ID A0A2P8AWQ3_9ACTN Unreviewed; 1046 AA.
AC A0A2P8AWQ3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN Name=hsdR_2 {ECO:0000313|EMBL:PSK64836.1};
GN ORFNames=B0E53_03210 {ECO:0000313|EMBL:PSK64836.1};
OS Micromonospora sp. MH33.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1945509 {ECO:0000313|EMBL:PSK64836.1, ECO:0000313|Proteomes:UP000240342};
RN [1] {ECO:0000313|EMBL:PSK64836.1, ECO:0000313|Proteomes:UP000240342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH33 {ECO:0000313|EMBL:PSK64836.1,
RC ECO:0000313|Proteomes:UP000240342};
RA Thatcher L.F., Myers C.A., O'Sullivan C.A., Roper M.;
RT "Draft genome sequences of Micromonospora sp. MH33 and MH99.";
RL Submitted (FEB-2017) 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:PSK64836.1}.
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DR EMBL; MUYZ01000092; PSK64836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8AWQ3; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000240342; 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.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 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, ECO:0000313|EMBL:PSK64836.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000240342};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 302..512
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1046 AA; 115567 MW; 5923A87642A994BA CRC64;
MRADHNEVVF ESEICAYLES HGWLYSASGT GYDRERALFP EDVFGWLEET QKAAYEKALK
AAGSQAKFLD VLTTALDKPL EHGGGTLNIL RNGVQYIGGG RLKMAQFRPE TSLNATTNEQ
YAAMRVRVMR QVHFSTADQR SIDLVFFVNG LPVATVELKT DFTQSLDEAI NQYRKNRHPL
TNGRPEPLLS FGHRALVHFA VSNDLAAMTT KLEGETTHFL PFNMGHESGA GNPPGEGGRS
ATAYLWERVW EKDAWLTIIG RLMIVETKEE WDVATGTSVR RTSMLFPRFH QWEAVTNIVA
AVREEGVGHR YLIEHSAGSG KTNTIAWTAH RLARLHVNDE KFFDSVIVVV DRTVLDGQLQ
EAIRQIDGSG KIVATISPQD VRKAGAKSKS GLLATALKNG ELIIAVTVQT FPFALDEIRA
DSSLKGRRFA VIADEAHSSQ SGQISSKLKA VLTAEEVKEI EEGGEVDVEA ILASEMTERA
ESENISYFAF TATPKNKTLE LFGRNGPDGK PVEFHLYSMR QAIEEGYILD VLRGYQSYDT
ALKIAGRAES GDGDEEVEEA AARKGLMRWV KLHPTNISQK VQIIVEHFHA NVAHLLEGKA
KAMVVTDSRK AAVKYKKAID AYIAKRAAKD ASYNYRTLVA FSNSVKMAEN EEWASDWGPQ
PSKDDEFTEA SLNPGAGPDL AAAFKGTTYK IMLVANKYQT GFDQPLLSAM YVDKKLSGVT
AVQTLSRLNR THRTAGGEQK RKTFILDFVN KPEHIRTAFE PYFTNATLET ETDPYIVVHL
ANKLAQAGIY TPEQVREVAG LWVTRKGNKA LSAAISPAKN DFARRYTAAI EADDKVTLNT
LDLFRKDVST YVRLYDFMSQ IVDYGDPYME MLSIFLRLLE KVIADASWAA EVDLSDVVLV
GVKHTKGTAV DISLTGDGEL KGIGAAGTGT RKEPKYVALQ VVIDKMNDLF GAESFSASQV
REFVQGLVQR LLAYPDLVNQ VKVNSKKQFM ESQDFQAAVT EAVVDNQEAH NTMADYFFSD
GPGISAVIMA LADAFYEAAI DQGTDV
//
