ID A0A178ACX8_9PLEO Unreviewed; 813 AA.
AC A0A178ACX8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 23.
DE RecName: Full=Tubulin gamma chain {ECO:0000256|ARBA:ARBA00018848};
DE AltName: Full=Gamma-tubulin {ECO:0000256|ARBA:ARBA00033229};
GN ORFNames=IQ06DRAFT_352616 {ECO:0000313|EMBL:OAK95596.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK95596.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK95596.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK95596.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636}.
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DR EMBL; KV441722; OAK95596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178ACX8; -.
DR STRING; 765868.A0A178ACX8; -.
DR InParanoid; A0A178ACX8; -.
DR OrthoDB; 5476567at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0000930; C:gamma-tubulin complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR CDD; cd02188; gamma_tubulin; 1.
DR CDD; cd08570; GDPD_YPL206cp_fungi; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR InterPro; IPR002454; Gamma_tubulin.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF7; TUBULIN GAMMA CHAIN; 1.
DR Pfam; PF03009; GDPD; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01164; GAMMATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS51704; GP_PDE; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT DOMAIN 69..310
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
SQ SEQUENCE 813 AA; 91701 MW; AB127BE63F2E6B02 CRC64;
MDSREDLDNA LDAQTPIVEN MVVGVPPVFE GLTRQLDKIV EQPLLGPKTE FPRASFAFAR
KDVSGSRRPQ AIAHRGYKAK FPENTMGAFK GAVNVGAEAL ETDIHLSKDG VVVLSHDKNL
KRCFGRDEKI IDCDYEFLSK LRTLKEPHEA MPRLVDLLEY LARPGLEDIW VMLDIKLDNN
ADDVMRLIGD AIRSVPPSPD RPWQNRIVLG IWAAKYLPLC SRYVPGFPIS HIGYSTVVAR
YFFKVPNVSF NMAQAVLMTP WGKAFIRKVQ RDKRPVYAWT VNDAAKMRWD IRHGLDGVIT
DDPKLFLEVR KSWHEGTEDG LGIMNALDIA RINFFMVIYT ILFCIVFGLS ESRWKRKEII
TLQAGQCGNS VGQQFWQQLC QEHGINRDGN LEDFATEGGD RKDVFFYQSD DTRYIPRAIL
LDLEPRVLNS IQSSAYKNIY NPENFYIHKD GTGAGNNWGM GYGMGEQVHE DVLDMIDREA
DGSDSLEGFM LLHSIAGGTG SGLGSFMLER LNDRFPKKLI QTYSVFPNTQ EGDIVVQPYN
SLLSMRRLTE NADSVVVLDN GALSKIAADR LHVLNPSFEQ TNQLVSTVMS ASTTTLRYPG
YMHNDLVGIV ASLIPTPRCH FLMTSYTPFS GENVEQAKTV RKTTVLDVMR RLLQPKNRMV
STNPTKKSCY MSILNIIQGE ADPSDVHKSL MRIRERRLAT FIPWGPASIQ VALTKKSPYV
QSSHRVSGLM LANHTGIATL FKRIVAQYNT LRKRNAFLEP YKREAPFKDG LGEFDEAKEV
VTSLIEEYEE AENADYLTKE VAPTDEGDDK RVG
//
