ID A0A0D1ZBC3_9EURO Unreviewed; 455 AA.
AC A0A0D1ZBC3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 35.
DE RecName: Full=Tubulin gamma chain {ECO:0000256|ARBA:ARBA00018848, ECO:0000256|RuleBase:RU000352};
GN ORFNames=PV11_06004 {ECO:0000313|EMBL:KIV84028.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV84028.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV84028.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV84028.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN846952; KIV84028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1ZBC3; -.
DR STRING; 1016849.A0A0D1ZBC3; -.
DR HOGENOM; CLU_015718_1_0_1; -.
DR OrthoDB; 5476567at2759; -.
DR Proteomes; UP000053599; 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-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:UP000053599}.
FT DOMAIN 48..246
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 248..392
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
SQ SEQUENCE 455 AA; 50776 MW; 0C34283E5C842038 CRC64;
MPRELITIQA GQCGNAIGSR FWQQLCQEHG ISRDGTLEDF AIEGGDRKDV FFYQSDDTRY
IPRAILVDLE PRVLNSIQTG PYKNIYNPEN FFVGDDGMGA GNNWAAGYAA GERVQEEIFD
MIDREADGSD SLEGFMLLHS IAGGTGSGLG SYLLERMNDR FPKKIIQTYS VFPDTAIGDV
VVNPYNSLLT MRRLTQNADS VVVLDNGALS RIASERLHVQ EPSFQQTNQL VSTVMSASTT
TLRYPGYMHN DLVGIIASLI PTPRCHFLMT AYTPFTGDSV DAAKTVRKTT VLEVMRRLLQ
PKNRMVSITP PKSSCYISIL NIIQGEADPT DVHKSLLRIR ERRMANFIPW GPASIQVALT
KKSPYLQNTH RVSGLMLANH TSVATLFKRI VVQYEKMRKR NAYLEQYKKE APFAEGLGEF
DEAKEVVMDL IGEYEAAEKD NYLDPDAGQT KTDGA
//
