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Database: UniProt
Entry: A0A0B7I935_9FLAO
LinkDB: A0A0B7I935_9FLAO
Original site: A0A0B7I935_9FLAO 
ID   A0A0B7I935_9FLAO        Unreviewed;       780 AA.
AC   A0A0B7I935;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   Name=pcrA {ECO:0000313|EMBL:CEN46413.1};
GN   ORFNames=CCAND38_340013 {ECO:0000313|EMBL:CEN46413.1};
OS   Capnocytophaga canis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=1848903 {ECO:0000313|EMBL:CEN46413.1, ECO:0000313|Proteomes:UP000045051};
RN   [1] {ECO:0000313|EMBL:CEN46413.1, ECO:0000313|Proteomes:UP000045051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CcD38 {ECO:0000313|EMBL:CEN46413.1,
RC   ECO:0000313|Proteomes:UP000045051};
RA   MANFREDI Pablo;
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; CDOI01000145; CEN46413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7I935; -.
DR   Proteomes; UP000045051; 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; 3.40.50.300; 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; 1.
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:UP000045051}.
FT   DOMAIN          6..290
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          291..573
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         27..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   780 AA;  88979 MW;  C40308BF19F41C31 CRC64;
     MEKYLAQLND AQRAPVLQKE GPLMVIAGAG SGKTRVLTYR IANLIHLGVD AFNILALTFT
     NKAANEMKKR ITEIVGNEAK NLWMGTFHSV FAKILRIEAD KLGYPQNFTI YDTQDSQRLI
     NSIIKEMELD KDVYKYKQIQ SRISSFKNSL ITVRAYFNNP ELMEADAMSK RPRMGEIYQA
     YVERCFKAGA MDFDDLLLKT NELLNLYPDV LAKYQHRFQY ILVDEYQDTN HSQYLIVKAL
     ADRFQNICVV GDDAQSIYAF RGANINNILN FQQDYQNARV YRLEQNYRST KNIVEAANSV
     IDHNKTKLEK VVWTANELGE PIKIHRSPTD SDEGRFVAGS IFENKMNLQL PNSAFAVLYR
     TNSQSRAIED ALRKRDIPYR IYGGLSFYQR KEVKDMLAYL RLIINPNDEE ALVRIINFPA
     RGIGGTTLEK LTFAANHYKK SIFEIMYKIN QIDGLNMNAS TKQRLTDFVV MILNFQSLSK
     TSNAFEIAEQ VARKTGLLQE LKKDGTPEGI AKMENIEEML NGIKDFVEGQ EDVADSTASL
     AEYLEDVALV TDMDKDTGDD DRVALMTIHL AKGLEFPYVY IVGMEEDLFP SAMSVNSRAE
     LEEERRLFYV ALTRAEKQAY LTYAENRYRW GKLSDAEPSR FIDEINNQYV QYLTAPINNP
     NYRYKPLINR DIFGEVDKSR LRLQKPTNST PPPSHAPKGD ELQRLRKLKP MNSSSIGNGS
     NPNQGVALSE GMFVFHERFG KGKIISLEGV GSDRKASIDF ESGGVRKILL KFAKLQVIEK
//
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