ID V2QCT9_9BACT Unreviewed; 1058 AA.
AC V2QCT9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=N508_001510 {ECO:0000313|EMBL:USF24424.1}, N508_00960
GN {ECO:0000313|EMBL:ESJ98305.1};
OS Mucispirillum schaedleri ASF457.
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Mucispirillaceae; Mucispirillum.
OX NCBI_TaxID=1379858 {ECO:0000313|EMBL:ESJ98305.1};
RN [1] {ECO:0000313|EMBL:ESJ98305.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF457 {ECO:0000313|EMBL:ESJ98305.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF24424.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF24424.1};
RA Proctor A.L., Phillips G.J., Wannemuehler M.J.;
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF24424.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF24424.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (JUN-2022) 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; AYGZ01000014; ESJ98305.1; -; Genomic_DNA.
DR EMBL; CP097562; USF24424.1; -; Genomic_DNA.
DR RefSeq; WP_023275806.1; NZ_FTRD01000031.1.
DR AlphaFoldDB; V2QCT9; -.
DR STRING; 1379858.N508_00960; -.
DR REBASE; 86325; Msc457ORF964P.
DR GeneID; 78588245; -.
DR PATRIC; fig|1379858.3.peg.957; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_0_1_0; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000017429; 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; 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 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000017429};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 314..473
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 934..961
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1058 AA; 122618 MW; 57B0B2A7B42A81B2 CRC64;
MNNTLPNYDE KSTSQFSAVK QLINMGYNYL TREKVRDILH KQDYKYLLEE ITFQAMRKLN
DESVSDKSIL NRIYEIQKTN FDNGSESASL NIYNMLTMAE SAQEFVDGKK TDGSIKIIDW
ENVENNIYHV TTEYNIIDKK NIRIDIVVFI NGIPCAIIEN KKPSVAVDEA IKQIIKNSTG
SDALYFFLFP QIYIATNITN LKYGTYKTPN AYYNMWKEKY TTDEYNDKLL YTINNKLDDD
TLNKVLKDLS IKKYNYTIND EPSEQDIGIY GLLQKERVID IIKNFILFDK NIKKIARYNQ
YFAVKKTFAS LSTYNENGVR NGGLIWHTQG SGKSLTMVIL AKLILKKIPL ARIFIVTDRI
DLDEQIKDTF VNNNLGTKIE KASSGKDLVD RLKTKEYNSI TTTLIHKFNI TECIDDDSDI
FIFVDEAHRT QDGITHATMR AVMPKACIIG FTGTPLMTKT ESRTIQKFNN NLIDTYKMKD
AEIDKAVCEL VYQGRFAEQK LDKIMADFKF DRITKTLNEK QKQDLIKKYV SSTLMKENSK
YIYVVATDIY EHFIANFKGS GLKGQIVAPS KYAAVCFHKW FQEYHQSVKK DKVLNTAVVI
SDDNKYDNTG STDDEDIDYN NVVAKFLENI KKEKSLKKYE RETIDKFKKD TDEIEILIVV
NKLLTGFDAP RNTVLYLVKQ LENHNLMQAI ARVNRVFDGD NNKQKKNNGL IIDYSANAQN
LKDAMQLFSG FNPSDVENML KNTDDLIAEL QNIFNQMRKT FKNIPNTAPI EKYVDFLKQA
DNSFERELFY NNVNKCIDVF NSCLSLPDFY TKLSPAAISE YKNTLKSYVE IKKATKIAMA
EIIDFSKYKN QLKKILDEHL SADEVTVLTK EINISNSKEF NSFIEDNKTG LSKKSQADAI
AAQTKKIIKE RYSQDEEFYQ KFSDIIDDII KRLKLIKEED IDALLQEVKQ VQEQVTAYKD
NSENLPDSIR NNTNTHPYFR KLKNEFRDKN LQEVAEITLY IYNIIAQNKK VDFHKKIDIK
NKVLNMIQDY FIDELELTDY NKIGTLSEEI WNIAVANR
//
