ID A0A151XIN2_9HYME Unreviewed; 737 AA.
AC A0A151XIN2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=ALC60_00581 {ECO:0000313|EMBL:KYQ60175.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ60175.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ60175.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ60175.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ60175.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1
CC subfamily. {ECO:0000256|ARBA:ARBA00043999}.
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DR EMBL; KQ982080; KYQ60175.1; -; Genomic_DNA.
DR RefSeq; XP_018306330.1; XM_018450828.1.
DR AlphaFoldDB; A0A151XIN2; -.
DR STRING; 64791.A0A151XIN2; -.
DR GeneID; 108724448; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
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:UniProtKB-EC.
DR CDD; cd17947; DEADc_DDX27; 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; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF14; DEAD-BOX ATP-DEPENDENT RNA HELICASE 28; 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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000075809}.
FT DOMAIN 150..178
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 181..356
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 367..547
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 529..576
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 150..178
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 27..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 84604 MW; 8CAE9C39331484D9 CRC64;
MTSNCDLIKT IEDDQEVPDY SENSDEEDDF QPRKQKKKEN KDFDKGFQFT SAEHNLDPWN
DLNKYIKRKP NTKLDDKIKK ARKEYGQAGT EDPIKIEPET GQDDDVISLS EDELKKDIFK
TKEKKGKIKN MKEKDEVINF EEYTDSQTYT TFYQMNLSRP LLKAITTMNF VQPTPIQAAT
IPAALMGRDI CGCAATGTGK TAAYMLPTLE RLLYRPLDGP SISRVLVLVP TRELGVQVYQ
VTKQLAQFTT IEVGLSVGGL DVKVQEGVLR KNPDIVIATP GRLIDHVKNA PIFSLDSIEV
LILDEADRML DEYFAEQMKY IVKQCSRTRQ TILFSATMTE EVEDLAAVSL DKPIKIFVDS
NQEVAFNLRQ EFIRIRTERE GDREAILAAL VCRTFHDHTM VFLQTKKQAH RLHILLGLLG
VKVGELHGNL TQPQRLENLR KFKDEEIDIL LATDVAARGL DISGVKTVIN FVMPATLQHY
IHRVGRTARA GRGGVSVSLA GEQERTLVKK IIKQAKNPVK NRIIPPDIIE KYNKKLESLE
PDVQQILQEE KSEKELAKVE NEANRIEKIL KVEDSKEQRS WFQSKKERKK EKDNFRLTKK
QVGKNKKHEK EPSNIVQEKK KKAQNEPQKD TAEDRAKKEL EKIAAYQARL AKKSNRQKKI
RTVIDENNRD FAKKRSLKRP KSSFAADLTD TSKKGVKRMR YEANKKKEVK KNQNTFKSQQ
KSKFATKGKN QKKFKKR
//
