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Database: UniProt
Entry: A0A2U9BA91_SCOMX
LinkDB: A0A2U9BA91_SCOMX
Original site: A0A2U9BA91_SCOMX 
ID   A0A2U9BA91_SCOMX        Unreviewed;      1274 AA.
AC   A0A2U9BA91;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Dynactin subunit 1 {ECO:0000256|ARBA:ARBA00016574};
GN   ORFNames=SMAX5B_012878 {ECO:0000313|EMBL:AWP00868.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP00868.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP00868.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-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}.
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DR   EMBL; CP026246; AWP00868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U9BA91; -.
DR   Proteomes; UP000246464; Chromosome 4.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; 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:UP000246464}.
FT   DOMAIN          54..96
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          103..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          961..1052
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1097..1124
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        103..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1274 AA;  141559 MW;  29E9D06F7075E46C CRC64;
     MALNRRHSYT PRLTSALISK MSSGGMVESS KPPKIGSTVE VTGKGQRGTV AYIGATLFAS
     GKWVGVILDE PKGKNDGTVQ GKRYFTCEEN HGIFVRQSQI QVVEEGSSAT SPDTPESGTA
     KMLKLKDIAE TPKTSKQSST RRSAKWSMPR LAPATSLPSL LVRSTGRPSL QLMASRESLS
     SSLSGDVSEV GLSSHQGALG APVVPQPSGS PAPAAAPVPA TPSKEEDSLR AQVKDLEEKL
     ETLKMKRTED KAKLKELEKH KIQLEQLQEW KIKMQEQQTD LQKQLKEVKK EAREAQEAKD
     RYMEEMADTA DAIEMATLDK EMAEERAESL QVEVDTLKEK VEELSMDLEI LRHEISEKGS
     DGAASSYHVK QLEEQNGRLK EALVRMRDLS SSEKQEHVKL QKQMEKKNTE LETLRTQKEK
     LQEEVTQAEA TVDELKEQVD AALGSEEMVE TLTERNLDLE EKVRELRETV TDLESINEMN
     DELQENGRET EMELREQLDL SGAKVREAEK KVEAAQETVA DYQHTISKYR ELTTRLQDDN
     RELISQQNAN AEQVQQPPAD LFDFKIKFAE TKAYAKAIEM ELRKMEVAQS NRQVSLLTSF
     MPDSFLRHGG DHDCILVLLL IPRLICKGEL LSKQAQEKFD LNGNVTQGTG LRGPPGEQRS
     FATGLVYSLS LLQATLHKYE QALNTCSVEV FKRMGTLYSE MNFHERSLDY FIDLLHKDQL
     DETVQVEPLT KAIKYYQQLY SVHLADHTED CTVQLADHIK FTQGALDCMG VEVARLRAFL
     TAGQESSGLA VLLKDLDTSC SDIRQFCKKI RRRMPGTDVV GVPAALNFGP QVSESLTECR
     RQLTRVVAVL QELAAAGSQM VAPLAEQEGL NALRLEDIAC KAVEQVYGSH GLSGPECLRQ
     SCCSVVATMN KMATAMQEGE YDADKPQGMT PPVEMRAATV RAEITDAEGL GVKLEDRETA
     IKELKKSLKI KGEELSEANI RLSLLEKKLD TSTKDADERV EKIQTKLNEN LALLKKKEKE
     FEETMDALQA DIDQLEAEKA ELKQRINNQS KMTIEGLRGP PASGIASIVQ GSTGVGLAPS
     MAGPLEVVDS PLLRQQVEAQ RLGIKHLKNE NNRLKAEKIR AQLASLPPLC PPKLPQVSKE
     SSMPPVGLNT GIYRRTDQLL ATLLKLSAEF KVVDITGKTA VSASSQLLEQ TARLQNLSDA
     LDKLKGEVTE HVVTHQRGAK ASSDFATFPV SSFVKVKAFG ISYKTYQCFQ YLKEKKWLKR
     SGTLAHIRLY HVVS
//
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