Y4059_DICDI
ID Y4059_DICDI Reviewed; 1280 AA.
AC Q54Q80;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=SET and MYND domain-containing protein DDB_G0284059;
DE EC=2.1.1.-;
GN ORFNames=DDB_G0284059;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Probable methyltransferase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AAFI02000063; EAL65370.1; -; Genomic_DNA.
DR RefSeq; XP_638717.1; XM_633625.1.
DR AlphaFoldDB; Q54Q80; -.
DR SMR; Q54Q80; -.
DR STRING; 44689.DDB0238659; -.
DR PaxDb; Q54Q80; -.
DR EnsemblProtists; EAL65370; EAL65370; DDB_G0284059.
DR GeneID; 8624387; -.
DR KEGG; ddi:DDB_G0284059; -.
DR dictyBase; DDB_G0284059; -.
DR eggNOG; KOG2084; Eukaryota.
DR HOGENOM; CLU_263198_0_0_1; -.
DR InParanoid; Q54Q80; -.
DR OMA; NRCLCLV; -.
DR PRO; PR:Q54Q80; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 2.170.270.10; -; 2.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Metal-binding; Methyltransferase; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; TPR repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1280
FT /note="SET and MYND domain-containing protein DDB_G0284059"
FT /id="PRO_0000389436"
FT REPEAT 272..305
FT /note="TPR 1"
FT REPEAT 383..416
FT /note="TPR 2"
FT DOMAIN 822..965
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REPEAT 1218..1251
FT /note="TPR 3"
FT ZN_FING 533..572
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..468
FT /evidence="ECO:0000255"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 533
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 549
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ SEQUENCE 1280 AA; 144701 MW; F2B9427767308688 CRC64;
MTKKIKLSNS ESNKVNNNNN NNHGNGHNHN HSHNHGEMCH GHGIIGIVDS VTGENIIQVN
GENLRSVPNG HSLIHNINSI INSHSKHGKI KNILKDSTII SSSINLSDKP INKITEENSP
PSSPTLSSST NTTTDRQELP QQQQQPQQQQ SQPSTPPPQQ QTNQKQQPEF NRYQANDILF
RNKLTRSLSR NIPPLSLLKQ NFKDEMENSF HTAISNIKDL NEKVEMVNLI FQHNLSENNA
MVNVDSIIHS STSGLLSEYK QITETFDWEQ TSKGYKNKGN ELFQKKQYSD ALLLYNESLR
IYDMELAAAA TSTNLNEKEN GGGGNVGGSA TATATTINTP DVSILSSIHS NRCLCLVNLE
RYKEGAIEAT RGIDLVGSSS VLHKLYYRRG ICYYHLRKHY KAKKDFLRAH TLIEKRDSSD
LASIENYLFK IQKLSLPLQK DEEIEQELDN KNNNSNDDEK QQQQQQQQDI DVTISSILEK
SESLIDSRVE FLYQSDLVGR ISEASDFIPS NTVLYQEEPY VSCLDRNYHS QYCYNCFKEI
LSPIYCKECS NSQYCSNKCL NEDYVKQHGR ECGKGFLIIC SHESLLVIRL LARKGRDYRE
ANKGKKEEEP QQQQQKQQKS RKLPNLTFIP KPNPTQIDQN LNKPKIVLPE PTTAAINTAL
SSASTPTTAT ATTTTTTTTA TTPTTLAETL SSTSLTENKS DSTPPPTPLP PSSSSSSSSS
SSTTTTTFSF NMSELQNLQI SQDDELFDVP TDPALFGKSN TYSQSYELIN SFNPHFEHHS
NDSMANMIFD AFVIERFLLY YQKDLGILSE DIDVHVILRH LCQLTTYTFA IPGYIDNHDS
LVLKTLQLQQ QQQQQQQQQQ NQQSNQQPNQ QSNQQSNQQS NQQSQPNQSP IIQSQNPPHA
SPFSPLRYSV QKYSQDKIGY AVYPMASLMN HSCDNNTHLQ YDGCSLTIKS LFNIEKGEEI
LGCYGPHAFL NPLKDRLINL YNEFFFVCRC KACSEKSGPD PIKCPGSYHD HLNSPESSPV
ECSGTLLESI NMNQLVTMAK LQQQQQQQQQ HQQQNDKKKF NSNPTNLGSN NNNNYLNNNF
NNPLRNGNPF LLKQTYDRYD DHEHRYFCCS KCGIELNGFD SFSLTSQIII SDNLFEMGFK
AMTLYGNLSK DIETMLLRAL ELRKSIFKPC SKKIGDIYDS LSRFSISRED GASAAKYLEL
LIENVISRLG HSNSADLGRE YSKLGQIYLT LGEIEKSEDA IEKAESILMS WKSNDPTDEE
VLFLLTNRRK LFTAAHLINK
