ID A0A0W7Z2S5_9BURK Unreviewed; 1033 AA.
AC A0A0W7Z2S5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE Short=R protein {ECO:0000256|RuleBase:RU364115};
DE EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
GN ORFNames=AS359_01870 {ECO:0000313|EMBL:KUF41571.1};
OS Comamonas kerstersii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=225992 {ECO:0000313|EMBL:KUF41571.1, ECO:0000313|Proteomes:UP000053300};
RN [1] {ECO:0000313|EMBL:KUF41571.1, ECO:0000313|Proteomes:UP000053300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12322-1 {ECO:0000313|EMBL:KUF41571.1,
RC ECO:0000313|Proteomes:UP000053300};
RA Ming D., Wang M., Hu S., Zhou Y., Jiang T.;
RT "Complete genome sequence of a multi-drug resistant strain Acidovorax sp.
RT 12322-1.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
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 ECO:0000256|RuleBase:RU364115};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S. {ECO:0000256|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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:KUF41571.1}.
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DR EMBL; LPXH01000022; KUF41571.1; -; Genomic_DNA.
DR RefSeq; WP_058879694.1; NZ_LPXH01000022.1.
DR AlphaFoldDB; A0A0W7Z2S5; -.
DR Proteomes; UP000053300; 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 CDD; cd18030; DEXHc_RE_I_HsdR; 1.
DR CDD; cd22332; HsdR_N; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
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; IPR004473; Restrct_endonuc_typeI_HsdR.
DR InterPro; IPR040980; SWI2_SNF2.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF15; TYPE I RESTRICTION ENYME HINDI ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 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, ECO:0000256|RuleBase:RU364115};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000313|EMBL:KUF41571.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364115};
KW Reference proteome {ECO:0000313|Proteomes:UP000053300};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 275..440
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1033 AA; 116805 MW; 37629669829FD213 CRC64;
MSEQARPERK TQNRVAALFT DASRPDCLGY DHLGEWSKRD NNRCIEADCL RSNLKKRGYS
DAHISAALQK LLTAADSTGI TLYQANLRTY QLLRYGIPVQ IAAGQAHETV HLIDWETPGN
NDFGLAEEVT LRGGYERRPD LVIYINGIAV AVIELKRSSV EVADGVRQLI TNQEEIFNKG
FFSTVQLVLA GSDSQGLRYG TTGTPEKFFV EWKERKDKGA ATSEPLAEGA LLDIPLAQMF
DKVRLLDLIR NFIIFDGGQK KVPRVHQYYG VKAAQERVKQ QEGGVIWHTQ GSGKSILMVL
IAKWLLEFDP DARVLVITDR DELDKQIVGV MRNAGVVGED VASPRITSRA ELIEKLGAAT
PRLMCALIHK FDTSDLKGTP PRVTGRIYVF VDECHRTQGG DMNKQMKRWL ENAIFIGFTG
TPLLRKDKQT TREVFGTYIH TYKFDEAVAD KVVLDLKYEA RNVPQRLTSK KHIDAWFEKS
TKGLNNFQRS VLRKRWATME ELMSAGERKQ RIIADIIHDF GVKPRLNNDR GTAILVAASI
YDACHYFRLF QNTSFGKYCG IITSYEPNHN AISREPKDSD ERYKFDTYTQ HVLQKDQTTK
DYEDKTKQRF IDEPTNLKLL IVVSKLLTGF DAPSCTYIYL DNELRDHNLF QAICRTNRLD
GDDKDYGHIV DYKELFEKVQ DSIAVYTSDE LDIDEGGDDG NVAVKDWLKE GKAQLDAARE
ALRYLCEPVA IPRKMEQYLH YFCGDANDPE ALLNTEPLRI SFYKLTATFL RAYAAIAQNL
EDAGYSAADI AALKTEIDFY SDTRTAIKKH SGEELDIKPY EADMRHLINT YIQADPAEDL
GNLSSLSLTE LIIETGIHDA IAKKLNQKGK LSKKAIAEGI INNIRKTIIR DQLTDPRFYD
EISKLLEDLI EQKRDDTAAY EKFLQKAEEL VKKMAAKNTS SHPHVLNGHS EAIALFNNLS
SIPATTFVCP TDDDGKATLA LELDQAMREQ APAGWKGDDI REKQVLNALF PIMSRDRVAT
QAIFEIIKNQ PGY
//
