ID A0A1I1GD90_9GAMM Unreviewed; 1093 AA.
AC A0A1I1GD90;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN02745724_00909 {ECO:0000313|EMBL:SFC09435.1};
OS Pseudoalteromonas denitrificans DSM 6059.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1123010 {ECO:0000313|EMBL:SFC09435.1, ECO:0000313|Proteomes:UP000198862};
RN [1] {ECO:0000313|EMBL:SFC09435.1, ECO:0000313|Proteomes:UP000198862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6059 {ECO:0000313|EMBL:SFC09435.1,
RC ECO:0000313|Proteomes:UP000198862};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOLO01000004; SFC09435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1GD90; -.
DR STRING; 1123010.SAMN02745724_00909; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000198862; 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; 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:UP000198862};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 340..508
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1093 AA; 124089 MW; F725BC2EA5BCE621 CRC64;
MTNIIPNFKE EFSSKIPALT MLSMLGYSFI PPSECEKYRG NSYSGKATSQ VMLLSVMREF
LSNQTFPFAG KEHKLSAAAI DKIMHELNPA MNEGLKSANE KLYNALMYGV GVTEFIDGKK
ASPTIQLIDW QNIKNNHFHF TEEMVVQNSE GTGVRIPDIV CFVNGLPWVV VEAKRPDSST
EGKSTLSEAV SQQIRNQGQA EIPHLFAYSQ LLISVNGHDG LYGTCGTPEK FWAKWVEEDI
IEAEFVRLKN KTLNEQQLDG IFGHRPAAAK DEYLSLLAGG ELTVTAQDRL LVSLLRPDRL
LDMTRLYTLF DKKAGKIVAR YQQVFGIKAL IERITSFDEI KRPGARNGGV IWHTTGSGKS
FTMVFLSKAL IWLQELAQCR VIIVTDRVDL EDQLSRTFAS GGVLSERDKR DAMATSGKRL
AEQIGKGNER VIFSIINKFG SAIKYDECYN DSPNILVLVD EGHRSQNGEN NIRMLQTLPK
AAFIAFTGTP LLKDDKTENK FGSIIHSYTM QQAVEDKTVT PLLYEERIPE LNVNDKAIDA
WFDRITEKLT EKQRTDLKKK FSQKGQIYQT EGRIELIAHD ISDHFQNFKQ QGLKGQLACD
SKASAIRYKE ILDKIGKVTS VVAMSSPDTR EGHEVVDQDS KDIVQNWWKA NVGNVDEKTY
TKDIINAFSQ DEGPDLMIVV DKLLTGFDEP KNTVLYIDKP LKEHNLIQAI ARVNRLHSKK
QFGYLIDYRG ILKELDMTIE KYQELAERNQ NGFDVDDLKG LYNRMDTEYK KLPGLYNDLW
AIFADVKNKQ DHAALRQALT PKVEDVHGQF IDKNIKKRDE FYTALTAFLN CMKVALQSAS
FFEDKSFDDK RDHYKETLKM FVNLRKQVRE DANETVDYDE YAEDVRQLLD KHIAGIEVRE
PDGAYLVGNL GKDVKPQDLT DDEARNQTDK ITGRITKMIE QDLADDPYAQ EYFSNLLKKA
IDEAKAMFDA PVKQYMLFAD FEQEVKQRKV EGIQDMFTDG EGKQNKHAQA YFGLFKHLFP
DVNQTEDKLV QYAFDIDGVV KTAVAEFSIN PSEIENAISM KLLPMLFAEL GLENAQSLIE
EVLKITRLGL SRG
//
