ID A0A059C0U3_EUCGR Unreviewed; 474 AA.
AC A0A059C0U3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Tubulin gamma chain {ECO:0000256|RuleBase:RU000352};
GN ORFNames=EUGRSUZ_E00075 {ECO:0000313|EMBL:KCW71530.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW71530.1, ECO:0000313|Proteomes:UP000030711};
RN [1] {ECO:0000313|Proteomes:UP000030711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BRASUZ1 {ECO:0000313|Proteomes:UP000030711};
RX PubMed=24919147; DOI=10.1038/nature13308;
RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D.,
RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D.M.,
RA Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., Hussey S.G., Pinard D.,
RA van der Merwe K., Singh P., van Jaarsveld I., Silva-Junior O.B.,
RA Togawa R.C., Pappas M.R., Faria D.A., Sansaloni C.P., Petroli C.D.,
RA Yang X., Ranjan P., Tschaplinski T.J., Ye C.Y., Li T., Sterck L.,
RA Vanneste K., Murat F., Soler M., Clemente H.S., Saidi N., Cassan-Wang H.,
RA Dunand C., Hefer C.A., Bornberg-Bauer E., Kersting A.R., Vining K.,
RA Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A.E., Liston A.,
RA Spatafora J.W., Dharmwardhana P., Raja R., Sullivan C., Romanel E.,
RA Alves-Ferreira M., Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D.,
RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J.,
RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., Potts B.M.,
RA Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P.,
RA Grima-Pettenati J., Salse J., Van de Peer Y., Rokhsar D.S., Schmutz J.;
RT "The genome of Eucalyptus grandis.";
RL Nature 510:356-362(2014).
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 -!- 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. {ECO:0000256|ARBA:ARBA00002783}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center {ECO:0000256|ARBA:ARBA00004267}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR EMBL; KK198757; KCW71530.1; -; Genomic_DNA.
DR RefSeq; XP_010055050.1; XM_010056748.2.
DR AlphaFoldDB; A0A059C0U3; -.
DR EnsemblPlants; KCW71530; KCW71530; EUGRSUZ_E00075.
DR GeneID; 104443383; -.
DR Gramene; KCW71530; KCW71530; EUGRSUZ_E00075.
DR KEGG; egr:104443383; -.
DR eggNOG; KOG1374; Eukaryota.
DR OrthoDB; 5476567at2759; -.
DR Proteomes; UP000030711; 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:UP000030711}.
FT DOMAIN 48..247
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 249..395
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
SQ SEQUENCE 474 AA; 53359 MW; 86EE601DBE9DF966 CRC64;
MPREIITLQV GQCGNQIGME FWKQLCLEHG ISKDGMLEDF ATQGGDRKDV FFYQADDQHY
IPRAILMDLE PRVINGIQNS EYRNLYNHEN IFVSDHGGGA GNNWASGYHQ GKGVEEDIMD
MIDREADGSD SLEGFVLCHS IAGGTGSGMG SYLLETLNDR YSKKLVQTYS VFPNQMETSD
VVVQPYNSLL TLKRLTLNAD CVVVLDNTAL NRIAVERLHL SNPTFAQTNS LVSTVMSAST
TTLRYPGYMN NDLVGLLASL IPTPRCHFLM TGYTPLTVER QANVIRKTTV LDVMRRLLQS
KNIMVSSYAR TKEASQAKYI SILNIIQGEV DPTQVHESLQ RIRERKLVNF IEWGPASIQV
ALSRKSPYVQ TAHRVSGLML ASHTSIRHLF SKCLNQYEKL RKKQAFLDNY RKFPMFADND
LSEFDESRDI IESLVDEYKA CESPDYIKWG MEDPDHILTG EGNATGTVDP KLAV
//