ID   A0A428PT01_9HYPO        Unreviewed;      1335 AA.
AC   A0A428PT01;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Dynactin, 150 kDa isoform {ECO:0000313|EMBL:RSL56026.1};
GN   ORFNames=CEP54_009058 {ECO:0000313|EMBL:RSL56026.1};
OS   Fusarium duplospermum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL56026.1, ECO:0000313|Proteomes:UP000288168};
RN   [1] {ECO:0000313|EMBL:RSL56026.1, ECO:0000313|Proteomes:UP000288168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL56026.1,
RC   ECO:0000313|Proteomes:UP000288168};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00011010}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RSL56026.1}.
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DR   EMBL; NKCI01000096; RSL56026.1; -; Genomic_DNA.
DR   STRING; 1325734.A0A428PT01; -.
DR   Proteomes; UP000288168; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR022157; Dynactin.
DR   PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR   PANTHER; PTHR18916:SF6; DYNACTIN SUBUNIT 1; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12455; Dynactin; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Dynein {ECO:0000256|ARBA:ARBA00023017};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288168}.
FT   DOMAIN          24..66
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          76..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1039..1175
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        129..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1335 AA;  148740 MW;  689C43C14E28B7AE CRC64;
     MPDFKPGQIV QLSDGRKGTV RFAGPTHFQV GEWVGVELEE KTGKNDGSVQ GERYFDCPMG
     YGMFVKPMMA TIIAQAPAPR PARKPSRPSS FNPAAGRTSS AGDSGLGRRK SLNAPSPSPV
     PRVARPTSIA RSPTKSPTKQ LSGTSSAAVS RTGTPSNPRV PSAGSKSRPS VGGSRTSMGP
     PPPPATRTTR QASTSSVSSR AGGPIPRTAS GRLSLSGPRA VSVSRPSSRP SSVTRRTSVD
     SLAGRDHGSS DRDSIASPVK DNGDILSPQP RSPVQARTKA LEKLTGGTTS RTSTPPVSRK
     PAPAARPAGS TAASREIEDL KAKLKVLERK RAEDRDKLKQ LEKVQGERDK FESVIQMLQQ
     KYQPQQQENN ELKKLLKEAE MRLESIEEIQ AEHDSIIELA TLDREMAEET AEVLKVELDA
     LKEKAEELEL EVEILREENE EYSKGMTPEE RSSTGWLQME RTNERLREAL LRLRDLTQAS
     EEELKDQIAG LEDDLKEFNT VKEEYGVCRE KLEQSQSAVE DLRQQLDNAL GAEDMIEDLT
     ERNMSMAEQI EELKAVIDDL ESLKEINDEL EINHVQNEKE MQEELDFKDS VITEQARRAG
     QQEESLEDME YTLSRFRELV TSLQSDLDDM RASQAVTEGE SEKLNDRSRA MMDLNMKLQI
     SAAKAQVKTI DLELRRLEAQ EAEQHLEIVK LFLPDTYKED QDSVLALLRF RRLTFKANLL
     NGFIRERLNG QPHPGHEDDV FAGCDASDKL VWVSNMCDRF VNDISHCSIE QFSRYQNALH
     ELEPVERALN VWIDGLRRDD LKEQKCADEL HRTIALLSHL GEVHISNNLA NYADDAHMKA
     MLMQSHLDSA AVTFTTLRNL VHRVVPAEGE EEELAQHFAK KSEAVITQTR GAKVIAGKAV
     RALQDLRTRS LSLLPDTSEA FEQCCEATQE LADLARQIGL GLHELLTSDE TRTEPFTYVE
     VQSAVHKTVL AVSTSSESDL FSSYLAKLRT VTTQITDLAS LATDLDQVQE FDVAPAPWRL
     RSQELKALKT IPVDAEEELR RLKEEHSEAR RTIAQRDEHL STAVLKIETL ESRMRDAQAN
     IERISNLQIE LEASGQQIGS LKEDIEKQDR ELKNLESERD KWKKIASDSR AFADGADAAG
     AKAGQERAVA TAREMDALKK DIESLQSAVR YLRDDNRRAR TSEQQRYDWL AEPLQKPKTV
     TEQRRGLIAA EGRDVLGELV KMASSASLYN FSALPEDKLV WKPARSTPQY HAAKQMEDYA
     AWTSWEDSVL HKAHALQGQT ANVERRKAAA PSHNPAARLR IRLPGADGKV VPGSGRDVQI
     VGSREWEALQ GRIAV
//