SPNE_ANOGA
ID SPNE_ANOGA Reviewed; 1463 AA.
AC Q7QCW2;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 5.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable ATP-dependent RNA helicase spindle-E;
DE EC=3.6.4.13;
GN Name=spn-E; ORFNames=AGAP002829;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: Probable ATP-binding RNA helicase which plays a central role
CC during gametogenesis by repressing transposable elements and preventing
CC their mobilization, which is essential for the germline integrity. Acts
CC via the piRNA metabolic process, which mediates the repression of
CC transposable elements during meiosis by forming complexes composed of
CC piRNAs and Piwi proteins and govern the methylation and subsequent
CC repression of transposons (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Component of the
CC nuage, also named P granule, a germ-cell-specific organelle required to
CC repress transposon during meiosis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; AAAB01008859; EAA07697.5; -; Genomic_DNA.
DR RefSeq; XP_312084.5; XM_312084.5.
DR AlphaFoldDB; Q7QCW2; -.
DR SMR; Q7QCW2; -.
DR STRING; 7165.AGAP002829-PA; -.
DR PaxDb; Q7QCW2; -.
DR PRIDE; Q7QCW2; -.
DR GeneID; 1273132; -.
DR KEGG; aga:AgaP_AGAP002829; -.
DR CTD; 1273132; -.
DR VEuPathDB; VectorBase:AGAP002829; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_002601_1_0_1; -.
DR InParanoid; Q7QCW2; -.
DR OMA; DPCRTVY; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; Q7QCW2; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0010529; P:negative regulation of transposition; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.90; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00567; TUDOR; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Developmental protein; Differentiation; Helicase;
KW Hydrolase; Meiosis; Nucleotide-binding; Reference proteome;
KW RNA-mediated gene silencing; Spermatogenesis.
FT CHAIN 1..1463
FT /note="Probable ATP-dependent RNA helicase spindle-E"
FT /id="PRO_0000391911"
FT DOMAIN 131..296
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 348..531
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 951..1016
FT /note="Tudor"
FT MOTIF 243..246
FT /note="DEAH box"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1463 AA; 167374 MW; 4F115C15981FF2D0 CRC64;
MEDDDVADFF DFSKPFKRTV VSGGYINGAV KPQKLNIQTL PERAHQGTEY AEKFCREEEA
RLMEGWVDET LNKSTASRLE QVDDMSSVME EDTQHLQRVR AKELMEPLFS RYNFTVTPNR
LTIHQSKQDI LKAIRENPVV VLQGMTGCGK TTQVPQYLLE DAYNRKEWCN IVVTQPRKIA
ASSIARRVAE ERNCALGSLV GFKVGLKEMV SEDTRLTYVT TGVLLNKLIT SKSISSYTHI
ILDEVHEREV DMDFLLIIVR RLLATMRNTK IILMSATIES SEFAQYFKIP GPNSLFAPQL
AVSNVTQHDV SVYYLEDLEK LRVDFTIKYE QPDVHEKMYF LAAKVAVVCD RFIDEFESAS
TIDYKPSIIM FLPGINEIER MAEVLRNFLG DSNVNSQEQT KFTILKLHSM LPSEEQALVF
TKPSPGYRKV ILSTNIAESS ITIPDVKFVI DFCLHRVLVA DTLNNFTTLR TQWASRNNCI
QRAGRCGRVM NGRVYRLVNK HFFEHGMAQS IEPEMVRCPL SNVVLKTKLL DMGPPHTILA
LAMSPPNLSD VSNTVLQLKE LGALLRTAKG VYDLQDGDIT YLGNIMSTLP LDIHLAKLVV
LGYVFSVLEE AIVIAAGMNV KNIFCQLRTI EALRVKRHFA NGSASDGIAI LNAYNWWRSI
REQGTGGDTT DWCNRYMLDR KSLIEMAELV QEITMRLKTA NIRVVSGANN ARWTDRERTV
VLKVVMAGAF YPNYFIPTCV TDRELSDKMV YTEIGGRDPF STVFFCGFDH SNYIGPLYRN
EIRALLTERK PTSEKHQVKV EFERSTNKIF VQFQYPPDQQ SGKSLYEERN SADRVHPGVY
EAIKLRQLRH NQSELLVMHH NDAVAYATEH RLGVWRNHEW HPRSVEIPNA HLSVEPPIHW
NRVTATVTHV EHPNKFYLRP HDEKNDNIYH DIMEKLNGCD AVLRAFPEGY AFKQRDIVAA
PLPNMVTGKM ARAKLLQQCL VRGVEHWTVF FMDFGLTAGV SVKSFRQLRG TPLDMFTKFP
DRVFLASLAE VQPSAVRSPK DVWMEETIKH FRQLVHGQQF DVEVYSVVNR VTMVVLRHNP
DDPIDLTVNR ALINSHHAQL SEESYMSKMN HEKRKRVQFE MELDPMYKTQ ILNDISEQQR
FLEDDDVDSL ELPRDLLKVR LMLRGPYSPL EVKCSSTVFS GYRKPVIIEK ESLNSVLLDT
NPQNTHEKLL VAGCVNETSN SRLIARMTTM MPNIPGLPAL MTLIFAPTCL VKKDPDETRV
VGLLAGLGTD PRTGESMYPE HDMSLAVDIA IDDDDIADIN ALRYTMDSIL HGGHNEQTPM
FGEYSIESLM VKVKDYLIKI LQRDRPIQDN RSMAHDFSWV KENPSTSTSS QKRLRSTAID
IYTKAIFPLY HNLNLRPMTA DRMEFLRQHC KDLHLLTQSR VPLPKGGITC RLCNVTLESD
HTLRIHFYSK LHCDLELKIN YRR
