ID A0A095WWQ4_9ACTO Unreviewed; 1009 AA.
AC A0A095WWQ4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=HMPREF1628_04145 {ECO:0000313|EMBL:KGF01831.1};
OS Actinomyces sp. S4-C9.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=1219581 {ECO:0000313|EMBL:KGF01831.1, ECO:0000313|Proteomes:UP000035029};
RN [1] {ECO:0000313|EMBL:KGF01831.1, ECO:0000313|Proteomes:UP000035029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4-C9 {ECO:0000313|EMBL:KGF01831.1,
RC ECO:0000313|Proteomes:UP000035029};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-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:KGF01831.1}.
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DR EMBL; JRMU01000008; KGF01831.1; -; Genomic_DNA.
DR RefSeq; WP_034508274.1; NZ_JRMU01000008.1.
DR AlphaFoldDB; A0A095WWQ4; -.
DR eggNOG; COG0610; Bacteria.
DR Proteomes; UP000035029; 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; 1.20.58.910; -; 1.
DR Gene3D; 3.90.1570.50; -; 2.
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; 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 Helicase {ECO:0000313|EMBL:KGF01831.1};
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:UP000035029};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 308..472
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 928..955
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1009 AA; 115716 MW; 2AFCB2436E955A48 CRC64;
METRKFDPVA LSSQSTVVAE YVPDNNDASG YQSEAQLEAE FIRQLQAQGY EYADIRDEQH
LETNLRVQLS KLNEVEFTDA EWNRFYKTNI ANTSDTVEDK TTRIQEDHIQ LLEREDGTTK
NIRLIDKDNI HNNHLQVINQ YAVNKTDGAK HSNRYDVTIL VNGLPLAHIE LKRRGVPLRE
AFNQINRYRD ESFSTGAALF DYAQIFVISN GTSTKYYSNT TRLAHVNETN KKDKKSFVFT
SYWADAQNQP IEDLIAFAKT FFAKRTILNI LTKYCVYTEN RQLLVMRPYQ IVATERILTR
ILTSTNAGTL GTTAAGGYIW HTTGSGKTLT SFKTAQLATK VEGVEKVLFV VDRKDLDYQT
KLEYDRFQKG AANGNTSTAQ LKRQLESADP AKKIIVTTIQ KLATFIKANQ GHTVYNGHVV
LIFDECHRSQ FGDMHIAIKR AFKKYNLFGF TGTPIFAENA GSGKHVNLKT TAQAFGEKLH
TYTIVDAITD KNVLPFRIDY INTIEEGSFK DKDVRAIDVE SAMMHPERIR QVAQYILDHF
DQKTKRNSVY MVGGKRKQGF NALFATSSIE AARAYYGMFS KLQLNVPDAQ KLKIGMIYSY
GANDQPEDGI IEDESFDAEK LSESDRGYLE DVINDYNDMF STNFNTSGSS FQDYYEHLSK
QLKDRELDLV IVVNMFLTGF DAPTLNTLFV DKNLRSHGLI QAYSRTNRIL NTVKTYGNIV
SFRNLEQQTQ DAIALFGNKD ASGIVMLRPY QEYLDEYKAQ LKELRAVYAD PTNPIPASET
AQKEFINIFG AVLRLQNILS SFDDFKSDNQ FSERELQDYK SRYMDLYDQW KPRTDNDRED
IRQDVLFEIE LVKQVEINVD YILMLVEQRH EAGTDSEDKE IRAKIDRALS SSPSLRPKRK
LIEEFVDTVS INTSVQDEWR EYVNGKREEE LTAIINEERL NRDKAEQLIS NALRSGHVPT
AGQSVARVLP PISRFRPDNA RGETMQRVYA KLQEFVDRFR PLLRSDFED
//
