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Database: UniProt
Entry: A0A1G7XH95_9FLAO
LinkDB: A0A1G7XH95_9FLAO
Original site: A0A1G7XH95_9FLAO 
ID   A0A1G7XH95_9FLAO        Unreviewed;       586 AA.
AC   A0A1G7XH95;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=SAMN04488027_108115 {ECO:0000313|EMBL:SDG83598.1};
OS   Psychroflexus sediminis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Psychroflexus.
OX   NCBI_TaxID=470826 {ECO:0000313|EMBL:SDG83598.1, ECO:0000313|Proteomes:UP000199296};
RN   [1] {ECO:0000313|EMBL:SDG83598.1, ECO:0000313|Proteomes:UP000199296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19803 {ECO:0000313|EMBL:SDG83598.1,
RC   ECO:0000313|Proteomes:UP000199296};
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; FNCW01000008; SDG83598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7XH95; -.
DR   STRING; 470826.SAMN04488027_108115; -.
DR   OrthoDB; 9785240at2; -.
DR   Proteomes; UP000199296; 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; 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:UP000199296};
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          232..378
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          529..586
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        529..566
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   586 AA;  66162 MW;  F6A828255D9496B2 CRC64;
     MTTFESLGLS PEILKAIEDL GFESPSEVQE QTIPVLLEEP TDMVALAQTG TGKTAAFGFP
     LIQNIDLNSK KTQGLILSPT RELCMQITNE LKQYAKYYQN LNTVAVYGGA SITDQARQIK
     RGAQIIVATP GRMKDMIQRN IIDISNINIC ILDEADEMLN MGFFEDIKEI LSHSSDQKNT
     WLFSATMPKE VSMIAKKFMK SPKEITVGQK NISTKSVSHE YFIVGGRDRY SAVKRVVDAN
     PDIYAVIFCR TKRDTQKVAE KLIEDGYSAS ALHGDLSQAQ RDMVMNSFRK KQIQMLVATD
     VAARGIDVDD ITHVINYQLP DEIETYTHRS GRTGRAGKEG KSLVIVTKSE VRKIRQVEKI
     IGQKFTQEEL PSGDEICKRQ LFHLADEIKS TKINPDIDSF IPDLEAQFED LSKEEIIKKF
     FSVEFTRFHN YYKNAPKITQ HSADESYSSG KDYGDETRFF INIGEKDGFN WMSMKDFLKE
     QLNLDRDGVA KVDVKNTFSF FNVATDDVDK VVSTFDNFML KGRHVNVEIT KDQKSGSGRK
     GGGGGRDRGD RKPRKRFDKN KSSDFKGKKS GGSSVKSSFE RRRKKS
//
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