ID A0A022KUX6_9MICO Unreviewed; 1039 AA.
AC A0A022KUX6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=D641_0107455 {ECO:0000313|EMBL:EYT49657.1};
OS Brachybacterium muris UCD-AY4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1249481 {ECO:0000313|EMBL:EYT49657.1, ECO:0000313|Proteomes:UP000019754};
RN [1] {ECO:0000313|EMBL:EYT49657.1, ECO:0000313|Proteomes:UP000019754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-AY4 {ECO:0000313|EMBL:EYT49657.1,
RC ECO:0000313|Proteomes:UP000019754};
RX PubMed=23516213;
RA Lo J.R., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT "Draft genome sequence of an Actinobacterium, Brachybacterium muris strain
RT UCD-AY4.";
RL Genome Announc. 1:E0008613-E0008613(2013).
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:EYT49657.1}.
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DR EMBL; AORC01000008; EYT49657.1; -; Genomic_DNA.
DR RefSeq; WP_017825020.1; NZ_KB403093.1.
DR AlphaFoldDB; A0A022KUX6; -.
DR STRING; 1249481.D641_0107455; -.
DR REBASE; 62892; BmuAY4ORFDP.
DR HOGENOM; CLU_010804_0_0_11; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000019754; 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:0004386; F:helicase activity; 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.
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 Helicase {ECO:0000313|EMBL:EYT49657.1};
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:UP000019754};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 285..523
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
FT REGION 648..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1039 AA; 115985 MW; F8B4507D31B41CFF CRC64;
MSASGLHQEL PFQDEIASHL EDHGWRRSRN SVDYDKERAL FPEDLLGWLK DTQPKEYEKI
VTPGLNDEGR EKAEARILDR VVKVLASDEA HGGGTLGLLR KGFDMVGLRH GFKAMQMPPA
DDRNPDLTAR YAKNRLRVMQ EVVYSKDKTD RIDLVLFCNG LPVATIELKT DYTQTLAQGI
AQYRDDRSPV NEPLLTEFRG ALVHFVVTDT RIVMTTKLEG PGTTFLPFDM GHDNGAGNPP
ETGTSFFWKD VLDRDAWLAI LAKFIYINHE TREDPLTGEV TDKRRIRFPR FHQWRAVTRL
TAAARNEGPG HHYLIQHSAG SGKTDSIAWT AHRLSTLHTP EGTKVFDTVI VIADRQVLDR
QLQDAVDQLV TTTGTFQAIT RGSGSSKTKL LREALTAGVP IIGVTIQTFP YVLTALKDAA
EKGEDSSIAG KRFAVIADEA HSSQSGEASA AVRKVVYLND PASGLDEDAE PGADQDALVT
MAAKVDTDQR ISFFAFTATP KAKTLEQFGR PGPDGKPAPF DLYSMKQAIE EGFILDVLKN
YTTYERAARI SLKAGGEDIE VDARTGTKAY LTAVNLHPTN IDQKVREIIR HYRAAVQPEL
GGRAKAMVVT DSRAAAVRYA RSFRRICTEE KLDLHALVAF SGDVPDPEIT ALPGTRPPTV
TETSENPQLK GRDLAKVFAG PDEHVLIVAN KYQTGFDQPL LVGMYVDKQL SGIAAVQTLS
RLNRMAPGKS DTYVLDFVND PEQILAAFRE YYEDAEITTE SDPDLVMDMH AKLEQAGIHT
PQEMDLFWEA WTRKGAKHTD PERHIKPAED RFGDRWRRAL LTGDRAERDA LIDYRSTLTQ
YIKAYAFFSQ LVDYGNPRYE KFSAFADLLA RRLRGFTDED PTPDEVDVSD IVLTHYRLQK
IREDDLKLGE IEPEGLKGMT EAGMAAARER KRERKTEIID KVNRYLGGLD VPDDYKLSGV
ESLIAEVVSD HTMQAIAHSN SRIDFAAAPG MKTVVENAVW SVEESSGAVI KHLRDMPWEE
LRTMLLDVGL YERLQEAAS
//
