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Database: UniProt
Entry: A0A3R9PAP6_9BACT
LinkDB: A0A3R9PAP6_9BACT
Original site: A0A3R9PAP6_9BACT 
ID   A0A3R9PAP6_9BACT        Unreviewed;       942 AA.
AC   A0A3R9PAP6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=EDE15_2991 {ECO:0000313|EMBL:RSL17456.1};
OS   Edaphobacter aggregans.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Edaphobacter.
OX   NCBI_TaxID=570835 {ECO:0000313|EMBL:RSL17456.1, ECO:0000313|Proteomes:UP000269669};
RN   [1] {ECO:0000313|EMBL:RSL17456.1, ECO:0000313|Proteomes:UP000269669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB153 {ECO:0000313|EMBL:RSL17456.1,
RC   ECO:0000313|Proteomes:UP000269669};
RA   Deangelis K.;
RT   "Sequencing of bacterial isolates from soil warming experiment in Harvard
RT   Forest, Massachusetts, USA.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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:RSL17456.1}.
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DR   EMBL; RSDW01000001; RSL17456.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R9PAP6; -.
DR   Proteomes; UP000269669; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.30.160.800; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF21196; PcrA_UvrD_tudor; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000269669}.
FT   DOMAIN          10..295
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          296..703
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          500..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          821..854
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..524
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..615
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         31..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   942 AA;  104684 MW;  F9239562B2162109 CRC64;
     MCSALSELLM NMNPQQQEGI KSVDGPVLLL AGAGSGKTRV ITHRIAYLIQ ERGVPADSIL
     AVTFTNKAAK EMEERVNKIL GHTSLAKPML ATFHSFCVRV LRRDIEALRV NGVGLTKTFA
     IYDETDQQAV VKSALKRLAI DDKSLKPRVA LGRISWAKNH MIDPQEYFLA STNPMEEKIA
     HIFEIYKKEL FKANALDFDD LLLETVRLLK SSAEVRERYN RRYRYVMIDE YQDTNRPQYE
     LMKLLAGSHG NICVVGDEDQ SIYSWRGADI KNILDFEKDF PDVKTIRLEQ NYRSTQMILE
     GAGAVVAQNT QRKGKNLWTA REGGSLIGYY EAPDGENEAL FIADRVQRYL REAGQQEEQP
     RCAVLYRTNS QSRLVEEALR RYQIQYHMVG GFSFYDRAEV KDILSYLKLV QNVHDSIALN
     RVINSPARGI GKTTMETLER MALASGMSTW DAMGRAIEDK LLPQRALINL SGFRRLIEDA
     RAMLGPGFAE KLSEDVAPLA EEEGDTSFGF GAEDSDDDEV PVETGAGDAA DTSFDTSFNF
     GFDFGPTEEL STIAPENARD SDELHGIDAV SFNPFAPVVL KSSAASRRTK ADPPPSTKDD
     KGEGKDLEER PAFRKPGDAA TLPELIKFLN DRSGYIRALE EEATPESFSR IENLKELANA
     AQDAQERGET LEEFLDHAAL VSDADQYSAE AKVTLMTLHA AKGLEFPLVF LAGMEEGLFP
     HSRTLMDPSG MEEERRLCYV GMTRAMDTLV MTRARYRRRY GSDMPEASVA SRFLEEVPSR
     LVEDLGSPPA RPQFSGSRYG GMYATPYPKA NRFGAGREEG ERHYSYEDED QSAPRGGGVS
     SGARAKSGAR AASGGGSIDN IASFFAGRGQ AAGQKFSRPK VDVPEPTGKT GLKQGSRVRH
     PKYGEGIVFR REGDGDDAKI TVQFQQHGVK KLVEKFAQLE RL
//
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