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Database: UniProt
Entry: A0A0F4GFD8_9PEZI
LinkDB: A0A0F4GFD8_9PEZI
Original site: A0A0F4GFD8_9PEZI 
ID   A0A0F4GFD8_9PEZI        Unreviewed;       783 AA.
AC   A0A0F4GFD8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=Spindle pole body component {ECO:0000256|RuleBase:RU363050};
GN   ORFNames=TI39_contig831g00002 {ECO:0000313|EMBL:KJX96099.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX96099.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJX96099.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJX96099.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center {ECO:0000256|RuleBase:RU363050}.
CC   -!- SIMILARITY: Belongs to the TUBGCP family.
CC       {ECO:0000256|ARBA:ARBA00010337, ECO:0000256|RuleBase:RU363050}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJX96099.1}.
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DR   EMBL; LAFY01000823; KJX96099.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4GFD8; -.
DR   STRING; 1047168.A0A0F4GFD8; -.
DR   OrthoDB; 1328394at2759; -.
DR   Proteomes; UP000033647; 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:SF13; GAMMA-TUBULIN COMPLEX COMPONENT 2; 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, ECO:0000256|RuleBase:RU363050};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|RuleBase:RU363050};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU363050};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033647}.
FT   DOMAIN          162..496
FT                   /note="Gamma tubulin complex component protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17681"
FT   DOMAIN          501..779
FT                   /note="Gamma tubulin complex component C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04130"
FT   REGION          1..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   783 AA;  87854 MW;  18992DBB4AC06AFB CRC64;
     MASRPPARGA TLAERRASAS VRQQSNRPTS AALPSPTAET SSKSNVHTRT TTTDTTRRDV
     LTREAVIKRT TISPTKAPDR NGSFRKSVSA ERPKSQGKAQ VKPRSDSVAA PPWSPHASLL
     APSTAPLASR ISVPPVAAQA PISLHPPGLG SLSLQAQEKA IIEDLLFVLM GFEGQYIQFA
     NSYDPLDEKS QLAGPQFGIQ PGLDPSLRDL AQSMLKTATH FCAVEAFVEV QSREEMGSVN
     HALCAAMRKL TKDYMILIAQ LEHQMLTNEA FTLHQLSLHL KPTAHMMHQL YNVGNEILKE
     NSMLDREEDL DETDDFENIL ESLREGKDTG VPGKKVCKGG AVLRLLTKRM AAMAGDPAAR
     QLLTLLLREA SRPYMAMLNE WLHNGNVQDP HQEFLIKEQK SIRREGLEQD YTDEYWEKRY
     TLRQDLVPPQ LDSIKDRVLL AGKYLNVVRE CGGIENVTRD LDASTDVPHT FEDPRFLENV
     SGAYAFANRS LMTLLLTTHA LPARLRSLKH YFFLDRSDFF SYFLELTHSE LRKKPARNVN
     VGKLQSLLDI VLRQPGSVAA EDPFKEDVKV VMNDVGLTGW LMRVVNVQGM DADATSLTAY
     TPAAGNSTNS DAREEKDISG YEALTLDYAV PFPLSLVVSR VTLTRYQLLF RYLLSLKHLE
     TLLTNSWTEH TKGKPWHHKA AAKTPVTRKI ENWKRRAWCL RSRMLCFVQQ LLYFCTSEVI
     EPNWQSFMAR LAQPEGEEVT DAAETTPKVE RTVDELMQDH VDFLATCLKE CMLTNSKLLR
     VSF
//
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