ID F0T1T3_SYNGF Unreviewed; 996 AA.
AC F0T1T3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN OrderedLocusNames=Sgly_0848 {ECO:0000313|EMBL:ADY55197.1};
OS Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Syntrophobotulus.
OX NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY55197.1, ECO:0000313|Proteomes:UP000007488};
RN [1] {ECO:0000313|EMBL:ADY55197.1, ECO:0000313|Proteomes:UP000007488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RX PubMed=21886864;
RA Han C., Mwirichia R., Chertkov O., Held B., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Syntrophobotulus glycolicus type strain
RT (FlGlyR).";
RL Stand. Genomic Sci. 4:371-380(2011).
RN [2] {ECO:0000313|Proteomes:UP000007488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Syntrophobotulus glycolicus DSM 8271.";
RL Submitted (FEB-2011) 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; CP002547; ADY55197.1; -; Genomic_DNA.
DR RefSeq; WP_013624068.1; NC_015172.1.
DR AlphaFoldDB; F0T1T3; -.
DR STRING; 645991.Sgly_0848; -.
DR REBASE; 33842; Sgl8271IP.
DR KEGG; sgy:Sgly_0848; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_010804_0_0_9; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000007488; 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; 1.
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:UP000007488};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 290..494
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 996 AA; 115046 MW; 9461BB0DA9E34361 CRC64;
MSITTENTFE SALVQSLVEQ GGYTEGNAPD YSPELGMFKY EVIKFLQESQ PKRWDKIYSI
HGEDANNRVI QRLYKELDLR GSLDVLRNGF VDYGVRFQMA FFQPASGLNP DAIDLYNKNS
LKVYRQIFYS TKNKNSLDVL LSLNGIPVAT FELKNQFTGQ DVGNALKQYA STRDNREILF
AFRKRSLVHF AVDQDEVFMT TKLDGSKTYW LPFNKGANSG KGNPLNPNGY RTAYLWENIL
QKDSWMEIIQ RFVHLQTEEI EVEGKVYKKE KLIFPRYHQL DAVRRISEKV LEVGTGKNYL
IQHSAGSGKS NSIAWLVYRL SSLHNATDER IFDSVIVVTD RKVLDQQLQN TIYQFEHKTG
VVQKIDKDSS QLASALGYGT NIIITTLQKF PFVVDKVGEL PDRKYAVIID EAHSSQGGEA
SKKLKEVLAE KSLEKAETED TDDYNGDDFV REQIERTAAS RGQQPNISFF AFTATPKYKT
LQVFGDKDSE GKPKPFHLYS MRQAIEEGFI LDVLHYYVTY ELYFKLTKAI KEDPNLNKKR
AAKAIGKFVS LHPHNLAQKT EIIIEHFREI VSKKIGGKAK AMLVCGSRLH AKRYFEEFNR
YIKTKGYANE IKILVAFSGK VTDDNYPDGV SEPQMTGYGE KELPAIFDKD EYRILIVADK
YQTGFDQPLL HTMYVDKKLS GVKAVQTLSR LNRIHPGKED TFVLDFANDR QTILDSFQPY
YEITSVIEET DVNHLYDLKA RLDEFKIYWK EEIEAFANIY FDPKTKLNNS KQQKLLYAFT
DPAVDRYKDI PEHERQDEFK KGLRSWTNLY AFLSQIMPFF DAESEKFYAY AKLLQTRLPR
RGLSESLQLD DEVALEYYRL QKIKEGSIEL QKGEEGELSG TSEAGLKRAK EEKALLSEII
NMLNEQFGTE FDEADNLFFD QIEAELMEDE TLQTQAKVNK IDTFKFAFDD KFIDKLIGRM
DQNQEIFEKI LEDKAFGDLV KQLMMKKIYR RMNELV
//
