ID A0A0D6S303_9PSED Unreviewed; 1137 AA.
AC A0A0D6S303;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=SZ55_4780 {ECO:0000313|EMBL:KIV62887.1};
OS Pseudomonas sp. FeS53a.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1604022 {ECO:0000313|EMBL:KIV62887.1, ECO:0000313|Proteomes:UP000032531};
RN [1] {ECO:0000313|EMBL:KIV62887.1, ECO:0000313|Proteomes:UP000032531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FeS53a {ECO:0000313|EMBL:KIV62887.1,
RC ECO:0000313|Proteomes:UP000032531};
RA de Souza R., Sant'Anna F.H., Ambrosini A., Tadra-Sfeir M., Faoro H.,
RA Alvarenga S.M., Pedrosa F.O., Souza E.M., Passaglia L.M.;
RT "Genome of Pseudomonas sp. FeS53a associated with rice cropped in iron-
RT stressed soils.";
RL Submitted (JAN-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:KIV62887.1}.
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DR EMBL; JYFT01000075; KIV62887.1; -; Genomic_DNA.
DR RefSeq; WP_044412596.1; NZ_JYFT01000075.1.
DR AlphaFoldDB; A0A0D6S303; -.
DR REBASE; 111870; PspS53aORF4780P.
DR PATRIC; fig|1604022.3.peg.4422; -.
DR Proteomes; UP000032531; 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 CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.90.1570.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR025285; DUF4145.
DR InterPro; IPR013670; EcoEI_R_C_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF13643; DUF4145; 1.
DR Pfam; PF08463; EcoEI_R_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 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, ECO:0000313|EMBL:KIV62887.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000032531};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 367..524
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 599..760
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 157..205
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1137 AA; 128300 MW; 2AB6AFB41AF31F80 CRC64;
MSNFDFLKAE WPALHAEALK AEAGVLADPR SACFYARRTL ELMVAWLFQA DRSLRPPYKS
DLSAFLFEPS FKALVGPMLH AKMEIIRKRG NDAVHSTRQV RQQDAQAVLS ELFHVTYWLG
RTYARHASSK PDAALRFDPN LLPPPPAQAV ARSLAQLKTL EQDAAQRDAE LAVAREQNAA
LDEEVRRLRA EVEAAKAANT QVADTHDYNE AQTRDLFIDQ LLHEAGWTLE AERDREFPVE
GMPNASGQGS VDYVLWGDDG LPLALIEAKR TQKDPYDGQR QAELYANCLE ARYGRRPLIY
FTNGYEHWLW DDRLYPARLV QGFHKKAELE LMQQRHASRR PLGEASIDPA IVERHYQVRA
IRRIGETFER DRQRKALVVM ATGAGKTRTV IALCDLLMRC NWAKRILFLA DRVALVNQAA
NAFKTFLPSA SPVNLVTEKG GEGRVYVSTY PTMMGLIDEK QAGQRRFGVG HFDLIVIDEA
HRSVYQKYRA IFSYFDALLV GLTATPKDEI DRNTYSLFNL ESGVPTDAYT LEDAIAEGYL
VRPRAVSVPL KFQREGIRYD DLSEDEKDQW DELDWGDEDA APKEVGAEAV NRWLFNTDTV
DKMLETLMTR GHKVAGGERI GKTIIFAKND DHATFIAKRF DANYPDKAGH FARMVTYKAP
YAQTLIDDFS IKDKAPHIAI SVDMLDTGID VPEVVNLVFF KVVRSKAKFW QMVGRGTRLC
TDLFGPGQDK EDFFIFDFCQ NFEFFNENPE PAEGSLTEPL SQRLFKARLA MLAALDRRRA
QAGVREPAGA YETSYSDDEL REDIALMLHE RVAAMTLDNF LVRPKRRWVE TYAQVGIWND
LGPAQLQELA EHLSGLPCTL AEEDEEAKRF DLLILRLQLC ILNAEPGFAR YSEAVQELAQ
ALLEKCAQVP AIGAHALLIE AVAGQEWWED VTVSMLEQAR RKLRGLIRLL EPGRGRTVYT
NFADELGRVE EVAMPTMINP ASFERFREKV RAFLRQHQDH LSLQKLRRNQ PLTALDLQAL
EQMLVDSGAA AGEINLAKEH AHGLGLFVRS LVGLDREAAT EALAAFLVGK TLSANQIEFV
DLVVQHLTEF GVMEPYRLYE SPFTDLTPAG PDGLFSTEQV DELLGVLERV KSSAMVA
//
