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Database: UniProt
Entry: A0A182QXG8_9DIPT
LinkDB: A0A182QXG8_9DIPT
Original site: A0A182QXG8_9DIPT 
ID   A0A182QXG8_9DIPT        Unreviewed;      2171 AA.
AC   A0A182QXG8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=U5 small nuclear ribonucleoprotein 200 kDa helicase {ECO:0000256|ARBA:ARBA00034541};
OS   Anopheles farauti.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF018820-PA, ECO:0000313|Proteomes:UP000075886};
RN   [1] {ECO:0000313|Proteomes:UP000075886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AFAF018820-PA}
RP   IDENTIFICATION.
RC   STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF018820-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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DR   EMBL; AXCN02001526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 69004.A0A182QXG8; -.
DR   EnsemblMetazoa; AFAF018820-RA; AFAF018820-PA; AFAF018820.
DR   VEuPathDB; VectorBase:AFAF018820; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000075886; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR   CDD; cd18019; DEXHc_Brr2_1; 1.
DR   CDD; cd18021; DEXHc_Brr2_2; 1.
DR   CDD; cd18795; SF2_C_Ski2; 2.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041094; Brr2_helicase_PWI.
DR   InterPro; IPR048863; BRR2_plug.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR   Pfam; PF21188; BRR2_plug; 1.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 2.
DR   Pfam; PF18149; Helicase_PWI; 1.
DR   Pfam; PF02889; Sec63; 2.
DR   PIRSF; PIRSF039073; BRR2; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00490; HELICc; 2.
DR   SMART; SM00973; Sec63; 2.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          517..700
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          711..948
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1364..1540
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1573..1781
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          51..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..240
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2171 AA;  246697 MW;  18FB40A7480AD50B CRC64;
     MADAAARQLQ YEYKANSNLV LQADVRLIER PRRDEATGEV ISLVGKLDGT RMGDRAQRSK
     PEKTEERKAK RQKRDEAQYD FNSMKGATLL SEGIDEMVGI VYRPKTQETR QTYEVLLSFI
     QEAIGDQPRD ILRGAADEIL AVLKKDRMKD REKKREIDGL LGTVADERFA LLVNLGKKIT
     DFGSEAATAI GGAGQAGPGG DEPIDETYGI NVRFEESEEE SDEDKYGEVR EDDGQDEGEE
     ARDDGILHAE NLGGGEDMNK KEKALDPRDI DAHWLQRCLR KYYNDSMTSQ SKALEVLSVL
     KESSDDRECE NQLVILLGFD CFDFIKQLKK NRQMILYCTM LAQSQCESDR AKIRERMKAD
     AALAKILRQL DTGKQEVQEG RDYANGGADG SESKPSLRSR REDGIMDDME EKMGGGSGGD
     RSAAGQGQIV GNRNVLELDE LAFTQGSHLM ANKRCQLPDG SFRKQRKGYE EVHVPALKPR
     PFDEDEELIA IEKLPKYVQP VFNGFKTLNR IQSRLYKSAL ESDENMLLCA PTGAGKTNVA
     LLAMMREIGK HINDDGTINV DEFKIIYIAP MRSLVQEMVG NFGRRLATYN LTVAELTGDH
     QLSREQIAAT QVIVCTPEKW DIITRKGGEK TYTQFVRLII IDEIHLLHDE RGPVLEALVA
     RTIRNIETTQ EDVRLVGLSA TLPNYQDVAT FLRVRPETGL FYFDNSYRPV ALEQQYIGVT
     EKKALKRFQV MNDIVYEKVM EHAGRNQVLV FVHSRKETGK TARAVRDMCL EKDTLGSFLR
     EGSASLEVLR SEADQVKNQE LKDLLPYGFA IHHAGMTRVD RTLVEDLFAD RHIQVLVSTA
     TLAWGVNLPA HTVIIKGTQV YNPEKGRWVE LGALDVLQML GRAGRPQYDT KGEGILITNH
     SELQYYLSLL NQQLPIESQL ISKLPDMLNA EIVLGTVQNV KDAVTWLGYT YLYIRMLRQP
     TLYGVSIDAV QEDPLLEQFR ADLIHTAAIR LERSGLIKYD RKSGHLQVTE VGRIASHYYC
     THDTMLTYHQ LLKPTLSEIE LFRVFSLSGE FRNITVREEE KLELQKLMER VPIPIKESME
     EPSAKVNVLL QAYISQLKLE GFALMADMVY VTQSASRLLR AIFEIVLHRG WAQLADKCLT
     LCKMIDRRMW QSMSPLRQFR KMPEEIVKKI EKKNFPWERL YDLEANEIGE LIRVPKLGKT
     IYRYIHQFPK LELSTHIQPI TRSTLRVELT ITPDFQWDEK VHGQSEAFWI LVEDVDSEVI
     LHHEYFLLKA KYCTDDHLVK FFVPVFEPLP PQYFLRIVSD RWIGAETQLP VSFRHLILPE
     KNLPPTELLD LQPLPISALR DPSFEALYTD RFPQFNPIQT QVFNAVYNSE DNVFVGAPTG
     SGKTTIAEFA VLRLLSQNPA GRVVYLVARD PLADLVFHEW HQRFGQSSLG CKVVKLTGET
     GTDLKLIAKG QIIITTADKW DVLSRRWKQR KNVQNVQLFI VDELQLIGGE DGPVLEVACS
     RMRYISSQTE QPIRIIALSA SLADARDIAQ WLGCGTNATF NFHPSVRPIP LELHVQGLNI
     THNASRVAAM SKPVYNAITK FSPHKPVIVF VTSRKLARLT AIDVLTYCAA EMQPNRFFHA
     EEDDIKPFLD RMTDKTLKET LSQGVAYMHE GLTASDQRMV EQLFDSGAVQ IAICTRDLCW
     ALNISAHLVI IMDTQFYNGR SHSYDDYPIT DVLQMIGRAN RPLDDDDAKA VLMCQSSKKD
     FYKKFLNEPL PVESHLDHRL HDHFNAEIVT KTIENKQDAV DYLTWTFLYR RLTQNPNYYN
     LQGVTHRHLS DHLSELVEST LSDLEQSKCI GVEDEMDALP LNLGMIAAYY YINYTTIELF
     SLSLNSKTKI RGLLEIISSA AEYEDLIVRH HEDNILRSLA SRLPNKLTGP NGTAPKYNDP
     HIKTNLLLQA HLSRLQLGAE LQGDTEQILG KAIRLVQACV DVLSSNGWLS PAVAAMELAQ
     MVTQAMWSKD SYLKQLPHFT AEIIKRCQEK GIETVFDIME LDDDDRTRLL QMTDQQMSDV
     ARFCNRYPNI ELTFAVLDKD RIHSGSSVDV EVTLEREDDV SGPVIAPFFP QKREEGWWVV
     IGDPKTNSLL SIKRLTLQQK AKVKLNFVAP SPGHHEYTLY YMSDSYLGCD QEYKFSINVG
     DFQSESESES D
//
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