ID   A0A1Y2WNN2_9PEZI        Unreviewed;      1351 AA.
AC   A0A1Y2WNN2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=CAP-Gly domain-containing protein {ECO:0000259|PROSITE:PS50245};
GN   ORFNames=K445DRAFT_322139 {ECO:0000313|EMBL:OTB11353.1};
OS   Daldinia sp. EC12.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX   NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB11353.1, ECO:0000313|Proteomes:UP000243732};
RN   [1] {ECO:0000313|EMBL:OTB11353.1, ECO:0000313|Proteomes:UP000243732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC12 {ECO:0000313|EMBL:OTB11353.1,
RC   ECO:0000313|Proteomes:UP000243732};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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   EMBL; KZ112964; OTB11353.1; -; Genomic_DNA.
DR   STRING; 1001832.A0A1Y2WNN2; -.
DR   OrthoDB; 9423at2759; -.
DR   Proteomes; UP000243732; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:UP000243732}.
FT   DOMAIN          24..66
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          75..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1068..1133
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1158..1192
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        87..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1351 AA;  149925 MW;  98E160A9C7E4F4D4 CRC64;
     MSEVEVGQTI RLTDGRNAIV RYVGQTHFAV GDWIGIELED EGGKNDGSVQ GERYFDCSPG
     RGMFVRPATV AAVLQPAPAP RSSAPVRRGS RTGTARPSSV TGRPSSVAGR SNSVTDHSVG
     KRMSLNAPSP SPVPRRASRT SSMVRSPTKS PTKQLGMTAP PSVSNSRTGT PSNARVSSIG
     TRPRPPAVNT RTSMGPPALP SAGSRRQAST SSTTRSVSGA TRPSGPRVST APVRGSARPT
     AGRVRSGDSL SGNEGGNRSD LGSPFKSDGE QTISPVRSRT KALEKLTSGP SSTASSKAPA
     SAASAKAPAG AAAAARTSAT SAARENEDLK AKLKVLERKR LEDREKIKDL EMIQEQRDKF
     ESINKKIEAK YQTTAQENSA LRKQLKEAEE RLEQIEALQA EHETVMELAT LDREMAEETA
     EVYKAELEAL KQKAEELELE VEVLREENAE YSQGMSPEER ASAGWLQMER HNERLREALI
     RLRDLTQEQE EESKAQIKAL EKDLEDFEAI KEQYQIAKEK LLESEARAED LRQQLDDNVG
     AESMVEQLSY EKLQQSEHIN ELKAMIDDLE ALKEINDELE VNHVQNEKEM QDELDFKDSI
     IAEQARRAAE KDDTIGDLEY TLSRFRELVT NLQTDLEDMR ASHAMNEAES EQLNSKSKAM
     MDLNQKLQLS AVKTQIKTID LELQRMDAQE AQQHLQIVKL FLPESYNADR DSVLALLRFR
     RLAFKANLLH GFVKERVNGQ PHPGLEDDAL AGCDALDKLT WVSSMCDRFV NAISHCSLEE
     FAKYEGALYE LEPVERALNT WIDGLRRDEL KEKQCASELQ RTIALMTHLG EVHISQGLES
     FADEMQMKTV LMQSHLESAA TAFNIIKDMV QRVVPPNGEE DELAQHFAKK SEAVITQTRS
     AKVIVSKAVR SLEDLRARSL ALTPDTADAF EQCEAASQEL AEMSRKIGVD LHALLSEEGR
     AEPFTYPEVQ SAIHNTVMTA FSSDESDLFS TYLSKLRALT SQITDLAAVC ADLSQTQEFE
     RSQAPWLLRA QELKALKTIP IDAEEELRQL KEHYNEARRT IALRDENLST AALRIETLEA
     RMRDANAKAS RMADLEAQLE DAKKHMESLK KDIEQQDREA KTLEADRDKW KKIAGDSRAF
     GDETGSTGSR AKAGQERAVA TAREMDALKN DIANLQAAVR YLREDNRRAR ATEQARHDWL
     AEPLQKPVPV MEQRKALVAA EGRDALGELL KLATSAKVYD LSTLPKDKMA WRPAKVTPQY
     HAAKQAEDYA TWSSWQESVI QKTRVVLSAE QGRKKHHDSD HAKMMRKAAA RLQIRLPDAD
     GKVIPGVGGR EVQIVGSREW EGLQGRLAAA M
//