ID   TBG_PHYPA               Reviewed;         475 AA.
AC   Q9XFG3; A9THV1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
GN   Name=TUBG1; ORFNames=PHYPADRAFT_170153;
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WT;
RA   Wagner T.A., Sack F.D., Oakely B.R., Oakely C.E., Schwuchow J.;
RT   "Characterization of gamma tubulin from Physcomitrella patens.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
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, suggesting that it is involved in the minus-end
CC       nucleation of microtubule assembly.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center {ECO:0000250|UniProtKB:P38557}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; AF142098; AAD33883.1; -; Genomic_DNA.
DR   EMBL; DS545123; EDQ56966.1; -; Genomic_DNA.
DR   RefSeq; XP_001778184.1; XM_001778132.1.
DR   AlphaFoldDB; Q9XFG3; -.
DR   SMR; Q9XFG3; -.
DR   STRING; 3218.PP1S234_17V6.1; -.
DR   EnsemblPlants; Pp3c19_7110V3.1; Pp3c19_7110V3.1; Pp3c19_7110.
DR   EnsemblPlants; Pp3c19_7110V3.2; Pp3c19_7110V3.2; Pp3c19_7110.
DR   Gramene; Pp3c19_7110V3.1; Pp3c19_7110V3.1; Pp3c19_7110.
DR   Gramene; Pp3c19_7110V3.2; Pp3c19_7110V3.2; Pp3c19_7110.
DR   eggNOG; KOG1374; Eukaryota.
DR   HOGENOM; CLU_015718_1_0_1; -.
DR   InParanoid; Q9XFG3; -.
DR   OMA; RRESMFK; -.
DR   OrthoDB; 687389at2759; -.
DR   Proteomes; UP000006727; Chromosome 19.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   CDD; cd02188; gamma_tubulin; 1.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 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; PTHR11588; 2.
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; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..475
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048476"
FT   REGION          455..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   475 AA;  53291 MW;  DFEF33A2DEDDEBB1 CRC64;
     MPREIITLQV GQCGNQIGME FWKQLCLEHG ISKDGILEDF ATQGGDRKDV FFYQADDEHY
     IPRALLIDLE PRVINSIQNS EYRNLYNHEN VFVADHGGGA GNNWASGYHQ GEQVEEDIMD
     MIDREADGSD SLEGFVLCHS IAGGTGSGMG SYLLEALNDR YSKKLVQTYS VFPNQMETSD
     VVVQPYNSLL TLKRLTLNAD CVVVLDNTAL NRIAVDRLHI PNPTFAQTNS LVSTVMSAST
     TTLRYPGYMN NDLVGLVASL IPTPRCHFLM TGYTPLTVER QANAIRKTTV LDVMRRLLQA
     KNIMVSSYAR TKEASQAKYI SILNIIQGEV DPTQVHKSLQ RIRERKLANF IEWGPASIQV
     ALSRKSPYVQ TAHRVSGLML ASHTSIRHLF SKCISQYEKL RKKQAFLDNY RKFPMFADND
     LSEFDESREI VQNLVDEYKA CESADYIKWG MEDRGKQVSG EGNTSGTVDS RVGAS