ID A0A1J7JDY3_9PEZI Unreviewed; 469 AA. AC A0A1J7JDY3; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 02-OCT-2024, entry version 31. DE RecName: Full=Nuclear distribution protein PAC1 {ECO:0000256|HAMAP-Rule:MF_03141}; DE AltName: Full=Lissencephaly-1 homolog {ECO:0000256|HAMAP-Rule:MF_03141}; DE Short=LIS-1 {ECO:0000256|HAMAP-Rule:MF_03141}; DE AltName: Full=nudF homolog {ECO:0000256|HAMAP-Rule:MF_03141}; GN Name=PAC1 {ECO:0000256|HAMAP-Rule:MF_03141}; GN Synonyms=LIS1 {ECO:0000256|HAMAP-Rule:MF_03141}; GN ORFNames=CONLIGDRAFT_655588 {ECO:0000313|EMBL:OIW27912.1}; OS Coniochaeta ligniaria NRRL 30616. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta. OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW27912.1, ECO:0000313|Proteomes:UP000182658}; RN [1] {ECO:0000313|EMBL:OIW27912.1, ECO:0000313|Proteomes:UP000182658} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW27912.1, RC ECO:0000313|Proteomes:UP000182658}; RG DOE Joint Genome Institute; RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V., RA Van Elsas J.D., Nichols N.N.; RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass RT hydrolysates."; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_03141}. CC -!- SUBUNIT: Self-associates. Interacts with NDL1 and dynein. CC {ECO:0000256|HAMAP-Rule:MF_03141}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|HAMAP- CC Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle pole CC {ECO:0000256|HAMAP-Rule:MF_03141}. Note=Localizes to the plus ends of CC microtubules at the hyphal tip and the mitotic spindle poles. CC {ECO:0000256|HAMAP-Rule:MF_03141}. CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required to CC activate dynein. {ECO:0000256|HAMAP-Rule:MF_03141}. CC -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family. CC {ECO:0000256|HAMAP-Rule:MF_03141}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KV875099; OIW27912.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1J7JDY3; -. DR STRING; 1408157.A0A1J7JDY3; -. DR InParanoid; A0A1J7JDY3; -. DR OrthoDB; 1798470at2759; -. DR Proteomes; UP000182658; Unassembled WGS sequence. DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:TreeGrafter. DR GO; GO:0000776; C:kinetochore; IEA:TreeGrafter. DR GO; GO:0005875; C:microtubule associated complex; IEA:UniProtKB-UniRule. DR GO; GO:0005635; C:nuclear envelope; IEA:TreeGrafter. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. DR GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule. DR GO; GO:0051010; F:microtubule plus-end binding; IEA:TreeGrafter. 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:0031023; P:microtubule organizing center organization; IEA:TreeGrafter. DR GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule. DR GO; GO:0007097; P:nuclear migration; IEA:TreeGrafter. DR GO; GO:0047496; P:vesicle transport along microtubule; IEA:TreeGrafter. DR CDD; cd00200; WD40; 1. DR Gene3D; 1.20.960.30; -; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR InterPro; IPR050349; WD_LIS1/nudF_dynein_reg. DR PANTHER; PTHR44129:SF1; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT BETA; 1. DR PANTHER; PTHR44129; WD REPEAT-CONTAINING PROTEIN POP1; 1. DR Pfam; PF00400; WD40; 6. DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF109925; Lissencephaly-1 protein (Lis-1, PAF-AH alpha) N-terminal domain; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50896; LISH; 1. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 5. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP- KW Rule:MF_03141}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP- KW Rule:MF_03141}; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP- KW Rule:MF_03141}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03141}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212, ECO:0000256|HAMAP- KW Rule:MF_03141}; KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|HAMAP- KW Rule:MF_03141}; KW Mitosis {ECO:0000256|ARBA:ARBA00022776, ECO:0000256|HAMAP-Rule:MF_03141}; KW Reference proteome {ECO:0000313|Proteomes:UP000182658}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_03141}; KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE- KW ProRule:PRU00221}. FT REPEAT 112..153 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 154..188 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 199..248 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 249..283 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REPEAT 355..389 FT /note="WD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221" FT REGION 81..100 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 420..441 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 420..435 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 469 AA; 50715 MW; 67F722BB05BFBD4C CRC64; MTQILTTRQA EELHKSIIAY LSANNLSNAA AALRADVGLG EDVFDTNTAK KYEGLLEKKW TSVVRLQKKI MDLESRNATL QSEIDNATPT SLSKRNQDPV SWLPRSPARH NLQSHRSAIT SVAFHPIFSS LASGSEDCTI KIWDWELGEL ERTIKGHTKA VLDLDFGGPR GGTLLASCSS DLTIKLWDPA DEYKNIRTLP GHDHSVSAVR FIPSGAAGAP ASGNLLVSAS RDKTLRIWDV STGYCVKTLR GHADWVRDVC PSLDGRFLLS AGVDQSARLW DISLSTPETK VTLFGHEHTI ECCVIAPPAA YQYLAPLAGL KKPPPASSPA EFMATGSRDK LIKLWDGRGN CIKTLVGHDN WVRGLVFHPG GKYLLSVADD YSLRCWDLSQ EGKCVKTLGD AHGHFVSCIR WAPSIIKNDP AANGNGTSGQ NGGEANGTPK KGAIAAPEVQ IRCVLATGSV DTSVRVFAN //