GenomeNet

Database: UniProt
Entry: A0A0A2JYC7_PENEN
LinkDB: A0A0A2JYC7_PENEN
Original site: A0A0A2JYC7_PENEN 
ID   A0A0A2JYC7_PENEN        Unreviewed;      1203 AA.
AC   A0A0A2JYC7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Spc97/Spc98 {ECO:0000313|EMBL:KGO57150.1};
GN   ORFNames=PEX2_001240 {ECO:0000313|EMBL:KGO57150.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO57150.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO57150.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO57150.1,
RC   ECO:0000313|Proteomes:UP000030143};
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   -!- SIMILARITY: Belongs to the TUBGCP family.
CC       {ECO:0000256|ARBA:ARBA00010337}.
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:KGO57150.1}.
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DR   EMBL; JQFZ01000152; KGO57150.1; -; Genomic_DNA.
DR   RefSeq; XP_016598838.1; XM_016737402.1.
DR   AlphaFoldDB; A0A0A2JYC7; -.
DR   STRING; 27334.A0A0A2JYC7; -.
DR   GeneID; 27672821; -.
DR   HOGENOM; CLU_007738_0_1_1; -.
DR   OrthoDB; 1328394at2759; -.
DR   Proteomes; UP000030143; 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};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143}.
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..132
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   1203 AA;  135227 MW;  458A355722DFD6F7 CRC64;
     MSANDRAAYM SAPRPRAVSN RVDSETRGPS PLQVENKDPL RHSTSSQKHR TSRDQKSMPD
     KRTERMVITS REKAVRRNPV NPVKESISAA NRGDWDKTRP RKPVQLDEAN PSPQAGEKDL
     ADTPWNPQAS LIPHSTAPLA CRVSVPPLAS TAPQALHPRP LRELSPDAQE AAILEDLLFV
     FMGFEGQYVH YASSYDPSIE KDRLTGPAFQ IAPGLDPTLR DLIQSMLKMA THYSAMEAFV
     EIQSRAECGA VSHSLCASIR KLLKDYLILI AQLEGQLLNN PTFTLHLLRL HTMPTSQCLA
     QLYSMGQELL LKNGLLDEEL EESIDDFDED VDNILEQLKE GGDLVPGSMA RKKMCKGGNI
     LGLLTERLAS FSGDPITKTL LQALLRDASR PYMAMLNEWL HHGGIRDPHA EFLVKEQKWI
     KREKLEEDYT DEYWEKRYTI REHEVPPQLK SVQDKVLLAG KYLNVVRECG GVDVSKEVKD
     VPKTLDDPRF LDNVNSAYTY ANASLLNLLV TKNSLTTRFR SLKHYFFLDR SDFFSYFLEL
     GASELRKPAR AVNEGKLQSL LDIVLRQPGS VAALDPFKED VKVRMNKIGL TKWLMQVVNV
     SGVNQDGAEA EKQQVSAVHS ADEDKDILGF DALELDYSVP FPLSLVISRK TVLRYQLIFR
     HLLSLRHLET LLVTSWADQN KTTSWRHKSS DRRLEIWKRR AWNLRAKMLV FVQQLLYFCT
     AEVIEPNWVG LMDRVNSVHA DASEMEENDM KQVNRTVDEL MQDHVDFLDT CLKECMLTQA
     KLLKIHSKLV TCCTMFASWT AASLSRALAS ADPDLAGGKV PGADARGYDP TRIGKLEDTL
     KRYEDHFSRH LRILMDSLNY FAATESVVLL KLAHSLTSIS REEKMRLGVL AMGTRSKALQ
     TYDVCCHLKL GEAETCDIDT NTTNMPITTL TSILRIPFPH PNIPQNRLTL ALSATALLVS
     TLILPAAYRD YKIFKSYGPG GPPHNALGWI VVRALFQPFG REMFSTDEYV KRIAAAEGHG
     KGDDGFLFLP EEQLGSRCGE ERPVVGPHVA PQRQMTQLPD EAVMEKFRSV FNAFGHRNHH
     LVKFQRSNLE RHADGLFVAD HIPVFGIAKT MQREIAHVHS GGDHSVHVVL APADCIKVIE
     AGWGQRHAFS GTPAMSILSL GMRPDIPAEY VLIYAPRTEA EIETVMKIVS AGVEFMTGRE
     DVR
//
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