GenomeNet

Database: UniProt
Entry: A0A0L7R2V8_9HYME
LinkDB: A0A0L7R2V8_9HYME
Original site: A0A0L7R2V8_9HYME 
ID   A0A0L7R2V8_9HYME        Unreviewed;       715 AA.
AC   A0A0L7R2V8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=WH47_04701 {ECO:0000313|EMBL:KOC65111.1};
OS   Habropoda laboriosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Habropoda.
OX   NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC65111.1, ECO:0000313|Proteomes:UP000053825};
RN   [1] {ECO:0000313|EMBL:KOC65111.1, ECO:0000313|Proteomes:UP000053825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0110345459 {ECO:0000313|EMBL:KOC65111.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Habropoda laboriosa.";
RL   Submitted (JUL-2015) 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; KQ414666; KOC65111.1; -; Genomic_DNA.
DR   RefSeq; XP_017790603.1; XM_017935114.1.
DR   AlphaFoldDB; A0A0L7R2V8; -.
DR   STRING; 597456.A0A0L7R2V8; -.
DR   EnsemblMetazoa; XM_017935114.1; XP_017790603.1; LOC108572806.
DR   GeneID; 108572806; -.
DR   OrthoDB; 5477821at2759; -.
DR   Proteomes; UP000053825; 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; 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; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF73; RNA HELICASE; 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:UP000053825}.
FT   DOMAIN          106..134
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          137..312
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          340..487
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           106..134
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        1..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   715 AA;  80351 MW;  232437D12CB5EA2D CRC64;
     MYNNSYSNHT SYRPRSNRDS SSRNGGGTFW NSQQQKDKPI KKQVQRRTPG DSLKKPSWDL
     AKLPVITKNL YIPHINVLKR SIEEVTKYHI GKEITVKGNS TPSPIQAFEE SNFPEYVMEE
     IRKQGFAEPT AIQAQGWPIA LSGRDLVGIA QTGSGKTLAY ILPATVHINN QPRLNRGDGP
     IVLILAPTRE LAQQIQTVAR DFGSSSCIRN TCIFGGSPKG PQARDLERGV EICIATPGRL
     IDFLEKGTTN LRRCTYLVLD EADRMLDMGF EPQIRKIIEQ IRPDRQVLMW SATWPKEVQA
     LAEDFLTDYI QINIGSLTLA ANHNIRQIVE ICQEHEKEAK LSGLLREIGK DRGGKMIIFV
     ETKKKVDDIT KTIKREGWPA ISIHGDKSQP ERDYVLSEFR NGKTMILVAT DVAARGLDVE
     DVKYVINFDY PNSSEDYIHR IGRTGRCQSA GTAYAYFTPN NARQAKELIS VLEEAGQAIN
     PQLADLANSI KSAYGKGRQR WSHSRSNKDN NSTGSPRNNS SPTGSNWQNH QVQSVQHSTA
     SNQERTVVRQ QNGYQPTRQN SFQSSYQQQQ QQQQQQQQHP QHQQHQQQHQ RQSGSYTNGC
     QTSNGYQASY QNANIPRYHG RTGGFQGSRY HNRQSAYNAN QTAGGQSVYS MPPPFMLPSG
     GHTDSGMQSL VNNKFFQTNR PPPNTGACAY QSMGYSQFQA VPPYSYPYPP TPVQQ
//
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