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Database: UniProt/TrEMBL
Entry: E9FYA9_DAPPU
LinkDB: E9FYA9_DAPPU
Original site: E9FYA9_DAPPU 
ID   E9FYA9_DAPPU            Unreviewed;       357 AA.
AC   E9FYA9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=[histone H4]-lysine(20) N-methyltransferase {ECO:0000256|ARBA:ARBA00012187};
DE            EC=2.1.1.361 {ECO:0000256|ARBA:ARBA00012187};
GN   ORFNames=DAPPUDRAFT_311914 {ECO:0000313|EMBL:EFX87804.1};
OS   Daphnia pulex (Water flea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX87804.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX87804.1, ECO:0000313|Proteomes:UP000000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21292972; DOI=10.1126/science.1197761;
RA   Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA   Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA   Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA   Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA   Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA   Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA   Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA   Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA   Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA   Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA   Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA   Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT   "The ecoresponsive genome of Daphnia pulex.";
RL   Science 331:555-561(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC         Evidence={ECO:0000256|ARBA:ARBA00000350};
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; GL732527; EFX87804.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9FYA9; -.
DR   STRING; 6669.E9FYA9; -.
DR   EnsemblMetazoa; EFX87804; EFX87804; DAPPUDRAFT_311914.
DR   KEGG; dpx:DAPPUDRAFT_311914; -.
DR   eggNOG; KOG1085; Eukaryota.
DR   HOGENOM; CLU_047978_2_0_1; -.
DR   InParanoid; E9FYA9; -.
DR   PhylomeDB; E9FYA9; -.
DR   Proteomes; UP000000305; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005700; C:polytene chromosome; IBA:GO_Central.
DR   GO; GO:0042799; F:histone H4K20 methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0140944; F:histone H4K20 monomethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd10528; SET_SETD8; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR016858; KMT5A-like.
DR   InterPro; IPR047266; KMT5A-like_SET.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   PANTHER; PTHR46167; N-LYSINE METHYLTRANSFERASE KMT5A; 1.
DR   PANTHER; PTHR46167:SF1; N-LYSINE METHYLTRANSFERASE KMT5A; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51571; SAM_MT43_PR_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          220..342
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   357 AA;  40420 MW;  72164A8ADB56B056 CRC64;
     MVKRGSTTAK RGRKPAASLE SSSNPTNEVV AVNQQQAVTP KEAVNKTKSS FRGKLSHTSP
     ILDSSSREKK ITVYFSAVTS EEASKVEHEK IDKEVGQVAK SLALQRVFGK SQSPEKKEVT
     PHKILLEEEP QQLIAETQEV SEKIIKEEII VDQSVKEPKV KAMKAKRKLN VNQSLNQDSS
     QNHKLTEYFA VRRSVRKPKT AILEEKQRNL EESVLSGKED GLQVHNFPGK GRGIVATQLF
     RRGEFVVEYS GDLIDMIEAR EREKLYAADQ NTGCYMYYFQ HKNQSYCVDA TLESQRLGRL
     VNHSRQSGNL MPKVIEIKDR PHLLLVARSD ILPGEELLYD YGDRSRVSLK YHPWLAS
//
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