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Database: UniProt
Entry: A0A0F5JTN1_9BURK
LinkDB: A0A0F5JTN1_9BURK
Original site: A0A0F5JTN1_9BURK 
ID   A0A0F5JTN1_9BURK        Unreviewed;       879 AA.
AC   A0A0F5JTN1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
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   ORFNames=WM40_24635 {ECO:0000313|EMBL:KKB61183.1};
OS   Robbsia andropogonis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Robbsia.
OX   NCBI_TaxID=28092 {ECO:0000313|EMBL:KKB61183.1, ECO:0000313|Proteomes:UP000033618};
RN   [1] {ECO:0000313|EMBL:KKB61183.1, ECO:0000313|Proteomes:UP000033618}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP2807 {ECO:0000313|EMBL:KKB61183.1,
RC   ECO:0000313|Proteomes:UP000033618};
RA   Lopes-Santos L., Castro D.B., Ottoboni L.M., Park D., Weirc B.S.,
RA   Destefano S.A.;
RT   "Draft Genome Sequence of Burkholderia andropogonis type strain ICMP2807,
RT   isolated from Sorghum bicolor.";
RL   Submitted (MAR-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   -!- 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:KKB61183.1}.
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DR   EMBL; LAQU01000062; KKB61183.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F5JTN1; -.
DR   STRING; 28092.WM40_24635; -.
DR   PATRIC; fig|28092.6.peg.5806; -.
DR   OrthoDB; 5298826at2; -.
DR   Proteomes; UP000033618; 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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; 2.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE   4: Predicted;
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:UP000033618}.
FT   DOMAIN          147..670
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   REGION          80..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         168..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   879 AA;  99211 MW;  DC5B1C322A238002 CRC64;
     MQVLHVCVES GQSKSRALPF EDFARGGPHE FKKQGDFKTR MLQRSVAGSP VLRGLSMMHW
     FLQLWANVLA FLGLARTRES KDVTRTPEPV QQSLPMKPQQ PKSAPTSAVV TVKDVYAGDA
     FEIKASTQRN AREHMYREKE PGSSKLIGPT DNQLRLIFST RAALPVLAGA GSGKSTSLVN
     RFLLATNYLN VQLRHITVFT FTRKSRRDFI EKLIEESQFW PTPITLKEAE ASVRTFHSKA
     LQLFRAKRGR DVAVFEFLKD EIPAAKNSAE ATIPTSDVAP PSDDLLSEEE FRANDVDSLM
     PGNLSRIQLR LLHDAYTTRF SQSNSFRLVV RELLKASFLS PPIAKDDKDA LEAIRFERQI
     LRRDEQWSAY VEADWRRRGL WPLPGVRELN SPDERRPLIA ENGQYAAHGY IASVDTYVVL
     GVHSEISNKV NGFGGTTLVK NFQASKNKQA LLLAQCEQKI RYVTDEKDLT ALKKQLHWAA
     LPETNVAPKF KIRIPGERKL LPVFYALFTF GQFAENLAVD PCTLDQLHLL AKGSVEEQFG
     RACAEYYSSF YEALGARRVW TFNQIFKALA DEQDVLGEMD AADLSPIQHL LIDEFQDISP
     AIVKFVTAAQ TRLWKKSGDA IQPTLIAVGD DWQSIYGWRG SSPKFFMDFH KYFRGSPRQA
     LQLNQNFRSS ANIIRAAEAA LVDLRERLEG KLNGEAESRY KNLPIPVCQV TEFKSDDVVR
     VVRMLLQGKK KGERVFVLSR AKLDATAKAV RDVFRAVSER DLLVTTLHQS KGLEADYVIL
     LGEIRYVGRN VLRNSVYLKA ELVGSAHGRE RAYDLAQQDE ALRLAYVGIT RAKQFCIWFA
     EPKSEGVFER LPRRSNYSTQ VTVADVISLA KQVGSMEKV
//
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