GenomeNet

Database: UniProt
Entry: H3GGU0_PHYRM
LinkDB: H3GGU0_PHYRM
Original site: H3GGU0_PHYRM 
ID   H3GGU0_PHYRM            Unreviewed;       593 AA.
AC   H3GGU0;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblProtists:Phyra75075};
OS   Phytophthora ramorum (Sudden oak death agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra75075, ECO:0000313|Proteomes:UP000005238};
RN   [1] {ECO:0000313|Proteomes:UP000005238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
RN   [2] {ECO:0000313|EnsemblProtists:Phyra75075}
RP   IDENTIFICATION.
RC   STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra75075};
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC       function by capturing and stabilizing tubulin in a quasi-native
CC       conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC       interaction with cofactor C then causes the release of tubulin
CC       polypeptides that are committed to the native state.
CC       {ECO:0000256|ARBA:ARBA00026055}.
CC   -!- SIMILARITY: Belongs to the TBCC family.
CC       {ECO:0000256|ARBA:ARBA00008848}.
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DR   EMBL; DS566008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H3GGU0; -.
DR   STRING; 164328.H3GGU0; -.
DR   EnsemblProtists; Phyra75075; Phyra75075; Phyra75075.
DR   VEuPathDB; FungiDB:PSURA_75075; -.
DR   eggNOG; KOG2512; Eukaryota.
DR   eggNOG; KOG3206; Eukaryota.
DR   HOGENOM; CLU_032612_3_0_1; -.
DR   InParanoid; H3GGU0; -.
DR   OMA; CEFFVAC; -.
DR   Proteomes; UP000005238; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR   GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR   Gene3D; 2.160.20.70; -; 1.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   Gene3D; 1.20.58.1250; Tubulin Binding Cofactor C, N-terminal domain; 1.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR027684; TBCC.
DR   InterPro; IPR031925; TBCC_N.
DR   InterPro; IPR038397; TBCC_N_sf.
DR   InterPro; IPR012945; Tubulin-bd_cofactor_C_dom.
DR   PANTHER; PTHR15139; TUBULIN FOLDING COFACTOR C; 1.
DR   PANTHER; PTHR15139:SF0; TUBULIN-SPECIFIC CHAPERONE C; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF07986; TBCC; 1.
DR   Pfam; PF16752; TBCC_N; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005238}.
FT   DOMAIN          190..223
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   DOMAIN          389..561
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          378..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  65138 MW;  C30C28458770E46A CRC64;
     MFVLAVLHLT AGDDHAGLRH PEEHGVRGLG IRAARGNQPE VGSPAGEDIP AEEGIPAEVG
     SLVGEGNLAV GEGSPAAADI LAAAAGNLAA EAGNLAAAGT PAAAARCDWL YPSHIWLAVI
     RRNILLSTNH TPTKTELYEP GRDAKMEPLT IGTRCELLSS GPSGSLRASI KRYGEIVYIG
     AIEGLPGDGW LGVRLDKPLG KGDGSFQGTR YFECKPLHGA IVRPERVNIK GEFPVLATHE
     ESLAHALEER RREKQGARSS TGWRLQRELT TDELATAFWE TFTKQEEHVR KQVGLFCEQK
     KQPLPCEPAK EVKLDALVLE VNTMRDAAAT AASLYLSPYD TRHTQLILAK LLELIDSTRA
     TFAPRKKFTF RAHAARKAKS KTAETQDEPE QDTSFRSADV VSNQQTAQKL MEFDELVHAN
     KQNEVIIIDS SSFSGSDDSK RRDLNFSRLT NCVVLVCVET SAIRGDALKN CVFYTGAIFG
     SLWLESCNGC EFFVACRQLR VHLSTATTFH LRISSHPIIE DCQQMLFGPY RLQFDGLTAQ
     LERLGVQKDS GLWAKVNDFK WHKAQQSPNW SIRDPKQPLP GIPVELENLV SYE
//
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