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Database: UniProt
Entry: R5BAJ3_9BACT
LinkDB: R5BAJ3_9BACT
Original site: R5BAJ3_9BACT 
ID   R5BAJ3_9BACT            Unreviewed;       466 AA.
AC   R5BAJ3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=BN689_00608 {ECO:0000313|EMBL:CCX52570.1};
OS   Alistipes sp. CAG:514.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1262696 {ECO:0000313|EMBL:CCX52570.1, ECO:0000313|Proteomes:UP000018254};
RN   [1] {ECO:0000313|EMBL:CCX52570.1, ECO:0000313|Proteomes:UP000018254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:514 {ECO:0000313|Proteomes:UP000018254};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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:CCX52570.1}.
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DR   EMBL; CAWO010000112; CCX52570.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5BAJ3; -.
DR   STRING; 1262696.BN689_00608; -.
DR   Proteomes; UP000018254; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
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   GO; GO:0006260; P:DNA replication; IEA:InterPro.
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; IPR007694; DNA_helicase_DnaB-like_C.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR046138; DUF6140.
DR   InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR   Pfam; PF03796; DnaB_C; 1.
DR   Pfam; PF19637; DUF6140; 1.
DR   Pfam; PF07669; Eco57I; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:CCX52570.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018254};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          107..207
FT                   /note="Type II methyltransferase M.TaqI-like"
FT                   /evidence="ECO:0000259|Pfam:PF07669"
FT   DOMAIN          285..386
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|Pfam:PF03796"
SQ   SEQUENCE   466 AA;  52386 MW;  48B5B2D8BB65D284 CRC64;
     MGRLAAYSGN KDVSILDPGC GLAILSCALI EHIVQEIVPE HISLTLYETD KKVVPLTEDV
     LSYLKTWCGD RKVKLDYQLN ESDFVLEKCE CLDGTDTIFG DLSGTEKFDY IISNPPYFKL
     AKDDIHTRSC ASIVDGQTNI YALFMAICAK LVAEDGQMIF ITPRSFASGR YFQSFRDFLF
     QHVSIDLIHL FNTRKDTFAK DEVLQELVII RMVPAGNGKL ITVSYSQGIS DLDHPYQKKY
     AASEIVDVSS EEKVVYLPVD GRDEAILSLF RSWDGNMEKP EPFRTNGPRE EEMDCVTKSL
     KKAAEELKVP IIVLSQLQRG PDRPQMDDIS DSKDLKELAD VIILMHNGIG WDKIDGQIIG
     EFIIAKNTRG NIGTVELTCD LKQGKFYEEI ISDGVTMKAF RITPKRIRRS NGQVLTPEMS
     VVVSTNLSNP FNNGAKEVAE AYMRIYGFDY KRSCCCKTDF DCVLLG
//
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