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Database: UniProt
Entry: A0A151WLJ5_9HYME
LinkDB: A0A151WLJ5_9HYME
Original site: A0A151WLJ5_9HYME 
ID   A0A151WLJ5_9HYME        Unreviewed;       890 AA.
AC   A0A151WLJ5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=ALC60_12222 {ECO:0000313|EMBL:KYQ48716.1};
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:KYQ48716.1, ECO:0000313|Proteomes:UP000075809};
RN   [1] {ECO:0000313|EMBL:KYQ48716.1, ECO:0000313|Proteomes:UP000075809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ48716.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYQ48716.1};
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};
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DR   EMBL; KQ982959; KYQ48716.1; -; Genomic_DNA.
DR   RefSeq; XP_018312969.1; XM_018457467.1.
DR   AlphaFoldDB; A0A151WLJ5; -.
DR   STRING; 64791.A0A151WLJ5; -.
DR   GeneID; 108728732; -.
DR   OrthoDB; 5488182at2759; -.
DR   Proteomes; UP000075809; 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:UniProtKB-EC.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:KYQ48716.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075809}.
FT   DOMAIN          256..420
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          445..618
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..882
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   890 AA;  101998 MW;  FD60E1F048EDA64A CRC64;
     MLSKTSKYRR EETSSEDTDS EEERRKKDIK ERDSFASRLR AKDESKRRNI ATLPGSGAAE
     AAKRLKIIET DTKDKLIPKL RIESRRKYLE KRKEDKVAEL EADILDDEYL FDENILTEKE
     KHERAHKKQL LHLAKEHEKA RELERMQRYH MPLEKGKTEP EPDTTEKEPP QSEQSKWESD
     QMSSAVFRFG AKDRKAQQEY NLLMEDEMIE FVQVLRMPGH KDKKWEESPP AHVKSLQTIQ
     ETKKSLPIYP FRKDLIQAIK DHQVLIIEGE TGSGKTTQIP QYLYESGFAD DGKIIGCTQP
     RRVAAMSVAA RVAHEMAVKL GNEVGYAIRF EDCTSQRTRI KYMTDGTLHR EFLSEPDLAS
     YSVMIIDEAH ERTLHTDILF GLVKDIARFR PNLKLLVSSA TLDATKFSEF FDDAPIFRIP
     GRRFPVDIYY TKAPESDYIE ACVVSIIQIH ITQPSGDILV FLTGQEEIET CQEMLQERVR
     RLGSKLAEIL ILPVYANLPS DMQIKIFQPT PPGARKVVLA TNIAETSLTI DNIVYVIDPG
     YAKQNNFNPR TGMESLIVVP ISKASANQRA GRAGRVAPGK CFRLYTAWAY QHELEDNTVP
     EIQRINLGNA VLTLKALGID DLMHFDFLDP PPPETLILAM EQLYALGALN HRGELTKLGR
     RMAEFPLDPM MAKMLLASEK YRCSEEVATI AAMLSVNGAI FYRPKDKIIH ADAARKNFHA
     PGGDHLTLLN VYNQWAQSDF STHWCYENFI QHRSMKRARD VREQLVGLMQ RVEMELVSGI
     TETVNIRKAI TAGYFYHVAR LSKGGCYKTA KHNQQVTIHP NSSLFQDLPR WLLYHELVLT
     TKEFMRQVTE IESKWLLEVA PHYYKPKEVE DSTNKKMPKV AGRSRPDGTN
//
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