ID U3GSZ9_9CORY Unreviewed; 1063 AA.
AC U3GSZ9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=CARG_02055 {ECO:0000313|EMBL:AGU14580.1};
OS Corynebacterium argentoratense DSM 44202.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1348662 {ECO:0000313|EMBL:AGU14580.1, ECO:0000313|Proteomes:UP000016943};
RN [1] {ECO:0000313|EMBL:AGU14580.1, ECO:0000313|Proteomes:UP000016943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44202 {ECO:0000313|EMBL:AGU14580.1};
RX PubMed=24092787;
RA Bomholt C., Glaub A., Gravermann K., Albersmeier A., Brinkrolf K.,
RA Ruckert C., Tauch A.;
RT "Whole-Genome Sequence of the Clinical Strain Corynebacterium
RT argentoratense DSM 44202, Isolated from a Human Throat Specimen.";
RL Genome Announc. 1:e00793-13(2013).
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; CP006365; AGU14580.1; -; Genomic_DNA.
DR RefSeq; WP_020975720.1; NC_022198.1.
DR AlphaFoldDB; U3GSZ9; -.
DR STRING; 1348662.CARG_02055; -.
DR REBASE; 69525; Car44202ORF2045P.
DR GeneID; 78249276; -.
DR KEGG; caz:CARG_02055; -.
DR PATRIC; fig|1348662.3.peg.408; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_2_1_11; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000016943; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; 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 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; 1.
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 Helicase {ECO:0000313|EMBL:AGU14580.1};
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:UP000016943};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 282..450
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1063 AA; 120593 MW; C0B2E7405EB75F0C CRC64;
MTTPFRCEAE FEAALIDLLT RHGWSDELLR YPTEQQLIDN WANILFANNR GRDLLGDVPL
TEGEMAQIIE QINVLRTPLA LNEFINGRTV TITRDAPQAH NFGVEISLKI YDRLEIAGGQ
SRYQIAVQPR FKTADELLPK RRGDLMLLIN GMPVFHIELK RTGVPVSQGA NQVAKYAHEG
VYQGIFSLVQ IFVAMTPEET LYFANPGSAK FNPDYFFHWA DFNNEPVNQW GDVARALLSI
PMAHQLIGFY TVADRASGNL LAMRSYQYYA ASRIADRVDR HDWDSGDQLG GYVWHTTGSG
KTITSFKTAQ LIADSHNADK VVFLLDRVEL GTQSLENYES YGGDSIAVED TSSAATLITL
LKNKRSTLIV TSLHKMSRVN ADSVKKADLD IIRSKRVVFI VDEAHRTTFG DMLATIKRTL
PNALFFGFTG TPIHDENQKK HSTTTTLFGN ELHRYSIADG IRDGNVLGFD PEMVETFREH
DVRTVVALRE AKAKSVNEAL ADPKKAAVYY KFMDKDQVPM ASVYETDTDS GTKRVAKGIE
DYLPITQYRH DNHRQAVASD INKHWAQLSR GSMFHAILAT SSIPEAVEYY RIFKAQYPHI
KVTALFDPNI DNTGDSQLFK EDGLLEILRD YNAAYGQHFT MPTHDEFKKD VSKRLAHKAP
YNTKAFLDDR SQHIDLLIVV DQMLTGFDSK WLNTLYMDKV IEYESIIQAF SRTNRIFGPE
KPFGSIRYYR KPHTMKNNID RAVKLYSGDK PFGLFVDHLD EHLKAINECF DIITALFTDP
ATGQTDFSKL PDSEADQGEF AKTFNRMYRE LQAAQVQGFT WEKDTYYFDA LPEPIVVTLT
EDVFTTLLTR YKELGKEGGD PTDPPGGTDD APFDIDVHIT HIDTDRIDAE YLNSKFEKYL
KALQDGVAEH MLDDLLEQLH DSFARLSQDD QRYANRWLHD LQAGDVALQP GKTVQDYINE
YRITERDRQL ARLHERLGLD TGLLRRILDS RVTAATINEY GRFDDLKASI DLDLATAYFT
EVTGAPVSKF KVRAMLDKLL RTYIIDGVLP AYLTVAEEEL AGE
//
