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Database: UniProt
Entry: A0A077FBM4_9PSED
LinkDB: A0A077FBM4_9PSED
Original site: A0A077FBM4_9PSED 
ID   A0A077FBM4_9PSED        Unreviewed;      1060 AA.
AC   A0A077FBM4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=PSAKL28_19780 {ECO:0000313|EMBL:AIL61199.1};
OS   Pseudomonas alkylphenolica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL61199.1, ECO:0000313|Proteomes:UP000028931};
RN   [1] {ECO:0000313|EMBL:AIL61199.1, ECO:0000313|Proteomes:UP000028931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KL28 {ECO:0000313|EMBL:AIL61199.1,
RC   ECO:0000313|Proteomes:UP000028931};
RA   Lee K., Lim J.Y., Hwang I.;
RL   Submitted (JUL-2014) 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}.
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DR   EMBL; CP009048; AIL61199.1; -; Genomic_DNA.
DR   RefSeq; WP_038609670.1; NZ_CP009048.1.
DR   AlphaFoldDB; A0A077FBM4; -.
DR   REBASE; 92610; PalKL28ORF19740P.
DR   KEGG; palk:PSAKL28_19780; -.
DR   eggNOG; COG0610; Bacteria.
DR   HOGENOM; CLU_010804_0_0_6; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000028931; 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   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, ECO:0000313|EMBL:AIL61199.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          301..505
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1060 AA;  118727 MW;  9D96A8112E71AB8D CRC64;
     MSHIHHECEL ERHIVEQLAA AGWLVGKSAD YDAARALFPD DVLGWLEESQ PQAMAKLHAM
     NGTGTLDVVL DRLVKQLENK VDGGTVNVLR YGFAVAGGGT LAMSQGLPED DRNETVIQRY
     ATNRLRVVPQ LRYSLDKTDE IDLAFFINGI PVATVELKTD FTQSVQAAMQ QYRMDRKPER
     KSGGFEPLLT FKRGAVVHFA MSDSDIRMTT KLAGDSTFFL PFNRGNDGAA GNPPGDNDSY
     PVSYLWKRVL QKDNWLHIFH RYVLQERKEA QDLNGKTYFK EGLIFPRFHQ WEGVTKMIDA
     VRIEGAGQPY LIQHSAGSGK TNTIAWTAHS LIRVRRPDGE PYFHSVIVVT DRQVLDQQLQ
     DAIQQIEHQA GVVCAIDRQQ SSLPKSQQLA KAMLDGVPII VCTLQTFPYA QKAILGETSL
     RDRRFAIIID EAHSSTGGST ADDLRYVLTG QSEDEWDKLS KEERLSVWQS SRSRPGNASY
     FAFTATPKHS TLSLFGRPRN AAQPVNQENP PAPFHLYTMQ QAIEEGFILD VLKNYTGYNV
     AFKIGSEFVD DKRVDEKSAR RKLAKWLSLN PVNVGQKVEL IVEHFRKNVA HLLGGQAKAM
     VVTSSRAAAV KYHLALLDYC QRKGYDNVQA MVAFSGEVPN SDVQETGLPA DHQFSETNLN
     PGLNGRDMRK VFDTPDYRVM IVANKYQTGF DQPKLVAMYL DKKISGVEAV QTLSRLNRTF
     PGKDKTYVID FANEAEEILA AFKTFYRDAQ VADIQDPNIV YDIKQRLDGM FIYEAAEVEA
     FGEAIVNRNV THQKLYSLTQ SATDRFNGKL KTLNDGIDQW EKAWEAAHDN GDEKGMEYSD
     VQRAEYCMGR DELMIFSESL TKFVRTYEYI AQLVEFGDPA LEAFASYARL LRKRLKGVSA
     EQVDLDDLKL SHYKIKKGEG LAGLSAVGEA PELYGITDNG LRDARDREKK YLTELIEKLN
     NAFGKDITDT DQVAFAVHVS EKLRGDTIVM AQVQNNTMDQ AMKADLPSKA IQAIASAMSS
     HTSMATKLLS DESTRDVFLT VVYELLKKDA GADLLGSART
//
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