ID A4CM25_ROBBH Unreviewed; 1006 AA.
AC A4CM25;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=RB2501_10342 {ECO:0000313|EMBL:EAR14717.1};
OS Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Robiginitalea.
OX NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR14717.1, ECO:0000313|Proteomes:UP000009049};
RN [1] {ECO:0000313|EMBL:EAR14717.1, ECO:0000313|Proteomes:UP000009049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC {ECO:0000313|Proteomes:UP000009049};
RX PubMed=19767438; DOI=10.1128/JB.01191-09;
RA Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL J. Bacteriol. 191:7144-7145(2009).
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};
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DR EMBL; CP001712; EAR14717.1; -; Genomic_DNA.
DR RefSeq; WP_015754038.1; NC_013222.1.
DR AlphaFoldDB; A4CM25; -.
DR STRING; 313596.RB2501_10342; -.
DR REBASE; 22070; RbiORF10342P.
DR KEGG; rbi:RB2501_10342; -.
DR eggNOG; COG0827; Bacteria.
DR eggNOG; COG1002; Bacteria.
DR HOGENOM; CLU_002539_2_0_10; -.
DR OrthoDB; 32195at2; -.
DR Proteomes; UP000009049; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.220.10; Adenine-n6-DNA-methyltransferase Taqi, Chain A, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR046817; MmeI_N.
DR InterPro; IPR023135; N6_DNA_MeTrfase_TaqI_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF20464; MmeI_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR Pfam; PF12950; TaqI_C; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EAR14717.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009049};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..186
FT /note="MmeI-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20464"
FT DOMAIN 433..670
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 763..881
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
FT COILED 964..991
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1006 AA; 117872 MW; BC35706699E30E6E CRC64;
MPIYQNSVLK KYLKTLDADT IGNAYERYTR HFHNASIQEN IRNAKEEQYQ GEFLIDLFVN
ILGYTKNPHP DFNLTTELKN VKDAKKADGA ILKGETALAV IELKGTDTTD LGKVEAQAFG
YKNNQPGCKY VITSNFEKLR FYIDNAVDFE EFHLFQLPRE RFEILWLCLS SECLLKDLPK
KIKEESLTQE EKITKTLYKD YSAFRTAVFQ NISEANPQYD KLLLFKKTQK LLDRFLFIFF
AEDRLLLPPN SIRTILQQWT DLKDKYDEYF PLYERFQKYF GYLNSGYKGK KHDIFAYNGG
LFEEDEILDS ITIDDNLLYE HTRNLSNYDF ESEVSVNILG HIFEHSLTEI ENIQAEIEGA
EIDKSKTKRK KDGVFYTPKY ITKYIVENTV GKLCEEKKAE LDITDEAYQP AKQRSRKRLQ
KLQDYRDWLL QLTICDPACG SGAFLNQALE FLIAEHRYID ELSAKYNKDA LILSDVENTI
LENNLFGVDI NEESVEIAKL SLWLRTAQKG RKLTSLSDNI KCGNSLIDDP KVAGDKAFNW
QEEFPEVFEK GGFDVVIGNP PYGAKLNTSA INYFREVYKT VIGHSEAYYL FIDITINKLL
QPDALLGFII PNAWLSNKYA KELRRLVLFE TRMLSLINFN RQIIFEDASV ETSIVITKKV
NPKPDDRVRV GQNTNELYPY LQLEWSRNSN YLLSFSPDLR IHEIVSKLNS SEKKLVECLD
ISNGFKPYQA GYGQNLQGKP LTSEDVKGRI YHSEIPLDDS YVKEIKGKGV HRYSLNWTPS
YVKWGKWLMS PKSEHYYKQH KILLRQITGE YFFAVLDMEQ YFADQSLYVC TYYNSKPKTN
LWFYLALLNS RLYGFYFRKY YSEEDDLFPK IKVNELKELP VKHCSNLLQI SLGSKAKLMQ
EQNEKMDLIN QSFCRHLQEK FNFEKLSKRL KNWSKQNFAE FLKELKKQKI KLTLSEEGEW
LFYFNEQKDK VQVLQNQIDQ TDREIDQMVY ELYGLTKEEI QIVENS
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