ID A0A5E4F8X5_PRUDU Unreviewed; 1780 AA.
AC A0A5E4F8X5;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=PREDICTED: histone-lysine N-methyltransferase {ECO:0000313|EMBL:VVA23900.1};
GN ORFNames=ALMOND_2B023136 {ECO:0000313|EMBL:VVA23900.1};
OS Prunus dulcis (Almond) (Amygdalus dulcis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3755 {ECO:0000313|EMBL:VVA23900.1, ECO:0000313|Proteomes:UP000327085};
RN [1] {ECO:0000313|Proteomes:UP000327085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Texas {ECO:0000313|Proteomes:UP000327085};
RX PubMed=31529539; DOI=10.1111/tpj.14538;
RA Alioto T., Alexiou K.G., Bardil A., Barteri F., Castanera R., Cruz F.,
RA Dhingra A., Duval H., Fernandez I Marti A., Frias L., Galan B.,
RA Garcia J.L., Howad W., Gomez-Garrido J., Gut M., Julca I., Morata J.,
RA Puigdomenech P., Ribeca P., Rubio Cabetas M.J., Vlasova A., Wirthensohn M.,
RA Garcia-Mas J., Gabaldon T., Casacuberta J.M., Arus P.;
RT "Transposons played a major role in the diversification between the closely
RT related almond and peach genomes: results from the almond genome
RT sequence.";
RL Plant J. 101:455-472(2020).
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DR EMBL; CABIKO010000075; VVA23900.1; -; Genomic_DNA.
DR EnsemblPlants; VVA23900; VVA23900; Prudul26B023136.
DR Gramene; VVA23900; VVA23900; Prudul26B023136.
DR Proteomes; UP000327085; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd15571; ePHD; 1.
DR CDD; cd10518; SET_SETD1-like; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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 PANTHER; PTHR45838:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE TRITHORAX; 1.
DR PANTHER; PTHR45838; HISTONE-LYSINE-N-METHYLTRANSFERASE 2 KMT2 FAMILY MEMBER; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:VVA23900.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000327085};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:VVA23900.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 1277..1327
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1408..1532
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 1635..1756
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1764..1780
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 900..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1780 AA; 195586 MW; 707DB314781F119C CRC64;
MPNISNDLSH MVCSSGGSAS SQQSLDGVAL SKNLFTNQNL VVGAVENKQQ RNIQDGNTIF
LKGFTGTPQS NLHGMADNLI LERPISMSKL VGSGLQDGGQ SVSAYVESMK NGNSSIIYPA
MKIGNSSITH PSLKDRRIMG KGSNFCGTVN AKDGAFRDAA ISNIELRLGQ PYQLGQSLGN
SNPPAVGPQL LDTLVNPLKS LFPEQMIPNT NCREEMEFRQ SLYFSAVPSA STKSDHKQLN
RGNNAFVIGN AIDAARVEKS TSNLGQDSVI SFLTNLNAPP EDNTRPKANK YICNVGEHAM
QNTLHYEPQS AKYGIVNVPR NGSNSVERQL DMSQLGSYRL IDKDKGVSFV TDDSHLSKDL
GFRNCKEMEI SSSFNGLSGT GDPRFLTAHK NSCYSHQLSG VAPDGPDSRK YSNFPDKVLY
FGNRGQVGHV NHRPLASSVG SGLTFPSQTV SKGIPLVSAS ISVSDQTPAL SRENLIEVST
QLPDDNSRLL ALREIMELSK QHHALPSLPM NRGKGIFDCS SYMQNSLVDT SASGKQERKL
SLTSKNAVSE ATIKSHQSGA SCRIGSDEGF TSLTGVNTCC HFSTLKQGNA LHSKEVDLKH
QISFVPLCNE QPSLRSGKNI IEPSEHERCC HKVPYGYFRG SCSCAASINC LGRDFESRVG
CFPDAFKEQM GTVNGEASMI FAPKFANNHI VPKDKTTSLD PRGQVNGKIP KNVCHASQWR
DVPSKVKGVS DVTRVDRLAN LFDARRRDRE QLGDNYVNHF NGTVQMVDSS KEHEIYNNSS
GGSAPAVTQA SIEVNKMDSS TVDAGDIGCV SNLVVDEGSG VDKCWSSDDA LESEKSAEFL
TSTGNTSLRK GGSFKNLNHQ SSCSLLDELK LLNSLTWLKG QNKLPAGLAL HEKNEYPQNF
ERGLEDGKKK REMGSESYPT SGPYTVHEEN PECNDSAQFL SCPSKSVKTL FPLRQSITHT
FGTCVTQPSS KPRLPKTCLA KKLSRKRDLR RLYDDNDREV NDVNQTELNG GTDNCEISKV
SVGNKCKRDF SSNGFRQFLT QESGHEGARK RKHNSVGLKS CSSQQVNICY RKARPIVCGK
YGELANGNLD GDMPKPAKVV PLSRVLNSAR RCTLPKNCNP KSTSMRELKK TSPNGAVVSS
DVCHNDTGCG KINDTPMEKA KKECSVGDKK NRKELTKLEH LGDDQSEKDH SKLGGIAHAQ
LKLKSKEIRK RSIYELTDKG KDPSFESSSF SKISNCLPAK KEGRLLKTAE DSKLGLCKLS
SESSTLEHQC HSDLDSDAFC CVCGSSNKDD INNLLTCSQC SIKVHQACYG VSKLPKGHWC
CRPCRTSSKD IVCVLCGYGG GAMTQALRSR TVVKSLLRAW NAETECMAKN KLSSVKTLQK
DSSGLHCSGY GHQDNSSFFV LQRENGQPLV SAVCKRGMSY KFDVMHNSIT VGLLDSATKQ
WVHMVCGLWT PGTRCPNVDT MSAFDVSGAH PRADVVCCIC KRAGGSCIQC RVANCSAQFH
PWCAHQKGLL QSEVEGIDNE NIGFYGICEL HAIHPMCESN HDPVNTEAGC IEEEELTCAR
TEGYKGRKRD GFRHNYCDQS KGNGGCLVPQ EQLNAWVHIN GQKSSTQGLP KLPVSDIEHD
CRKEYARYKQ AKFWKHLVVY KSGIHALGLY TSRFISRSEM VVEYVGEIVG LRVADKRENE
YQSGKKLQYK SACYFFRIDK EHIIDATCKG GIARFVNHSC VPNCVAKVIS VRNEKKVVFF
AERDIFPGEE ITYDYHFNHE DEGKKIPCFC NSKNCRRYLN
//
