ID T0E483_HELPX Unreviewed; 2805 AA.
AC T0E483;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=N206_07700 {ECO:0000313|EMBL:EPZ73736.1};
OS Helicobacter pylori UM111.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1352345 {ECO:0000313|EMBL:EPZ73736.1, ECO:0000313|Proteomes:UP000015461};
RN [1] {ECO:0000313|EMBL:EPZ73736.1, ECO:0000313|Proteomes:UP000015461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UM111 {ECO:0000313|EMBL:EPZ73736.1,
RC ECO:0000313|Proteomes:UP000015461};
RX PubMed=24051312;
RA Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA Loke M.F., Vadivelu J.;
RT "Multiple genome sequences of Helicobacter pylori strains of diverse
RT disease and antibiotic resistance backgrounds from malaysia.";
RL Genome Announc. 1:E00687-E00713(2013).
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 -!- 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:EPZ73736.1}.
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DR EMBL; AUSR01000019; EPZ73736.1; -; Genomic_DNA.
DR RefSeq; WP_021308984.1; NZ_AUSR01000019.1.
DR PATRIC; fig|1352345.3.peg.969; -.
DR Proteomes; UP000015461; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR41313; ADENINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR41313:SF1; N6_MTASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:EPZ73736.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000313|EMBL:EPZ73736.1};
KW Hydrolase {ECO:0000313|EMBL:EPZ73736.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EPZ73736.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1796..2048
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 2262..2455
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 445..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2768..2805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 703..730
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1296..1356
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1571..1598
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2480..2528
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2679..2713
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 450..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2768..2797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2805 AA; 322931 MW; 98C81B5CAC9185C1 CRC64;
MQKKKAKNPQ PNLFNILDNG DIATNIPSEE TDKVNETQES LPYVVKNQIN TARMISRNPI
EWARYLSFEK RIYKDNSRED VNFFANGEIK ESSRVYEANK EGFERCITKR YDLIDTIKNR
EFFSKEIDIL TYTNSLEELK SQGLEIELTS HYEVHRKTLE NGNEIVKEYD YLKDIYQEAE
RTKDNELVRE IIPSISSAEY FKLYNKPPFE SLNNENTKLN TNGNEEVKKL EFELAKEVHV
LILEQQLLSA TNYYSWIDKD DYASFAWKMH RLINENKLKE NHLSADNANK IKQFFFNNGF
ILGWTKEEQS TMQENRDYSL RSALLSLEEI AQAKIELQKY YEIVYVNGDG SKRGIKPFKE
