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SPNE_CULQU
ID   SPNE_CULQU              Reviewed;        1396 AA.
AC   B0XDC4;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Probable ATP-dependent RNA helicase spindle-E;
DE            EC=3.6.4.13;
GN   Name=spn-E; ORFNames=CPIJ017541;
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB;
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA   Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; DS232752; EDS45402.1; -; Genomic_DNA.
DR   RefSeq; XP_001867646.1; XM_001867611.1.
DR   AlphaFoldDB; B0XDC4; -.
DR   SMR; B0XDC4; -.
DR   STRING; 7176.CPIJ017541-PA; -.
DR   EnsemblMetazoa; XM_038251917.1; XP_038107845.1; LOC6051164.
DR   GeneID; 6051164; -.
DR   KEGG; cqu:CpipJ_CPIJ017541; -.
DR   VEuPathDB; VectorBase:CPIJ017541; -.
DR   VEuPathDB; VectorBase:CQUJHB009375; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   HOGENOM; CLU_002601_1_0_1; -.
DR   InParanoid; B0XDC4; -.
DR   OMA; DPCRTVY; -.
DR   OrthoDB; 278674at2759; -.
DR   PhylomeDB; B0XDC4; -.
DR   Proteomes; UP000002320; Partially assembled WGS sequence.
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:0003676; F:nucleic acid binding; IEA:InterPro.
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: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   InterPro; IPR013087; Znf_C2H2_type.
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.
DR   PROSITE; PS50304; TUDOR; 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..1396
FT                   /note="Probable ATP-dependent RNA helicase spindle-E"
FT                   /id="PRO_0000391912"
FT   DOMAIN          68..234
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          292..468
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          885..950
FT                   /note="Tudor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           180..183
FT                   /note="DEAH box"
FT   BINDING         81..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1396 AA;  158391 MW;  2E06F4195481C69C CRC64;
     MDEAAGPSTS RTSNLEDVDD EGASLAEEDE EHTKALKAKE MMAPLFQRYN FTMKKNDLPI
     NWNKPEILDK IRSNAVVVLQ GATGCGKTTQ VPQYLLEEAF ERKEYCNIIV TQPRKIAAIS
     IARRVAQERK CDLGTLVGYK VGLKEQHNED TRLLYVTTGV LLQSLINSKT MATYTHVILD
     EVHEREVDMD FLLIVVRRLL STNSKKTKVI LMSATIDAKG FSEYFKIPKK SGYLSAPVIS
     VERPRLHVVQ EFYFDDLEKL KVDFQIDYEA PGISEQMYNI AAKLVVVCDH LKGQEFGDSL
     EYKPSIIIFL PGINEIEKME GALEKLIASI QNAAQRPNLL IMKLHSTLPA DDQTAVFRKP
     GPNQRKVILS TNIAESSITV PDIKFVIDFC LQRILVTDTL TNFSTLRTEW ASKSNCIQRA
     GRAGRLMSGR VYRLVDRRFF ENNMDVSTSP EILRCPLETV VLKAKLLEMG TPPSILALAM
     APPNLDDIRN TILLLKEVGA MLRTVKGNYD QLDGDLTYLG RIMSKLPLDI RISKLIMLGY
     IFSVMEEAVT IGAGMNVKNI FLNQNSVKTY SQKMYWADGS GSDAIAILNA YTAWKSRQEQ
     AGDTADMYNW ARRMSLDRKS LIDMAELIHE VKDRLNRSGL KPVSGPNRVV WNAREKTVIL
     KVILAGAFYP NYFIPMSVGG KELMERQSFT ELGGRDPCNT VFFTGFDHER YIGPLYTVQI
     KKILSEGDYS KHQAMKVMYD RTTNRIFVTF LGTTDERDQR GSFMPGKVHA DVYRAIKLRK
     LGARNRITEI RTMRQRDAID YATSAGLGHW EDANGWVPRR KIVRNAHLSV LPPIFREKVV
     CQVTHVVHPN KFFLRPEDNR NKDIFREIHT QLNARQLHPF PADANFAMGQ MVAAPVQENQ
     ETYARAVLRS YRNVRTTGSV SWTVFFIDYG HTAAMEETAF RQLDDSLGQL KDIPPRAFEA
     TLTEIQPSAI ISPQGSWTTE SIHRFKELVL GKIFVAKVYS VVGVVASVEL SRDEIRMNSE
     LIRLKYAQYA EESYISKLDH DHRERKQREI MMDENLRNEV YRSAELTQNT YEDDELEDVN
     PPEDKLRCKV VLSGPHSPLE TSASATIRSS VMKPVSIESD SVNSILLDSN PQDTHEKLLV
     AGGVNEQGNR LVLRQTSVMP NIPGFGAIMS LIFCPTAQLK KDKDETRVVT VLSGLGYDPS
     TGEALYPEHD MALTLDVVLN DDDITNINAL RYTMDSILHT GEGQTDPKFG DASIQKLKLQ
     VKQYIIKILE HERRFLDLRH APNDYNWRCD LNLTAGSSSS KKMKGDFNIY DKKAIFPLLE
     PLNLLPVSAS QLTFLKKHCH ELHKLAHTDV QLPRHGITCQ LCNNVLETLP QLRIHLYSKL
     HRDRESQIKY RSPQMY
 
 
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