ID A0A106BTC6_THIDE Unreviewed; 1086 AA.
AC A0A106BTC6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=ABW22_03295 {ECO:0000313|EMBL:KVW98053.1};
OS Thiobacillus denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW98053.1, ECO:0000313|Proteomes:UP000064243};
RN [1] {ECO:0000313|EMBL:KVW98053.1, ECO:0000313|Proteomes:UP000064243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG {ECO:0000313|EMBL:KVW98053.1,
RC ECO:0000313|Proteomes:UP000064243};
RX PubMed=26712544;
RA Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT Chemoautotroph.";
RL Appl. Environ. Microbiol. 82:1486-1495(2015).
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:KVW98053.1}.
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DR EMBL; LDUG01000011; KVW98053.1; -; Genomic_DNA.
DR RefSeq; WP_059751926.1; NZ_LDUG01000011.1.
DR AlphaFoldDB; A0A106BTC6; -.
DR PATRIC; fig|36861.3.peg.100; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000064243; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
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:UP000064243};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 311..493
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 754..781
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 948..975
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1086 AA; 122396 MW; A9D61D0ABB77D8B6 CRC64;
MRVGYRHVEK PFLDQLASLG WTVIDQGQGC LPTNPAASLR ANFREWLLPE VFREAVRAIN
RTADGMAWLT DRQLDDLRDQ ILRQPNRTLL EANEAVQALF LKAQVDRNEV TGESDPVVSL
IDFARPERNV FHAINQFRID TPGCVKQCII PDIVLFVNGI PLVVVEAKIG DANTANPMHA
AFEQLLRYRN GRSETLAAGL REGEPRLFHT NLLLISTCGE KATYGSVTSG YEHFYAWKDI
WPESNRAYTP PLGVEREQER MIQGLLAPAT LLDVLRTCTV FMDTDSGKRV KVVCRYQQYR
AAHRIIERLR TGKTMAERSG VVWHTQGSGK SLTMVFVARM LRASADLADF KILLVNDRVD
LEVQLAATAR LIGGKVNVID STDQLREHLA TSASDINMVM VHKFMERAEA LPLKVAEALA
SYGTVPSGQT FGVVNSSDRI LLLIDEAHRT QSSDFGDNIF EAFPNATRIA FTGTPPMREL
HSDRYTVKRF GEYIDTYKLL MDAVHDGATL QILYEGRTAD TALKDKHGFD TKFEDLFKTR
SEAELLAIKK KYGASGDILE AEKRIEAIAR DLVNHYIDNI LPDSFKAQVV CHSKLAAVRY
QKSIRDALAE RLDSEQLKPK PDIELIRRIA FLKAAVVVSS DATNELALIT EARKEAKRWN
AVENFCKPFD FDDPDKDLTG IAFLIVCDML LTGFDAPVEQ VMYIDKRLKE HNLLQAIARV
NRVTKNKHRG FIVDYIGLAN HLALALAIYS KEDAQDIQEG LKNLLTELPI LEERYERLLQ
HFRAAGVSGI DAFVKDELPT PEAEVAVVHT AVGVLKDIKL RADFDVYLKT FLQSLNLILP
NQAGHPYRGP ARRFGYLLRM AKERYKDDTL DIADAGAKVK ALINEHLVEL GINPRIPPIE
LLADDFIANV QKHAQGDPEA KASEMEHAIR KHCTVHFDEA PAFYKRLSEK LEKLIQEHQN
NWQTLAEDYE QIRNEAMAGR TDAIEGLSKE ATTFYDYVVQ LAFDGGDVLP DSATPLKKLM
ARIVEILQGT IDIIDFWKKL NEVKKLRGEI DTEILLANIP QLTGKHERIT VEIVKLAEKR
HAELTK
//
