ID L8DP55_9NOCA Unreviewed; 1654 AA.
AC L8DP55;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=RHODMAR_5072 {ECO:0000313|EMBL:CCQ18455.1};
OS Rhodococcus sp. AW25M09.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1268303 {ECO:0000313|EMBL:CCQ18455.1, ECO:0000313|Proteomes:UP000011207};
RN [1] {ECO:0000313|EMBL:CCQ18455.1, ECO:0000313|Proteomes:UP000011207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AW25M09 {ECO:0000313|EMBL:CCQ18455.1,
RC ECO:0000313|Proteomes:UP000011207};
RA Hjerde E., Pierechod M.M., Williamson A.K., Bjerga G., Willassen N.P.,
RA Smalaas A.O., Altermark B.;
RT "Draft genome sequence of Rhodococcus sp. AW25M09. An Actinomycete isolated
RT from Atlantic Hagfish caught in Hadselfjorden, North- Norway.";
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 -!- 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:CCQ18455.1}.
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DR EMBL; CAPS01000146; CCQ18455.1; -; Genomic_DNA.
DR RefSeq; WP_008720917.1; NZ_CAPS01000146.1.
DR STRING; 1268303.RHODMAR_5072; -.
DR REBASE; 63819; RspM09ORF5072P.
DR eggNOG; COG0286; Bacteria.
DR eggNOG; COG1111; Bacteria.
DR eggNOG; COG4889; Bacteria.
DR OrthoDB; 9776021at2; -.
DR Proteomes; UP000011207; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; 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 CDD; cd22333; LlaBIII_nuclease-like; 1.
DR CDD; cd18785; SF2_C; 1.
DR Gene3D; 3.40.1350.10; -; 1.
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; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR039442; Mrr-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR041635; Type_ISP_LLaBIII_C.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13156; Mrr_cat_2; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF18135; Type_ISP_C; 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; SSF52980; Restriction endonuclease-like; 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 4: Predicted;
FT DOMAIN 189..388
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 669..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1654 AA; 181804 MW; C370AFD60FA202B5 CRC64;
MASVHEVIEA FRGEPSNSER GTKFEQLMVR YFELDPTLSQ QYEQVWRWID WPDRQGKADT
GIDLVARERD TGDYAAIQCK FYEPTTTLSK GDLDSFFTAS GQTFPTADGD RSFTNRVIIS
TTDRWGKNAE DAINHQTIPV QRIGLAEIAE APIDWDIAWP QGELTVELSE AVRNEPRPHQ
VEAIDAVFAG FSAGNDRGKL IMACGTGKTF TALKIAERTA AEAGGSARIL FAVPSISLLS
QTLREWTAQT QLDIRAFAVC SDSKVSRSAE DYSTVDVAIP VTTDPDNLAS HMAHRKRSKG
LTVVFTTYQS LPTVAAAQGM GVDAFDLVIC DEAHRTTGVT VAGADESNFV RVHDAEFLKA
SRRLYMTATP RIFDDAVKEK AADHSAELSS MDDVDIFGPE LHRLSFGDAV ERGLLTDYKV
IVLTVDEDLV AAPMQKQLAG TYSELQLDDA SKIVGCWNGL AKRAGRSPDG DGFAIGAPPM
KRAVAFAKDI AASKQVAEVF PDVVDAYRAL LDENENDGEQ VDATNRDLVV SARHVDGTFN
ALKRNEQLSW LKAPVPEGEC RILSNARCLS EGVDVPALDA VLFLHPRNSV VDVVQSVGRV
MRLSPGKDYG YIILPVAVPA GVSPSQALAD NRRFKVVWQV LNALRAHDDR FNAMVNSIAL
NATTKQAKAG QGNDRLLGGH IGPTTDSDET IGDGRPTPGT DPKPESGEGG TGGVASQMAL
FALSEWQEAI YARIVDKVGT RVYWEQWAAD VADIAAAQIA RINALLIGAS PETAKQFEKF
LTGLRDNLND SIGRDDAISM LSQHLITKPV FDALFAGHDF AAHNPVSIVM QQMLDTLGDA
NLESETAGLD SFYDSVRVRA SEVTSAEGKQ QVIAELYERF FRVAFKKQSD ALGIVYTPVE
IVDFILRAAD HVSKEHFGKG LTDTGVHILD PFTGTGTFLT RLLQSGLILP DDLSRKYRDE
LHANEIMLLA YYIAAVNIET TYHALTTPSG EEGQYESFEG IVLTDTFQMS ENGDTMDAIM
FPQNNDRVIR QQEAPINVIV GNPPYSKGQD SANDDNANLS YPTLDARIAA TYAGRSTATN
KNSLYNSYYR AYRWATDRVG DQGIVAFVSA GGWVDGNTAD GVRLSFADEF AHLWIYNLRG
NQRAAGELSS KEGGKVFGSG SRSTIVIFVG VKDAAHSGPA QIHYRDIGDY LDREEKLHIA
EVSTISNTEW REISPNSYGD WITQRDDAFG SWPVIGTKTQ SDSSPIFATY AYALLTARDA
TVYNFSRSAL FANVTAAAIA YSDVLAAYEQ QRSADGKPSA AGDIDQFLFG SQNTTTAIKW
SDSLKRHLVR GLPVMFDSSQ AVEAAYRPFN RTNLYFDPVL NHRRGLLPTM FPTGLHTNYG
LHLVAAGSDK PFSVLAVGMI PDLSFWGFGS SQFFPRYTYE NVGPPIDGVL DFDSTADSPS
EQEGGYRRVD NITDEILDVY RTALGSSVTR DQIFWSVYGQ LHVPGYRETY AADLKKMLPH
IPTPESLGRF TQLADAGEQL GTLHMQYEDV APYPLDVEIR AGVDEHERET WRVQKMKWRS
KSDHTAIVYN SKVTITGIPL EAEEYMLGAR SALAWVIDRY QVKTDKPSGI VNDPNLWCDE
HDDPTYIVEL IKKVTTVAVE TMRIVRELDI EKAA
//
