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Database: UniProt
Entry: I7K5E1_9CLOT
LinkDB: I7K5E1_9CLOT
Original site: I7K5E1_9CLOT 
ID   I7K5E1_9CLOT            Unreviewed;       993 AA.
AC   I7K5E1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=CAAU_0690 {ECO:0000313|EMBL:CCJ32774.1};
OS   Caloramator australicus RC3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Caloramator.
OX   NCBI_TaxID=857293 {ECO:0000313|EMBL:CCJ32774.1, ECO:0000313|Proteomes:UP000007652};
RN   [1] {ECO:0000313|EMBL:CCJ32774.1, ECO:0000313|Proteomes:UP000007652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RC3 {ECO:0000313|EMBL:CCJ32774.1,
RC   ECO:0000313|Proteomes:UP000007652};
RX   PubMed=21421756; DOI=10.1128/JB.00193-11;
RA   Ogg C.D., Patel B.K.C.;
RT   "Draft genome sequence of Caloramator australicus strain RC3T, a
RT   thermoanaerobe from the Great Artesian Basin of Australia.";
RL   J. Bacteriol. 193:2664-2665(2011).
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}.
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:CCJ32774.1}.
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DR   EMBL; CAKP01000031; CCJ32774.1; -; Genomic_DNA.
DR   RefSeq; WP_008908050.1; NZ_CAKP01000031.1.
DR   AlphaFoldDB; I7K5E1; -.
DR   STRING; 857293.CAAU_0690; -.
DR   eggNOG; COG0610; Bacteria.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000007652; Unassembled WGS sequence.
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; 3.
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, ECO:0000313|EMBL:CCJ32774.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007652};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          297..498
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   993 AA;  115106 MW;  0F44314CF9EB4035 CRC64;
     MSIDYTEKGF EENIEDFLVN INGYRKRRLE GQALDSFKKY AIDVEILFEF LESTQAKELE
     KLKSVYKSLY KERIIERINK ELNKRGLIDC LRHGIKDYGV HLKLAYNKPA NSLNYTLLNL
     YSKNIFTVSR QVHYSEKNNN SIDMLIMLNG LPIIVLELKN PLTGQTVDDA KLQFMHDRDP
     KELLFQFKKR TIVFFAVDTE EVYMTTKLDG KDTIFLPFNK GNNGGRGNPE VEGNYKTHYL
     WEEVFQKDSL LDILFNFVFI KKEQIKDSTG EIVEERENLI FPRYHQLDVV RNLEYDTKIN
     GTGKNYLIQH SAGSGKTNSI SWLAHRLAKL HDDENKPIFH SVIVITDRRV LDKQLQDAIY
     QIEHKAGMVA KIEKNSNQLA EAIKNGTRII VTTLQKFPFI IDKIKDVEER NYAIIIDEAH
     SSQTGRSAAA LRVVLSAKSL EEAEELDSQE EDDMEDRINK EIAKLGPHNN ISYYAFTATP
     KAKTLEFFGT QGIDGKYYPY HVYSMRQAIE EGFILDVLKN YVTYKTFYKI AKKIEDDPDV
     PARKAARAIA KYVSLHPHNI AQKTEIIIEH FRQVTRHKIG GRAKAMVVTS SRLHAVRYKQ
     AFDKYINEKG YKDLKALVAF SGTVIDDGIE YTEEGINGIR EKELPEKFKA DEYKILLVAE
     KYQTGFDEPL LHTMYVDKKL EGIKAVQTLS RLNRTCKGKN DTFILDFVND PEDIRKAFQT
     FYEVTELECA TDPNILYDLQ NELNAMQVYT DEEILEVVKL ELDKKIKSSK GQEKLNSILD
     KAVSRFKSLT KEQQEQFKSA AAKYIRTYSF ILQIGPFADS ELHKLYVYLN FLLRKLPKAD
     SIKLDLADEI ALEYYRNEKT FDGSISLVKE GEAVLQPTSF GKTIREEEKV KLSSIIEKLN
     QRFGTDFTET DRLTIDQLEQ DSMNNEDIIL SVNSNDFDNF KLDYTKTFMD ILINRREENE
     KLFLKIIMEE DFRNVIIDYL AKKVYDQLRA KSV
//
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