ID A0A0K9PW35_ZOSMR Unreviewed; 2417 AA.
AC A0A0K9PW35;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=ZOSMA_14G00030 {ECO:0000313|EMBL:KMZ73243.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ73243.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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|RuleBase:RU000417};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016, ECO:0000256|RuleBase:RU000416}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMZ73243.1}.
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DR EMBL; LFYR01000585; KMZ73243.1; -; Genomic_DNA.
DR STRING; 29655.A0A0K9PW35; -.
DR OrthoDB; 317994at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IBA:GO_Central.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd04708; BAH_plantDCM_II; 1.
DR CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR CDD; cd03044; GST_N_EF1Bgamma; 1.
DR CDD; cd14137; STKc_GSK3; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.70.1010; Translation elongation factor EF1B, gamma chain, conserved domain; 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; IPR001662; EF1B_G_C.
DR InterPro; IPR036433; EF1B_G_C_sf.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR039192; STKc_GSK3.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR00675; dcm; 1.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF12047; DNMT1-RFD; 2.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SMART; SM00439; BAH; 2.
DR SMART; SM01183; EF1G; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF89942; eEF1-gamma domain; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|PROSITE-
KW ProRule:PRU00519}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|PROSITE-
KW ProRule:PRU00519}; Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01016};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 775..908
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 947..1086
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1653..1936
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 2007..2088
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 2093..2221
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 2257..2417
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50040"
FT REGION 76..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2219..2246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2230..2246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1239
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 2417 AA; 274191 MW; B7F83CCDCDC9194B CRC64;
MKDSQNPRWF QKLIYPSFFL AVTYLNIPEL FYKYRRRRWQ KSHSWISKFL YFLIFISLSE
IDLSFQMASS AMNQASTTEN NSKNLASAAG KEDKARGRKR QTSKGKSATN LKEKKMKLSV
AEGEIDALHL TKIGSDEQPP CRKLVDFIFH DSEGKPQPFE MSEINDIFIT STIMPMDDDM
IEEKGRGVKC VGFGRIESWS ISGYDEGTPI IWISTCSADY EVVKPTASYK KLYVRFWEKA
RVCVEVFKAT SRPNGGNPDI SVEELLGKVA RSMSGTKTLP AGSSAIDFLL SLGDFIYNQL
IGLDESDAIF ASMPALISLR DRCQQSRVQI NRGSIASSSG RSLKIEEGNT SEDGKLARLL
QEEKNWKSLK QHNSRRNRSS RSKFYIKINE KELANDYPLP TYFKPVVQEM DEYIFYDNHN
SDYYTDGLPK RVLNNWSLYN SDSRLISLEL LPMKPCAETD VTIFGSGSMT EDDGSGFCFD
LDQAQSSTST SDEPVDTGIP IYLSSIKEWM IEFGCSIIFV SIRTDMAWYR LGKPSKQYSS
WYEPILKTGK LAVDIISLLK EQTRVSRLSF WDVIKRVSEF DKNRPSYISS DVVSVEKYLM
VHAQIILQLF AEFPDPLIKK SSFAALLSEK MEKRNHTKLE MKKKASPAKE INNMNPSASS
SMIPTVQSNR KAMRATTTKF INNLWREYYS GELSIGDLKI DQVLDDVVEE DEEDEVDDDV
DVQIQASDNI QIPHSPNKPG HSQSENKEIN WEGASSGTMS SSGWALYRCA MVRGCKINVG
GTVSVVATEA GGSVLILVEY MFETPNGGKM IHGRVLKKGS LTILGNTANK TEVFLTNECK
EYELSQVKES VVVEIRKILW GHQFRKKNAD ADKIYKKKAE DREKKGFPTE YFCKSLYSPE
RGAFFALSPD TIGLGSGVCH SCTVRETDGD GDFTVNVSEA KFIYKKVQYK VDDFVYVNAS
HFGNIREDSG THKAGRNKGL KAYVVCHLLD IVYENSKQPD LDNTKVRVRR FYRPEDISAE
RGYCSDIREV LYTDEMLNIP IQAIQGKCQV RKKIHLPMLD TPVNLEHIFF CDRFYDPQTG
SMKQLPPTNS LLFSRPSKDD DLYNKAKGKK KWDEREEEED SHLKWKGVPK EDRLSTLDIF
AGCGGLSEGL QKSGVSYTKW AIEYDQPAGM AFRHNNPHAL VYIDNCNIIL RAVMEKCGDA
DDSVSPSEAV ELVAKLDKEK IDNLPLPGEV DFINGGPPCQ GFSGMNRFSQ STWSKVQCEM
ILAFLSFADY FRPRFFLLEN VRTFVSFNKG QTFHLTIASL LEMGYQVRFG ILEAGTFGVS
QSRKRAFIWA ASPEEILPEW PEPMHVFAGP DLKVSLPGGL QYSAARSTAS GAPFRSITVR
DTIGDLPPVG NGASNFEIEY GSEPVSSFQK KIRGNMTVLS DHISKEMNEL NLIRCKHIPC
KPGADWRDLP EKKVKLSTGL MVDLIPWCLP NTAKRHNQWK GLFGRLDWEG NFPTSITDPQ
PMGKVGMCFH PDQDRILTVR EFARSQGFMD NFHFSGNIQN KYRQIGNAVP PPLAYALGTK
LKEAVDAKNL ADHMLSKQSV AKSTKHHKND YKDDHIYSSD FHDFIHPDSL ILVQTSIYLM
DIKLDSSKGT DADSGHIIVT TIDDRDGTKQ VSYTAEKIAG KGSFGIVFQA KCRETGEIVA
IKKVLQDKRY KNRELQIMHL LKDHPNIVSL KHCFFSTTNM EEDLYLNLVL EFIPETINRL
AKCYNRLNQH MPLIYVKLYI YQICRVLGYI HNCIGLCHRD IKPQNLLVNP HTHQLKLCDF
GSAKVLVKGE HNISYICSRY YRAPELIFDA TEYTTAIDIW STGCVMAELL LGQPIFSGDS
GVDQLVEIIK VLGTPTREDI KCMNPKYTEF KFPQIKAHPW HKKRLPSEAV DLVCRFLQYS
PNMRCTAWAA CIHPFFDELR DPNTRLPTGR PLPPLFNFNH QEINAMSPDI MNRLVPGNTR
MNRPPERVSR SQRSVSSFCI HRQQTSMALV LHTSPANKNA YKVLVAAEYS GVKVDLVDNV
QFGVTNVTAE FLKMNPIGKV PVLQTPDGPI FESNAIARYV TLQKSDNPLN GSSLIDQARV
AQWMDFSMSE IDRCIGLWLY PRLGFSPYLP PAEEFAITSL KRSLEALNKH LSTNTYLVGH
SVTLADIVMV CNLYYGFKTV MTKNFTSQFP HVERYLWTLV NQPNFKKVIG EVKQVESVPP
IQSKKSAPNP KAKKSPEKET PKAKEVAVVE EAPKPKAKNP LDLLPPSKMI LDDWKRLYSN
TKTNFHDIAI KGFWDMYDPE GYSLWFCNYK FNEENTVSFV TMNKVGGFLQ RMDLVRKYAF
AKMLIIGSSP PFKVKGLWLF RGLEIPQFVL DECYDMDLYE WTKVDIADEV QKNRVNAMIE
DLEPFEGEDL LDAKCFK
//
