDATEK GNIARLINHS CMPNCYARIM SVGDDESRIV LIAKTTVASC EELTYDYLFD
PDEPDEFKVP CLCKSPNCRK FMN
