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Database: UniProt
Entry: A0A150APU3_9BACT
LinkDB: A0A150APU3_9BACT
Original site: A0A150APU3_9BACT 
ID   A0A150APU3_9BACT        Unreviewed;       428 AA.
AC   A0A150APU3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=AVL50_03910 {ECO:0000313|EMBL:KXX71939.1};
OS   Flammeovirga sp. SJP92.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Flammeovirga.
OX   NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX71939.1, ECO:0000313|Proteomes:UP000075267};
RN   [1] {ECO:0000313|EMBL:KXX71939.1, ECO:0000313|Proteomes:UP000075267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJP92 {ECO:0000313|EMBL:KXX71939.1,
RC   ECO:0000313|Proteomes:UP000075267};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
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:KXX71939.1}.
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DR   EMBL; LQAQ01000018; KXX71939.1; -; Genomic_DNA.
DR   RefSeq; WP_062615339.1; NZ_LQAQ01000018.1.
DR   AlphaFoldDB; A0A150APU3; -.
DR   STRING; 1775430.AVL50_03910; -.
DR   OrthoDB; 974172at2; -.
DR   Proteomes; UP000075267; 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; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KXX71939.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075267}.
FT   DOMAIN          1..29
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          32..208
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          219..379
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          404..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1..29
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        413..428
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   428 AA;  49159 MW;  156E66D60E9DA1DD CRC64;
     MKFEKYSISS SLKRSLEEKG FKKPTDIQFK SIPPILRGED VLAIAQTGTG KTAAFAIPVM
     ERLLNKPNKG NRKKSIRTLV MAPTRELAQQ ITEVFETIGK YTKLDILCIY GGVEQDKQIE
     KLESGVDILI ATPGRMFDLQ HQGYVDLSRT EILVLDEADH MLEKGFIKDI KDVIRFLPKH
     RQTLFFSATI DEQIKKLAYS LVKNAIRIQI SPKDPVSKNV RHALSYVKMD DKRFFLENII
     REHPEKKILV FVRTKVRAER VHKAMERVGL ETVTIHGDKD QKARTHAMKT FKEGKVKVLI
     ATDVSARGID IPNVQIVVNY DMPDVPENYV HRVGRTGRGM EKGDAISFCD EQEKELKEEI
     EDFMGKEIAV HRLERGDYAN IVGFSAEQST DWKSVMKEIA QDQTDYKEIK KRSNRKKEKK
     KLAKRNKK
//
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