ID   J5SPU3_TRIAS            Unreviewed;       982 AA.
AC   J5SPU3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   28-JUN-2023, entry version 42.
DE   RecName: Full=Spindle pole body component {ECO:0000256|RuleBase:RU363050};
GN   ORFNames=A1Q1_04407 {ECO:0000313|EMBL:EJT46856.1};
OS   Trichosporon asahii var. asahii (strain ATCC 90039 / CBS 2479 / JCM 2466 /
OS   KCTC 7840 / NBRC 103889/ NCYC 2677 / UAMH 7654) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1186058 {ECO:0000313|EMBL:EJT46856.1, ECO:0000313|Proteomes:UP000002748};
RN   [1] {ECO:0000313|EMBL:EJT46856.1, ECO:0000313|Proteomes:UP000002748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 90039 / CBS 2479 / JCM 2466 / KCTC 7840 / NCYC 2677 / UAMH
RC   7654 {ECO:0000313|Proteomes:UP000002748};
RX   PubMed=23104369; DOI=10.1128/EC.00237-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Draft genome sequence of CBS 2479, the standard type strain of
RT   Trichosporon asahii.";
RL   Eukaryot. Cell 11:1415-1416(2012).
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:EJT46856.1}.
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DR   EMBL; ALBS01000274; EJT46856.1; -; Genomic_DNA.
DR   RefSeq; XP_014178248.1; XM_014322773.1.
DR   AlphaFoldDB; J5SPU3; -.
DR   GeneID; 25987920; -.
DR   KEGG; tasa:A1Q1_04407; -.
DR   VEuPathDB; FungiDB:A1Q1_04407; -.
DR   HOGENOM; CLU_011863_0_0_1; -.
DR   OrthoDB; 1333074at2759; -.
DR   Proteomes; UP000002748; 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:SF70; GAMMA-TUBULIN COMPLEX COMPONENT 6; 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}.
FT   DOMAIN          127..356
FT                   /note="Gamma tubulin complex component protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17681"
FT   DOMAIN          491..882
FT                   /note="Gamma tubulin complex component C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04130"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          915..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        915..940
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   982 AA;  110702 MW;  70ABE0039DE83439 CRC64;
     MVAAAHEAPF DSRSKEDVRD DEDVLAVMNT LGDEASAAAE EEGPKEDEAK PATEQELWAQ
     AAFAGPSRVE YFDPLITLSA PPLSLPRLQT PASNPPISSF RLLELMLRAT LGTAMNDSLR
     WSRREGRLVK GFLDIGTGVR RLEIIIEEHN ATPITPTHHA LLHSLSTVLT YVKERLAEGV
     RNVMAKMQEV NYDPKMAPWL RREMGLRDAR ELVTAWCEVM CWPLDQKRPV GLPARPSSLL
     SHLHSHLVAW MTTSSSQSNL VLSLAYILSR SSEPFLDLLH QWLGLAPCPE VDDESQPWLD
     LGITRERIEG RWEYSFTARR MPSFIPRTIR RTLFDAGCSL RALHEATNGA HPLCNDWSLR
     ANWGWGADAR VQREVDKWRG TRSRTISMSS AGSRWRSRPG SPCSSTSPSE PVDFWATLCE
     PPGSHLPQLW KAAPLDDIEN FVAFHTDEPL LGDSPTLELY ISSQLLSPLL THAQLISQAL
     ISLYLDDLSF LSHLDMLQEY WLGGNAGFVE RVGTALFTPS GGSSGLLSHR ERNRGKRGLE
     TEEDMGIGLG LGLSDRRRWP PGGGELAYAL RTTLLDEEQP NENGWNVEDL VSFAIRALPE
     ENDGRRAKWL DPTSLDFLYL SYSPPPVIST LLPPSIMEKY QSVHNLLLRL QRAETVLSSL
     FYDVMKFGDG KSSKEGVDLH KRNAHLTAPR RKDQSLFEGE ADVALRHLRF CMSWFVTAIT
     RYILDTAIRQ NWEVMRRRLD KLRKRAHLNV HTESRPMTPA DDDEFEDLDG EVFDVEGDEE
     DKTQLGTLSQ LQSAHSLVLY HHVIMNRILR ACLLSPQPGH QITFKILMSL LSLILDLSRT
     VKETERSGDV EKGAQHVLAI RLEWNDKFAV FLHELAKLAW SPHVQLNMNE ERPLSAKLCQ
     IRANNQFHAL ERLSLRTPGH TDRASTDKEH KAKTEADAEQ DLQLLLEGEV EDNSKTPGSA
     ELQELLLRLK LGVPASRTGR WK
//