ILRDINNFEK AYKERYNELV SLNEAIIQAK EGSNGQQNFS TNNNNTIKNT IETNTSIGNN
IIQNNDNNNP NLSIADLGLE QQNLGEQNGK ERTNRADEPN RTRAGIPQEI HRRSEHGRQQ
EGVERSSDEE LLHQDPSLFI EPREQGGTRG VYRSSDQQAV SEKSHRERDR LHEHVSRGDG
VSAKAEARAD SNGASSQASR MENGARSEEK GDNPSDERGV SQTPQSPSHQ QNSSRDLGLS
LSREQPRQTG RLRLFDHGQM GSLFPTDHEN QRESNDNELD RSSDRANENG DKSPRQNGSA
NQESARSERY GIAQGSSNQS VLPLAQSRLH HAGLSAPNGL GNLEENRDQK RGLLSNLDHL
ESLLNAIRNN TIASEPDFRS RLLEAIQNNE PLKDSLVGVQ LLKDPTTKIF YDKFQLKISP
KKVLEILENR IKKSIETTNE TLNAFNTLDS QAIDGNAISN SVGLNPIQEN EIADNSVELN
NTQEQTAQEQ DTQENAQTTI KQEAPTAPTI PLNPKIDFKP SEEVLIKGTK TRYKANIKAI
ELLKELQAKQ EILKGDYYAT QEEQEILAQF SGWGGLESYF KKDQRPEEFK ELNALLTKDE
FRRAYSSTRD AYYTPKLVID SIYQALDHLG FNNDNHQKEI FEPSLGTGKF IAHAPSDKNY
RFIGTELDPI SANISKFLYP NQVIINTALE NHQFYQEYDA FVGNPPYGNH KIYSSNDKEL
SNESVHNYFL GKAIKELKDD GIGAFVVSSW FMDGKNHKMR EHIAQNATFL GAIRLPNSVF
KATGTEVSSD IVFFKKGVDE ATNQSFTKAM PYYDKIIDSL DDDTLFALQN NRFDSFIPSD
QLKIVNAIAS HFGFKQEKLQ RWYEKIDTAN FGYKEQDYKI IKDFIDKVGE NNINLNEQTL
NEYFIHHPEN ILGHLSLEKT RYSFEINGEQ IYKYELQALE DKSLDLSQAL NQAIEKLPKN
VYQYHKTTLK TDALIIDANN KRYQEVQKLI KNLERGELVK WDNLYFQLEQ NNEMGVFLKP
TKTNSKVQDS RLKAYFKIKD ALNDLTSAEF NPLSSDLELE SKRVRLNLVY DEFVKKFGYL
NENKNRKDIK QDLYGAKVLG LEKDFEKEIT PRSAKMQNIE PRQAQAKKAQ IFFERTLNPK
KELIITNAKE ALIASINQKG CLDLHFIRDH FTTQSLETTI KELLEQKLIY KDHKDNGDYV
LANDYLSGNV KRKLKEVKEA INQGVEGLEA NVKDLELIIP KDLKATEIMA NINSPWIPTQ
YLEEFLIELA ANHYEKQYGD KMTDYQLGNL KEDIKVEHLS GAYEVFARNN DLNELYGIRH
KDKPHSYKAP FESLLNKVLN NKDLSVKYAQ VDPNDPKKEI FITDEEQSNL ARQKAEELKE
AFKDWIYKDY ARRTHLEQIY NDTFNNSVLK TYDGSQLELE GFNHHISLRP HQKNAIFRTI
QDRAVCLDHQ VGAGKTLCAI ASCMEQKRMG LVNKTLIAVP NHLTKQWGDE FYKAYPNANV
LVVESKDITE KERELLFNQI ANNNYDAVII AHTHLELLSN PRGIIEELKE EELVNTEKNF
ERQKLAYKNN PRETKKPNER AFKNKLDKIR AKYDAILEKQ GSHIDISQMG IDNLIVDEAH
LFKNLAFETS MEKIAGLGNQ QGSNRARDLF IKTRYLHQNN KKIMFLTGTP IANSLSEMYH
LQRYLTPDVL KERGLEFFDD WAKTYGEVVN DFELDTSAQS YKMVNRFSKF SDVQGLSTMY
RAFADIVSND DILKHNPHFV PKVYGDKPIN VVVKRSEEVA QFIGVADENG KYNEGSIIDR
MQKCEGKKSK KGQDNILSCT TDARKVALDY RLIDPNAKVE KEFSKSYAMA ENIYENYLET
NATKGTQLGF IGLSTPKTHS QKVSLEAPDN AHEIENKNPL DEAQELLESL SSYDENGNLI
APSKKELENE LKEKKAKSVN LDEEIAKSCS FDVYSDVLRH LVQMGIPQNE IAFIHDAKTE
EQKQDLFKKL NRGEVRVLLG SPAKMGVGTN VQARLVAMHE LDCPWRPDEL LQMEGRGIRQ
GNILHQNDPE NFRMKIYRYA TEKTYDSRMW QIIETKSKGI EQFRNAHKLG LNELEDFNMG
SSNASEMKAE ATGNPLIIEE VKLRAEIKNE EAKYKAFNKE NYFNEENLKN NSSKLDYLKQ
ELKDLETLQS SVMIPTHTEI KLYDLKKEES RDYELIKVKE VEPLKENASM SEELTHKKLK
EQNKQIAEQN KEKLDAIKKQ FASNLNDLFF NEERDCKLLE YKGFVVNAYK TKYQVEFSLS
PKYNPNVAYS PSNMVYKNDT ANMFSSYNFC GEIKFDGFLK RLDNAITKLP EKIKELENSL
KITQENIAKY TRLVEQKPPY SRLEYLQALK WDHKTLIDDL AKMSKDRDYK PVFNPKSQEV
LEKMNAGKRA SLENESLTEE IKEQANQEVH RPMKKVSSGD YDMGM
//