ID A0A147H8Y3_9BURK Unreviewed; 1024 AA.
AC A0A147H8Y3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=NS331_03720 {ECO:0000313|EMBL:KTT26390.1};
OS Pseudacidovorax intermedius.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Pseudacidovorax.
OX NCBI_TaxID=433924 {ECO:0000313|EMBL:KTT26390.1, ECO:0000313|Proteomes:UP000072741};
RN [1] {ECO:0000313|EMBL:KTT26390.1, ECO:0000313|Proteomes:UP000072741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS331 {ECO:0000313|EMBL:KTT26390.1,
RC ECO:0000313|Proteomes:UP000072741};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTT26390.1}.
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DR EMBL; LDSL01000028; KTT26390.1; -; Genomic_DNA.
DR RefSeq; WP_058640665.1; NZ_LDSL01000028.1.
DR AlphaFoldDB; A0A147H8Y3; -.
DR PATRIC; fig|433924.3.peg.2562; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000072741; 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; cd22332; HsdR_N; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 1.20.58.910; -; 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 InterPro; IPR022625; TypeI_RM_Rsu_C.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF12008; EcoR124_C; 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.
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:KTT26390.1};
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:UP000072741};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 277..458
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 576..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 376..403
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 585..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 115873 MW; 50552495505814E1 CRC64;
MPSSKSAYDP SSGASSPVVK EEHIEYGFIG KLQSLKYEYR PDIRDRAALE RNFREKFEAL
NRVHLSDGEF TRLLDDIVTP DVFTASRKLR ERETFTRDDG TPLNYTLVNI KDWCKNSFEV
VNQLRINTDY SHHRYDVLIL VNGVPCVQIE LKTLGISPRR AMEQIVDYKN DPGNGYSKTL
LCFLQLFIVS NRTDTWYFAN NNARHFAFNA EERFLPIYQF ADEANKKITH LDHFAETFLP
KCTLGQAISR YMVLVASEQK LLMMRPYQVY AVKAIVECIH QNSGNGYIWH TTGSGKTLTS
FKASTLLKDN RDIEKCLFVV DRKDLDRQTR EEFNRFQEGC VEENTNTGAL VRRLLSDDYA
DKVIVTTIQK LGLALDENSK RNKQRKKNDL KTYKEQLEPL SDKRIVFIFD ECHRSQFGDN
HEAIKTFFPK AQLFGFTGTP IFEKNATAKQ FEGEEGQFKT TEDLFQKQLH AYTITHAIED
ANVLRFHVDY YKPEGKNPPK PGEALAKKAV VEAILAKHDT ATAGRRFNAV LATASINDAI
EYHGLFDELQ KAKQAADPAF QPLNIACVFS PPAEGNPDVK QLQQDLQQEK ADNEEDPEGK
KAALKAILAD YNARYGTNHQ IGEFDLYYQD VQKRIKDQQW PNADFPAARK IDITIVVDML
LTGFDSKYLN TLYVDKNLKY HGLIQAFSRT NRVLNGSKPY GNILDFRQQQ ANVDEAIALF
SGENATEEER KIWLVDKAPV VIEKLDAAVQ KLADFMQTQG LPCAPEAVPQ LKGDDARTAF
IKAFKEVQRL KTQLDQYTDL TADNAAAIEA ILPREDLQAF RGVYLDTAQR LKAQQGKTLP
DAVDKTGADD VEQLDFEFVL FASAVIDYDY IMGLMSRFTQ QGTGGSKLKM SREQLIGIIA
ADAKFMNERD DIAAYINTLK AGEGLSETAI REGYLRFKKE RDSAELATIA TQHGLATPAL
QAFVDQTLQR LILDGDALSA LMEPLQLGWK ARAQAEAALM AELTPLLNKR AQGREISGLS
AYEQ
//
