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Database: UniProt
Entry: A0A0A2DZF5_9PORP
LinkDB: A0A0A2DZF5_9PORP
Original site: A0A0A2DZF5_9PORP 
ID   A0A0A2DZF5_9PORP        Unreviewed;       587 AA.
AC   A0A0A2DZF5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=JT26_00070 {ECO:0000313|EMBL:KGN71946.1};
OS   Porphyromonas sp. COT-108 OH1349.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=1537504 {ECO:0000313|EMBL:KGN71946.1, ECO:0000313|Proteomes:UP000030126};
RN   [1] {ECO:0000313|EMBL:KGN71946.1, ECO:0000313|Proteomes:UP000030126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-108 OH1349 {ECO:0000313|Proteomes:UP000030126};
RA   Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA   Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT   "Porphyromonas sp. COT-108_OH1349 Genome sequencing.";
RL   Submitted (AUG-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:KGN71946.1}.
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DR   EMBL; JRAH01000002; KGN71946.1; -; Genomic_DNA.
DR   RefSeq; WP_036844391.1; NZ_JRAH01000002.1.
DR   AlphaFoldDB; A0A0A2DZF5; -.
DR   OrthoDB; 9785240at2; -.
DR   Proteomes; UP000030126; 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:UP000030126};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT   DOMAIN          1..29
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          33..204
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          234..376
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          442..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..587
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        442..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  65701 MW;  79D02BB738B64260 CRC64;
     MTFNELGVSA PLLRAVEALG YDQPMPIQEA VIPHLLGESR DIIALAQTGT GKTAAFGLPL
     LQNLDTTQRI PQALILAPTR ELCVQIAGDL ADYSQYMKNV GIVAVYGGAS IEQQIRTIRS
     GVQIIVATPG RLIDLMKRGV VNLSTVRDVV LDEADEMLNM GFTESIEEIL AQVPSERHLL
     LFSATMPKEI AAIASGYMKK PTEIVIGAKN EGNKNIRHIY YMVAAKDKYL TLKRIADYYP
     NIYGIIFCRT RRETQEIADK LIQDGYNADS LHGDLSQAQR DYVMQKFRIR NLQLLVATDV
     AARGLDVNDL THVIHYGLPE DVESYTHRSG RTARAGKSGL SIAICHSREK GRLRDIEKII
     GSQIERAYVP TGREVCERQL FTLADKIEST LPDDEDQMLS AILPAIVSKL SWIDKEELIR
     RFISMESHRL LQYYRAAQEV EEVPDKPLHD DRSKGSERRG RKKQRENGIP EPGYARLQIN
     FGRRDKLYPN SLIELLNATT GGARVEVGKI DIYDTFSYFE VPERDAKTVI SSMNDFEVGS
     RAIMVRKAQP KGGAGEKESG HGRDRSSATS RKDMRRAGKS GNGRRRR
//
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