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Database: UniProt
Entry: A0A0D2HLC3_9EURO
LinkDB: A0A0D2HLC3_9EURO
Original site: A0A0D2HLC3_9EURO 
ID   A0A0D2HLC3_9EURO        Unreviewed;       945 AA.
AC   A0A0D2HLC3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIY02721.1};
GN   ORFNames=Z520_01186 {ECO:0000313|EMBL:KIY02721.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY02721.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIY02721.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY02721.1,
RC   ECO:0000313|Proteomes:UP000053411};
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 Fonsecaea multimorphosa CBS 102226.";
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; KN848063; KIY02721.1; -; Genomic_DNA.
DR   RefSeq; XP_016636843.1; XM_016771704.1.
DR   AlphaFoldDB; A0A0D2HLC3; -.
DR   STRING; 1442371.A0A0D2HLC3; -.
DR   GeneID; 27706932; -.
DR   VEuPathDB; FungiDB:Z520_01186; -.
DR   OrthoDB; 197975at2759; -.
DR   Proteomes; UP000053411; 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:UP000053411}.
FT   DOMAIN          219..520
FT                   /note="Gamma tubulin complex component protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17681"
FT   DOMAIN          523..898
FT                   /note="Gamma tubulin complex component C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04130"
FT   REGION          113..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          914..945
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        926..945
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   945 AA;  107382 MW;  4965F3081E6E6D1B CRC64;
     MADPRLNRVE GTLTSLLESL VPPLSPDQDD TDTEFRIERA IQNAKETVLA ADGRLPPDTN
     QAQDLIKRKL LRENASPEKA ARFSNLYSRL LAIPVLNQKW AILYLLYKLS DKSTPDARPR
     NPLADSEQVA NIPRRHTLSP ETTFTAEEEL DDEEEEPQLP KVSIRTRRAL STRSRKPNEQ
     VEIATEEEYQ SQTPEPKEEK PVAEKQEPRV IYPSELDLLR DLPFNLQGVS SAHLQFADNG
     ALKLPPSLPV PILSLLHALA EPCLLYRGLA EYAAGQDGGL IDQSLRSAIN NELRSYLSLV
     ASLETEVRQA LATVQNAQDP KAVRLTGVTL KRCLIWTREA TMALRLMKLI VEDSRQKRGG
     QLLSLIHNLS SSHGDPFVAS FAEKLLTHVA RPFYEMLRHW IYDGELIDPY HEFFITEPDP
     TAQPPVDHRH VATSVWEEKY KLDSGMVPSI ISSEFSRKVF LIGKSLNFIR NNCGDSDWVI
     KYSKSNSRSL DYANTANLAQ SIDVAYRTTM SRLTHLMSTK FGLFTHLTAI KKYMLLAQGD
     FFDLLIESLA QHLDRPVNSM YRHNLTSQLE HAIRHSNAQY DDAEVLRRLD ARMLELSSGE
     IGWDCFTLEY KISAPCDVVI TQWANTQYLK IFNLLWRIKR VEYSLSSTCK RCMTGGRGVL
     AAVSDKLGND WKRSRCVVAE MVHFVNQLQY YLLFEVIEAS WKKLEEALQK PEATLDDLIE
     AHTNYLNNIT KKGLIGQQRH PVTGQQEDSL IVQVHHILKC MLAYREVIDS LYSYSVAEYT
     RRQQFSAKIE RRTAQGKWGI TEKDLLGDSR ASTPTSVAGA GAFRSNQLVL EENDSSLPTN
     ENIHITDGET HLNSLRARQL NLSADFRSRL SMLLYDLAHQ PDVDLRFLGV VMNFNEVYQP
     VNIRRQQARR AREKRELERK AREATVSSEG NVSLEKDLNS STSKS
//
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