GenomeNet

Database: UniProt
Entry: E1W038_GLUAR
LinkDB: E1W038_GLUAR
Original site: E1W038_GLUAR 
ID   E1W038_GLUAR            Unreviewed;      1091 AA.
AC   E1W038;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   OrderedLocusNames=AARI_30390 {ECO:0000313|EMBL:CBT77241.1};
OS   Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS   JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Glutamicibacter.
OX   NCBI_TaxID=861360 {ECO:0000313|Proteomes:UP000006878};
RN   [1] {ECO:0000313|EMBL:CBT77241.1, ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RX   PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA   Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA   Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA   Vallaeys T.;
RT   "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT   adaptation to the surface of cheese.";
RL   PLoS ONE 5:E15489-E15489(2010).
RN   [2] {ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RA   Genoscope.;
RT   "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT   CIP 108037 / JCM 13566 / Re117).";
RL   Submitted (JUL-2010) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQ311875; CBT77241.1; -; Genomic_DNA.
DR   RefSeq; WP_013350346.1; NC_014550.1.
DR   AlphaFoldDB; E1W038; -.
DR   STRING; 861360.AARI_30390; -.
DR   REBASE; 28310; Aar117ORF30390P.
DR   KEGG; aai:AARI_30390; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_009503_1_0_11; -.
DR   Proteomes; UP000006878; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008170; F:N-methyltransferase activity; 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; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR041635; Type_ISP_LLaBIII_C.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   Pfam; PF18135; Type_ISP_C; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:CBT77241.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006878};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBT77241.1}.
FT   DOMAIN          311..499
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          686..1035
FT                   /note="Type ISP restriction-modification enzyme LLaBIII C-
FT                   terminal specificity"
FT                   /evidence="ECO:0000259|Pfam:PF18135"
SQ   SEQUENCE   1091 AA;  121051 MW;  1E86AE3FDFF35105 CRC64;
     MVKIADLVEQ YGALAKDLLN GPGEPEAALS QPVTELIIAV SNDLLQRKTV MHREVREDSG
     TVRPDYGARV DGLMTGHVEL KKPGTSLDPS TYAKTSHNAR QWQRLSNLPN LLHTNGTDWR
     LWRFGELIAD STLHTPSLAT HKGKLTAPAS FLPLITDFLT WTPTPITSVG RLVDTIAPLA
     VMLREEVLES LKADRRFAKA NNIDPGLRPF IGLHRDWRAS LYPRATDEEF ADGFAQTVVF
     ALVVGLSEGI ELEGLKIPEI ASRLKANHTL LGRALDLLTE HVAESTVGLA IETIVRALSA
     ARWQHISQGR QDVYLHLYEH FLSAYNPERR KQSGSFYTPV EVVDSMTRLT DEALKKYLNT
     PEGLSADTVA VIDPAMGTGT YPLSVLRQVA DNSSKYGQGA VSDAVTSAAQ RLYGIELQSG
     PFSVAELRLT QAIRDYGGSL PDGGLNLYVA DTLEDPKSGS SRQLSYTLQL IAEQRQRANK
     MKVETPIQVC IGNPPYKDKS EGLGGWIELG DPNRPNTPLD DFRLPGNGKF EYVLKNLYVY
     FWRWAMWKVF ESTPASHHGV VCFITATGYL NGPGFRGMRQ WIRENTSRGW IINLTPEGKQ
     PPANTAVFNI ETPVSIALFI RDQANDPTAP SEIKYTELHG LRKEKFGALD KLNLSDASFT
     LAGSDWTDGF VPAAGDEWTA FPALNDLFPW TAPGIKPNKT WVYNPNKEIL EQRWNDLILE
     DDKELKAAKF KETSSTGLHL TKKIPLIGSD TEQNTQDAFD SVAWPTQPSI VHVGYRSFDR
     QHIIADSRLL HRASPDLWAA RSKDQVFMVE QHAHEPGRGP GIMLSHLIPD MDYFNNRGGR
     VLPMLNPDGS PNVALDLLDT LSEQLGADLT VDDLFAYVAG ISAHPGYVER FSDEVKYGAN
     RVPITSDLEL WSKTVDIGRL VLWLHTFGER GVAPLGATSI LDHVTTGALP SYDVAVSSAM
     PETATYEPLT QTISLGSGQW SNVDPRVWSY AVGGREVIES WIGYRRKKPK GKRTSPLNDL
     VTTNWPSQWS REFSELLAVL THLVHLEEQQ ADLLEQVLDG PILSVSELED MGVQWPKVPK
     DRKPRMAGDL F
//
DBGET integrated database retrieval system