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Database: UniProt
Entry: A0A0M8MQZ2_9MICO
LinkDB: A0A0M8MQZ2_9MICO
Original site: A0A0M8MQZ2_9MICO 
ID   A0A0M8MQZ2_9MICO        Unreviewed;      1037 AA.
AC   A0A0M8MQZ2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=XI38_02820 {ECO:0000313|EMBL:KOS11871.1};
OS   Microbacterium chocolatum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=84292 {ECO:0000313|EMBL:KOS11871.1, ECO:0000313|Proteomes:UP000037737};
RN   [1] {ECO:0000313|EMBL:KOS11871.1, ECO:0000313|Proteomes:UP000037737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIT 101 {ECO:0000313|EMBL:KOS11871.1,
RC   ECO:0000313|Proteomes:UP000037737};
RA   Li X., Xu Y.;
RT   "Complete genome sequence of Microbacterium chocolatum SIT 101, a bacterium
RT   enantioselectively hydrolyzing mesomeric diesters.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KOS11871.1}.
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DR   EMBL; LAVO01000002; KOS11871.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8MQZ2; -.
DR   PATRIC; fig|84292.3.peg.586; -.
DR   Proteomes; UP000037737; 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   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; PTHR42927; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR42927:SF1; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000037737};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          296..527
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00487"
SQ   SEQUENCE   1037 AA;  113788 MW;  463C444FECC95ABA CRC64;
     MGETVNVAGA HLESVLENEI AEYLAANGWL YSPTDAGYDR ELALFPEDVL GWLEDSQPTE
     FAKVVRPSDT DAQREMAGRG ILTRLAKSLD LDPLKNGGTI RILHEGFSMV PLHGGAVKFR
     LAQFRPATTQ NPDTLEAYAK MRVRVMRQVH YSAKHPNKAL DLVLFVNGIP VATVELKTDF
     TQSIGNAVNQ YRFDRSPAGE PLFGFAKRSL VHFVVSNSQV RMTTKLAGPK TRFLPFNKGA
     DEGAGNPVNP DGSASAYFWE EILQRDTWLQ LLGSFVHLQV EVDVDPDTGK KTKTEKVLFP
     RYHQWRAVTR LVQAARVEGP GNRYLVQHSA GSGKTNSISW LAHRLSQLHD DQNQRVFDTV
     VVVTDRTVLD KQLQDAIGQF ETQAGVVQSI TKDAGESKSK QLAAALTGGK NIVIVTIQSF
     EALITAIQTL PELQGRRFAV IADEAHSSQT GSTAGALTKV LSPDEQAAVA EGAPIDSDAY
     LQWAMEVTAS APNISYFAFT ATPKAKTLEL FGRKPEGGEL PEPFDLYSMQ QAIEEGFILD
     VLQNYTPYKV AWKLQHPDSD YDGDGEVDES TAVKALVQYV RLHPTNISQK AKIVVDHFRA
     FVQPLLDGKA KAMVVTGSRI EAVRWKKYLD TYIADAGVLG VRSLVAFSGT VDDPDDVGEG
     LTERTQNPGV PSDLAEAFKP ATYNVMIVAE KFQTGFDQPR LVAMYVDKKL GGVQAVQTLS
     RLNRTYPGKD KTFVLDFVND PVEVLDAFLP YYRKATLTAT TDPNLIYDLV VKLDSAGIYD
     MAEVEQAFDA ALAGGVSANS KVSAATAPAV DRFQKRWVAA VLDDDKSEQD ELRLFKADVG
     NFVKFYDFIS QARNLEDTDL PRRHYFFRRI LPQLSTATIL EPVDISDVTL VGYKISAGES
     VKLNLEQGPG LDPITAIGSG AIHEKHRSAL EEIIQKLNER LGDKYGVGVI DLQMNHIVGK
     LALDVELANQ ASVNTEQQFA ESPALPKAFT KALLGVRDET PAFIDDLLGD GGLFSDLSKA
     LPAMLYEFLK DKGAARG
//
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