ID A0A1E3X6P4_9BACT Unreviewed; 972 AA.
AC A0A1E3X6P4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-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=SCARUB_03552 {ECO:0000313|EMBL:ODS31323.1};
OS Candidatus Scalindua rubra.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Scalinduaceae; Scalindua.
OX NCBI_TaxID=1872076 {ECO:0000313|EMBL:ODS31323.1, ECO:0000313|Proteomes:UP000094056};
RN [1] {ECO:0000313|EMBL:ODS31323.1, ECO:0000313|Proteomes:UP000094056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSI-1 {ECO:0000313|EMBL:ODS31323.1};
RA Speth D.R., Lagkouvardos I., Wang Y., Qian P.-Y., Dutilh B.E., Jetten M.S.;
RT "Draft genome of Scalindua rubra, obtained from a brine-seawater interface
RT in the Red Sea, sheds light on salt adaptation in anammox bacteria.";
RL Submitted (JUL-2016) 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:ODS31323.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MAYW01000126; ODS31323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3X6P4; -.
DR PATRIC; fig|1872076.5.peg.4229; -.
DR Proteomes; UP000094056; 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:0004386; F:helicase activity; 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; 2.
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 Helicase {ECO:0000313|EMBL:ODS31323.1};
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:UP000094056};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 283..482
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 972 AA; 113356 MW; D9741ECF940E84CD CRC64;
MKKSSITEKN FEVEHVTKTL VNNGYLERLP DDYNQELLLD QEILLNFVKN TQPDEWEKLQ
EQYPSNTENV FLKRISNEIG KRGTLDVLRN GVKDRGAKFE LAYFKPVSGL NPEHEKLYKQ
NKFSVIRQLP FSQKYQKTLD VSIFLNGIPI ITSELKNHFT GQDYTDAIKQ YKYTRDPKEP
FLKRCFAHFA VDNDKAYFTT KLEGEITQFL PFNKDIANPV DKRGFKVAYF YHDIWHPDSL
LEIISHYIQI VEKKDPKTRS KSKKLIFPRF HQLVSVRSLI DSAKNSGTGK HYLIQHSAGS
GKTFTISWLA HQLSQIHNQN DQRVFDNVIV ISDRKVIDKQ LKDAVKEFEK TLGVVLCTKK
SKDLKEGLET GKQIIVTTIQ KFPFVVEEIE KLKGKKFAVI IDEAHSSQGG ESMTKVKKTL
SFTSLEEAEE KDEEDRDIED QILEDMKARG KLSNVSFFAF TATPKQQTLE LFGSKQPDGS
YQAFSLYSMM QAIEEGFILD VLENYMTYKT YFKLVKMIED DPEYEKRKAT AVLKRYVDIH
EHAIKKKTEI MLDHFYRKVK GKINGKAKAM VVTRSRLHAV RYKQEFERQL KEKGSNVKAL
VAFTGTIKDD GHEFTESNMN GFPESQTVNK FDTDEYRIMI VAYKFQTGFD QELLQTMYVD
KKLQKVNAVQ TLSRLNRTSS GKDAVYVLDF VNETDDIKKG FQPYYETTIL SEGTDPNILY
EIERDILRFD IIDKSEIDVF TEFWHSTEDQ SKLHRVLEPA IDRFKGLSKE DKFTFKDNLR
RYTKAYGFIT QLVSFKDVSL EKLYLYCRFL LKKLPLDKDS LPREVVESID MDRYRIKPTY
KGGITLEKKE GELAPMTTDE KQPPVSEFEK LSAIIAKVNE IGSTHFNEDD KVKFTRLADT
IYDDEYFQES MKTNTKSNLK LLFKKLFDNV MADMYESDFN FYKKIEENQS VKDLIKDNLF
EDVFKRARKV QL
//
