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Database: UniProt
Entry: A0A165EB83_9APHY
LinkDB: A0A165EB83_9APHY
Original site: A0A165EB83_9APHY 
ID   A0A165EB83_9APHY        Unreviewed;       842 AA.
AC   A0A165EB83;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Spindle pole body component {ECO:0000256|RuleBase:RU363050};
GN   ORFNames=LAESUDRAFT_146540 {ECO:0000313|EMBL:KZT06643.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT06643.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT06643.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT06643.1,
RC   ECO:0000313|Proteomes:UP000076871};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR   EMBL; KV427623; KZT06643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165EB83; -.
DR   STRING; 1314785.A0A165EB83; -.
DR   InParanoid; A0A165EB83; -.
DR   OrthoDB; 1328394at2759; -.
DR   Proteomes; UP000076871; 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:UP000076871}.
FT   DOMAIN          113..486
FT                   /note="Gamma tubulin complex component protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17681"
FT   DOMAIN          491..836
FT                   /note="Gamma tubulin complex component C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04130"
FT   REGION          75..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   842 AA;  95394 MW;  5AFB7CA49190F154 CRC64;
     MEPYTPRRRK KNLTLSTKEY TKVTGTIASV RRTRQYVEDG YEEDPGVFSA RPSLDRAPEE
     PSFYAETSFV RAPLNSRVAS GTAPKDKSKG KGKAKAKESF EGVPLEVQEA LVLEDLLFVL
     MGIEGVYVTH LPDYSPDDED PLQGVTFVVS PSLDPSLRDL VERILPLATY YTAVTSFIEL
     RSHLDFGLVN HALCAAMRDM LKEYQTLLAQ LEHAFSTSSS FTLQKLWFYV HPTLHTLSLL
     YLLTTELARA DGTSDAQSES ESESSVDSEE AARNEALGLG GAKLKAMLSE INKGVDEGAS
     ATPVKGGEVL AIIFERMQNM SGDPAARALY GELLRAAGKP YIEMLQAWIL MGRLVDPYEE
     LCVKESKFID RGTLEVDYTD EYWERRYTLR DGSTTGGSSQ TAGVPPPRTP GGRLPGGACV
     PPMLEKWKHK ILLAGKYLNV IRECGIEIRR NSNQADDDLS LDNEKLYKSI DEAYTHANHT
     LLELLLRDQQ LIPRLRSFKR FFFLSQSTFI THLLDLSHSE LRRPAKGASL VKLQSLLDLA
     LNTDTQGEDA MFREDVCVTM ATSGLYEWLI DVLREHGVIG EDTGKRTDAH SREESKKDRD
     KDEKKSLQAI DALTLDYTVK FPLSLVISRK TVLRYQLIFR FLLHLKHVEQ TLTSMWLEQK
     MPIWRRAPPA SEWGMQLENW RKRVFLLRAR MLAFVQHILG FTTFEVLEPN WRKLEGKLEA
     RKVETVDQLL KEHVDFLDTC LKECMLTSSR LLGAYSRLMT TCSTFALYAA SFTKSLNSAF
     ASEGVPEGDK EFAKRWDYLN KFETHFNHWF KIHLDLVQYD ASRENVTLLP LVVRLSSIKS
     SL
//
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