ID N8ZW37_9GAMM Unreviewed; 1089 AA.
AC N8ZW37;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=F960_00082 {ECO:0000313|EMBL:ENV35695.1};
OS Acinetobacter gerneri DSM 14967 = CIP 107464 = MTCC 9824.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120926 {ECO:0000313|EMBL:ENV35695.1, ECO:0000313|Proteomes:UP000013117};
RN [1] {ECO:0000313|EMBL:ENV35695.1, ECO:0000313|Proteomes:UP000013117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107464 {ECO:0000313|EMBL:ENV35695.1,
RC ECO:0000313|Proteomes:UP000013117};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter gerneri CIP 107464.";
RL Submitted (FEB-2013) 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:ENV35695.1}.
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DR EMBL; APPN01000013; ENV35695.1; -; Genomic_DNA.
DR AlphaFoldDB; N8ZW37; -.
DR STRING; 202952.GCA_000747725_00394; -.
DR PATRIC; fig|1120926.3.peg.67; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_1_0_6; -.
DR Proteomes; UP000013117; 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; 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 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:UP000013117};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 328..516
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1089 AA; 121508 MW; D968D02E36C05924 CRC64;
MDKFRGSIQV TKMTESDIEL MAIEQLEGLG YTYVYGPEIE SKGINPLRSY KQVILEPKVL
EALQRLNPHL SEDKCIEALK QVTNLHSPDM LSNNHAFHRL LTEGINIEVS KDGNTQGEYA
WLVDFNNPTN NEFLVINQVT IKEDRWTRRP DIIIYVNGLP LVVIELKNAT DENATVEGAY
KQIQTYQSQI PSLFTYNAFN VISDGLEAKA GTVSADLSRY MAWKTSNGQT KAKSTQAQLE
VLLHGLLNPV TLLDMIRHFI VFESNKQEDA NGLITIKTIK KMAAYHQYYA VNAAVLSTIR
ASAMSSDSKS AELAMQHQGR SKLELVQQQA VGDKKAGVVW HTQGSGKSLS MVFYTGKIVL
ALDNPTVVVI TDRNDLDDQL FGTFAASSQL LRQTPKQAEN REELKELLKV GSGGVIFTTI
QKFQPDDGGS VYEQLSDRTN IVVIADEAHR SQYGFNAKEV DVKDENGKVV GKRTVYGFAK
YMRDALPNAT YLGFTGTPIE KTDVNTPAVF GNYVDIYDIS QAVEDGATVR IFYESRLAKI
AISEEGKELI EEFDDQFTED DLNQTQKERA KWARVEGLIG SKERVKAIAK DIVEHFEQRL
VANANQGKGM IVSMSRRIAV DLYNEIVAIK PEWHSDDLHD GVIKVVMTSS ASDGKEIAKH
HTTKQQRQIL ANRMKDNDDK LKLVIVRDMW LTGFDAPSMH TLYIDKPMKG HNLMQAIARV
NRVYKDKIGG LVVDYLGIAS DLKEALSFYS EAGGKGDPAL VQDEAATILQ EKLEVLDGIM
HGFNYQEYFK ADTSRKLNII LEAEEHILGV DQGEGKTRFL TAVAAMSQAF ALAVPHPHAM
EAAPVVAFFQ AVKARLAKFS DGSGKISGLS NTELEAKVKQ TIDQALVTEQ VVDIFDAAGI
QKPDISILSD EFMQEMKGYK HKNIALETLK KLLGDEIKMR EQRSVTQGKK LMEMLSSAIK
GYQNKVLTAA EVIDELIKLA KAIQESDKLA EELNLTEYEY AFYSAVADND SARELMQKEI
LRELAVVLTD SIRKNVTLDW TIKEAARAKL RVIVKRLLKK YGYPPDMALL ATETVLEQAE
QLADELSAA
//
