ID A0A316DH16_9BACT Unreviewed; 956 AA.
AC A0A316DH16;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=LV89_04614 {ECO:0000313|EMBL:PWK16956.1};
OS Arcicella aurantiaca.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Arcicella.
OX NCBI_TaxID=591202 {ECO:0000313|EMBL:PWK16956.1, ECO:0000313|Proteomes:UP000245489};
RN [1] {ECO:0000313|EMBL:PWK16956.1, ECO:0000313|Proteomes:UP000245489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22214 {ECO:0000313|EMBL:PWK16956.1,
RC ECO:0000313|Proteomes:UP000245489};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAY-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWK16956.1}.
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DR EMBL; QGGO01000040; PWK16956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316DH16; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000245489; 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; 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:UP000245489};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 257..422
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 956 AA; 111530 MW; 65AA2B6E0B570AE5 CRC64;
MAKQSEAVLE EQLVAKLQKL GYQYTTINDE KALIENLKNQ LEKHNWAALR RCPFSKTEFD
KVLNILNKGS VFEKSKTLRE KQHIIRDNGE NLYFEFINTD FWCQNQFQVT NQVTQEGKYK
NRYDVTILIN GLPLVQIELK RRGLELKEAF NQTNRYQRHS YGSGNALFQY IQIFIISNGV
NTKYYSNNRN QSFKQTFYWS DVNNKRLTNI LNGFTDAFLE PCHISKMICK YIVLNEAHKI
LMVLRPYQYF AVEALIDRVQ NSNKNGYIWH TTGSGKTLTS FKASQILMNL PQVHKVVFVV
DRKDLDYQTT KEFNSFSKGS IDGTDNTKAL VKQFTDDTKL IVTTIQKLNT AISKLKYENA
MADLKDKRIV FIFDECHRSQ FGDTHKRIKA FFGNSQMFGF TGTPIFADNS SKNELGKRTT
KDLFEDCLHK YVITDAIKDE NVLKFSVEYV GRYKHKDGRE SNIDIEVEDI DTQELMEDEK
RLNKITDYII ANHGRKTHSK EFTAMFCVDS VKTLIKYYDL FKQKKQEGKH NLNVATIFSY
AANEDDADAN GFIPDEVSIA EEPKVLYGLN LHSREKLDEF IEDYNQIFGT KFSTKDSESF
YNYYNDISKK VKERKVDILL VVNMFLTGFD SPSLNTLYVD KNLKYHGLIQ AYSRTNRILN
ELKSQGNVVA FRNLKNRTDE AITLFSNKDA IEVIIMKPYE NYTEQFDKAF GKLLEITPTV
DSVNELVTED DELAFVKAFR ELMRIKNILA SFSDFKWEDL TMTEQLFEDY KSKYLDLHDK
VKGDNSKEKV SILDDVDFEL ELIHRDDINV AYIIQLLIRL RAKNQKDTSK AEQEIMNLLS
TETTLRSKRE LIEKFIKENL PDITDTEEIQ QEFDNYWSEQ QKKAFADMVA EENLSATKTE
KLIENYLFAE REPLRDEVIE LLEGEKPSLL QRKKLGDRIL KRILDFVDTF INGMVG
//
