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Database: UniProt
Entry: A0A182QK28_9DIPT
LinkDB: A0A182QK28_9DIPT
Original site: A0A182QK28_9DIPT 
ID   A0A182QK28_9DIPT        Unreviewed;       591 AA.
AC   A0A182QK28;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=26S proteasome regulatory subunit 8 {ECO:0000256|ARBA:ARBA00040909};
DE   AltName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000256|ARBA:ARBA00016266};
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:AFAF011848-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:AFAF011848-PA}
RP   IDENTIFICATION.
RC   STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF011848-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. CPSF5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009710}.
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DR   EMBL; AXCN02000542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182QK28; -.
DR   STRING; 69004.A0A182QK28; -.
DR   EnsemblMetazoa; AFAF011848-RA; AFAF011848-PA; AFAF011848.
DR   VEuPathDB; VectorBase:AFAF011848; -.
DR   OrthoDB; 360215at2759; -.
DR   Proteomes; UP000075886; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005849; C:mRNA cleavage factor complex; IEA:InterPro.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR   GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR   CDD; cd19502; RecA-like_PAN_like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR016706; Cleav_polyA_spec_factor_su5.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR   PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR23073:SF166; 26S PROTEASOME REGULATORY SUBUNIT 8; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF13869; NUDIX_2; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          440..565
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   COILED          25..66
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   591 AA;  67207 MW;  5F78FE4BA5FBBAFE CRC64;
     MRDISSMDVD PPRGEGFRSY YVQKIEELQL IVAEKNQNLR RLQAQRNELN AKVRMLREEL
     QLLQEQGSYV GEVVKPMDKK KVLVKVHPEG KFVVDIDKNI DINDVTPNCR VALRNESYTL
     HKILPNKVDP LVSLMMVEKV PDSTYEMVGG LDKQIKEIKE VIELPVKHPE LFDALGIAQP
     KGVLLYGPPG TGKTLLARAV AHHTECTFIR VSGSELVQKF IGEGSRMVRE LFVMAREHAP
     SIIFMDEIDS IGSSRIESGS GGDSEVQRTM LELLNQLDGF EATKNIKVIM ATNRIDILDP
     ALLRPGRIDR KIEFPPPNEE ARLDILKIHS RKMNLTRGIN LRKIAELMPG ASGAEVKGVC
     TEAGMYALRE RRVHVTQEDF EMAVAKVMQK DSEKNMSIKK LWNYPLTNYT FGTKEPLFEK
     DPSVPARFQR MRDEFDKIGM RRSVEGVLLV HEHGLPHVLL LQLGTTFFKL PGGELGAGED
     EVEGLKRLLT ETLGRQDGVK QDWIVEDTIG NWWRPNFEPP QYPYIPPHIT KPKEHKRLFL
     VQLHEKALFA VPKNYKLVAA PLFELYDNSQ GYGPIISSLP QALCRFNFIY M
//
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