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Database: UniProt
Entry: A0A0B0ER45_9BACT
LinkDB: A0A0B0ER45_9BACT
Original site: A0A0B0ER45_9BACT 
ID   A0A0B0ER45_9BACT        Unreviewed;      1098 AA.
AC   A0A0B0ER45;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE            EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN   ORFNames=SCABRO_00663 {ECO:0000313|EMBL:KHE93618.1};
OS   Candidatus Scalindua brodae.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Scalinduaceae; Scalindua.
OX   NCBI_TaxID=237368 {ECO:0000313|EMBL:KHE93618.1, ECO:0000313|Proteomes:UP000030652};
RN   [1] {ECO:0000313|EMBL:KHE93618.1, ECO:0000313|Proteomes:UP000030652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU1 {ECO:0000313|EMBL:KHE93618.1};
RA   Speth D.R., Russ L., Kartal B., Op den Camp H.J., Dutilh B.E., Jetten M.S.;
RT   "Draft genome of anammox bacterium scalindua brodae, obtained using
RT   differential coverage binning of sequence data from two enrichment
RT   reactors.";
RL   Submitted (OCT-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}.
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:KHE93618.1}.
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DR   EMBL; JRYO01000046; KHE93618.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B0ER45; -.
DR   REBASE; 103245; SbrRU1ORF665P.
DR   PATRIC; fig|237368.3.peg.719; -.
DR   eggNOG; COG0610; Bacteria.
DR   Proteomes; UP000030652; 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; 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   Helicase {ECO:0000313|EMBL:KHE93618.1};
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          338..541
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1098 AA;  125223 MW;  FA04B47F9F6366E2 CRC64;
     MNDKSIESVF QNEMINQMVA NGWLLGKPEN YNRDLALYEE DLLGFIKETQ DGQWQKFCKL
     YPNNPEQKFL ERVASQLNKA DPNAANKEMR TFGTLGVLRH ELRDRGTRFT LCQFKPEHDL
     NPDTLARYEK NRLRIVPELV YSPWADISTL SQPSPKGEGD EHLAQAGAKA KAWRIDLVLF
     VNGLPIATLE LKSEFKQAVY NAIKQYKTTR FPIDPATKKP EPLLTFKRGA LVHFAVSQYE
     VFMTTHLKGE ETFFLPFNKG TEEGGAGNDT PKDVNRYATD YLWNDVLLPD NLLNILARYV
     HLQIEEKEDW EGRKFKVETM IFPRYHQWDV VNRLIDAART EGPGHKYLIQ HSAGSGKSNS
     IAWTAHQLSS LYNQAGNKQF DSVIIVTDRN VLDAQLQDTI YQFEHMDGVV GRINKEEGDG
     SKSEKLASAL ESSQPIIIVT IQTFPFVLKA IENSVSLKER NYAIIADEAH SSQTGSTARQ
     LKEVLMIEGS DEEELTADDI LDAAVASRRT SNNLSYFAFT ATPKTKTLEL FGRLPNPDEP
     PSKTNLPKSY HVYSMRQAIE EGFILDVLKN YTNYKVAYNL ALAIQSKDQE VESKKAKVKL
     NQWVRLHDYN ISQKVQVIIE HFRDNVMGLL GGQAKAMVVT SSRKEAVRYK LCFDKYITEK
     GYQTIHAMVA FSGEVEFNEN DPNTEGLIGE KFTENNMNPN LKGRDMRKAF ESKDYQVMIV
     ANKFQTGFDQ PKLCAMYVDK KLGGVECVQT LSRLNRIYPG KSDSGTFILD FFNEPEDILE
     SFKPYYQTAE LADVSDPDLI FNLFDKLRAA GIFLWSEVEQ FCEAFFKKSK SNAAIANICK
     PAVERWKIRY KSAVEAYKQA KEIFDRTKKS TDPVLIANAE NSLKECKREK DALDIFKKDL
     GTFVRFYEFM SQIVDYNDKD LEKLSLYSRN LRPMLRESLI DEDDIDLQSV ELSHYRLTAI
     RQQENLGISD SKDSTDEYKL MPGEGLGTAK AKDKKEELIS QVISRLNELF ITDQLTDNDL
     VNYAYTIRDK VKEDELVMKQ IANNTSEQAM LGDFHKAVDN AVIDSSEAHQ NQMMQLLSDP
     KKSAGFARVV FDLLKLAS
//
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