ID M3PXM0_HELPX Unreviewed; 2693 AA.
AC M3PXM0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=HMPREF1421_00515 {ECO:0000313|EMBL:EMH29673.1};
OS Helicobacter pylori GAM265BSii.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1159049 {ECO:0000313|EMBL:EMH29673.1, ECO:0000313|Proteomes:UP000011872};
RN [1] {ECO:0000313|EMBL:EMH29673.1, ECO:0000313|Proteomes:UP000011872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAM265BSii {ECO:0000313|EMBL:EMH29673.1,
RC ECO:0000313|Proteomes:UP000011872};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Antonio M., Secka O.,
RA Thomas J., Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2012) 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:EMH29673.1}.
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DR EMBL; APDY01000033; EMH29673.1; -; Genomic_DNA.
DR RefSeq; WP_001958587.1; NZ_KB642340.1.
DR PATRIC; fig|1159049.3.peg.480; -.
DR HOGENOM; CLU_000181_6_0_7; -.
DR Proteomes; UP000011872; 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: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; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 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; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR41313; ADENINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR41313:SF1; DNA METHYLASE ADENINE-SPECIFIC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07669; Eco57I; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:EMH29673.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000313|EMBL:EMH29673.1};
KW Hydrolase {ECO:0000313|EMBL:EMH29673.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EMH29673.1}.
FT DOMAIN 1686..1938
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 2152..2345
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 283..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2655..2693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2370..2418
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2569..2603
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 339..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2655..2673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2693 AA; 309762 MW; 306AB49DEAEBE727 CRC64;
MDFKKCPNFE KKCAFLCFSN LVLLIEIHSK GHKMQKKKAK NPQPNLFSIL DNGNEIAKEY
DYLKDIYQEA ETTKDGELIR EIIPSISSDE YFKLYNKLPF ESINNENTKL NTNDNEEIKK
LEFELAKEAH ALILEQQLLS ATNYYSWIDK DDYANFAWKM HRLINENKLK ENHLSADNAN
KIKQFFFNNG SILGWTKEEQ SAMQENRDYS LKSDLLSLEE IAQAKIELQK YYESVYVNGD
GNQRDIKPFK EILRDINNFE KAYKQRYNKL VSLNEAIIQA KESSNERQNY SANNNNPINN
TIETHTSNNI IKNNDNNHPN LSLADLELEQ QNLGEPNGKE RTNRADEPSR ARAGIPQEIH
