ID   KTU_DROVI               Reviewed;         906 AA.
AC   B4LMK1;
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=GJ21124;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
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; CH940648; EDW59988.1; -; Genomic_DNA.
DR   RefSeq; XP_002048795.1; XM_002048759.2.
DR   RefSeq; XP_015029557.1; XM_015174071.1.
DR   AlphaFoldDB; B4LMK1; -.
DR   SMR; B4LMK1; -.
DR   STRING; 7244.FBpp0235541; -.
DR   PRIDE; B4LMK1; -.
DR   EnsemblMetazoa; FBtr0237049; FBpp0235541; FBgn0208257.
DR   EnsemblMetazoa; FBtr0437938; FBpp0394730; FBgn0208257.
DR   GeneID; 6625677; -.
DR   KEGG; dvi:6625677; -.
DR   eggNOG; KOG4356; Eukaryota.
DR   HOGENOM; CLU_012715_0_0_1; -.
DR   InParanoid; B4LMK1; -.
DR   OMA; YSIKHSH; -.
DR   OrthoDB; 943252at2759; -.
DR   PhylomeDB; B4LMK1; -.
DR   Proteomes; UP000008792; 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..906
FT                   /note="Protein kintoun"
FT                   /id="PRO_0000365812"
FT   REGION          614..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..822
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..849
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..892
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         812
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0E9G3"
SQ   SEQUENCE   906 AA;  102871 MW;  A604C28C4C1851F6 CRC64;
     MSASTRNKHS KIHGNEKLDI TTDEFDRIRQ ALSNEEFRKL FFDYVDEIQD PENRKLYEKE
     ITQLEKERGV DVTFIHPQPG FVVKTSIDGE LKCFINIASS TVVERPNNEV SVNSQTGQKG
     LSWSIPMAQT PPRDDLDANN KQCKVFDVVF HPDALHLGKR NAQFRQCLID TALDGVEREY
     KVNLDRANLK FPKLDYKGLA RPTVLRKLSK DATAEELEPH PLEHMYPKKP AANADQPKVL
     PMKTKVTPAP TFAVPKYSIK HSHDVDLAEY TDELDAKLQV TMPRALVVEI ELPLLSSTAD
     CQLDVTEKSV YLLSERQGAK YRLKLDLPYT VNDKAGNARF DTEHRRLCIT LPVVRSTARE
     QRNLHDTVRV LTREDSGVEL NSNGESPVED EAEAEVEADA IVELQSHDQR DVSDAFPPTA
     VVSPRSFLKD NLHYKLPASF DCNILDNVIA FVLHVPNVQP DSVQTLQQAR SLHLQFASMG
     SGYYPTHYAF LVQLPDGLEP QLQIDHIDVD AADENVVLRL YMNENCMLLP SYLAGPDSTD
     LKEYPVFGHF NNNNNNEKEY EGCSLASEKS LYINMDHNDL EHALEVSIMP QESTDPLDSI
     ELLQQQQQQL QQLQQQKKLN KKQRKRNKKQ RSLSESACEE LKAAQEELQL QHEKQQQQQQ
     LPSTPKDASP ERLQNVSQPV DTLKLPQRKQ RSYSECNESS SCVQRGILKR FSRYGPRPSI
     SDSCSSIDDC SSTYSCSMDA PGMGFSQSFG GIPEERSGEG DVGLSESCKK TVRFNDHIMK
     QVFRLDSSIL GQRKKNQKRR DCKLRAQQRR LSEGDSADYE EVEHGNGQQP PAHKTAANAQ
     YFKQPNNNNG HDQDKNKKLS MHDSGLDLTN NNNHNNEEET KRNEADAKNA MMFEMDDDDE
     DEDEDM