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Database: UniProt
Entry: A0A078A1Q8_STYLE
LinkDB: A0A078A1Q8_STYLE
Original site: A0A078A1Q8_STYLE 
ID   A0A078A1Q8_STYLE        Unreviewed;       821 AA.
AC   A0A078A1Q8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Protein kintoun {ECO:0000256|HAMAP-Rule:MF_03069};
DE   AltName: Full=Dynein assembly factor 2, axonemal homolog {ECO:0000256|HAMAP-Rule:MF_03069};
GN   Name=Contig1422.g1558 {ECO:0000313|EMBL:CDW74714.1};
GN   ORFNames=STYLEM_3696 {ECO:0000313|EMBL:CDW74714.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW74714.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW74714.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW74714.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_03069}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03069}.
CC   -!- SIMILARITY: Belongs to the PIH1 family. Kintoun subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03069}.
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DR   EMBL; CCKQ01003584; CDW74714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078A1Q8; -.
DR   EnsemblProtists; CDW74714; CDW74714; STYLEM_3696.
DR   InParanoid; A0A078A1Q8; -.
DR   OMA; FINICAS; -.
DR   OrthoDB; 240826at2759; -.
DR   Proteomes; UP000039865; 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   CDD; cd06463; p23_like; 1.
DR   Gene3D; 2.60.40.790; -; 2.
DR   HAMAP; MF_03069; Kintoun; 1.
DR   InterPro; IPR007052; CS_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR034727; Kintoun.
DR   InterPro; IPR012981; PIH1_N.
DR   InterPro; IPR041442; PIH1D1/2/3_CS-like.
DR   PANTHER; PTHR22997:SF0; PIH1 DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR22997; UNCHARACTERIZED; 1.
DR   Pfam; PF04969; CS; 1.
DR   Pfam; PF08190; PIH1; 1.
DR   Pfam; PF18201; PIH1_CS; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   PROSITE; PS51203; CS; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03069};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865}.
FT   DOMAIN          623..723
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..776
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..797
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   821 AA;  95296 MW;  ADCBDF8CADBF6661 CRC64;
     MNPYASDDFS RMKVKSEPKP PKPEENPDMI DHPFFEGKKL EMSKKELKAF TMAMEQPEFK
     TLMADYVKEI SDPNNKQEYE TYLRQLEESG DLPVGTKLIE PTGLYCIKTT AKKLVSDTNK
     QYFDQKTFIN VCVHEDVEKP KKEFVQMPDG RQGNSWQLPY RVSKPRHDQD KHGNLCSTFD
     IVFHRDVAGF IIYDDFKRFV SDTAVEGVNR VLAEHKEKCS SDYKIMKHLQ CKGGKPGLLT
     IKVAIENKLL QNADVNKHET KLQKDISNQT DEFKKQQQEQ EALKKGQSAQ LGEIDEEDVE
     EEEPMPKSVV QPKYKIVYSY PVDLQDSWEG FSTNEGFEIQ KPVQKIPKEL TVTINVPHVE
     SMKLALLDIN QTNLIFEYPN LYYLDLNLKY ICDSNQGNAK FDKNKKTLTI RVPVKGLTEE
     SQKVFEENLK KYDEMKQKKD KDIENGKQRE DEEKKEDEDK KHKLDGISEA TSGESNTILP
     NIDVIGGDIL GDQYKKDDDE VDLKKLKEEA LKEDQVKQDD LSKQRENFLK VYKEDQDNQD
     FGEDDGQLKE VRFKNTLGDE DGINSNIKIT GLNDLASKPL IQEIKQNSQG NEKTSQAEQK
     IQENESILPQ VKQQVFDWDK TERIQAKFQF FHQKEFVFIN LNFKGYNKLT DVRFALSENE
     LVLEVKYPSA LWTKDNQVFQ INRLCYTLHK EIDVSQSSVE LLVDFIAIKL KKLDKESSWS
     SLGYEIKDFT IPMRGQMKSN FLKREVPQQE NKSDQKDNGV KADDNENKEN KQDASNMDQK
     DNNPQQSEDE KQAEQIHNEI KKSALQFNFM NLESSVIYKI Y
//
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