ID L8MYJ5_9CYAN Unreviewed; 753 AA.
AC L8MYJ5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=Pse7429DRAFT_2277 {ECO:0000313|EMBL:ELS32561.1};
OS Pseudanabaena biceps PCC 7429.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=927668 {ECO:0000313|EMBL:ELS32561.1, ECO:0000313|Proteomes:UP000011201};
RN [1] {ECO:0000313|EMBL:ELS32561.1, ECO:0000313|Proteomes:UP000011201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7429 {ECO:0000313|EMBL:ELS32561.1,
RC ECO:0000313|Proteomes:UP000011201};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:ELS32561.1}.
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DR EMBL; ALWB01000088; ELS32561.1; -; Genomic_DNA.
DR RefSeq; WP_009627338.1; NZ_ALWB01000088.1.
DR AlphaFoldDB; L8MYJ5; -.
DR PATRIC; fig|927668.3.peg.2648; -.
DR OrthoDB; 9765670at2; -.
DR Proteomes; UP000011201; 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:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; 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|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:ELS32561.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 12..341
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 362..629
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 753 AA; 84774 MW; 3C605C856B3C5186 CRC64;
MVSPEVLHEL RQTLRKGQQP MADWQGGELA VSAVPGAGKS TGMAVAAAIA IAKLQLHRHK
QLVIVTFTRS AVSNIRKKVS EHLKNLRLPQ SAFTVSTLHS LAYNIASTHR ELSGFGVGET
KIISESLKQK LIRNATYLWV KENPKLYDLL LEGRNFDGED TERLRRQTVL RTDVLPSLAR
EAIATAKSSG LSPWELRDAE APDGGNILEI AAGLYETYER LLRQEGAIDY DDMILGALRV
LRNDGVRKYW QERIFAVFED EAQDSSPLQT KLLEILAQHS LAQPPFSSEG AEVKNLMRVG
DPNQAINSTF TPADPRFFNE FCDRCHLNSQ LSTLDRAGRS TSNIMRAANY VLHWVNHSEY
ARIEKPFRPQ KIRPVDADDP QANANPEPIG KGVEIYTPDD IEREIEMIGD RILQLYALDP
QTSMAILVRQ HNQGRFVADA LAWLSKEHDI KIYDVEQSDR RSRVPMDMLA ILQFMERPHS
PDNLKSALEV LKDRQKISSQ QDLNALASNP EKFLYPTLLD PSLSPLAQET QSKCIGLLRA
KITLPLYNLI PFIAFTLYDE EAGLLATADK LGDRLNQQLV GNYSMQTIIE ALREIVESES
FEAVEDENLE GRYMAGGQVT IISLHKSKGL DWDVVFMPFL HKRICPGEAY IPEAVKFLGD
FGLPEVTRAQ IRAIVHGDRL PNAEEAWAQY NYLKQAEEFR LLYVGMTRAK KLLWLSASKA
APFSWNTLEN RTENAPICPA IAELARKFPE LLS
//