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Database: UniProt
Entry: D5SSU7_PLAL2
LinkDB: D5SSU7_PLAL2
Original site: D5SSU7_PLAL2 
ID   D5SSU7_PLAL2            Unreviewed;      1425 AA.
AC   D5SSU7;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   OrderedLocusNames=Plim_3080 {ECO:0000313|EMBL:ADG68898.1};
OS   Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS   (Planctomyces limnophilus).
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctopirus.
OX   NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG68898.1, ECO:0000313|Proteomes:UP000002220};
RN   [1] {ECO:0000313|EMBL:ADG68898.1, ECO:0000313|Proteomes:UP000002220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290
RC   {ECO:0000313|Proteomes:UP000002220};
RX   PubMed=21304691; DOI=10.4056/sigs.1052813;
RA   Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT   290).";
RL   Stand. Genomic Sci. 3:47-56(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000256|ARBA:ARBA00001279};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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DR   EMBL; CP001744; ADG68898.1; -; Genomic_DNA.
DR   RefSeq; WP_013111329.1; NC_014148.1.
DR   STRING; 521674.Plim_3080; -.
DR   REBASE; 69566; PliMORF3080P.
DR   KEGG; plm:Plim_3080; -.
DR   eggNOG; COG0827; Bacteria.
DR   eggNOG; COG1002; Bacteria.
DR   HOGENOM; CLU_252803_0_0_0; -.
DR   OrthoDB; 249114at2; -.
DR   Proteomes; UP000002220; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR   InterPro; IPR046816; MmeI_Mtase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; NF033455; BREX_6_MTaseX; 1.
DR   PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   Pfam; PF07669; Eco57I; 1.
DR   Pfam; PF20473; MmeI_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002220};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          323..402
FT                   /note="MmeI-like DNA-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF20473"
FT   DOMAIN          559..644
FT                   /note="Type II methyltransferase M.TaqI-like"
FT                   /evidence="ECO:0000259|Pfam:PF07669"
FT   REGION          672..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1393..1425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..692
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1425 AA;  160912 MW;  49736744E5229F07 CRC64;
     MTMTPDAKTK LSKTIRALRE RLLTELNEAV DREYKFTLKN PKLDTKTKIK RQRLEDWLAE
     QVRTQTGKVK RTKEVFRSDA EKQAAYTLLN RLVLLRILEA VGLRKPKVVT GGWNSQGYKD
     FRELAQALVQ SDDGEGYPFL LQLIFEDLAI DLPGLYGSAG VADLIPVPSP TIRAVVEALD
     DEALETCWTD DMTLGWVYQY WNDPEREALD AKINGGGKIE PHEIASKTQM FTERYMVDWL
     LQNSLGPMWL AMCQKHGWTP GVVADGTLDR LEQRRSEWRA KRDAGEVALT DLMPLETDAE
     RRWAYYVPQP IPEDAVDHAP PSLRDVKILD PAVGSGHFLV VAFDLLFALY KEEAKHRGQQ
     AGEQWTDQAI VERILEHNLH GIDLDPRAVQ IAAAALWLKA QLVAPSAQIK QLNLVASNLG
     ISRLADNDPS LVELRRAIEA ETGIPGKLTM QIVDALKGAD HLGSLLKIDQ AITEAMHSFE
     KSLGMKDKVD RVLFGPELGS EIVIQSGGVD RAATEAGILS ALENFLSRHT SSEELGLRLA
     GEQLAAGVRF VRLVKEGAYD LVVANPPYQG TSKMADVKYV ATHYKLAKAD LFAAFLLRGL
     QLVREHGVSA MLTMRNWMFI KQYSDLRQHL LQTYDLRALG DFDRGAFEEI LDEVVAVAAA
     CFARAPHRSE SVAQCPTPRE DRSRDNERTK RKRAATLCQV GRHTFDPAAL KVVPEWPLVY
     WWDRAFLKAY SEVGTVGANS PARKGVCTSN NGWFIRRPWE ISVNRIRHPR SVDPTCHWAP
     YVMGAAGKAW IEPVSFALEW SRHGLMVKVL NDYIYSSYSR TIQNQHLYFR KGVAFTTIGS
     AFTGRSFRVP SIFDTTGCSV FGADIANTTA LFNSSKARSV LTSLNPTIHF TNGDVNRLPL
     FPIENADDVF SLVETAFTNH ESHREPSVEF KRPGPSPWRQ AQEWAQLAVD RPEGAPLPEY
     IEELDPEPPT DHLSFALGVA LGRFGAGGEG ILDPTKDDLS KALPAGILFL DGALGDDDRR
     DSLGHHAAQI IHDNWSEYGP QIDKRRSLRD WLREKFFPDV HKGMYENRPI HWPLSSGKKT
     FVAWVTIHRW NDQTLRVLLA DHLEPALKRL DGEITDLTAA RNSADRKQAR GAEDRYADVK
     AWRDELAEFI HHVQECAERG PEPPDAKKPE REVDARYIPD LDDGVMINSA ALWPLLDPQW
     KDPKKWWKEL VAAQGKKDYD WSHLAMRYWP TRVDEKCQKD PSLGVAHGCF WKYHPARAWA
     WELRLQDEIG PEFEIKEASY RGDGGDSEHR INYLHKEPTE ALAAIEKEVL RRKRKQKQPQ
     SELTILEPIL WSIVPDECWE LELRLTEKQQ VEFRLLAPDE PECRARFEQA HPDRVKSRCA
     LVSKLSPPDL YVDLEDEDEA ASADAEDLDT EDADAIDANT GEVEA
//
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