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Database: UniProt
Entry: A0A091MU50_9PASS
LinkDB: A0A091MU50_9PASS
Original site: A0A091MU50_9PASS 
ID   A0A091MU50_9PASS        Unreviewed;       251 AA.
AC   A0A091MU50;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Dynein axonemal assembly factor 1 {ECO:0000256|ARBA:ARBA00024429, ECO:0000256|RuleBase:RU364076};
DE   Flags: Fragment;
GN   ORFNames=N310_08390 {ECO:0000313|EMBL:KFP80099.1};
OS   Acanthisitta chloris (rifleman).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC   Acanthisitta.
OX   NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP80099.1, ECO:0000313|Proteomes:UP000053537};
RN   [1] {ECO:0000313|EMBL:KFP80099.1, ECO:0000313|Proteomes:UP000053537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP80099.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cilium-specific protein required for the stability of the
CC       ciliary architecture. Plays a role in cytoplasmic preassembly of dynein
CC       arms. Involved in regulation of microtubule-based cilia and actin-based
CC       brush border microvilli. {ECO:0000256|RuleBase:RU364076}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000256|ARBA:ARBA00004138, ECO:0000256|RuleBase:RU364076}.
CC   -!- SIMILARITY: Belongs to the DNAAF1 family.
CC       {ECO:0000256|ARBA:ARBA00006453, ECO:0000256|RuleBase:RU364076}.
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DR   EMBL; KK836288; KFP80099.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091MU50; -.
DR   Proteomes; UP000053537; Unassembled WGS sequence.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0060271; P:cilium assembly; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR45973:SF19; DYNEIN AXONEMAL ASSEMBLY FACTOR 1; 1.
DR   PANTHER; PTHR45973; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT SDS22-RELATED; 1.
DR   Pfam; PF14580; LRR_9; 1.
DR   SMART; SM00365; LRR_SD22; 4.
DR   SUPFAM; SSF52075; Outer arm dynein light chain 1; 1.
DR   PROSITE; PS51450; LRR; 4.
PE   3: Inferred from homology;
KW   Cell projection {ECO:0000256|RuleBase:RU364076};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069, ECO:0000256|RuleBase:RU364076};
KW   Leucine-rich repeat {ECO:0000256|RuleBase:RU364076};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW   Repeat {ECO:0000256|RuleBase:RU364076}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP80099.1"
FT   NON_TER         251
FT                   /evidence="ECO:0000313|EMBL:KFP80099.1"
SQ   SEQUENCE   251 AA;  29326 MW;  638CD1F0D134D13A CRC64;
     RMTKKTLLDI CKQQDLYWTP YLNDTLYLHY KGFDRLENLE EYTGLKCLWL QCNCFTKIEN
     LEAQTELRCL YLQLNLITKI ENLEPLQKLG SLNISNNCIK TIENLSCLKV LQTLQIAHNK
     LQTVEDIQHL QECPSISVLD LSHNNLRDPN IITVLEAMPN LHVLNLMGNE VIKKIANYRK
     TLIVRLKKLT YLDDRPVFPK DRACAEAWAV GGLEAEKAER EKWETRERKK IQDSFDALAA
     IRQKAEEKKR Q
//
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