ID H2B299_KAZAF Unreviewed; 474 AA.
AC H2B299;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 22-FEB-2023, entry version 56.
DE RecName: Full=Tubulin gamma chain {ECO:0000256|ARBA:ARBA00018848, ECO:0000256|RuleBase:RU000352};
GN Name=KAFR0L01400 {ECO:0000313|EMBL:CCF60749.1};
GN ORFNames=KAFR_0L01400 {ECO:0000313|EMBL:CCF60749.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF60749.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF60749.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
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; HE650832; CCF60749.1; -; Genomic_DNA.
DR RefSeq; XP_003959884.1; XM_003959835.1.
DR AlphaFoldDB; H2B299; -.
DR STRING; 1071382.H2B299; -.
DR GeneID; 13886957; -.
DR KEGG; kaf:KAFR_0L01400; -.
DR eggNOG; KOG1374; Eukaryota.
DR HOGENOM; CLU_015718_1_0_1; -.
DR InParanoid; H2B299; -.
DR OrthoDB; 5476567at2759; -.
DR Proteomes; UP000005220; Chromosome 12.
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:UP000005220}.
FT DOMAIN 54..247
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 249..396
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
SQ SEQUENCE 474 AA; 53416 MW; 04C9838432E3021E CRC64;
MTGEIITIQI GQCGNHVGKQ FWSQLADEHN IGVDGRAKTD DDLTSFRDDD TNPFFKQYEQ
NRYIPRALLI DLEPSVINDT IAHLPGFFDT KNSWVSSERY GAGNSWANGY AEGDKNQETF
LNMVDKELDS TENLEGFQML HSVAGGTGSG LGSNLLEALA DRYPKKFLTT YSVFPSDESE
VVVQPYNTIL TLRRLAEDSD ASIVFDNNAL GNLTSRVLKT RNIDYNQTNQ LITAVLSSIT
NSIRFPNYMY TSLQSIFSTV VPTPELHFLT PAFTPFTSDY IKDARDIKQN TAYDVLLDLV
DDSNSLVSQT STKAIYFNVY NTVIGSNDTI NSSDITRAIS KLQRRIQFAP WSSTVIHVNV
GRRSPYLAHN VDRKHVNGMA LTNSSGIIPL FQKSCNQFDK IFSKKAFLNT FQQKDLFKEY
DEFIDSREVV RNVIDNYSAA EEKNYLDDIL LEDDNVVGDF NQDVEVDADG DNYM
//
