CMT1_DICDI
ID CMT1_DICDI Reviewed; 379 AA.
AC Q54JH6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=DNA (cytosine-5)-methyltransferase;
DE EC=2.1.1.37;
GN Name=dnmA; ORFNames=DDB_G0288047;
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).
RN [2]
RP IDENTIFICATION.
RX PubMed=15689527; DOI=10.1093/molbev/msi098;
RA Ponger L., Li W.H.;
RT "Evolutionary diversification of DNA methyltransferases in eukaryotic
RT genomes.";
RL Mol. Biol. Evol. 22:1119-1128(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16282589; DOI=10.1093/nar/gki952;
RA Kuhlmann M., Borisova B.E., Kaller M., Larsson P., Stach D., Na J.,
RA Eichinger L., Lyko F., Ambros V., Soderbom F., Hammann C., Nellen W.;
RT "Silencing of retrotransposons in Dictyostelium by DNA methylation and
RT RNAi.";
RL Nucleic Acids Res. 33:6405-6417(2005).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16400165; DOI=10.1128/ec.5.1.18-25.2006;
RA Katoh M., Curk T., Xu Q., Zupan B., Kuspa A., Shaulsky G.;
RT "Developmentally regulated DNA methylation in Dictyostelium discoideum.";
RL Eukaryot. Cell 5:18-25(2006).
CC -!- FUNCTION: Involved in epigenetic gene silencing. Methylates specific
CC cytosine residues in the retrotransposons DIRS-1 and Skipper.
CC {ECO:0000269|PubMed:16282589, ECO:0000269|PubMed:16400165}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000269|PubMed:16282589, ECO:0000269|PubMed:16400165};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed during vegetative growth and throughout
CC development. Levels decrease after aggregation and are lowest during
CC culmination. {ECO:0000269|PubMed:16282589}.
CC -!- DISRUPTION PHENOTYPE: Mutants exhibit altered gene expression, and
CC after undergoing 16 development cycles some mutant cells displayed
CC reduced growth on axenic medium. DIRS-1 expression was unaffected but
CC Skipper expression was increased in mutant cells after 16 cycles of
CC development. Mutants lacking dmaA exhibit culmination defects including
CC fragmented, transluscent sori, and fewer spores than wild type.
CC {ECO:0000269|PubMed:16282589, ECO:0000269|PubMed:16400165}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; AAFI02000107; EAL63449.1; -; Genomic_DNA.
DR RefSeq; XP_636955.1; XM_631863.1.
DR AlphaFoldDB; Q54JH6; -.
DR SMR; Q54JH6; -.
DR STRING; 44689.DDB0231095; -.
DR PaxDb; Q54JH6; -.
DR EnsemblProtists; EAL63449; EAL63449; DDB_G0288047.
DR GeneID; 8626430; -.
DR KEGG; ddi:DDB_G0288047; -.
DR dictyBase; DDB_G0288047; dnmA.
DR eggNOG; KOG0919; Eukaryota.
DR HOGENOM; CLU_049101_0_0_1; -.
DR InParanoid; Q54JH6; -.
DR OMA; VMDIIHP; -.
DR PhylomeDB; Q54JH6; -.
DR BRENDA; 2.1.1.203; 1939.
DR PRO; PR:Q54JH6; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IMP:dictyBase.
DR GO; GO:0003677; F:DNA binding; ISS:dictyBase.
DR GO; GO:0016427; F:tRNA (cytosine) methyltransferase activity; IDA:dictyBase.
DR GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; IDA:dictyBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0006306; P:DNA methylation; ISS:dictyBase.
DR GO; GO:0032776; P:DNA methylation on cytosine; IMP:dictyBase.
DR GO; GO:0010243; P:response to organonitrogen compound; IDA:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR GO; GO:0002946; P:tRNA C5-cytosine methylation; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IDA:dictyBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00675; dcm; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; DNA-binding; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..379
FT /note="DNA (cytosine-5)-methyltransferase"
FT /id="PRO_0000328901"
FT DOMAIN 4..366
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT REGION 178..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 379 AA; 44115 MW; 3C9B2D277BA9D25A CRC64;
MEQLRVLEFY SGIGGMHYGL QESGVDFQVI QSFDINTNAN LNYKYTFNED SSQKSIESYS
VEELEGFKAN AWLMSPPCQP FTRLGLQKDD QDNRTNSFFH LLDVLTKIKD PPTYILIENV
FGFAKKGSSN TRDHLLDTLI KMNYSFQEFH LSPQQFGLAN QRLRYFCIAK RNGKLNFKKE
QDKHNEKVDE NKLNNNSNNN NEQNKYDNLK ILDHIPGYDF HTTLEECDEI SNYFDKDLTD
DELYEKYKVP HNLLLSKGML FDIKQKDSKT SNCVTKSYGK FIEGTGSIIQ MDNNFKADIN
DNKSLIPLKL RYFSPKEITR LHGFPEEFKF SPKLTTIQCY RLIGNSLNVK IVSELLKVLV
SPNEEEEQQE QQKEKEGKK
