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Database: UniProt
Entry: G4MBU0_9BURK
LinkDB: G4MBU0_9BURK
Original site: G4MBU0_9BURK 
ID   G4MBU0_9BURK            Unreviewed;       493 AA.
AC   G4MBU0;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=ATP-dependent RNA helicase Bcep18194_A5658 {ECO:0000313|EMBL:CCD38619.1};
GN   ORFNames=BKIR_c32_4002 {ECO:0000313|EMBL:CCD38619.1};
OS   Candidatus Paraburkholderia kirkii UZHbot1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1055526 {ECO:0000313|EMBL:CCD38619.1, ECO:0000313|Proteomes:UP000003511};
RN   [1] {ECO:0000313|EMBL:CCD38619.1, ECO:0000313|Proteomes:UP000003511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot1 {ECO:0000313|EMBL:CCD38619.1,
RC   ECO:0000313|Proteomes:UP000003511};
RA   Carlier A.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCD38619.1, ECO:0000313|Proteomes:UP000003511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot1 {ECO:0000313|EMBL:CCD38619.1,
RC   ECO:0000313|Proteomes:UP000003511};
RA   Carlier A.L., Eberl L.;
RT   "Draft genome sequence of Candidatus Burkholderia kirkii.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492}.
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:CCD38619.1}.
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DR   EMBL; CAFE01000184; CCD38619.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4MBU0; -.
DR   STRING; 1055526.BKIR_c32_4002; -.
DR   HOGENOM; CLU_003041_1_3_4; -.
DR   BioCyc; CBUR1055526:G10QW-1595-MONOMER; -.
DR   Proteomes; UP000003511; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   CDD; cd00268; DEADc; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003511}.
FT   DOMAIN          17..45
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          48..226
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          237..397
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          393..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           17..45
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        393..445
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  54078 MW;  DC5A2AEF5A7B04F4 CRC64;
     MSDSVATNTS TAQAAAPTFD QFGLSSDILK AVRESGYTTP TPIQAQAIPV VLSGRDVMGA
     AQTGTGKTAS FSLPIIQRLL PTANTSASPA RHPVRALMLT PTRELADQVA ANVQTYSKHT
     PLRSTVVFGG VDMNPQSDAL RRGVEILIAT PGRLLDHVQQ KTVNLGQVQM LVLDEADRML
     DMGFLPDLQR ILNLLPKECQ TLLFSATFSA EIKKLASTYL RNPQTIEVAR SNSTNANVRQ
     IVYEVHESDK SGAVAQLIRE RKLKQVIVFC NSKIGASRLA RVLERDGIVA TAIHGDRTQS
     ERMQALDAFK RGEIEALVAT DVAARGLDIA ELPAVINFDL PFNAEDYVHR IGRTGRAGAS
     GDALSLCSAN ERKQLADIEK LIKRPLEVDP LEVTTRARRE GPGSRRDERF GRSERGKHRH
     SSREEAGSRR RAMGTHDRPR GRQQPIDEFF LKPYEPSPSA MKRQEETEPE RKSMPKQPLA
     ALLGGLGMPR KSS
//
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