ID C0QCH5_DESAH Unreviewed; 1005 AA.
AC C0QCH5;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 Name=hsdR2 {ECO:0000313|EMBL:ACN15052.1};
GN OrderedLocusNames=HRM2_19510 {ECO:0000313|EMBL:ACN15052.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN15052.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN15052.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
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; CP001087; ACN15052.1; -; Genomic_DNA.
DR RefSeq; WP_015903833.1; NC_012108.1.
DR AlphaFoldDB; C0QCH5; -.
DR STRING; 177437.HRM2_19510; -.
DR REBASE; 20387; DauHRMORF19490P.
DR KEGG; dat:HRM2_19510; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_1_0_7; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000000442; 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; 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:UP000000442};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 278..452
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1005 AA; 115222 MW; 33EAB9D473F4BFB4 CRC64;
MTSQTPEYLQ SELPAIQLFQ KLGYTYLDGS TNEERSSIRE VILESRLKGA IKRLNPWLNE
NNVNNAFKEI TSVVATSLME ANETIHKLLS CQEYTPKQIV DGKETYKGVS FIDFENIDNN
EFLVVNQMKF RGLEKNSIPD IVVFINGMPL AVIECKSPKA LGAETEAIGD LQHYQIQSEK
LFKYNQVCVG IYKHGGRYGA IGAREEHYQV FKVKDTTALQ AILGHEPTPQ DILLYSIFKK
EYFLDLIRNF VIYQVSEGSK IKILPRYQQI RATNKTIKRL QDENKGGVVW HTQGSGKSIT
MLYLATKLRR EESGFKNPTI IIMTDRTDLD DQISNTFRRC GFPNPIQATS VRHLKQLLQD
DYGKTITTTI HKFQETDEDG NIIKVSNEEI EVVSEKENLF VMVDEAHRSQ YGFLAGFMRQ
ALKNAKFIAF TGTPIDTEQK STLGKFYGGG YLDIYNIKQS VEDGATLPIL YEDGIPELYV
EKELLEKQFE YYFEKETDEK KAKLKQEATS LKKYMSGKQR IKRIAEHIID HYKNKIYPDG
YKGMVVCYNR PSAIAYKKAF DKLKAAGKHG FSSRVVMSFA PKKDPDEYFK LATPDTEVKQ
AIEDFKLPFG DDTQLNKAGK KQFNNDALMI VSDMLLTGYD VPVAMVMYLD KPLKAHNLLQ
AIARVNRTRG AKAAGLIVDY CGIANHLVDA MKIFSGDLEP ADVMVNISAE ITRLRLRHNC
LVAFFQDMGI DRKKNRQDYI DRAVHHLEPI DIRDTFKDLL KRFNKSLNII LPDEAALEYK
DDFTLYNQIR LEASNAYMDK TLQISKDESK KLQSLIDEHL RAKGITSLLD EPVSIIDVEK
FQQEIDKTLN PKSKELKRTN RLKHKITVEL EKNPDFYQPL SDKLEALIKA RRENRITQLE
LFAEYDKIQE KILNKNKEAE NLGFQTEREF AVFKTMETQM GWEAKGITQN LFTALEGELS
ITDWHHKNDV VKAVRVKIKD GLRGKVDAKE LPKLAVSLVD LIKRN
//
