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Database: UniProt
Entry: A0A0C1G0S3_9FLAO
LinkDB: A0A0C1G0S3_9FLAO
Original site: A0A0C1G0S3_9FLAO 
ID   A0A0C1G0S3_9FLAO        Unreviewed;       632 AA.
AC   A0A0C1G0S3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=OA93_07855 {ECO:0000313|EMBL:KIA98792.1};
OS   Flavobacterium sp. KMS.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1566023 {ECO:0000313|EMBL:KIA98792.1, ECO:0000313|Proteomes:UP000031466};
RN   [1] {ECO:0000313|EMBL:KIA98792.1, ECO:0000313|Proteomes:UP000031466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:KIA98792.1,
RC   ECO:0000313|Proteomes:UP000031466};
RA   Smith A.K., Newman J.;
RT   "Flavobacterium sp. KMS.";
RL   Submitted (OCT-2014) 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:KIA98792.1}.
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DR   EMBL; JSYP01000006; KIA98792.1; -; Genomic_DNA.
DR   RefSeq; WP_039112599.1; NZ_JSYP01000006.1.
DR   AlphaFoldDB; A0A0C1G0S3; -.
DR   STRING; 1566023.OA93_07855; -.
DR   OrthoDB; 9785240at2; -.
DR   Proteomes; UP000031466; 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; 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; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47963:SF8; ATP-DEPENDENT RNA HELICASE DEAD; 1.
DR   PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 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   SUPFAM; SSF54928; RNA-binding domain, RBD; 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:UP000031466};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT   DOMAIN          2..30
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          34..205
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          225..378
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          439..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2..30
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        440..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..594
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..632
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   632 AA;  70369 MW;  739C1E32FD709E6C CRC64;
     MNKFEQLGLS ESLLKAILDL GFENPTEVQE KAIPLLLEKD TDMVALAQTG TGKTAAFGFP
     LIQKIDANNR NTQALILSPT RELCLQITNE IKNYSKYEKG INVVAVYGGA SITEQARDIK
     RGAQIIVATP GRMQDMINRG LVNISQINYC VLDEADEMLN MGFYEDIVNI LSTSPDEKST
     WLFSATMPQE VARIAKQFMH EPLEITVGAK NSGSSTVSHE FYLVNARDRY EALKRLADAN
     PDIFSVVFCR TKRDTQAVAE KLIEDGYSAA ALHGDLSQAQ RDGVMKSFRG RQIQMLVATD
     VAARGIDVDS ITHVVNYQLP DEIETYNHRS GRTGRAGKLG TSIVIVTKSE LRKISSIERI
     IKQKFEEKTI PSGIEICEIQ LLHLANKIKD TEVDHEIDNY LPAINNVLEG LSKEELIKKM
     VSVEFNRFIA YYKKNRDISN QSSGSERRDD RDGAARPNNN GGATRYFVNI GSRDNFDWMS
     LKDYLKETLD LGRDDVFKVD VKEGFSFFNT DPEHTDKVME VLNNVQLEGR RINVEISKND
     GGGRRDHNGR SSGGGFGGGR SSAPRREGSG GGFRSDRNSA PREGGFRSDR NSAPREGGFR
     SSAPRSEGGS DRAPRRSESF GDSSRPRRPR RD
//
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