ID G8BS10_TETPH Unreviewed; 479 AA.
AC G8BS10;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Tubulin gamma chain {ECO:0000256|ARBA:ARBA00018848, ECO:0000256|RuleBase:RU000352};
GN Name=TPHA0D04510 {ECO:0000313|EMBL:CCE63085.1};
GN OrderedLocusNames=TPHA_0D04510 {ECO:0000313|EMBL:CCE63085.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE63085.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE63085.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC chain is found at microtubule organizing centers (MTOC) such as the
CC spindle poles or the centrosome. {ECO:0000256|RuleBase:RU000352}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR EMBL; HE612859; CCE63085.1; -; Genomic_DNA.
DR RefSeq; XP_003685519.1; XM_003685471.1.
DR AlphaFoldDB; G8BS10; -.
DR STRING; 1071381.G8BS10; -.
DR GeneID; 11531114; -.
DR KEGG; tpf:TPHA_0D04510; -.
DR eggNOG; KOG1374; Eukaryota.
DR HOGENOM; CLU_015718_1_0_1; -.
DR OMA; HRYISIL; -.
DR OrthoDB; 5476567at2759; -.
DR Proteomes; UP000005666; Chromosome 4.
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-UniRule.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR CDD; cd02188; gamma_tubulin; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 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; 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; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000352};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666}.
FT DOMAIN 52..248
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 250..401
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 32..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 53993 MW; 831D0772170B5902 CRC64;
MAGEIITIQI GQCGNQVGKH FWNQLSKEHG IDRDGSCKFD DDPQKNIRDD DTNPFFKKND
SHRYTPRALL FDMEPGAVQD VTNTFPNFFD PRNVSVSRDE LGAGNSWSKG YDYGVSNQDE
LLNIIDKEID NTENFEGFQL IHSVAGGTGS GLGSNLLELI SDRYHKKFIS TYSVFPSDES
EVVVQPYNTL LTLRRLAENS DASIVFDNNA LLNLSSQVFK DPNTSYIHTN QLISSTMSSI
TNTIRFPSYM YNSMSSIFST LVPTPDLHFL LPGFTPFTSD YVNNGKDYKR NTAYDVILDL
FDKSNSLVSS RVDNPTYFNI YTSLIGSTEQ NDISRAILKL QSRINFAPWS STSIHVNVGR
RSSFLPQPEQ AVNGFGNRNY VNGMMLANST SILSVFERTV RTFDKIFAKG AFLNTFRNGK
MFQNDWDEFS ECREVAQNLI NSYSTAEQEN YLDDILIEEE NIIGNAEAEN DIGLDSNII
//
