ID   KTU_DROMO               Reviewed;         885 AA.
AC   B4KSY3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Protein kintoun {ECO:0000255|HAMAP-Rule:MF_03069};
DE   AltName: Full=Dynein assembly factor 2, axonemal homolog {ECO:0000255|HAMAP-Rule:MF_03069};
DE   AltName: Full=PP1-interacting protein 20 {ECO:0000255|HAMAP-Rule:MF_03069};
GN   Name=Nop17l {ECO:0000255|HAMAP-Rule:MF_03069};
GN   Synonyms=Ppi20 {ECO:0000255|HAMAP-Rule:MF_03069}; ORFNames=GI19552;
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Required for cytoplasmic pre-assembly of axonemal dyneins,
CC       thereby playing a central role in motility in cilia and flagella.
CC       Involved in pre-assembly of dynein arm complexes in the cytoplasm
CC       before intraflagellar transport loads them for the ciliary compartment.
CC       {ECO:0000255|HAMAP-Rule:MF_03069}.
CC   -!- SUBUNIT: Interacts with Pp1alpha-96A, Pp1-87B, Pp1-13C and flw.
CC       {ECO:0000255|HAMAP-Rule:MF_03069}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03069}.
CC   -!- SIMILARITY: Belongs to the PIH1 family. Kintoun subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03069}.
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DR   EMBL; CH933808; EDW08480.1; -; Genomic_DNA.
DR   RefSeq; XP_002004545.2; XM_002004509.2.
DR   AlphaFoldDB; B4KSY3; -.
DR   SMR; B4KSY3; -.
DR   STRING; 7230.FBpp0168769; -.
DR   EnsemblMetazoa; FBtr0427058; FBpp0384702; FBgn0142289.
DR   GeneID; 6578637; -.
DR   KEGG; dmo:Dmoj_GI19552; -.
DR   eggNOG; KOG4356; Eukaryota.
DR   HOGENOM; CLU_012715_0_0_1; -.
DR   InParanoid; B4KSY3; -.
DR   OMA; YSIKHSH; -.
DR   OrthoDB; 943252at2759; -.
DR   PhylomeDB; B4KSY3; -.
DR   Proteomes; UP000009192; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IEA:EnsemblMetazoa.
DR   GO; GO:0070286; P:axonemal dynein complex assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0060285; P:cilium-dependent cell motility; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03069; Kintoun; 1.
DR   InterPro; IPR034727; Kintoun.
DR   InterPro; IPR012981; PIH1_N.
DR   InterPro; IPR041442; PIH1D1/2/3_CS-like.
DR   Pfam; PF08190; PIH1; 1.
DR   Pfam; PF18201; PIH1_CS; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..885
FT                   /note="Protein kintoun"
FT                   /id="PRO_0000365808"
FT   REGION          208..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          819..871
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..834
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        835..853
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        854..871
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         376
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0E9G3"
FT   MOD_RES         784
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0E9G3"
SQ   SEQUENCE   885 AA;  100383 MW;  6ED7C24FC3B42ECD CRC64;
     MSASTRNKHS KIHGNEKLDI SNDEFDRIRD ALKNEEFRKL FFDYVDEIQD PENRKIYEEE
     ITQLEKERGV DVTFIHPQPG FVIKTSIDGE LKCFINIASC KVVERPNNEV SVNSQTGQKG
     LSWSIPLAQI PPRDDLDANN KLCKVYDVVF HPDALHLAKR NAQFRQCLID TALDGVEREY
     HVNLDRANLK FPKLDYKGMA RPSVLRTLSK NPTAEEKEPH PLEHMYPKKP EADAGQSKVL
     PMKTKVTAVP KFAVPKYCIK HSHDVDMAEY TDELDAKLQV TVPRALVVEI ELPLLSSTAD
     CHLDVTEKSV YLLSEKQGAK YKLKVDLPYT VNDKAGNARF DTDHRCLRIT LPVVRSTPRE
     ERNLHDTVRN LSREDSGVEL NSNGESPVED EELVVELSEH NQENDSNAFP PTAVVSPRSF
     LKSNLHYLLP AQFNCNILDN VIVFVLHVTN VQPDSVQTLQ QARSLHLQFA SMGTGYYPTH
     YAFLMQLPDG VQPELRIDQV EVDTGDENVV LRLTMNEHCM LLPSYLAGTD SNDLKEYPVF
     GHQNNNNEKE TEVEVAEMEK CDLVSEKSLQ INMDHNDVEH ALEVTIEPQE NEAPLDSLEL
     LHEHQQELQQ LHHQKKLNKK QRKRNKKQRS LSESACEDLK LAQEHHEQPM DTLKLPHRKQ
     RSYSECNESS LGSSCVQRGI LKRFSRYGPH PSISDSCSSI DDCSSTYSCS VDAAGTGFSQ
     SFGSIPEERG GDEAGLSESC KKTVRFNDHI MKQVFRLDSS ILGQRKKNQK RRDCKLRAQQ
     RRLSEGDSAD YVEVDSTHGS GDQPAHKTAA NAQYFKQHNN NHPHVKDNKK QSLHDSGLDL
     TNGSINNKNN HSNENATKRN EADAKNTMMF EMDDVDEEAQ DAANI