GenomeNet

Database: UniProt
Entry: A0A1J0VHV2_9GAMM
LinkDB: A0A1J0VHV2_9GAMM
Original site: A0A1J0VHV2_9GAMM 
ID   A0A1J0VHV2_9GAMM        Unreviewed;       563 AA.
AC   A0A1J0VHV2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=BOX17_11920 {ECO:0000313|EMBL:APE31594.1};
OS   Halomonas aestuarii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1897729 {ECO:0000313|EMBL:APE31594.1, ECO:0000313|Proteomes:UP000181985};
RN   [1] {ECO:0000313|Proteomes:UP000181985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hb3 {ECO:0000313|Proteomes:UP000181985};
RA   Koh H.-W., Rani S., Park S.-J.;
RT   "Halolamina sediminis sp. nov., an extremely halophilic archaeon isolated
RT   from solar salt.";
RL   Submitted (NOV-2016) 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; CP018139; APE31594.1; -; Genomic_DNA.
DR   RefSeq; WP_071944866.1; NZ_CP018139.1.
DR   AlphaFoldDB; A0A1J0VHV2; -.
DR   KEGG; hsi:BOX17_11920; -.
DR   OrthoDB; 9805696at2; -.
DR   Proteomes; UP000181985; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   CDD; cd00268; DEADc; 1.
DR   CDD; cd12499; RRM_EcCsdA_like; 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; IPR034415; CsdA_RRM.
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   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   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   Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT   DOMAIN          9..37
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          40..211
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          222..382
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          435..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           9..37
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        446..464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..563
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  61148 MW;  7285DF7FE7A87599 CRC64;
     MTSTSVVSPT FGDLALLPAV LSAVESQGYE TPSPIQAQTI PALLEGRDML GQAQTGTGKT
     AAFALPLLSR LDLARREPQV LVMAPTRELA QQVAVSFSKY GQNLKGLEVA TLCGGQEYRE
     QLSALRRGAH VVVGTPGRII DHLDRGSLKL DGLSALVLDE ADEMLRMGFI DDVKRVVADT
     PKNAQRVFFS ATLPAEIERI VNRYLVDPVK VAIESKTGTA ASIEQRMVRV DGGAKQEALA
     RILEVEPVDG AIVFVRTRAA CTTLMEQLSA RGMSVASLSG DLDQSLRERT IQRLKRGKVD
     VLIATDVAAR GLDVPRITHI INYDLPQDGE AYTHRIGRTG RAGRTGIAIT FVGFREGRKV
     GWLEQATGQK MTEMAVPDEA AIRGHRDEMF HQRVVAALTA GADEQRALVE RMVEEGHDPV
     ELACAFARMA RADEPPIGRL QAPRAERNTA DSKPKRRDSA PREGMTRYRV AVGHQDGVKP
     GQLVGALANE GGIEGNRIGR IDIRTAFSVV ELPSSLPESI LAKMARARVA GRPLEISEDR
     GAPERAPRRR QDSDAPIRRR TSA
//
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