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Database: UniProt
Entry: A0A1P8X3L9_9SPHN
LinkDB: A0A1P8X3L9_9SPHN
Original site: A0A1P8X3L9_9SPHN 
ID   A0A1P8X3L9_9SPHN        Unreviewed;       615 AA.
AC   A0A1P8X3L9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=DEAD/DEAH box helicase {ECO:0000313|EMBL:AQA00835.1};
GN   ORFNames=BWQ93_12130 {ECO:0000313|EMBL:AQA00835.1};
OS   Sphingopyxis sp. QXT-31.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1357916 {ECO:0000313|EMBL:AQA00835.1, ECO:0000313|Proteomes:UP000188055};
RN   [1] {ECO:0000313|EMBL:AQA00835.1, ECO:0000313|Proteomes:UP000188055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QXT-31 {ECO:0000313|EMBL:AQA00835.1,
RC   ECO:0000313|Proteomes:UP000188055};
RA   Liang J.S.;
RT   "Microbe-microbe interactions indirectly alter the fate of arsenic in
RT   presence of MnII.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492}.
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DR   EMBL; CP019449; AQA00835.1; -; Genomic_DNA.
DR   RefSeq; WP_077032366.1; NZ_CP019449.1.
DR   AlphaFoldDB; A0A1P8X3L9; -.
DR   STRING; 1357916.BWQ93_12130; -.
DR   KEGG; sphq:BWQ93_12130; -.
DR   OrthoDB; 9805696at2; -.
DR   Proteomes; UP000188055; Chromosome.
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:UniProt.
DR   CDD; cd00268; DEADc; 1.
DR   CDD; cd12252; RRM_DbpA; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   PANTHER; PTHR47959:SF19; ATP-DEPENDENT RNA HELICASE DBPA; 1.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   Pfam; PF03880; DbpA; 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.
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:UP000188055}.
FT   DOMAIN          30..205
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          228..384
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          427..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..460
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  67331 MW;  D511F60E201D1300 CRC64;
     MTFENLSPVL SDALTARGYE AFTPVQTHVT EDEAKGRDLL VSAQTGSGKT VAFGLAMADQ
     LIEGDRLPFA TSPLALIIAP TRELALQVSR ELSWLYAKAG ARIATCVGGM DASKERRALS
     QGVQIVVGTP GRLRDHLERG ALDLAALRVA VLDEADEMLD MGFREDLEEI LDATPETRRT
     LMFSATIPKP IAQLAKRYQR DALRISTVGE DRGHGDISYQ AVTVAPADIE GAVINLLRLH
     DAETAMLFCA TRDNVRRLHA SLTDRGFAAV ALSGEHSQNE RNSALQALRD RRAKVCVATD
     VAARGIDLPS LSLVIHVEIP RDAETLQHRS GRTGRAGKKG TAVLIVPYPR HRRVDGMLRG
     ARINAEWMDA PTAADVRLKD QERLIEKLLA PVEHEPEDIE LAQRLMAERT PEDIAASLVR
     AHRASMPVPE DLIDNSARGR DSAGRPERGE RFERPERSGE RREGFDDSVW FKLNIGRRQN
     ADPRWILPLL CRRGHVTKQE IGAIRIGPSE TMFNIPRAIA DRFAEAVVRS ANEDGEDDAG
     VAITPAPDGP TYPPRREKGS GDRPPRATLG RGPGGDRDRA PGPRGPRGPS TPGGPTERYK
     PKPFGQRGPR KTGKY
//
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