ID   LIS1_ASPOR              Reviewed;         455 AA.
AC   Q2UGU1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   25-MAY-2022, entry version 107.
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}, pac1;
GN   ORFNames=AO090023000713;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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. Cytoplasm, cytoskeleton,
CC       spindle pole {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the
CC       plus ends of microtubules at the hyphal tip and the mitotic spindle
CC       poles. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE59224.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007157; BAE59224.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001821226.2; XM_001821174.2.
DR   AlphaFoldDB; Q2UGU1; -.
DR   SMR; Q2UGU1; -.
DR   STRING; 510516.Q2UGU1; -.
DR   VEuPathDB; FungiDB:AO090023000713; -.
DR   Proteomes; UP000006564; Chromosome 3.
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; 3.
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..455
FT                   /note="Nuclear distribution protein nudF"
FT                   /id="PRO_0000240422"
FT   DOMAIN          9..41
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT   REPEAT          113..154
FT                   /note="WD 1"
FT   REPEAT          156..196
FT                   /note="WD 2"
FT   REPEAT          200..239
FT                   /note="WD 3"
FT   REPEAT          242..281
FT                   /note="WD 4"
FT   REPEAT          287..347
FT                   /note="WD 5"
FT   REPEAT          349..388
FT                   /note="WD 6"
FT   REPEAT          392..438
FT                   /note="WD 7"
FT   REPEAT          440..455
FT                   /note="WD 8"
FT   REGION          408..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          61..88
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ   SEQUENCE   455 AA;  50557 MW;  FA338E21ECDD82C5 CRC64;
     MPPLLTNRQA EELHKSMIAY LVASDLPDTA AALRREVNLS EDVFDPTTAK RYEGMLEKKW
     TSIARLQKKI MDLESRNATL QSELDNSTPA SRLKRNQDPA SWLPSTVRYS LESHRDKVNC
     VAFHPTFSSI ASGSDDCTIK IWDWELGELE RTLKGHTRAV RDVDYGGPRD NVLLASCSSD
     LSIKLWKPTD NYKNIRTLQG HDHIVSAVRF IPSRNLLVSA SRDNDMRIWD VTTGYCVKTI
     NGHTDWVRDV SISFDGRFLF STGQDMTARL WDISTVSNIE HKRTMLGHEN FIECCAFAPP
     TSYQFLAPLA GLGKRPSSTN GADFMATGSR DNTIKIWDSR GTCLMTLVGH DSWVQALVFH
     PGGKYLLSVS DDKTLRCWDL NQQGKCVKTL DAHESFVTSL RWAPGVAKNV PGGDGAAEGE
     GNDKNGAGSE NPANIQMRCV VATGGWDQKL KIFAG