ID C4XFR4_MYCFP Unreviewed; 1032 AA.
AC C4XFR4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN OrderedLocusNames=MBIO_0721 {ECO:0000313|EMBL:BAH69986.1};
OS Mycoplasmopsis fermentans (strain ATCC 19989 / NBRC 14854 / NCTC 10117 /
OS PG18) (Mycoplasma fermentans).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC Mycoplasmopsis.
OX NCBI_TaxID=496833 {ECO:0000313|EMBL:BAH69986.1, ECO:0000313|Proteomes:UP000006810};
RN [1] {ECO:0000313|EMBL:BAH69986.1, ECO:0000313|Proteomes:UP000006810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19989 / NBRC 14854 / NCTC 10117 / PG18
RC {ECO:0000313|Proteomes:UP000006810};
RX PubMed=19219498; DOI=10.1007/s00284-009-9362-6;
RA Ishida N., Irikura D., Matsuda K., Sato S., Asano K.;
RT "Molecular cloning and expression of a novel cholinephosphotransferase
RT involved in glycoglycerophospholipid biosynthesis of Mycoplasma
RT fermentans.";
RL Curr. Microbiol. 58:535-540(2009).
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 -!- SIMILARITY: Belongs to the HsdR family.
CC {ECO:0000256|ARBA:ARBA00008598}.
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DR EMBL; AP009608; BAH69986.1; -; Genomic_DNA.
DR AlphaFoldDB; C4XFR4; -.
DR REBASE; 21888; Mfe18ORF720P.
DR KEGG; mfp:MBIO_0721; -.
DR PATRIC; fig|496833.3.peg.315; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_015458_1_0_14; -.
DR Proteomes; UP000006810; 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 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; IPR040980; SWI2_SNF2.
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; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006810};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 329..505
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 863..915
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1032 AA; 122080 MW; 975B1C9ED559F387 CRC64;
MMEFNEDTRV KLPATIHFLK LGYNYQTVRS PEINRDNNIF EERFHRAIEK INKKKFAKEE
INELISDISR KIKNKDLGKE FYNRLISTDY PIKLIDFENI ENNDFAIVNE LTFRSNANSN
YDSFRPDITI LVNGMPLAFL EVKVKNNKNG IQAEFIRMWE DRLKVDEYRK FFNMLQIVSF
TNNMDYEEFN DAEASLLKQG SFYTTPNGKD NTTFSAFRED EPNYHANYSF EEIDNDKIKE
ILIDNNIKTS HVDSDWFQTN LSDTTPCNRF ITSIFDKERF LYFIKYGMMY LSQIKEIKNE
TLNKVEQLPI NQKHIMRYPQ FFATRAIIKR FKRTNKNGII WHTQGSGKTA LSAFATKVIK
DYWSKKKINA RFFFIVDRLD LMRQASAEFA NRGFNVVNVD SKEAFAKELN ETIDRNNNGI
GTICVVNIHK FMDSSKMPEA KNDYNIRTQR IFFIDEAHRS YTMHGEFYKN LMTCDRDGIY
IAMTGTPLLT KRERSNLKFG DYIHKYFYDK SIADGYTLRI KKEQIKTEAR ATIIRNLNIE
IEKLESRIIY ESDDYVKSVS QYIEKDFIDF RFICRNDLTI GGMIVCRSND QAKKIHEWFK
KNSKLTTGLV LSDTDNPLQD NINKNNQKTF KESNYPDILV VHYMLTTGYD VKRLKKMYLL
RGPKAQNLLQ TISRVNRPYR SPNGQEYQYG YIVDFIDIEK EYNNTIDAYR KEIEEEYDFE
EEDTSLSGLI IDKTDIKKRY DVLKSDLEKF VNNYNLETFV DKINNFDKDT LQKIKKILVN
IKNCSIEFKL SQADEYSKLI NDYEINVFIK EVQKKINFLN LRSDPIDTIQ LIDNKEVVQI
IYDFLLKNIT VLDLGKFDKE NKMELIKQKF MKMQKEIKEN KNTRDVKFMN LNALIKKLLD
KLAVEELTYE EVEDELDLIY NSTKKINEEN KEISKDFGNS LAFVTTMNIV LAETKLDRSI
LKNFLLMVYD ELKGNISDEI LIKQGKNGFI DSTKSKITTR LIKKNLYKQI KDNYDYILNE
LYFNLLNYKE TL
//