RRSEHGGQQE GMERSSDEEF LHQNPNLFIE PREQGGTRGV YRSSDQQAVS EKPHRKRDRL
HEHVFGGDGI SARADGNGAS NQASRMENGA RSEEKGDNPP NERGIPQPPQ SPSHQQNSSR
DLGLSFSREQ PGQTGRLRLF DHGQMGSLFP TDHENQRSQN NNEFDKSSDR ANENGDRSPR
QNGSANQEGA RGERFGIAPG SSNQSVLLPA QSRLHLAGLS APNGLRDLEE NRDQEGRLLS
NLNHLESLLN AIRNNTIASE PDFRSRLLEA IYHNEPLKDS VVGTQLLKDP TTKIFYDKFQ
LKISPKKVLE ILENRIQKSI ETTNEALNAF NAPDSQAIDK NAISNSVELN PTQENEITDN
SVELNNAQEQ TAQEQDTQET EQTTLKQETQ EQETPTTLPI PLNPKIDFKP SEEVLIKGAK
TRYKANIEAI RLLKELQAKQ EILKGDYYAT LKEQEILAQF SGWGGLESYF KKDQHPKEFE
ELKALLTKDE FRRAYSSTRD AYYTPKLVID SIYQALDQLG FNNDNHPKEI FEPSLGTGKF
IAHAPSDKNY RFMGTELDPT SASISQFLYP NQVIQNTALE NHPFHQDYDA FVGNPPYGNH
KIYSSNDAEL SNESVHNYFL GKAIKELKDD GIGAFVVSSW FMDAKNPKMR EHIAKNATFL
GAIRLPNSVF KATGAEVTSD IVFFKKGVDE ATNQSFTKSM PYYDKILNSL DDETLFALQN
NRFDSFIPSD QLKIVNAIAN HFGFKQEKLQ RWYEKIDATN FGYSAQDYKI IKDFMDKVGE
NNINLNEQTL NEYFIHHPEN ILGRLSLEKT RYSSEINGEQ IYKYELQALE DESLDLSQAL
KQAIEKLPKD VYQYHKTTLK TDALIIDPSN ERYQEVQKLI KNLERGELVK WDNLYYKLEQ
DNEIGIFLRP TKINSKAQDS RLKAYLKIKD ALNGLTSAEL NPLSSDFELE NKRAKLNLVY
DGFVKKFGYL NENKNRKDIK QDLYGAKVLG LEKDFEKEIT PRSAKMQNIE PRQAQAKKAQ
IFFERTLNPK KELIITNAKE ALIASINQKG GLDLHFIRDH FKTQSLETTI KELLEQKLIY
KDHKDNGDYI LANDYLSDNV KRKLKEVKEA INQGVEGLEV NLKDLELIIP KDLKATEIMA
NINSPWIPTQ YLEEFLMELS ANHYEKQYGD KMTDYQLENL KENIKVEHLN GAYEVSIRSD
GLNELYGIRH KDKPHSYKAP FESLLNRVLN NKDLSVKYAQ VDPNDPKKEI FIADEEQSNL
AKQRAEELKE AFKDWIYKDY ARRTHLEQIY NDTFNNLVLK TYDGSQLELE GFNHNIKLRP
HQKNAIFRTI QDRSVCLDHQ VGAGKTLCAI ASCMEQKRMG LVNKTLIAVP NHLTKQWGDE
FYKAYPNANV LVVDSKDITE KERELLYNQI ANNNYDAVII AHTHLELLSN PREIIEGLKE
EELVNAETIF ERQELAYKNN PRENKKPNER AFKNKLDKIR AQYDAILEKQ GSHIDISQMG
IDNLIVDEAH LFKNLAFETS MEKIAGLGNQ QGSNRARDLY LKTRYLHQNN KKIMFLTGTP
IANSLSEMYH LQRYLTPDAL KERGLEFFDD WAKTYGEVVN DFELDTSAQS YKMINRFSKF
SDVQGLSTMY RAFADIVSND DILKHNPHFV PKVYGDKPIN VVVKRSEEVA QFIGVADENG
KYNEGSIIDR MQKCEGKKNK KGQDNILSCT TDARKVALDY RLIDPNAKVE KEFSKSYAMA
ENIYENYLET HATKGTQLGF IGLSTPKTHS QKVSLEVLDN AHELENTNPL DETQELLESL
SSYDENGNLI APSKKELENE LKEKEAKSVN LDEELAKGCK FDVYSDVLRH LVQMGIPQNE
IAFIHDAKTE EQKQDLFKRV NRGGVRVLLG SPAKMGVGTN VQTRLVAMHE LDCPWRPDEL
LQMEGRGIRQ GNILHQNDPE NFRMKIYRYA TEKTYDSRMW QIIETKSKGI EQFRNAHKLG
LNELEDFNMG SSNASEMKAE ATGNPLIIEE VKLRAEIKSE EAKYKAFNKE HYFNEESLKN
NASKLDYLKQ ELKDLETLQR SVIIPTHTEI KLYDLKNEES KDYELIKVKE VEPLKENASM
SEELTHKKLK EQNKQIAEQN KEKLDAIKKQ FASNLNTLFV NEEEDYKLLE YKGFVVNAYK
TKYQVEFSLS PKDNPNIAYS PSNMIYKNDT GNMFSSYNFC GEIKFDGFLK RLDNAITKLP
EKIKELENSI ETTKENISKY TRLVEQKLPY PRLEYLQALK LDHKTLIDDL AKMGKDRDYK
PAFNPRSKEV LEKMNAEKRA SLENEREEVK EQANQEAYSP MKKAANDDYD MGM
//
