ID A0A2A2GSK9_9HELI Unreviewed; 1232 AA.
AC A0A2A2GSK9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=B9T66_05085 {ECO:0000313|EMBL:PAU99945.1};
OS Helicobacter sp. TUL.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1848928 {ECO:0000313|EMBL:PAU99945.1, ECO:0000313|Proteomes:UP000218502};
RN [1] {ECO:0000313|EMBL:PAU99945.1, ECO:0000313|Proteomes:UP000218502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUL {ECO:0000313|EMBL:PAU99945.1,
RC ECO:0000313|Proteomes:UP000218502};
RA Van Der Mee-Marquet N., Benejat L., Diene S.M., Gaia N., Cherkaoui A.,
RA Lemaignen A., Ducournau A., Lacomme S., Gontier E., Bernard L., Megraud F.,
RA Goudeau A., Lehours P., Francois P.;
RT "Helicobacter caesarodunum: a novel human pathogen identified in a
RT bloodstream infection.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PAU99945.1}.
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DR EMBL; NESU01000008; PAU99945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2GSK9; -.
DR Proteomes; UP000218502; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 InterPro; IPR025931; TaqI_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; PF20473; MmeI_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 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:PAU99945.1};
KW Hydrolase {ECO:0000313|EMBL:PAU99945.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:PAU99945.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218502};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 492..655
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
FT DOMAIN 804..910
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT DOMAIN 1017..1171
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 1232 AA; 143228 MW; 9D9170E0365C22DF CRC64;
MRYISKPLQE FLHTYTLPNP TTQSLNTFKE HLEHFLAQCH KHTAQDTSES EEFQKNLIAD
FLKQAFSYPK INTKRKIDLA IYEDDEVKTF FEVKSIANKS EFPKSTQSLD SKALYEALLY
YMREQNEGNN NLKYILLCNV ESFYLISAKE FEKLSQNKEL QQAYKNVDKK QGNDTSTKKF
YEKAQEILST LDMEMTFTHF GIKDTEPVLL YQVFSPHMLL GYKTHIDSNV LNQNFYEELL
YILGLEETKD GANKLIKLSD TPNTLSYAIR ENLGLDCVRD FESIFELIIT WNNRLLFLRL
LESMLLSFKH IPKPFLDSSV IESFAKLNTL FFEILALREN VRKSIPKELD SIPYLNSSLF
DKTELEKQGK EIKLLDSKPL ALYKKSILKD TKKPLPLLEY LFDFLNAYDF TTTPKDIQDN
VKINHDKLIN AAVLGLVFEK LNGYKEGSFY TPSFITNYMC KQSLQQVVIQ KFNTAKNWDC
KDLQSLKLRL DKLTDSKEGY KEANEIFDSI KVCDPAVGSG HFLVSMLNNM IELKFHLKIL
CDENFERLKD IQLRLENDEI VLQDSTGNPH IYQIPSHQNI ESHKLQKAIF HNKRTLIESC
LFGVDINHNS CEITKLRLWI ELLKYSYYIF ENGKNTNTLQ TLPNIDINIK CGNSLISYFD
ITQSLSHYPN INTKIKDYKQ AVQNYKEGLY QDKQALDSKI KELHTAFKNF CFKDKFKSQI
KAFEKECDKY STQYGNYLAK DDKNLSIYVK AGFFLEFDEA VAQKDFATLQ ESYNALFNLE
SNKPFEWRFA FPEVLDNNGN FKGFDLVIGN PPYIRQEEIK HLKPHLQKAF SIYKGTSDIY
TYFFEQGYKI LKSKALLSFI TSNKYTRAGY GEPLRAFILA NTQILHYIDL NGLKIFDSAT
VDTSIITFAK TPPSLESSFD YLAPTQPSLD TDELHAQPIH QSSLSKDSFI FQDQANQALK
AKIESLGTPL KEWDISIYRG ILTGYNEAFI IDSAKREEIL NNCKDKSEKT RTSKLIKKML
RGRDIKRYGY EWAGLWLICT FPSLNLDIEK YPSLKAYLES FRPRIDQSGE KGCRKKTSNK
WFETQDNIAY HEEFEKEKVV WAEMTNAPSF IYDNNSFFIN QTCYFLIHEH NKYLLGILNS
NLIHNYMKSI SSNLGDGAFR WIKQYIEKLP IPKIDSTNKA LSDEIISLVE QILDSKAKDP
TKDTKELESR IDSLVYKLYN LTNDEIKIIE GK
//
