ID G3W4E5_SARHA Unreviewed; 1506 AA.
AC G3W4E5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=DNA (cytosine-5)-methyltransferase {ECO:0000256|PIRNR:PIRNR037404};
DE EC=2.1.1.37 {ECO:0000256|PIRNR:PIRNR037404};
GN Name=LOC100934323 {ECO:0000313|Ensembl:ENSSHAP00000010300.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000010300.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000010300.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000010300.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|PIRNR:PIRNR037404};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037404}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family.
CC {ECO:0000256|PIRNR:PIRNR037404, ECO:0000256|PROSITE-ProRule:PRU01016}.
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DR Ensembl; ENSSHAT00000010390.2; ENSSHAP00000010300.2; ENSSHAG00000008894.2.
DR GeneTree; ENSGT00390000005100; -.
DR HOGENOM; CLU_003040_0_0_1; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd04760; BAH_Dnmt1_I; 1.
DR CDD; cd04711; BAH_Dnmt1_II; 1.
DR Gene3D; 1.10.10.2230; -; 1.
DR Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
DR InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
DR InterPro; IPR010506; DMAP1-bd.
DR InterPro; IPR017198; DNMT1-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002857; Znf_CXXC.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF06464; DMAP_binding; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF12047; DNMT1-RFD; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR PIRSF; PIRSF037404; DNMT1; 2.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00439; BAH; 2.
DR SMART; SM01137; DMAP_binding; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 1.
DR PROSITE; PS51912; DMAP1_BIND; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037404};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR037404};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037404};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR037404};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037404};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 5..107
FT /note="DMAP1-binding"
FT /evidence="ECO:0000259|PROSITE:PS51912"
FT DOMAIN 534..580
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 643..767
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 859..987
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 116..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1007
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1116
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1506 AA; 170427 MW; FB9A2951E70CEE48 CRC64;
MLAGDASWDP QGGLQGIKVG DGRLKDLEKD EDILTEKEFV KKKLSLLHEF LQAEVQHQLF
DLEIKLHKEE LSEEGYLSKV KFLLNKELFL ENGDHPLTSR VNGCLENGIY TSDEDFEKSV
EEDSTVEMEE ATGSSTSLSK TRKSRRSKSD GEAKKSSASS RVTRSSGKQP TIVSLFSKGS
GKRKSEGATG EIKQEMNIEK EEEKEQGEKK MKFELKEGSE IKVVQGKAVL PVKSTPPKCM
DCRQYLDDPD LKFFQGDPDG ALDEPEMLTD ERLSIFDANE DGFESYDDLP QHRVTSFSVY
DKKGHLCPFD TGLIEKNIEL YFSGTVKPIY DDNPCLDGGV RAKKLGPINA WWITGFDGGE
KALIGFTTAF ADYILMAPSE EYAPIFALMQ EKIYMSKIVV EFLQNNPDVS YEDLINKIET
TVPPAGLNFN RFTEDSLLRH AQFVVEQVES YDEAGDSDEQ PVIITPCMRD LIKLAGVTLG
KRRAARRQAI RHPTKINKEK GPTKATTTKL VYLIFDTFFS EQIEKNERED DKENVTKRRR
CGVCEVCQQP ECGKCKACQD MVKFGGSGRS KQACLQRRCP NLAVKEADED EEVDDNIPEM
PSPKKMLQGR KKKQNKTRIS WVGAPIKSDG KKDYYQKVCI DSETLEVGDC VSVSPDDPTK
PLYLARITAL WEDSSGQMFH AHWFCAGIDT VLGATSDPLE LFLVDECEDM QLSYIHGKVN
VIYKAPSENW SMEGGLDMEI KMVEDDGRTY FYQMWYDQDY ARFESPPKIQ PTEDNKYKFC
ISCARLAEMR QKEIPRVTEP LEELDHKVLY GLGMKNGVQY RTGDGVFFLP EAFGFNMKLC
SPTKRSKKES VDEELYPEHY RKYSEYIKGS NQDAPEPYRI GRIKEIFCNK RNNGKPNEAD
IKLRVNKFYR PENTHKSMKA SHHADINLLY WSDEEAIVDF KAVQGRCIIE YGEDLTECIQ
DYSAGGSDRF YFLEAYNAKT KSFEDPPNHA RSPRNKGKGK GKGKGKSRGK SVAVEPSEQE
TIEVKLPKLR TLDVFSGCGG LSEGFHQAGI SETLWAIEMW EPAAQAFRLN NPGTTVFTED
CNVLLKLVMS GEKTNSLGQK LPQKGDVEML CGGPPCQGFS GMNRFNSRTY SKFKNSLVVS
FLSYCDYYRP RFFLLENVRN FVSFKRSMVL KLTLRCLVRM GYQCTFGVLQ AGQYGVAQTR
RRAIILAAAP GEKLPMFPEP LHVFAPRACQ LSVVVDDKKF VSNITRMNSA PFRTITVRDT
MSDLPEIRNG ASALEISYNG EPQSWFQRQI RGSQYQPILR DHICKDMSAL VAGRMRHIPL
APGSDWRDLP NIEVRLSDGT TTRKLRYTHH EKKNGRSNTG ALRGVCSCAE GKPCDPADRQ
FNTLIPWCLP HTGNRHNHWA GLYGRLEWDG FFSTTVTNPE PMGKQGRVLH PEQHRVVSVR
ECARSQGFPD TYRLFGNILD KHRQVGNAVP PPLAKAIGLE IKFSVLAKLK EKATEKIKKE
NLESMD
//
