ID A0A1J7JDY3_9PEZI Unreviewed; 469 AA. AC A0A1J7JDY3; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 31-JUL-2019, entry version 16. 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; OC Sordariomycetes; Sordariomycetidae; Coniochaetales; Coniochaetaceae; OC 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 RT biomass hydrolysates."; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Positively regulates the activity of the minus-end CC directed microtubule motor protein dynein. May enhance dynein- CC mediated microtubule sliding by targeting dynein to the CC microtubule plus end. Required for nuclear migration during CC vegetative growth as well as development. Required for retrograde CC early endosome (EE) transport from the hyphal tip. Required for CC localization of dynein to the mitotic spindle poles. Recruits CC additional proteins to the dynein complex at SPBs. CC {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 CC of 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 CC to 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, ECO:0000256|SAAS:SAAS00869406}. 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 EnsemblFungi; OIW27912; OIW27912; CONLIGDRAFT_655588. DR OrthoDB; 995692at2759; -. DR Proteomes; UP000182658; 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; IPR017986; WD40_repeat_dom. 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; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_03141, KW ECO:0000256|SAAS:SAAS00869426}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_03141, KW ECO:0000256|SAAS:SAAS00869415}; KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_03141, KW ECO:0000256|SAAS:SAAS00869405}; KW Complete proteome {ECO:0000313|Proteomes:UP000182658}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03141, KW ECO:0000256|SAAS:SAAS00869399}; KW Cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03141, KW ECO:0000256|SAAS:SAAS00869427}; KW Microtubule {ECO:0000256|HAMAP-Rule:MF_03141, KW ECO:0000256|SAAS:SAAS00869425}; KW Mitosis {ECO:0000256|HAMAP-Rule:MF_03141, KW ECO:0000256|SAAS:SAAS00869394}; KW Reference proteome {ECO:0000313|Proteomes:UP000182658}; KW Repeat {ECO:0000256|SAAS:SAAS00998418}; KW Transport {ECO:0000256|HAMAP-Rule:MF_03141, KW ECO:0000256|SAAS:SAAS00869424}; KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221, KW ECO:0000256|SAAS:SAAS00998547}. FT DOMAIN 9 41 LisH. {ECO:0000259|PROSITE:PS50896}. FT DOMAIN 112 396 WD_REPEATS_REGION. {ECO:0000259|PROSITE: FT PS50294}. FT REPEAT 112 153 WD. {ECO:0000256|PROSITE-ProRule: FT PRU00221}. FT REPEAT 154 188 WD. {ECO:0000256|PROSITE-ProRule: FT PRU00221}. FT REPEAT 199 248 WD. {ECO:0000256|PROSITE-ProRule: FT PRU00221}. FT REPEAT 249 283 WD. {ECO:0000256|PROSITE-ProRule: FT PRU00221}. FT REPEAT 355 389 WD. {ECO:0000256|PROSITE-ProRule: FT PRU00221}. FT REGION 81 100 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 420 441 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 420 435 Polar. {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 //