ID A0A0D7K4T9_9BURK Unreviewed; 1051 AA.
AC A0A0D7K4T9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=RP29_18950 {ECO:0000313|EMBL:KJA08992.1};
OS Acidovorax temperans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=80878 {ECO:0000313|EMBL:KJA08992.1, ECO:0000313|Proteomes:UP000032566};
RN [1] {ECO:0000313|EMBL:KJA08992.1, ECO:0000313|Proteomes:UP000032566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KY4 {ECO:0000313|EMBL:KJA08992.1,
RC ECO:0000313|Proteomes:UP000032566};
RA Sheng K.-Y., Chin P.-S., Chan K.-G., Tan G.S.;
RT "Isolation of bacteria from lake water.";
RL Submitted (DEC-2014) 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:KJA08992.1}.
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DR EMBL; JXYQ01000078; KJA08992.1; -; Genomic_DNA.
DR RefSeq; WP_044402435.1; NZ_JXYQ01000078.1.
DR AlphaFoldDB; A0A0D7K4T9; -.
DR STRING; 80878.RP29_18950; -.
DR PATRIC; fig|80878.5.peg.3765; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000032566; 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; 3.
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; 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};
KW Helicase {ECO:0000313|EMBL:KJA08992.1};
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:UP000032566};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 304..487
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1051 AA; 117305 MW; 4CD4FD955F3ACB75 CRC64;
MLESDLEQLA ATWFQDSGWD YRSGADIAPD SDTPERSDYR QVLLQRELRE ALSRLNPHTP
AHVLDEVAHQ IGKPDHPSLI QSNRAFHEAL VGGVPVEVEI HGERRGDRVQ LVDFESPERN
HFLVVSQFTV QGQSAKGTQL RRPDLVCFIN GLPVAVVELK NVAAEQVGVR EAYQQLQTYK
DELSDLFVYN AALVASDGLQ ARVGSLTASF ERFLPWRTVK NENDRPLLAY ELEKVVRGFF
APALLLDYLR YFVLFEMADG QIVKKIAAYH QFHAVRSAVK AAVLAATQPV PNTAQEQWAS
YADKVQPGSR MGGIVWHTQG SGKSMSMVCF AAKLMQQKEM QNPTLVVVTD RNDLDGQLFQ
TFVGARSLLR ELPQQAGNRE ELRTLLAGRP SGGIIFTTVQ KFTPDVGEDS FPLLSDRHNI
VVIADEAHRS QYGFRAVLDK KSGRYKYGFA KHLRDALKNA TFVGFTGTPI EGADHDTRAV
FGDYVSIYDI QDAVDDGATV PIYYESRLAR LNLNPAEMEQ LNAEVEEVFE DEEDAALKEA
EKTRWAALEK LVGAQPRVDQ VAADIAQHFV ARTAAVEGKG MVVAMSREIC ARLYAAIVAL
RPDWHSDDPA QGAIKVVMTG SAADDALLQP HLYNPATKKL LERRFKDPAD PLKLVIVRDM
WLTGFDVPCL HTMYVDKPMQ GHNLMQAIAR VNRVFRDKEG GLVVDYIGIA AELRSALRTY
TESKGKGQPA LDATEPLAKL KELMGVARHL LHGFDFSAYR TQAAALLLPA ANFVLGLEDG
KKRWADVVLG ITKAFSLCGT LDEAAAMREE IAFFQAIKAV IAKATTSDAK LTEERRHAVL
KQILDNAVVA EGVDDIFKLA GLERPDIGIL SDAFMEEVRQ LPQKNLAVEL LQKLLQDQVK
SRMRTNVVLE RKFSERLQDA LNRYQSRAVQ SAQVIEELIA MAKEFREAAQ RGEAMGLNDS
ELAFYDALAD NASAVETMGD ETLKAIAREV TEKLRSSTSV DWQKRESVRA RLRNLVRITL
RRYKYPPEGQ EEAIRLVLEQ AERLSQEWSA I
//
