LIS11_TALMQ
ID LIS11_TALMQ Reviewed; 459 AA.
AC B6QC56;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Nuclear distribution protein nudF 1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=Lissencephaly-1 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=LIS-1 1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=nudF-1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Synonyms=lis1-1 {ECO:0000255|HAMAP-Rule:MF_03141}; ORFNames=PMAA_066550;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995900; EEA25550.1; -; Genomic_DNA.
DR RefSeq; XP_002146097.1; XM_002146061.1.
DR AlphaFoldDB; B6QC56; -.
DR SMR; B6QC56; -.
DR STRING; 441960.B6QC56; -.
DR EnsemblFungi; EEA25550; EEA25550; PMAA_066550.
DR GeneID; 7023797; -.
DR KEGG; tmf:PMAA_066550; -.
DR VEuPathDB; FungiDB:PMAA_066550; -.
DR HOGENOM; CLU_000288_57_15_1; -.
DR OrthoDB; 995692at2759; -.
DR PhylomeDB; B6QC56; -.
DR Proteomes; UP000001294; 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; 2.
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..459
FT /note="Nuclear distribution protein nudF 1"
FT /id="PRO_0000405090"
FT DOMAIN 9..41
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 114..155
FT /note="WD 1"
FT REPEAT 157..197
FT /note="WD 2"
FT REPEAT 201..240
FT /note="WD 3"
FT REPEAT 243..282
FT /note="WD 4"
FT REPEAT 288..349
FT /note="WD 5"
FT REPEAT 351..390
FT /note="WD 6"
FT REPEAT 395..440
FT /note="WD 7"
FT REPEAT 442..459
FT /note="WD 8"
FT COILED 61..88
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 459 AA; 50783 MW; 9CA0C139F887643A CRC64;
MSRLLTIRQA EELHKSIIAY LSANNLSNAA SALRGELGLS EEVFDTGTMV KYETLLEKKW
TSIVRLQKKI MDLEARCGAL QTELNNATPT SLSKRNQDPA SWLPKVPARY SLESHRNTIN
CLAFHPKFSS IASGSDDCMI KIWDWELGEL ETTLKGHTRA VLDVDYGNTQ SGVLLASCSS
DLSIKIWNPL EDYKNIRTLL GHEHSVSAVR FIPGRNLLTS ASRDKDLRIW DVTTGFCVKT
IQGHSGWVRD VCPSFDGNYL FSAGDDVTAR LWDITNISNP EAKLTMVGHD HVIECCAVAP
QTSYQYLAPM AGLKKEALSK MSAVEFTATG SRDKTIKVWD RRGSCLMTLV GHDNWVRAIV
FHPGGKYLLS ASDDKSIRCW DLSQDGKCVK TLSDAHGRFV TCLRWAPSVV KEVAPSAESA
NGQTDTNDLL KSKDNQPQVQ IRCVVASGGV DQKLNIFAN
