ID A0A0A3X3N9_9GAMM Unreviewed; 958 AA.
AC A0A0A3X3N9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, 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=GW12_13990 {ECO:0000313|EMBL:KGT47563.1};
OS Acinetobacter sp. HR7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1509403 {ECO:0000313|EMBL:KGT47563.1, ECO:0000313|Proteomes:UP000032870};
RN [1] {ECO:0000313|EMBL:KGT47563.1, ECO:0000313|Proteomes:UP000032870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR7 {ECO:0000313|EMBL:KGT47563.1,
RC ECO:0000313|Proteomes:UP000032870};
RA Ahn S., Kim B.-C.;
RT "Genome sequencing of Acinetobacter sp. strain HR7.";
RL Submitted (OCT-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:KGT47563.1}.
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DR EMBL; JPQO01000156; KGT47563.1; -; Genomic_DNA.
DR RefSeq; WP_034585577.1; NZ_JPQO01000156.1.
DR AlphaFoldDB; A0A0A3X3N9; -.
DR STRING; 1509403.GW12_13990; -.
DR REBASE; 104260; AspHR7ORF13950P.
DR PATRIC; fig|1509403.3.peg.1383; -.
DR eggNOG; COG0610; Bacteria.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000032870; 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; 1.20.58.910; -; 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; 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 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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 254..420
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 958 AA; 111497 MW; 59CE5DDE47C36FB8 CRC64;
MTVQSEYQLE NELIGQLQQL GYASVTLKDE SQLLSNLKTQ VERANGLAPL SETEWKQVIS
FLNTGTVFER AKNLRDLFPV KFDDGTSKHL FFLSDDPSKN IYQVTNQITI DHRDYNGRTS
RFDVTLLVNG LPLVQIELKK RGMEIAEAFN QTQRYTREAY WAGQGLFGFI QLFVISNGAN
TRYYSNGTTG IEFAFPWADV HNKHINEIVD FAEAFLNQRH LTQMLTQYMV LLETTKSLMV
LRPYQIYAVQ KIVQHVQNSN QNGYIWHTTG SGKTLTSFKA SQIIMQMPDV EKVLFVVDRN
DLDTQTSREF NAFKADSVDS TDNTSTLVKQ LDQRHDKLIV TTIQKLNRAI STERYLESID
YLKNKKVVFI FDECHRSQFG ETHQNIKKFF SNAQMFGFTG TPIFEKNSQS KAGLKLTTDY
LFNECLHKYV IVDAIRDRNV LQFQIDYRGK YTAKGMATNE SYEEDVEGID TKELYDNPQR
LEMIARYIVN IHDTKTRNRE FTAMFCVSSV ETLTQYYDLF EKVQAEKQIE DEAQGRIFKP
LTIATIFSYA ANEAVPTDDL TGLIHEEAAD IPSQVNSSSR DKLDRYIANY NRQFKTNYNS
GDQFYAYYRD IAQRVKNRQI DILIVVNMFL TGFDSKPLNT LYVDKNLKYH GLIQAFSRTN
RVYNDKKPFG NIICFRNLKR ATDEALALFS NKDAQKVVLV PSFEEIKQDY DAAVQKLLKI
TPDYQSVDDL MTEDQQLEFI KAFREVMRYN AQLQTFIEYD QNQTALDKQH FANFASKYAD
LCRDVRKTTK KEKVSVLDDV DFQLDLLHSD RINVGYIINL LQMALDSGDE AKRKKYEAQI
HDLIGNEVTL HDKQELIQKF IEENMPKMIN GQSVQDAFAQ FWDIEKEQAY QQLCEQENLK
PEAMKEVLDH YEYTHRLPRK EELKDLPNYK VKLFERDNVL TSLMVKTRQL IEKFYVGF
//
