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Database: UniProt
Entry: Q28NL8_JANSC
LinkDB: Q28NL8_JANSC
Original site: Q28NL8_JANSC 
ID   Q28NL8_JANSC            Unreviewed;       817 AA.
AC   Q28NL8;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE   AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN   OrderedLocusNames=Jann_2777 {ECO:0000313|EMBL:ABD55694.1};
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=290400 {ECO:0000313|EMBL:ABD55694.1, ECO:0000313|Proteomes:UP000008326};
RN   [1] {ECO:0000313|Proteomes:UP000008326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1 {ECO:0000313|Proteomes:UP000008326};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA   Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABD55694.1, ECO:0000313|Proteomes:UP000008326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1 {ECO:0000313|EMBL:ABD55694.1,
RC   ECO:0000313|Proteomes:UP000008326};
RX   PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA   Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA   Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA   Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA   Saunders E., Buchan A.;
RT   "Ecological genomics of marine Roseobacters.";
RL   Appl. Environ. Microbiol. 73:4559-4569(2007).
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; CP000264; ABD55694.1; -; Genomic_DNA.
DR   RefSeq; WP_011455898.1; NC_007802.1.
DR   AlphaFoldDB; Q28NL8; -.
DR   STRING; 290400.Jann_2777; -.
DR   KEGG; jan:Jann_2777; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_004585_5_2_5; -.
DR   OrthoDB; 9806690at2; -.
DR   Proteomes; UP000008326; Chromosome.
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; 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:UP000008326}.
FT   DOMAIN          32..312
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          313..608
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   817 AA;  90273 MW;  CBFC41258E458B2D CRC64;
     MSQFDDSDAF EAAATSSLAS RAMAARPQPY MDGLNPAQIA AVNQLDGPVL MLAGAGTGKT
     RALTARIAHL MSTGTARPNE ILAVTFTNKA AREMKTRVGH LLGQPAEGMP WLGTFHAICV
     KLLRRHAELA GLKSNFTILD TDDQTRLMKQ LIIAEEIDDK RWPARALGSI IDGWKNRALT
     PDKVPSADHG AFNHQGVKLY AQYQARLKAL NACDFGDLLL HVIQIFQDND DLLQQYQRWF
     RYILVDEYQD TNVAQYLWLR LLAAGHKNIC CVGDDDQSIY GWRGAEVGNI LRFEKDFPGA
     HVVRLEQNYR STGHILAAAS GVIAGNTGRL GKTLWTDGED GEKVRLIGHW DGDEEARWIG
     EEIEAMGKGT RGMEPIGPNS IAILVRASHQ MRAFEDRFLT IGLPYRVIGG PRFYERMEIR
     DAMAYFRVVV SPDDDLAFER IVNTPKRGLG DKAQQTIQRM ARSNGVSLLE GARLCVETQA
     IGGKGGRELR TLVDGLARWR IQLTGALRAA GPSDDLIEED ADPSEVPKIS HIELAEIILD
     ESGYTSHWQN DKTPEGPGRL ENLKELVKAL ENFENLQGFL EHVSLIMDNE QDDQEPKVTL
     MTLHAAKGLE FPAVFLPGWE DGLFPSQRSM DESGQAGLEE ERRLAYVGIT RAEEVCTISF
     AGNRRVYGQW QSQMPSRFID ELPEDHVEVL TPPGLYGHQG SVSATASPVE REMAGSNLHE
     KAASADVYNS PGWRRLQARQ GQYGTRQPSE AKAMTIDAEA ISAFTVGDRV FHQKFGYGEV
     VSVEGDKLGI EFDKAGSKHV VGRFLVAAGE EGGEVPF
//
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