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Database: UniProt
Entry: A0A1G8ZNA8_9GAMM
LinkDB: A0A1G8ZNA8_9GAMM
Original site: A0A1G8ZNA8_9GAMM 
ID   A0A1G8ZNA8_9GAMM        Unreviewed;       566 AA.
AC   A0A1G8ZNA8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=SAMN04487954_11273 {ECO:0000313|EMBL:SDK16517.1};
OS   Halomonas gudaonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=376427 {ECO:0000313|EMBL:SDK16517.1, ECO:0000313|Proteomes:UP000198525};
RN   [1] {ECO:0000313|EMBL:SDK16517.1, ECO:0000313|Proteomes:UP000198525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6133 {ECO:0000313|EMBL:SDK16517.1,
RC   ECO:0000313|Proteomes:UP000198525};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNES01000012; SDK16517.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8ZNA8; -.
DR   STRING; 376427.SAMN04487954_11273; -.
DR   OrthoDB; 9805696at2; -.
DR   Proteomes; UP000198525; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000198525};
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          437..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..566
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        438..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  61698 MW;  E9B78AB19841822B CRC64;
     MTSTSVASPS FGDLALLPAV LAAVETQGYQ TPSPIQAETI PALLEGRDML GQAQTGTGKT
     AAFALPLLSR LELTRREPQV LVLAPTRELA QQVAVSFSKY GQNLKGLEVA TLCGGMEYRD
     QLQALKRGAQ VVVGTPGRVI DHLDRGSLKL EGLSSLVLDE ADEMLRMGFI DDVKRVVADT
     PKDAQRVFFS ATLPAEIERI VNRYLVDPVK VAIESRTTTG ENIEQRLVRV DGGAKLEALA
     RILEVEPVDG AIVFVRTRAA CTTLMEQLSA RGINVASLSG DLDQSLRERT IQRLKRGKVD
     VLIATDVAAR GLDVPRLTHI INYDLPQDSE AYTHRIGRTG RAGRTGISIT FVGFREGRKV
     GWIEQATGQK MTEMEVPDEA AVRAHRDEAF HQKVIAALTA GAEEQRALVE RLVEEGHDPI
     ELACAFARLA RADEAPIGRL QAPRKERSER APRDGKPPRR DRGPSEGMTR YRVAVGHKDG
     VKPGQLVGAL ANEGGIEGNR IGRIDIRNAF SVVELPSSLP ASILAKMARA RVAGRPLEIR
     EDNGSPERAP RRRIDGEAPI RRRDRA
//
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