ID F6DB03_THICA Unreviewed; 726 AA.
AC F6DB03;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=Thicy_1578 {ECO:0000313|EMBL:AEG32336.1};
OS Thiomicrospira cyclica (strain DSM 14477 / JCM 11371 / ALM1)
OS (Thioalkalimicrobium cyclicum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=717773 {ECO:0000313|EMBL:AEG32336.1, ECO:0000313|Proteomes:UP000009232};
RN [1] {ECO:0000313|EMBL:AEG32336.1, ECO:0000313|Proteomes:UP000009232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14477 / JCM 11371 / ALM1
RC {ECO:0000313|Proteomes:UP000009232};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Kappler U., Woyke T.;
RT "Complete sequence of Thioalkalimicrobium cyclicum ALM1.";
RL Submitted (MAY-2011) 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; CP002776; AEG32336.1; -; Genomic_DNA.
DR RefSeq; WP_013836109.1; NC_015581.1.
DR AlphaFoldDB; F6DB03; -.
DR STRING; 717773.Thicy_1578; -.
DR KEGG; tcy:Thicy_1578; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_6; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000009232; 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; 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:UP000009232}.
FT DOMAIN 8..286
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 287..568
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 726 AA; 81527 MW; F4D9DA21FF046AB3 CRC64;
MDVNYILDGL NDAQRQAVTL ETGHGLVLAG AGSGKTRVLV HRIAWVVEVL GASPYNVLAV
TFTNKAAREM RGRMEALMGP AAKSVTMGTF HGIAYQLLRQ HYQAAGLPQA FQILDSDDQK
RMVKRLLKAM NLDETQWPVK QVVGFINSEK EEGRRAKHVD AGHNPYLKTL VAVYESYEQQ
CQQAGLVDFA ELLLRAHELW LRSPEVLAFY QQRYQHILVD EFQDTNSLQY AWLRVLAGGR
GRLFVVGDDD QSIYGWRGAK VENIRLFEQQ FAEVALVRLE QNYRSTNRIL LAANHLISHN
TERMGKNLWS DGEPGEPILI YEAFNDLDEC QYVIEQIQGW LREGGTREQV AILYRSNSQS
RVFEQGLLQA EMPYRIYGGL RFYDRAEIKD VLAYLRLIMN SADDAAFERV YNLPTRGLGD
KTMQQVRDLA RDQACSMWQA SELLLNQGGL AARAKGALQG FLNLITELAS LQPSLALADF
VLQVMQDSGL QAHYEKDRSE QGQSKLENLD ELVNAAASFE KRQDLQADTD NDNSLLNFLA
QATLEAGDNQ ASAGESAIQL MTLHAAKGLE FPLVFMVGME EGLFPSQSSQ DDPSRLEEER
RLAYVGITRA EQRLFMCAAQ RRRLHGNEIY SQPSRFLREL PEDAVNWVRM SGRVQPTRAW
GNEASTQNAA TNETGLSLGQ AVFHQKFGQG VVMATEGSGD HTRIQVSFKH AGVKWLVMAY
ANLTPA
//
