ID   KTU_DROAN               Reviewed;         843 AA.
AC   B3MG50;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=GF11794;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13;
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; CH902619; EDV36745.1; -; Genomic_DNA.
DR   RefSeq; XP_001959923.1; XM_001959887.2.
DR   AlphaFoldDB; B3MG50; -.
DR   SMR; B3MG50; -.
DR   STRING; 7217.FBpp0114986; -.
DR   EnsemblMetazoa; FBtr0116494; FBpp0114986; FBgn0088834.
DR   GeneID; 6494656; -.
DR   KEGG; dan:6494656; -.
DR   eggNOG; KOG4356; Eukaryota.
DR   HOGENOM; CLU_012715_0_0_1; -.
DR   InParanoid; B3MG50; -.
DR   OMA; YSIKHSH; -.
DR   OrthoDB; 943252at2759; -.
DR   PhylomeDB; B3MG50; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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..843
FT                   /note="Protein kintoun"
FT                   /id="PRO_0000365804"
FT   REGION          212..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..574
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..794
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         779
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0E9G3"
SQ   SEQUENCE   843 AA;  94872 MW;  BF72D9CE8D9AD68F CRC64;
     MSAGSRNKHS KFRNDDQLDI SKEEFSRIKE ALGNEEFRKL FFDYVDEIQD PANRKIYEEE
     ITQLEKERGV EVRFIHPQPG FVVKTSLDGE LKCFINIASS PEIEAPHNEV ATNPENGNRG
     LSWYIPMAQT SSRDDADAKN NHCKVFDVVF HPDALHLAKR NSQFRKCLVD TALDAVEREY
     QVSLDRANLK FPKLDYKGIA RPTVIRKLAE NPTAEQLEPH PLQNIYPTAP PTSNPEPRVH
     PMKTKAAPVP EFTIPRYSIK HSHDVDLSEY TDELDAKLHV TVPRNLVVEI ELPLLRSTAE
     CQLDVTSKSV YLLSEKPGAK YRLKMDLPFT VDDKAGSARF DTDLRRLSIT LPVVRSSVPQ
     QRDMHDTLRH FSREDSGVEL HSNSESPVEE EEADADLSDS KADTSETVTP TATPVHSAPT
     PFLKKSVHYQ LPAKFDCNVL DNVMAFVLHV ANVQPDSIEQ LREQRSLHIQ FATIGSGYYP
     THYAFYVELP ADEEGGSAIE NVEAEAWDNN VVLKLCLSSQ SKSPIRYMAG LDATDLNEYP
     VHGQYTVKPK RRDAQNKESA PLDVKFDHNK ESLEVTIRPV PSATEEDEVE EQHEESHEEH
     QQHAQNKKPS KKQRKRNKKE RSLSESACED IVQEQHAENP APPAKNFLKL PQRKQRSYSE
     CNDSSVGSGA SQRGILKRFS RYGPRPSMSD SCSSIDDYSS SYSCSVDASG ASLFSQSFGG
     IPEEDRSDAG LSESCKKTVR FNDHITKQVF RLDSSILGQR KKNQKRRDLK LRAQQRRLSE
     GDSVDYEESR GDALKPQGKA SNKGNKLHDS GLDLTGTAAG HGSHSDADAK NAMMFEMDED
     DVM