ID A0A088F0L9_9SPHI Unreviewed; 1003 AA.
AC A0A088F0L9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=KO02_17995 {ECO:0000313|EMBL:AIM38369.1};
OS Sphingobacterium sp. ML3W.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1538644 {ECO:0000313|EMBL:AIM38369.1, ECO:0000313|Proteomes:UP000028992};
RN [1] {ECO:0000313|EMBL:AIM38369.1, ECO:0000313|Proteomes:UP000028992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML3W {ECO:0000313|EMBL:AIM38369.1};
RX PubMed=25614576;
RA Smith S.A., Krasucki S.P., McDowell J.V., Balke V.L.;
RT "Complete Genome Sequence of Sphingobacterium sp. Strain ML3W, Isolated
RT from Wings of Myotis lucifugus Infected with White Nose Syndrome.";
RL Genome Announc. 3:0-0(2015).
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; CP009278; AIM38369.1; -; Genomic_DNA.
DR RefSeq; WP_038700301.1; NZ_CP009278.1.
DR AlphaFoldDB; A0A088F0L9; -.
DR STRING; 1538644.KO02_17995; -.
DR REBASE; 92814; SspML3WORF17980P.
DR KEGG; sht:KO02_17995; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_10; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000028992; 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; 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; 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:AIM38369.1};
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:UP000028992};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 260..431
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1003 AA; 116100 MW; 3C199EC60ED20349 CRC64;
MTKESNIEDS LIAKLQDLKY TYRPDIIDRK SLEQNFRQKF NELNRVHLSE TEFNRLREEI
ITPDVFAASK LLREKNTFIR EDGTPLQYTL VNIKDWCRND FEVINQLKIN TENSNQRYDV
IILINGIPVV QLELKSLQIS PRRAMQQIVD YKNEAGSGYN NSLLCFMQLF IVSNRSNTYY
FANNRNQHFS FNADEQFLPI YKLADIDNKK IDNLFDFSEK FLSKCTLGEM ISRYMVLVES
EQKMLVMRPY QIYAVQAIVD CIEQNRGNGY IWHTTGSGKT LTSFKASTLL KDNPNIEKCL
FVVDRKDLDR QTREEFNKFQ EGSVEENTNT ESLVRRLLST DYSDKVIVTT IQKLGLALDA
ESKNNYKERL LPLKDKRMVF IFDECHRSQF GDNHQAIKDF FPNAQLFGFT GTPIFDENAS
YTIRENESGS YKTTKDIFEK ELHAYTITHA IEDKNVLKFH VDYFKTDGVD AANLSESQKQ
KAVVEAILKK HDAVTDQKRF NAIFATGSIN NAIAYYRLFN EVQKQRLEAD EDYRALNIAC
VFSPPAQAVA KDGESNNTKN VADIKQLQND LLQEREDNKV DPEGKKKALI EIISNFNKQY
GTNHSIGEFD LYYQDIQSRI KDQKYSNTDY PHKNKIDIVI VVDMLLTGFD SKYLNTLYVD
KNLKHHGLIQ AFSRTNRVLN DTKPHGSILD FRQQRDAVNE AIALFSGEDT GRSREIWLVD
PAPKVIEKYE DALESLNQMM HSFGLECAPE EVNNLKGDAA RAEFITKFKE IQRLKTQLDQ
YTDLTEEQAS KINLLLPEDD LRSFRSMYIE TAQRLKTKQD KAAKKGDEDV DPSVEQLDFE
LVLFASTIID YDYIMGLIAE MTQKKPSKQK VTKQQLINLL ISNANLMDER EDIIAYINSL
DMDKPLEENN IREGYEHFKK EKNNKDLAII AEKHGVTFES LQVFVAEIMD RMVFDGEKLT
DFLAPLGLNW KVRAQKELAL MEDLVPYLNK LAQGREISGL HYE
//
