ID   LIS1_NEOFI              Reviewed;         441 AA.
AC   A1DP19;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Nuclear distribution protein nudF {ECO:0000255|HAMAP-Rule:MF_03141};
DE   AltName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
DE            Short=LIS-1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN   Name=nudF {ECO:0000255|HAMAP-Rule:MF_03141};
GN   Synonyms=lis1 {ECO:0000255|HAMAP-Rule:MF_03141}; ORFNames=NFIA_058910;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Positively regulates the activity of the minus-end directed
CC       microtubule motor protein dynein. May enhance dynein-mediated
CC       microtubule sliding by targeting dynein to the microtubule plus end.
CC       Required for nuclear migration during vegetative growth as well as
CC       development. Required for retrograde early endosome (EE) transport from
CC       the hyphal tip. Required for localization of dynein to the mitotic
CC       spindle poles. Recruits additional proteins to the dynein complex at
CC       SPBs. {ECO:0000255|HAMAP-Rule:MF_03141}.
CC   -!- SUBUNIT: Self-associates. Interacts with nudE and dynein.
CC       {ECO:0000255|HAMAP-Rule:MF_03141}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC       Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus ends of
CC       microtubules at the hyphal tip and the mitotic spindle poles.
CC       {ECO:0000255|HAMAP-Rule:MF_03141}.
CC   -!- DOMAIN: Dimerization mediated by the LisH domain may be required to
CC       activate dynein. {ECO:0000255|HAMAP-Rule:MF_03141}.
CC   -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
CC       {ECO:0000255|HAMAP-Rule:MF_03141}.
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DR   EMBL; DS027698; EAW16540.1; -; Genomic_DNA.
DR   RefSeq; XP_001258437.1; XM_001258436.1.
DR   AlphaFoldDB; A1DP19; -.
DR   SMR; A1DP19; -.
DR   STRING; 36630.CADNFIAP00004828; -.
DR   EnsemblFungi; EAW16540; EAW16540; NFIA_058910.
DR   GeneID; 4584953; -.
DR   KEGG; nfi:NFIA_058910; -.
DR   VEuPathDB; FungiDB:NFIA_058910; -.
DR   eggNOG; KOG0295; Eukaryota.
DR   HOGENOM; CLU_000288_57_15_1; -.
DR   OMA; TQECKCV; -.
DR   OrthoDB; 995692at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:UniProtKB-UniRule.
DR   GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.130.10.10; -; 1.
DR   HAMAP; MF_03141; lis1; 1.
DR   InterPro; IPR017252; Dynein_regulator_LIS1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR037190; LIS1_N.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 6.
DR   PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF109925; SSF109925; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Mitosis; Reference proteome; Repeat; Transport; WD repeat.
FT   CHAIN           1..441
FT                   /note="Nuclear distribution protein nudF"
FT                   /id="PRO_0000405085"
FT   DOMAIN          9..41
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT   REPEAT          87..128
FT                   /note="WD 1"
FT   REPEAT          130..170
FT                   /note="WD 2"
FT   REPEAT          174..221
FT                   /note="WD 3"
FT   REPEAT          224..263
FT                   /note="WD 4"
FT   REPEAT          266..326
FT                   /note="WD 5"
FT   REPEAT          328..367
FT                   /note="WD 6"
FT   REPEAT          372..402
FT                   /note="WD 7"
FT   REPEAT          403..440
FT                   /note="WD 8"
FT   REGION          390..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  47894 MW;  8B1E1E88DC757D19 CRC64;
     MSQLLTARQA EELHKSIIAY LASVNLTESS AALRAELGDS VSIDDATLKK YEGLLEKKWT
     SVVRLQKKNQ DPTSWLPRSP ARHILEGHRE PVTCVAFHPV FSSLASGSDD TTIKIWDWEL
     GELERTVKGH TKAVLDVDYG GPRGGTLLAS CSSDLTIKLW DPSDNYKNIR TLPGHDHSVS
     SVRFIPSGAA GSPMSGNLLV SASRDKTLRI WDVTTGYCVK TLSGHVDWVR AVAPSLDGRF
     LFAAGDDRIP RLWDLSSAET KSTFLGHEHV IECVAIAPAA SYPHLAVLSG LKKPPPVSSS
     AEFFATGSRD KTIRLWDSRG NLIKTLVGHD NWVRALAFHP GGKHLLSVAD DKTIRCWDLT
     QECKCVRVIS DAHGHFVTCL RWAPPLIKDG GANGESETNG APAATATTNG VRPDPNAANK
     ISIRCVIATG SVDRKVRIFA T