ID B0MVR9_9BACT Unreviewed; 1079 AA.
AC B0MVR9;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=ALIPUT_01185 {ECO:0000313|EMBL:EDS04122.1};
OS Alistipes putredinis DSM 17216.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=445970 {ECO:0000313|EMBL:EDS04122.1, ECO:0000313|Proteomes:UP000005819};
RN [1] {ECO:0000313|EMBL:EDS04122.1, ECO:0000313|Proteomes:UP000005819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17216 {ECO:0000313|EMBL:EDS04122.1,
RC ECO:0000313|Proteomes:UP000005819};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS04122.1, ECO:0000313|Proteomes:UP000005819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17216 {ECO:0000313|EMBL:EDS04122.1,
RC ECO:0000313|Proteomes:UP000005819};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Alistipes putredinis (DSM 17216).";
RL Submitted (NOV-2007) 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:EDS04122.1}.
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DR EMBL; ABFK02000017; EDS04122.1; -; Genomic_DNA.
DR AlphaFoldDB; B0MVR9; -.
DR eggNOG; COG1061; Bacteria.
DR HOGENOM; CLU_005929_0_0_10; -.
DR Proteomes; UP000005819; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease 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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:EDS04122.1};
KW Hydrolase {ECO:0000313|EMBL:EDS04122.1};
KW Nuclease {ECO:0000313|EMBL:EDS04122.1}.
FT DOMAIN 162..335
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 683..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 123459 MW; 62970A8ABC6EB38D CRC64;
MKFTSSLKLK LIYVFRINDA AHKGCLKVGE ATCDNDNVFG LAPNSKALNE SAKKRINQYT
QTAGIAYDLL YTELTIYNSK YGLCSFNDKE VHSVLERSGI KKKIFDTENK ANEWFITDLE
TVKRAIIAVK EGRESLSSAE VSHDKSPIVF RPEQREAIEK TKKQFKKGNQ MLWNAKMRFG
KTLSALQEVK DMDFSRTLIL THRPVVDSGW FEDFGKIFYD RRDFAYGSKN NGDSHTSLET
RAKQGQCKYV YFASMQDLRG SELVGGNFDK NNEVFATAWD CIIVDEAHEG TQTDLGKAVM
QELTKDKTKI LRLSGTPFNL LDDFKEDEIY TWDYVMEQRA KASWDELHFG DPNPYASLPT
MNIYTYDLGR LLNEFVDEDV AFNFREFFRV NDNGTFVHDK DVSAFLNLIT KEDRESCYPF
ANEEYRNIFR HTLWMLPGVK EARAMSAMLQ THSVFQHFKV VNVAGNGDED EESKDALVAV
EEAIGKDPDA TRTITLSCGR LTTGVSVKAW TAVFMLSGSY NTAASSYMQT IFRVQTPAAI
NGKVKEQCYV FDFAPDRTLK VIAETAKISS KTGKTSGNDR KIMGEFLNFC PIISIEGSKM
NQFDVPRMLE QLKKVYVERV VRNGFEDRSL YNDELMKLND LELQEFDDLK KIIGQTKAMP
KTNQVDINNQ GLTDEQYEEL ESLEKKSKKK GKDKQPLTEE EKQRLEELKK KKNNREAAIS
ILRGISIRMP LLIYGAELKD ESQEITIDNF ASLIDPQSWE EFMPKGVTKQ KFNNIKKYYD
PEIFCAAGKR IRAMARAADK LSVEERIERI TDIFSTFRNP DKETVLTPWR VVNMHLGDCL
GGYNFFEQGY ETTLSEPRFI DKGEVTANVF AEDSRILEIN SKSGLYPLYM AYSIYRTRVK
NSLFSVSSIE DEQQIWDKVV AENIFVICKT PMAKSITKRT LIGFRKAKVN TRYFEDLINQ
IKNKPEHFIK QVDKFVSERT GIKNMKFNAI VGNPPYQVMD GDAQASSVPV YQYFVSIAKK
VQPNFISMIM PARWYAGGRG LDDFRADMLS DKTIRSLHDY PKASDLFSNV GSKVDYAIS
//
