ID I3UT13_PSEPU Unreviewed; 1633 AA.
AC I3UT13;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, 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=YSA_03453 {ECO:0000313|EMBL:AFK68634.1};
OS Pseudomonas putida ND6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=231023 {ECO:0000313|EMBL:AFK68634.1, ECO:0000313|Proteomes:UP000005268};
RN [1] {ECO:0000313|EMBL:AFK68634.1, ECO:0000313|Proteomes:UP000005268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND6 {ECO:0000313|EMBL:AFK68634.1,
RC ECO:0000313|Proteomes:UP000005268};
RX PubMed=22933774; DOI=10.1128/JB.01190-12;
RA Li S., Zhao H., Li Y., Niu S., Cai B.;
RT "Complete Genome Sequence of the Naphthalene-Degrading Pseudomonas putida
RT Strain ND6.";
RL J. Bacteriol. 194:5154-5155(2012).
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};
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DR EMBL; CP003588; AFK68634.1; -; Genomic_DNA.
DR RefSeq; WP_014754487.1; NC_017986.1.
DR REBASE; 49072; PpuND6ORF3453P.
DR KEGG; ppi:YSA_03453; -.
DR PATRIC; fig|231023.4.peg.1672; -.
DR HOGENOM; CLU_002151_1_0_6; -.
DR Proteomes; UP000005268; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:AFK68634.1};
KW Helicase {ECO:0000313|EMBL:AFK68634.1};
KW Hydrolase {ECO:0000313|EMBL:AFK68634.1};
KW Nucleotide-binding {ECO:0000313|EMBL:AFK68634.1}.
FT DOMAIN 179..382
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 479..650
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1633 AA; 182879 MW; 19BB998938653734 CRC64;
MSALSALLTT YRSASVTERE KGTYFEELVC TYLRNEATYR DLYEKVWTYA QWAKEQGLSG
KDAGIDLVAR TQGTGQYHAI QCKLYAEDYK VQKKDIDSFF TASGKTPFSH RVIVTTTNNW
SEHAEDALQG QQPPVSKIDL QALEDSQIDW AKYQPNQAVA LKAKKQLRDH QQTALNAVAA
GLKDAERGKL IMACGTGKTF TSLKIAEQQT GKGKRVLFLV PSLSLLSQTL TEWTQESTTP
LHSFAVCSDS DVGKKRKAED DAVQVFTHEL RYPATTQADR LAAEMLKRHD AEHMSVVFST
YHSIDVISRA QHEHDMATFD LVICDEAHRT TGATFDDDDE STFVRIHDAD YIRASKRLYM
TATPRIYGDN AKLKAESGEV TLCSMDDEAL YGKELFVINF SEAVQRGLLT DYKVLVLTVE
ESTISRRLQD MLKDENNQLK VDDAAKIVGC WKALAKQGLA ENLVGDDQPM KRAVAFCQVI
SPNYKGTKHK VSSINIASMF QSVVEAYQES ENIDEASRII CEAAHVDGGM NASAKEAKLN
WLKEEPPANT CRILSNVRCL SEGVDVPALD AVLFLTPRNS QVDVVQSVGR VMRNAPGKKR
GYVVLPVVIP AGMEPHEALN DNQTYKVVWQ VLQALRSHDD SFDAMVNKLD LIGSDPRKME
VIAITDKAEK KARKASGTSN GQAGKGQYGI GEKRAKYDVE GQMTQQAELA YEVGEIEKAI
YAKIVDKCGN RHHWEDWAND IAKIARTHID RIQGILENPA NIQEKTAFNA FATELRDDLN
DSISDGEIVE MLAQHLVTKP VFDALFDEYS FASHNPMSKA MQGVLDALHE HHLAKEADTL
DKFYASVRQR AAGINNAQGK QKIIVELYDK FFRNAFPKMT ERLGIVYTPV EVVDFILHSV
NHLLQQEFSQ TLGSKGVHII DPFTGTGTFI TRLIQSGLIK PDELPHKYRH EIHANELVLL
AYYIAAINIE AAYHGEVIDE YTPFEGICLT DTFQMYEKDD LVSALLEDNS ARRQRQKDLD
IRVIVGNPPY SVGQGDANAN NANVPYPSLD ARIRDTYGAR SEATNKNSLY DSYIRAIRWA
SDRIGDAGII GFVTNAGFVD ASTTDGLRKC LNDEFSSLYV FHLRGNARTS GETRRKEKDN
VFGMGSRAPI AISLLVKNPN AEACGQINFN DIGDYLSREE KLEKIAGFSS VAGIEQWQPI
TPDEHGDWVK QRDDSFNQFI VLGEKDDKSA LTLFDNYSNG VKTQRDAWAF NSCKAKLATN
MEGMIGFYNA EVKRFNAAHP GLDTKGRQAQ VDGFIDTDPT RISWTRALKQ DLGKDRSYAF
EVDCLVPALY RPFTKQWLYF NRRFNEMVYQ MPRIFPDAVA ENLVIGVSAT GEKVAFSALI
SRHVPSLHFV DIEGSQCFPL YLYDETAQAS KKDLFSEPTE AGLRRRDAIT DAGLAHFNTT
YPGEQISKED LFYYVYGILH SPDYRERFAD NLSKELPRIP AVKKAADFWA FSKAGRALAD
LHLNYETVEP YPLTIEAKGT LTDADYRVEK MKFAKKGDKT TVIYNPRITL KGIPEVAWDY
VVNGKAALDW VMERQAVRTD KASGIVNDAN DWATETMGNP KYPLELFQRV VTVSLETQKI
VKGLPKLDIG TDD
//
