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Database: UniProt
Entry: A0A2A4J8G6_HELVI
LinkDB: A0A2A4J8G6_HELVI
Original site: A0A2A4J8G6_HELVI 
ID   A0A2A4J8G6_HELVI        Unreviewed;      1981 AA.
AC   A0A2A4J8G6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Dynein axonemal assembly factor 1 homolog {ECO:0000256|ARBA:ARBA00024433};
GN   ORFNames=B5V51_5930 {ECO:0000313|EMBL:PCG67824.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG67824.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG67824.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG67824.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG67824.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT   response to modern agricultural practices.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cilium-specific protein required for cilia structures.
CC       {ECO:0000256|ARBA:ARBA00003843}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000256|ARBA:ARBA00004138}.
CC   -!- SIMILARITY: Belongs to the DNAAF1 family.
CC       {ECO:0000256|ARBA:ARBA00006453}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCG67824.1}.
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DR   EMBL; NWSH01002624; PCG67824.1; -; Genomic_DNA.
DR   STRING; 7102.A0A2A4J8G6; -.
DR   Proteomes; UP000218220; Unassembled WGS sequence.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR45973:SF9; CENTROSOMAL PROTEIN 97KDA, ISOFORM B-RELATED; 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|ARBA:ARBA00023273};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218220}.
FT   REGION          171..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1025..1151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1253..1372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1509..1650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1782..1802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1833..1867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          439..466
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          654..684
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        171..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..602
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1065
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1261..1344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1526..1542
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1543..1565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1566..1621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1633..1650
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1841..1867
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1981 AA;  225489 MW;  6DFF4DAFD654550E CRC64;
     MEAPDAQKDN NFIEKKREEL RIFFQDAKLP KEMIEKAIEN ELKPLTVGVN RPYIAASHPG
     EVKTEQEVMA GQPFTKIDDH NKPFTLEQIK DMFKDNPIIA EKARQIQIMA QNDSFNKQIA
     IPLDEINVAD YNDMRKELDA AKGDKEAINK LNYKNMLSLM TSVSDYKKKC ARKSDESVSK
     QSERAESDDD EKEYDAIEKV VSQYTTKSYE TRFQETKDML GKMADNYDEA QSSQDAKLTQ
     PIEIEKNQVL KDSSTQLIKG KRRRSQFDEV KEKYAINEAM NIPLKDNPVT PDLSGKCKTK
     PEKPKQIDED IEVEDLFPKN FESKLKDTEK ALREINLVLN NSLTPSPTSD KVSKNTDSNE
     IIQERKKIDV QEIIPEPANK NESQKFNAEM EQTLQNNLEN IFELSNEGQP ENNEMELKEM
     KSLARNIVEG AENLSTLIRE DITNKLNSMN ELLNDVNEAL ENSRKSNIAY EKIKEEGDML
     RNEIKIDRKM EESQEEEENP PETVSDPQMD SIHDAISKLT SELKHHEHRI NESKARYEKR
     NTECRTFIKE VDEILLKSQD ILHPMKKRAE QEMENQIQVE KKALAENKPE NSESEKFTAD
     TSIDQTEENC VNSRKELWDV DFSYLDEKNK KIAESQKQEA ERSKRINNLL HDIKDNMKDN
     KEVLRLANNM LRREEMRKKS LSDNSGKIRE LPSEEIDTRA QGDHIEAAES QSAGIKEEQL
     IIDGKPDELQ TDEVTKKQAE EKKKREDAEK ERLRQREFQR KVEKELEEMN KTPRMTKEFI
     KNHCRQHKLY CTPYLNDILY LHFKGFSKIE NLEEYTGLKC IFLENNGIQR IEGLDTLSEL
     KCLYLHNNVL RKIENLNGCP KLDTLNIDHN FVGKIENLDV VPDLHTLSIA HNMLSGVEDL
     LHLKFCRNLS VLDLSYNRLE DPLIVDVLAD MIILKVLVLT GNPVVRNIPA YRKTLTLRLK
     ELLNLDNRPV FPRDRACAEA WQRGGVQEEI AERRRWIAKD QEKVMQSVRY LIKMRDEKKA
     IREAREKEEL EKKGLPPKEE QNPREIKADD TTESKEPDLP EEEGPSTLEQ KFGPVEVKVK
     DGVAVDMLSG SEEDDSTSED SSDDSDKKED GPETGNIEWS QIDRGKRLVQ EINAEPPPPL
     PEEYWSGYGN VKPKNERPDI VSDFQAINNL LFNQQPHTGR KGVTKILEDS KNRKDNLTIT
     EIDQDEGKAS AVAEKKPLIE IIDSCDNKDV DKKETDASDK NVIIEDVTKP TNQIIEKANS
     NDSKENTEQG KEFNQETYID AKDKGSIILD HKKKTTAEKP TTNKKIPIKE IPLDKKAVPK
     DSPKKPEEQK ESVQKQDEKS TPQEETKAST SQGQGERRPS AQAEGEGVAL INYMHRMNKE
     DYDDKDLDLE PSAEDLEIFA ELEQEQVERQ ARIDRGEPAV DPMKLYDKKM MDAYYKEKES
     LPAHLVKEKT MFTTYRNDNA FDRVALSQLT AGEKPDEAKV KLTHVPGAVL LEYVDQTPIT
     DVQYEIGEED IESPPSSGET VSIHLLSETS EEESKEEIPF TLIKKSSNRQ PIATNSKQNQ
     KDTTKGTGAS KDKGKPSGKD KTSTEKKTVE KKKGAEKGSQ KQDRKSFGKR RGTHDSDDTA
     SGVPADDVTP SASGDAGASS SYPSGSGTLP SSYDTMINID RQEAKKSIIS TINSYEDKRF
     PSQGVNVSNM VENARIEQNV ASEILDRTLQ YEERELYRQY DVMTSHAGNI DNRTNAIIEH
     ISDQLENEYT LPEVSRILEA HMDVAEQRWR AGEYVPFVPS SPPESVHDGN DDNEATLIPS
     HNTSLSLEDT LTDENVNKMA AIVEDDSGIG NDITLSDTTE VNDRSVDEMK SDNVGESTPR
     NKEAKDGRAR VLQVTTSDIA SGSGDASFSN FKDLDKTIDN DTNEFVDNDG ELDDSKIYES
     VLGDDNFIND VSTDDIFEDC VDDIPAGEEA SKDSDEAQFN RVEQNYSLEM KLALGIEDGK
     M
//
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