ID A6VPU3_ACTSZ Unreviewed; 1087 AA.
AC A6VPU3;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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 OrderedLocusNames=Asuc_1637 {ECO:0000313|EMBL:ABR74990.1};
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR74990.1, ECO:0000313|Proteomes:UP000001114};
RN [1] {ECO:0000313|Proteomes:UP000001114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z
RC {ECO:0000313|Proteomes:UP000001114};
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
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; CP000746; ABR74990.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VPU3; -.
DR STRING; 339671.Asuc_1637; -.
DR REBASE; 15749; Asu130IP.
DR KEGG; asu:Asuc_1637; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_0_1_6; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000001114; Chromosome.
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; 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 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 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:UP000001114};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 329..498
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1087 AA; 123437 MW; A185BAB46BF508F8 CRC64;
MHPTPKLQEK YTFKIPAIIL LNNLGWQYLS PKQALALRGG KLGNVVLETV LRAELEKRTF
EFAGRERALS AKAVDTLVAE LLDPKLNESL LTANEHLYNH LLYGITVTEF IDGKKISRTV
PVIDWDNLEN NAFHFSEEFS VENVQGSSVR TPDLVCFING LPLVVIEGKR PDGKEKSTIE
EGISQTLRNQ RPNEIPHLFA YTQLVLSLNG VDGRYGTCGT PSKFWAAWRE EMFGESEMAE
IKNVVNSPQN LTACLPNEAD CLWYQQLIAQ GKLAVTGQDR LLIGLLTKSR LFEMIRYFTL
FDRKSQIRVA ARYPQVFGVK RLLERVTTQN EKGARNGGVI WHTTGSGKSF TMVFFSKALL
LHPALKSCRI LVVTDRVDLE NQLSNTFYNS GELATKRERQ NSLATTGKRL AEQISQGSER
IIFSLIQKFN TAIAQPDCFN PSENIIVLID EGHRTQGGEN HTAMRRALPN AAFVAFTGTP
LLKDDETTQK FGSIIHAYTM QRAAEDHTVT PLLYEERIPE LDVNERAIDN WFERITKALN
ERQKADLKRK FTRKGQIYQA DERIHLIALD LAEHLANKIP QGLKGQLACE SKSTAIRYKK
YLDEIGLFES AVVISPPDSR EGNSELDEQA SDEVVRWWNA NVQGGEAVYT QQVLNRFADP
DSPLRLLIVV DKLLTGFDEP SNAVLYIDKP LKQHNLIQAI ARVNRLHKQK EFGLLIDYRG
ILKELDTTIA KYQDLANRTQ GGYAIEDLAG LYRPMKSEYL RLPSLYKALR AIFAAAENQA
DIEQLRRVLM PNMVLDETSG LFFDKNSKLR DDFYLALREF NRCLQVALQS EDFYQDPNFS
ENDRTLYKET AKQFGYLRRL VQQDAGEQVD YGDYADQVAQ LIDKHLVAIS VKEPNGVYAV
NKMGKAENKA WDDTKTRNEA DKIRSRLART IDVELNGDPY AKARFSELLQ QAIKEAEALF
DNPMKQYLLF ESFETQLNAR KLPEIPDRFA DNRSAQAYFG VFKTVLPESL ANDETQWIEL
AFTVDQLVVQ IVAQYSLNTD QVEKEIRKQL LPMMFRTCQS VGAGMEQAKE IVERIVQIVR
VGQANGS
//
