ID A0A2I6S4G8_9RHOO Unreviewed; 1065 AA.
AC A0A2I6S4G8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, 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=C0099_03825 {ECO:0000313|EMBL:AUN94145.1};
OS Pseudazoarcus pumilus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Pseudazoarcus.
OX NCBI_TaxID=2067960 {ECO:0000313|EMBL:AUN94145.1, ECO:0000313|Proteomes:UP000242205};
RN [1] {ECO:0000313|EMBL:AUN94145.1, ECO:0000313|Proteomes:UP000242205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY39 {ECO:0000313|EMBL:AUN94145.1,
RC ECO:0000313|Proteomes:UP000242205};
RA Fu G.-Y.;
RL Submitted (JAN-2018) 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}.
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DR EMBL; CP025682; AUN94145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I6S4G8; -.
DR REBASE; 226506; AspSY39ORF3810P.
DR KEGG; atw:C0099_03825; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000242205; Chromosome.
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; 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; 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:AUN94145.1};
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:UP000242205};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 304..486
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1065 AA; 118009 MW; 088809E6FDF0AC50 CRC64;
MAFLSEAQLE AALLEQLIEL GYACASDDRI GPDGENPERA AYDEVVLTAR LAAAVSRLNP
SLPSEAQADA IRRLTQSELP TLLEENRRIH RLLIEGADVE YYAEDGTLTA GKVRLIDFET
PANNDWLAVQ QFTVVAGQHK RRPDVVVFVN GLPLAVIELK APGAENATLA GAFNQLQTYK
QQIPALFRSN ALLVTSDGLS ARVGSLSADQ ERFMPWRTTD GARIEPKGTP ELATLIEGVF
EHGRLLELLR HFTVFGETSN GLIKIIAGYH QFHAVKKAVI STLRASQSSI AEDPAKYRLR
SVKDQPPGDH KAGVIWHTQG SGKSLLMAFY AGLLVFEPRM ANPTLVVLTD RNDLDDQLFG
TFAMCRDLLR QTPVQAQDRE HLRTLLNRAS GGVIFTTLQK FSPASEESDF PMLTDRPNVV
VIADEAHRSQ YGFKAKVASK TGEIAYGFAK YLRDALPNAS FIGFTGTPIE ATDVNTPAVF
GHYIDIYDIS RAVEDGATVP IYYESRLARI ELDEDEKPCI DAEIEALLED EDEPSAERAK
QKWSTVESLV GSKKRLTMVA ADLVQHFEDR VAALKGKAMV VCMSRRICVA LYEEIVKLRP
DWHSPNDNEG SVKIVMTGAV TDPEGWQQHI GNKTRRDLLA KRARDPDDPL RLVIVRDMWL
TGFDAPSMHT MYIDKPMRGH GLMQAIARVN RVFRDKPAGL IVDYIGIAQN LKSALAQYSR
PDQDKTGVDE AEAVAVMLEK YEIVRDMFHG FDYQTALAGT PGERLAMMAG AIEWILDKQQ
QWAAAEKTPE AKKQAQRRFA DGVLALSKAF ALAASSDEAR GIREEVGFFQ AIRAALVKSA
AGSGKSREDR ELAIQQIVSR AVVSTEIVDI LAAAGIQSPD ISILSDEFLL EVQQMEKKNL
GLEALRKLLN DSIRSRTRTN VVETRAFTER LEDAIARYHA NAITTAEVLQ ELIKLAQDIR
AARTRGEEQG LSEEEVAFYD ALAENESALQ VMGDDKLKVI AHELLVSLRE NVAVDWAHRE
SARARLRVLV KRILRKYGYP PDLQDAAVQT VLQQAEVLSA AWGVR
//
