ID Q0V2V1_PHANO Unreviewed; 922 AA.
AC Q0V2V1;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=Spindle pole body component {ECO:0000256|RuleBase:RU363050};
GN ORFNames=SNOG_01663 {ECO:0000313|EMBL:EAT91312.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT91312.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445326; EAT91312.2; -; Genomic_DNA.
DR RefSeq; XP_001792299.1; XM_001792247.1.
DR AlphaFoldDB; Q0V2V1; -.
DR STRING; 321614.Q0V2V1; -.
DR EnsemblFungi; SNOT_01663; SNOT_01663; SNOG_01663.
DR GeneID; 5969144; -.
DR KEGG; pno:SNOG_01663; -.
DR VEuPathDB; FungiDB:JI435_016630; -.
DR eggNOG; KOG2001; Eukaryota.
DR HOGENOM; CLU_007738_0_1_1; -.
DR InParanoid; Q0V2V1; -.
DR OrthoDB; 1328394at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IBA:GO_Central.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0000931; C:gamma-tubulin ring complex; IEA:EnsemblFungi.
DR GO; GO:0008275; C:gamma-tubulin small complex; IEA:EnsemblFungi.
DR GO; GO:0061496; C:half bridge of mitotic spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0061497; C:inner plaque of mitotic spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0031021; C:interphase microtubule organizing center; IEA:EnsemblFungi.
DR GO; GO:0035974; C:meiotic spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0071957; C:old mitotic spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:1990734; P:astral microtubule anchoring at mitotic spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IEA:EnsemblFungi.
DR GO; GO:0098863; P:nuclear migration by microtubule mediated pushing forces; IEA:EnsemblFungi.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
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:UP000001055}.
FT DOMAIN 182..513
FT /note="Gamma tubulin complex component protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17681"
FT DOMAIN 518..902
FT /note="Gamma tubulin complex component C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04130"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 103573 MW; 2A0851CC54DC6A9D CRC64;
MSTRIPPGTK PSTAERRSAN ANYTSTARPR VASAATGDES DRRASATTSH TRKQSHAMGG
TGASSGERRI EKKEVRERET EIRRTRTRSP LKHSSESRVN ARSRGEKPPK ETERPPRSAH
SAKSSPEEAQ TPWEPKASLV PHTTAPLATR ISIPPLASTA PIALQPTPLA QLSLDAQEKA
IIEDLLFVFM GFEGQYIRFS ETYNPHEEKE RLVGPQFRIL PGLDPSLRDL TKSMLKTATH
YIAVETCIEV LSREEYGAVN HALCAAIRRL MKDYLTLIAQ LEHQLLTNDS FTLHVLNLHT
KQTSHMLFQL YTTGIELLKA NDILEDDKDE DSADDDSNDF ENILESLREG GNATKKLCKG
GSVLGLITKR LSSMSGDPAA RTLLTTLLRE ASRPYMAMLN EWLHHGGIKD PHSEFLIKEQ
RSIKRERLDQ DYTDEYWEKR YTMRDALVPP QLEAVKDKVL LAGKYLNVVR ECGGVDVSKI
VQDAPTSFDD PRFLDNVSSS YAYANSSLLN LLLTTHQLPA RLRSLKHYFF LDRSDFFTYF
LEMGELELKK PAKAVNVGKL QSLLDLATRH AGSVAVEDPY KEDIKVHMND TGLTNWLMKI
VNVQGLDQDA AAASISNYTP ANTAPITDDS NITGFQALQF DYAMPFPLSL VVSRVTLTRY
QLLFRYLLSL KHLETDLAKC WGEQGKNAAW KHRSRNPRIE LWKRKAWTLR ARMLVFVQQL
TYYCTAEVIE PNWTSLMSRL NEEKKGDAKG KSKQADDDSG GPQVKRTVDE LMQDHVDFLA
TCLKECMLTN TNTKQINNKI MSTCSMFASF TYSLSRYLIT GDPDLVTQVN AALNPASNPR
PNAARSTANT QFVYDPQRVE KMFDMLAKYE ENFTRHLKIL LDTLNYLAAT ETVVFLSLCA
RLTSAGEGLS GFQAPMGMEG IV
//
