ID F5YM91_TREPZ Unreviewed; 1232 AA.
AC F5YM91;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=TREPR_0411 {ECO:0000313|EMBL:AEF86014.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF86014.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF86014.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
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; CP001843; AEF86014.1; -; Genomic_DNA.
DR RefSeq; WP_015709600.1; NC_015578.1.
DR AlphaFoldDB; F5YM91; -.
DR STRING; 545694.TREPR_0411; -.
DR REBASE; 36232; TprZAS2ORF411P.
DR KEGG; tpi:TREPR_0411; -.
DR eggNOG; COG0286; Bacteria.
DR eggNOG; COG0827; Bacteria.
DR eggNOG; COG1002; Bacteria.
DR HOGENOM; CLU_267543_0_0_12; -.
DR OrthoDB; 353422at2; -.
DR Proteomes; UP000009223; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR041635; Type_ISP_LLaBIII_C.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF18135; Type_ISP_C; 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 ECO:0000313|EMBL:AEF86014.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009223};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 653..746
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT DOMAIN 866..1210
FT /note="Type ISP restriction-modification enzyme LLaBIII C-
FT terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF18135"
SQ SEQUENCE 1232 AA; 140972 MW; 789FEB20C0275E5C CRC64;
MTKSECMELL KQSYSADLSR TLLREIFLDS FIPVSNIGAG EAIKKIGTVR RLGRILLNKD
TDKAEAYEVL DIETDPKIHI EHNRVSLNMG TKDYFDGIGV RGILAFFHNP QEKAWRLTYA
AKSFSFDKKT GKELINRTGT KRYTYVLGPS AATGTAAVRL LSIRSVMPYG NSKHLTEAFS
MEAVSKEFFE TYRSFYRRFT EALSEKKKYR SLFNISAFPD AKAQESADKP FRDFAKKLLG
RLVFLKFLEK KGWLGAKDYA AADGDTEFLN HLYRDHGDSS GNFYTSALVP LFFETLNTKR
KGDLFSLTGT KIPFLNGGLF ENDYPLDTNR ALSFPANLFK ELLEFLSSYN FTIDENDPGD
ADIGVDPDML GRIFEQLIED NEKDMNGTIY TPFEVVRFMC RESLVLHLCR ILDCDRDSKK
AQAVKALIVR GEIEGLTKKE QATLDTAIKT VKVLDPAVGS GAFPMGMLKE ILAARIALEG
DTADRETLKR EIIRNSIYGV DIDHGAVDIA RLRFFLSLVV DSKEPEPLPN LDFKLMQGDS
LAEEYEGVDL SMESENIHDT KKKKQYSMDF SGKALTRETL IKAVNEFYST TDHQKKLELE
ESIRATVVGF IRERMEEENK PVKLDNLEAM LKRNSPFFLW HLFFKDVFDT GGFDIIIGNP
PYRANQENEN DQAKNKVYPH IYSRIKETFV AKSTAQKTKV YDLFACFFRL AMDFSLKAEK
KSIIAFITNY AFIGARTYDG FRRDVRENFG SLRVVNLGGD VRSNQKLSGP VNSIFGIQAG
VAISFYQPKM NDTNAFNLRY TVTEEEATRG EKIEFLAGYD KTDMIFDTIT PDGKENWVNQ
SDSDFQSLLP LCSKEAKSGK GEGKTVFELF SLGVVTNRDD WVYDFDEKNL IGKIKYFINA
FNDSVSNDKN NMSIKWTRAV LNDFTKGKKY KFSQMFIIKS LYRPFINAFL YYSKELNEMR
YQLPKIFPDN LVITISGVPG TKSFSTLAAS IVYCLDLLEK TQCLPLYRYE KNKKLDNITV
WALAEFQNHY KDKNITKEDI FHYVYAVLHN PLYREKYAID LKQDYPRIPL YREFKKWAAW
GKELMDLHIG FEKTAPHKGI TVITAPADYR ATKTHRLDYT KDEQGEKVFS GSLTFCDGSG
LKGIPPRAFD YKLGNKSAIE WVLDQYVAPS WPTDAELASG KRKIREDEKV LRDKFNTFKF
ADYREKVIDL IRRLATVSLR TLEIQGMMGE EK
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