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
//