ID   A0A2H3EIB4_9HELO        Unreviewed;      1596 AA.
AC   A0A2H3EIB4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   31-JUL-2019, entry version 9.
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=BUE80_DR010925 {ECO:0000313|EMBL:PBP18366.1};
OS   Diplocarpon rosae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Diplocarpon.
OX   NCBI_TaxID=946125 {ECO:0000313|EMBL:PBP18366.1, ECO:0000313|Proteomes:UP000218527};
RN   [1] {ECO:0000313|EMBL:PBP18366.1, ECO:0000313|Proteomes:UP000218527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DortE4 {ECO:0000313|EMBL:PBP18366.1,
RC   ECO:0000313|Proteomes:UP000218527};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PBP18366.1, ECO:0000313|Proteomes:UP000218527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DortE4 {ECO:0000313|EMBL:PBP18366.1,
RC   ECO:0000313|Proteomes:UP000218527};
RA   Klein E., Featherston J., Rees J., Debener T.;
RT   "A draft genome sequence of the rose black spot fungus Diplocarpon
RT   rosae reveals a high degree of genome duplication.";
RL   Submitted (SEP-2017) 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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PBP18366.1}.
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DR   EMBL; MVNX01000150; PBP18366.1; -; Genomic_DNA.
DR   OrthoDB; 995692at2759; -.
DR   Proteomes; UP000218527; 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:0003676; F:nucleic acid binding; IEA:InterPro.
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   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_03141; lis1; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   InterPro; IPR017252; Dynein_regulator_LIS1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR022783; GCFC_dom.
DR   InterPro; IPR037190; LIS1_N.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR022159; STIP/TFIP11_N.
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; PF01965; DJ-1_PfpI; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF07842; GCFC; 1.
DR   Pfam; PF12457; TIP_N; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF109925; SSF109925; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   PROSITE; PS50174; G_PATCH; 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 {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:UP000218527};
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:UP000218527};
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      111    393       WD_REPEATS_REGION. {ECO:0000259|PROSITE:
FT                                PS50294}.
FT   REPEAT      111    152       WD. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00221}.
FT   REPEAT      153    187       WD. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00221}.
FT   REPEAT      198    247       WD. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00221}.
FT   REPEAT      248    289       WD. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00221}.
FT   REPEAT      324    343       WD. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00221}.
FT   REPEAT      352    393       WD. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00221}.
FT   DOMAIN      653    699       G-patch. {ECO:0000259|PROSITE:PS50174}.
FT   REGION       81    108       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      463    653       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      688    755       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      837    864       {ECO:0000256|HAMAP-Rule:MF_03141}.
FT   COMPBIAS     81     99       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    489    505       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    548    563       Acidic. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    700    730       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1596 AA;  175277 MW;  617B61E22660A729 CRC64;
     MTQILTSRQA EELHKSIIAY LSSKNLTSSA AALREELSIG DSFDEATSKK YEGLLEKKWT
     SVVRLQKKIM DLESRNATLQ TEIDSATPTS LSRRNQDPKQ WLPRSPARHT LQSHRQPITC
     VAFHPVFSSL ASGSEDSTIK IWDWELGELE RTVKGHTKAV HDVDFGGPRG GILLASCSSD
     LTIKLWDPSD EYKNIRTLPG HDHTVSAVRF VPSGAAGSPS SGNLLVSASR DKTLRVWDVS
     TGYCVKTIRG HADWVRDVSP SFDGRFLIST GTDQTARIWD ASSGEPKATL LGHENTVECC
     VFAPPASYEN ISKLAGLRKP PSGSSSAEFV ATGSRDKSIR IWDSRGTLIK NLVGHDNWVR
     GLVFHPGGRY LLSVADDKTL KCWDLEQEGK MVKSLDEAHG HFVSCIRWAP GAVKETPATN
     GVNGTPNGAS SKDVLANVSI KCVIATGSVD MNRAAMSSLH AFTHGSSSES SGEDDDFLHP
     LTDPNADEIA DYNPRKRRRT GRDAKESAAL GVFGSESEDE GPGKRWKKKT LRGKRMAFVT
     TGQKKQDEDE DEEPEDEAED IEDEAATPRT WGLGTPKGLG SQSPAPAKKT FPLAQSNAPL
     GRGFVPSSAT APILQEAADD VPTPRISRPS AFSTPVSDGR GGKRAQATSG VNAGSFAARM
     MAKMGYKEGG GLGKEGQGRS GVIEVTLRPQ GVGLGAVKEK SQQEIEEEKR QAKLKGEVYE
     DSDEERKKLR RKKSRANLES RSGSGMSAPR RAPKPRFRTL EEVQRAAPGL EIPEAFAPIL
     DMTAPGQRLI TSTSGLSTPT TGGFETAEQA ESKKLARRAQ NDLSAYVEEW KNLVERKAYI
     EMNIHQQQQK IDEEQQEYDR MKSFADVVKS ISQAVNDLQW DPVIEALIAA DRSAEPGLSG
     ASEELSRIAV AAVHPFLRQA VEGWRPLDDP KLNGMAPQLL QIRHILGSTS SGGNAFASQS
     YLRNDGSHRI YSKPTTAYES MIYMIIFPKI VSAVNQTWNV HDPTPLLKLF DAWEGLLPPF
     VRSQILDQTV VEKLNGAVSS WNPKKRRTKE LPHLWLFPWL QYLPPHHVDP RSSTGLVSDI
     KRKFRHLVEG WDFRKGVVPG LEQWRILLCP SPQNDQWTPL IMNHVLPVMS RFLRNPEYFL
     VDPNDQSPYM QTLEGVLAWS EILKPRTLGQ VIVETIFPMW HNTLHQWLTV VGPNQEIGQW
     FEWWRDSVFP DSIKSLTSIE AEFEKGHDMI NQALDLGSKA ATQLPLPSQN RRISASPPAP
     ITPAKPAPIV EETTFRHRVE DWCIENDLQF LPEKKVLHSA GPLYRITAAG NGKNGTLAYF
     NGDSLVALSK KGSQQIDVRI TWESADARDA LLEMAWQNES KQIADKMSPQ PKVLFVLTSH
     GQMGNTGKPT GWYLPEFAHP YEVLAPHASI TIASPNGGAS PLDPSSVEQT KDDAISVNFL
     KTKEALWKNT EKLGDFVGKA GEFDAIFFVG GHGPMWDLSQ DATSHKIINE FASAGKIVSA
     VCHGPAALAF VRTPSGEYLL KDHAVTGFST REEDGVGLTS TMPFILEDQL NAASGGKYEK
     ADADWGPKVV VSGKIITGQN PASASGVGEA ILKELR
//