ID Q1GY15_METFK Unreviewed; 1022 AA.
AC Q1GY15;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN OrderedLocusNames=Mfla_2607 {ECO:0000313|EMBL:ABE50872.1};
OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylobacillus.
OX NCBI_TaxID=265072 {ECO:0000313|EMBL:ABE50872.1, ECO:0000313|Proteomes:UP000002440};
RN [1] {ECO:0000313|EMBL:ABE50872.1, ECO:0000313|Proteomes:UP000002440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT / ATCC 51484 / DSM 6875 {ECO:0000313|Proteomes:UP000002440};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT "Complete sequence of Methylobacillus flagellatus KT.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC fragments with terminal 5'-phosphates, ATP is simultaneously
CC hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000256|ARBA:ARBA00000851};
CC -!- SIMILARITY: Belongs to the HsdR family.
CC {ECO:0000256|ARBA:ARBA00008598}.
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DR EMBL; CP000284; ABE50872.1; -; Genomic_DNA.
DR RefSeq; WP_011480825.1; NC_007947.1.
DR AlphaFoldDB; Q1GY15; -.
DR STRING; 265072.Mfla_2607; -.
DR REBASE; 12132; MflKTORF2604P.
DR KEGG; mfa:Mfla_2607; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_010804_0_0_4; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000002440; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR040980; SWI2_SNF2.
DR PANTHER; PTHR42927; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42927:SF1; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002440};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 302..520
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1022 AA; 115237 MW; 3804979E0F50E817 CRC64;
MSGHTENDFE TAIEAGLIGT GGYVKRSPNA YDESLALFPD DVTGFLKDSQ ATKWAQLEAL
LGVKTEATVL DSLAKELEIK GTLHVLRHGF KCYGKTFRLA YFRPNSGMNP EAAALYAANR
LTITRQVAFT SVMKNAEGKH RRCIIDVTLS LNGLPVVTAE LKNPLTGQRA ADAVRQYVEA
RDERDLLFAF KKRALVHFAV DPDEVWMTTR LKGKETVFLP FNRGHNHGAG NPPVEGNWKT
HYLWDEVLQA DSLLDILQRF MHLEVKERQV KTDKGARTIR KETMIFPRYH QLDAVRKMVA
HAREQGSGRN YLIQHSAGSG KSNSIAWLAH RLASLHDAQD QKVFHSVVVV TDRRVLDQQL
QNTIYQFEHK TGVVEKIDED TQQLARALSQ GTPIIITTIQ KFPFISQALS TLERKGAGVK
IDTAGRRFAV IVDEAHSSQS GETATALRGM LNRDGIEAAI AAQMSDEEDD DLSAEARAAL
LRDALKRARQ PNLSFFAFTA TPKFKTKVLF DEPGPSGTSP FHEYTMRQAI EEGFIMDVLQ
NYTTYKRFFG LIKQVENDPE VPRKKAAKAL TRYLELHPVN IEQVVSVIVE HFRLYVMHEL
GGRAKAMVVT GSRLAAVKYK LAFDQYIKAN GYTGIRSLVA FSGTVEDPDD PGASYTEVSM
NDGLAESELP ETFERDDYRV LLVAEKYQTG FDQPLLQTMY VVKKLAGVQA VQTLSRLNRM
APGKARTFVL DFANEEDDIF KAFKPYYEAT PIGENADPHR LSELQHKLLE WAIFAPADVG
AFAEVWYRPK REHSASDHRV MNALLDTVVH RFGEREEHEQ EEFRGQLTAY RNLYAFLSQI
IPYQDSELEK LYTFVRNLIA KLPPPGDGQA FVLDDEVALR YFRLQQMTEG SIELGKGYAA
PLKGPTDVGT LRVAEEPVTL SSLVDKLNER FGTDFNEADQ LFFDQIRATA EGNEQIIEAA
RANNLGDFSS YLERALDELF IDRMEGNEEI FSRIMTDKAF RSAAHEHLAL EIFRRVREDA
EK
//
