ID D9SFZ0_GALCS Unreviewed; 964 AA.
AC D9SFZ0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=Galf_1412 {ECO:0000313|EMBL:ADL55437.1};
OS Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea
OS capsiferriformans (strain ES-2)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Gallionella.
OX NCBI_TaxID=395494 {ECO:0000313|EMBL:ADL55437.1, ECO:0000313|Proteomes:UP000001235};
RN [1] {ECO:0000313|EMBL:ADL55437.1, ECO:0000313|Proteomes:UP000001235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES-2 {ECO:0000313|EMBL:ADL55437.1,
RC ECO:0000313|Proteomes:UP000001235};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Shelobolina E.S., Picardal F., Roden E., Emerson D.,
RA Woyke T.;
RT "Complete sequence of Gallionella capsiferriformans ES-2.";
RL Submitted (AUG-2010) 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}.
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DR EMBL; CP002159; ADL55437.1; -; Genomic_DNA.
DR RefSeq; WP_013293376.1; NC_014394.1.
DR AlphaFoldDB; D9SFZ0; -.
DR STRING; 395494.Galf_1412; -.
DR REBASE; 27383; GcaESORF1415P.
DR KEGG; gca:Galf_1412; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_4; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000001235; 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; 1.20.58.2040; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000001235};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 265..431
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 964 AA; 111335 MW; 8651578ABC2EAE83 CRC64;
MSTQSEYALE AALIAQLKGM EYDSVTLDDE TAMLANLKQQ LQIHNKDIQF TPTEFDRILN
HLNTGSVFER AKILRDKFAL KRDNDETAYI SFLNCDDWCM NEFQVTNQVS MQGKRKNRYD
VTLIINGLPL VQIELKRRGA ELKVAFHQIN RYQHDSYDAG FGLFQYVQLF IISNGVNTKY
FSNNKQQSFK QTFYWTDKEN KRLSDLLEFS AEFLKPCHIA KMMTHYMVMT EEQVIKVLRP
YQFYATEALV DRVKNSNEFA SRRHLSDAQS SHNAYIWHTT GSGKTLTSFK AAQIIQRMPK
VHKVVFCVDR KDLDYQTAKE FNGFCKGSVD ETTNTHTLVK QLNDDSTKLI LTTIQKLNNA
IVKEHYLSRV THLQDKKFVF IFDECHRSQF GDTHQNIKQF FRNAQMFGFT GTPIFADNAT
GSIGQQKTTK DLFGECLHKY VIVDAIKDEN VLRFAVEYVG KYKRVDNANE IDIDVEAIDT
KELLDSPIRL GKITDYILAY HPQKTKSPDF TAMFCVSSVE TLIKYYDLFK QKQVGAAKPL
KIATIFSYAA NEEDPNANGL TSGLIPEENP IPEGKINQRS RDKLDEFIED YNGMFGTKYS
TRDSQSYYNY YQDIAKRVRA GQVDILLVVN MFLTGFDSPR LNTLYVDKNL KFHGLVQAFS
RTNRILNDKK SQGNIICFRN LKEATDEAIA LFSNKDAKET VLLEPYEDYV TQFNEATEAL
LALTPTVASV DALPDEKAEL EFVTKFRALL RLKNIITSFA EFSETDLAMA EQLFEDFKSK
YLDIHDKVKK QTDPEKVSVL EEVDFELSLI HRDEINVAYI LNLLVNLKNL PPEEARKRQK
AILDMLAGEV QLRSKRKLIE AFIEDNLPKL KPDDNVIAEF ESYWMRQRQS AFVQLCRDEQ
IEPAQFEKLL QNYVFANRLP RDQEIVESLS FKPKILERKS ILERIGDKIQ EFIHTYVEGM
GGSV
//
