ID   A0A0A2LC87_PENIT        Unreviewed;       887 AA.
AC   A0A0A2LC87;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Spindle pole body component {ECO:0000256|RuleBase:RU363050};
GN   ORFNames=PITC_071750 {ECO:0000313|EMBL:KGO77692.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO77692.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO77692.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO77692.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO77692.1}.
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DR   EMBL; JQGA01000108; KGO77692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2LC87; -.
DR   STRING; 40296.A0A0A2LC87; -.
DR   HOGENOM; CLU_007738_0_1_1; -.
DR   OMA; QNMSGDP; -.
DR   OrthoDB; 1328394at2759; -.
DR   PhylomeDB; A0A0A2LC87; -.
DR   Proteomes; UP000030104; 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:UP000030104}.
FT   DOMAIN          174..512
FT                   /note="Gamma tubulin complex component protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17681"
FT   DOMAIN          515..875
FT                   /note="Gamma tubulin complex component C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04130"
FT   REGION          1..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   887 AA;  100152 MW;  53B6824027E65E12 CRC64;
     MSANDRAAYM SAPRPRAVSN RVDSETRGPS PLQVENKDPL RHSTSSQKHR TSRDQKSMSD
     QRPERMVITS REKAVRRNPV NPVKESISAA NRGDWDKTRP RKPAQLDDAN PSARTGEKDL
     ADTPWNPQAS LIPPSTAPLA CRVSVPPLAS TAPQALHPRP LRELSPDAQE AAILEDLLFV
     FMGFEGQYIH FASSYDPSIE KDRLTGPVFQ IAPGLDPTLR DLIQSMLKMA THYSAMEAFV
     EIQSRAECGA VSHSLCASIR KLLKDYLILI AQLEGQLLNN PTFTLHLLRL HTMPTSQCLA
     QLYSMGQELL LKNGLLDEDL EESIDDFDED VDNILEQLKE GGDLVPGAMT RKKMCKGGNI
     LGLLTGRLAS FSGDPITKTL LQTLLRDASR PYMAMLNEWL HHGGIRDPHA EFLVKEQKWI
     KREKLEEDYT DEYWEKRYTI REHEVPPQLK SVQDKVLLAG KYLNVVRECG GVDVSKEVKD
     VPKTLDDPRF LDNVNSAYTY ANASLLNLLV TKNSLTTRFR SLKHYFFLDR SDFFSYFLEL
     GASELRKPAR AVNEGKLQSL LDIVLRQPGS VAALDPFKED VKVRMNKIGL TKWLMQVVNV
     SGVNQDGAES EKQQASAVHS ADEDKDILGF DALELDYSVP FPLSLVISRK TVLRYQLIFR
     HLLSLRHLET LLVTSWADQN KTTSWRHKSS DRRLEIWKRR AWNLRAKMLV FVQQLLYFCT
     AEVIEPNWVG LMDRVNSVHA EASEVEENGM KQVNRTVDEL MQDHVDFLDT CLKECMLTQA
     KLLKIHSKLV TCCTMFASWT AASLSRALAS ADPDLAGGKV PGADARGYDP TRIGKLEDTL
     KRYEDHFSRH LRISMDSLNY FAATESVVLL KLAHSLTSIS REESKED
//