ID A0A171KRN1_9BURK Unreviewed; 1072 AA.
AC A0A171KRN1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-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=AAV32_10125 {ECO:0000313|EMBL:KKO71548.1};
OS Kerstersia gyiorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Kerstersia.
OX NCBI_TaxID=206506 {ECO:0000313|EMBL:KKO71548.1, ECO:0000313|Proteomes:UP000078084};
RN [1] {ECO:0000313|EMBL:KKO71548.1, ECO:0000313|Proteomes:UP000078084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1 {ECO:0000313|EMBL:KKO71548.1,
RC ECO:0000313|Proteomes:UP000078084};
RA Greninger A.L., Kozyreva V., Chaturvedi V.;
RT "Genome sequence of Kerstersia gyiorum CG1.";
RL Submitted (APR-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:KKO71548.1}.
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DR EMBL; LBNE01000006; KKO71548.1; -; Genomic_DNA.
DR RefSeq; WP_068371168.1; NZ_LBNE01000006.1.
DR AlphaFoldDB; A0A171KRN1; -.
DR STRING; 206506.AAV32_10125; -.
DR REBASE; 128509; KgyCG1ORF10115P.
DR PATRIC; fig|206506.3.peg.2166; -.
DR Proteomes; UP000078084; 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 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; 4.
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 InterPro; IPR021810; T1RH-like_C.
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 Pfam; PF11867; T1RH-like_C; 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, ECO:0000256|RuleBase:RU364115};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Helicase {ECO:0000313|EMBL:KKO71548.1};
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:UP000078084};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 286..500
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 524..554
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1072 AA; 120143 MW; 0685140E7A1BD1EB CRC64;
MTEDQLEQEA LGWLAETGYT LRSGPDIAHD GTDPQRSGYT QVVLTARLRA AMAKLNPGIP
AAALDDALQQ VEHLDTPVQL VANRAFHKLL VNGVPVQYQK DGETRGDLVR LVDWSNPQNN
EFWAVSQFTI KGPHHTRRPD IVLFVNGLPL VLMELKNSVN ENADIWKAYG QIQTYKAQIP
DIFDYNEILV ISDGSEARFG SLSANAERFM QWRTINGVTL DPLGQFNELE TLIRGLLAPH
YLLDYLRYFV LFEDDGKFIK KVAGYHQFHA VRFAIEEVVR ASSPDAQHDK RGKGGVVWHT
QGSGKSITMT CFAARVMQEP ALQNPTIVVI TDRNDLDGQL FGVFSLSQDL LREQPVQAAT
RQQLRTLLGN RPSGGIVFAT IQKFMPGEDE DIFPELSNRS NIVVIADEAH RTQYGFESKL
KTRKHNPNSQ SAYNLTPDGV PSSALTVEFA GAEYQTKYQA GYAQHLRDAL PNATFVAFTG
TPVSSTDRDT RSVFGDYIHV YDMQQAKEDG ATVAILYESR LAKLKLKEAD LEAIDEEVDE
LAEDEEENTQ ARLKSKWAAL EKVVGAEPRI ASVAADLVEH FEERNKAQDG KAMVVGMSRD
ICVHLYNEIV KLRPDWHDDD PEKGAIKVIM TGSASDKALL QPHIYSSQVK KRLEKRFKDP
ADPLKMVIVR DMWLTGFDAP CVHTMYIDKP MKGHNLMQAI ARVNRVFRDK QGGLVVDYIG
IGNELKAAMK EYTASNGRGK PTVDAHEALA VMLEKLDVLR AMLHGYDYCG FKTGGHKTLA
GAANHILSLR PPPSQKDSKL DGKKRFADAA LALSKAFSLC CTLDEAKALR DEVAFMQAVK
VILTKRDIST QKKTDEQREV AIRQIISQAV VSEHVVDIFD AVGLEKPNIG LLDDEFLAQV
RNLPERNLAV ELLERLLEGE IKSKFSSNIV QQKKFSELLS GVITRYQNRS IETAQVMEEL
VEMAKKFREA AGRGEELGLS EDEIRFYDAL ATNESAVLEL TDETLKKIAH ELTENLRKNI
TVDWSKRESV RASLRLMVRR ILRKYKYPPD MADAAVELVL QQAEVLGEQW SQ
//
