ID   A0A3Q2VP67_HAPBU        Unreviewed;      1259 AA.
AC   A0A3Q2VP67;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Dynactin subunit 1 {ECO:0000256|ARBA:ARBA00016574};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000009943.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000009943.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   ---------------------------------------------------------------------------
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   RefSeq; XP_005939278.1; XM_005939216.2.
DR   AlphaFoldDB; A0A3Q2VP67; -.
DR   STRING; 8153.ENSHBUP00000009943; -.
DR   Ensembl; ENSHBUT00000031499.1; ENSHBUP00000009943.1; ENSHBUG00000011710.1.
DR   GeneID; 102295202; -.
DR   GeneTree; ENSGT00940000155378; -.
DR   OrthoDB; 9423at2759; -.
DR   Proteomes; UP000264840; Unplaced.
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:UP000264840}.
FT   DOMAIN          54..96
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1105..1128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          980..1032
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1076..1103
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        8..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1259 AA;  139639 MW;  4CBB3B439DB1EFB5 CRC64;
     MALNRRHSYT PRLTSPLISR MSSTGTVESS KPPKIGSIVE VTGKGQRGTV AYIGATLFAS
     GKWVGVILDE PKGKNDGTVQ GKRYFTCEEN HGIFVRQSQI QVVEDGSSAT SPDTPESGTA
     KTLKQKEIPE TPKTSKQQPA SIKKASRESL SSSLSGDVSE AGLSSQQGAL GAPVIPQPSG
     SPAAAAAASV PATPSKVEPA ISKQEEESLR AQVKDLEEKL ETLKMKRTED KAKLKELEKH
     KIQLEQLQEW KNKMQEQQAE LQKQLKEAKK EAREAQEAKE RYMEEMSDTA DAIEMATLDK
     EMAEERAESL QVEVDSLKEK VEELSMDLEI LRHEISEKGS DGAASSYQVK QLEEQNSRLK
     EALVRMRDLS ASEKQEHVKL QKQTEKKNVE LETLRTQKEK LHEEVKQAEA TIDELKEQVD
     AALGSEEMVE TLTERNLDLE EKVRELRETV TDLEAINEMN DELQENARET EMELREQLDL
     SGAKVREADK RVEAAQETVA DYQQTINKYR ELTGSLQEAN RELISQQNAN AEQVQQPPAE
     LFDFKIKFAE TKAYAKAIEM ELRKMEVAQS NRQVSLLTSF MPDSFLRHGG DHDCILVLLL
     IPRLICKAEL ISKQAQEKFD LNGNPVQGTG LRGPPGEQRS FSSGLVYSLS LLQATLHKYE
     QALNTCSVDV FKRMGTLYSE MSFHERSLDY FIDLLHKDQL DETVQVEPLT KAIKYYQQLY
     SVHLADHTED CTVQLADHIK FTQSALDCMV VEVARLRAFL SSGQESSGLA VLLKDLDTSC
     SDIRQFCKKI RRRMPGTDVA GVPAALSFGP EVSETLTECR RQLTRVVAVL QEVAAAGAQM
     VPSLGEQEGL NALKLEDIAC KVVEQVYGSH GVNGPELLRQ SCSSVITTMN KMATAMQEGE
     YDAEKPQGKT LPVEMRAATV RAEMTDAEGL GVKLEDRETV IKELKKSLKI KGEELSEAHV
     RLSLLEKKLD TSTKDADERV EKIQTKLDEN LALLKKKEKE FEETMDALQA DIDQLEAEKA
     ELKQRLSNQS KMTIEGLRGP PASGIASIVQ GSAGGLPPSM GGPMQVVDSP LLRQQIEAQR
     LGIKHLKNEN NRLKAEKMRA QLASLPPLRP PKLPQVSKES SMPPEGLNTG IYRRTDQLLA
     TLLKLSAEVK VVDITGKTAV SASAQLLEQT ARLQNLSDAL DKLKGEVAEH VVSYQPGAKA
     SSDFATFPVT SFTKAKEEKQ GDTVFIGRVA IPCTRGQEQV HRLVLSKQQL QQVHSLLMV
//