ID   A0A0D1YJ13_9EURO        Unreviewed;       949 AA.
AC   A0A0D1YJ13;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW14926.1};
GN   ORFNames=PV08_07713 {ECO:0000313|EMBL:KIW14926.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW14926.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW14926.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW14926.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TUBGCP family.
CC       {ECO:0000256|ARBA:ARBA00010337}.
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DR   EMBL; KN847496; KIW14926.1; -; Genomic_DNA.
DR   RefSeq; XP_016235142.1; XM_016382040.1.
DR   AlphaFoldDB; A0A0D1YJ13; -.
DR   STRING; 91928.A0A0D1YJ13; -.
DR   GeneID; 27334796; -.
DR   VEuPathDB; FungiDB:PV08_07713; -.
DR   HOGENOM; CLU_003736_0_0_1; -.
DR   OrthoDB; 197975at2759; -.
DR   Proteomes; UP000053328; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000930; C:gamma-tubulin complex; IEA:UniProt.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR   GO; GO:0005816; C:spindle pole body; IEA:UniProt.
DR   GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
DR   GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR   Gene3D; 1.20.120.1900; Gamma-tubulin complex, C-terminal domain; 1.
DR   InterPro; IPR007259; GCP.
DR   InterPro; IPR040457; GCP_C.
DR   InterPro; IPR042241; GCP_C_sf.
DR   InterPro; IPR041470; GCP_N.
DR   PANTHER; PTHR19302; GAMMA TUBULIN COMPLEX PROTEIN; 1.
DR   PANTHER; PTHR19302:SF14; GAMMA-TUBULIN COMPLEX COMPONENT 3; 1.
DR   Pfam; PF04130; GCP_C_terminal; 1.
DR   Pfam; PF17681; GCP_N_terminal; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT   DOMAIN          223..524
FT                   /note="Gamma tubulin complex component protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17681"
FT   DOMAIN          527..903
FT                   /note="Gamma tubulin complex component C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04130"
FT   REGION          139..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          804..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          914..949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        810..824
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..930
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..949
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   949 AA;  107353 MW;  095A278ECFC69CC1 CRC64;
     MADPRSTRIE GTLTSLFESL VPPPNIDQDD TETEYRIDRA IQNAKDIVLN ADSRLPSDTN
     QAQDLIKRKL LRENASPEKA ARFSNLYSRL LAIPVLNQKW AILYLLYKLS DASVLDVHPR
     DPLADSAHFA NIPRRHTLSS AKPYQVDEQA YDDGGGDDDD DDVASAEVPF PRGRTIPPKA
     KADVKVEKEL PAQEAQSTEE EQEADPVQPM KERLVSPSEP ELLRDLPFNL QGVSSTHVEF
     TGVTSLKLPT TLPVPIISLL HALAEPCLLY RGLAEYTNGQ EGGLIDQSLR SAINNELRSY
     LSLVASLESE IRQALAALSQ SEDPQSLRVT SVTLKRCMIW TRDATMGLRL MKLIVEESQQ
     KRGGQLLSLI HSLSSSHGDP FVASFAEKLL AHVARPFYEM LRHWIYDGEL VDPFHEFFIT
     EPDPNVSQAV DHRHVATSVW EEKYKLDTAM VPSIISSEFS KKVFLIGKSL NFIRHNCGDS
     DWVIQYSKSN SKSLDFANTA NLPMSIDVAY KTTMSRLTHL MSTKFGLFTH LNAIKKYMLL
     AQGDFIDLLI ESLAQHLDRP VNSMYRHNLT SQLEHAIRHS NAQYDDPEVL RRLDARMLEL
     SSGEIGWDCF TLEYKISAPC DVVITQWANT QYLKIFNLLW RIKRVEFSLN TTCKRCMTGG
     RGVLAGVNDK LGRDWKRSMC VVAEMVHFIN QLLYYLLFEV IEASWKQLEE AVHKPDATLD
     DLIEAHTNYL NNITKKGLIG QQRHPITGQQ EDSLVAQVHH ILKCMLSYRE VIDSLYKYSV
     AEYTRRQQFN AKVEQRTAQG RWGITEKDLN GDTRASTPAS LAPSKTGRRV QLLPEEGDSP
     LVGPVGSLAP GDDETQLNSL RARQLHLSAE FRSRLSMLLY DLAHQPDVDL RFLGVVMNFN
     EVYQPVNVRR QQARRAREKR ELERKAREAA VSSEANTSME KDMNSSTRT
//