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Database: UniProt
Entry: W2ZKU3_PHYPR
LinkDB: W2ZKU3_PHYPR
Original site: W2ZKU3_PHYPR 
ID   W2ZKU3_PHYPR            Unreviewed;       965 AA.
AC   W2ZKU3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETP47992.1};
GN   ORFNames=F442_06163 {ECO:0000313|EMBL:ETP47992.1};
OS   Phytophthora parasitica P10297.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP47992.1, ECO:0000313|Proteomes:UP000018948};
RN   [1] {ECO:0000313|EMBL:ETP47992.1, ECO:0000313|Proteomes:UP000018948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P10297 {ECO:0000313|EMBL:ETP47992.1,
RC   ECO:0000313|Proteomes:UP000018948};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P10297.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TUBGCP family.
CC       {ECO:0000256|ARBA:ARBA00010337}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETP47992.1}.
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DR   EMBL; ANIY01001323; ETP47988.1; -; Genomic_DNA.
DR   EMBL; ANIY01001323; ETP47989.1; -; Genomic_DNA.
DR   EMBL; ANIY01001323; ETP47990.1; -; Genomic_DNA.
DR   EMBL; ANIY01001323; ETP47991.1; -; Genomic_DNA.
DR   EMBL; ANIY01001323; ETP47992.1; -; Genomic_DNA.
DR   EMBL; ANIY01001323; ETP47993.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2ZKU3; -.
DR   EnsemblProtists; ETP47988; ETP47988; F442_06163.
DR   EnsemblProtists; ETP47989; ETP47989; F442_06163.
DR   EnsemblProtists; ETP47990; ETP47990; F442_06163.
DR   EnsemblProtists; ETP47991; ETP47991; F442_06163.
DR   EnsemblProtists; ETP47992; ETP47992; F442_06163.
DR   EnsemblProtists; ETP47993; ETP47993; F442_06163.
DR   Proteomes; UP000018948; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR   GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
DR   GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR   Gene3D; 1.20.120.1900; Gamma-tubulin complex, C-terminal domain; 1.
DR   InterPro; IPR007259; GCP.
DR   InterPro; IPR040457; GCP_C.
DR   InterPro; IPR042241; GCP_C_sf.
DR   InterPro; IPR041470; GCP_N.
DR   PANTHER; PTHR19302; GAMMA TUBULIN COMPLEX PROTEIN; 1.
DR   PANTHER; PTHR19302:SF14; GAMMA-TUBULIN COMPLEX COMPONENT 3; 1.
DR   Pfam; PF04130; GCP_C_terminal; 1.
DR   Pfam; PF17681; GCP_N_terminal; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018948}.
FT   DOMAIN          314..616
FT                   /note="Gamma tubulin complex component protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17681"
FT   DOMAIN          619..953
FT                   /note="Gamma tubulin complex component C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04130"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   965 AA;  108448 MW;  249A40A9150CD8E9 CRC64;
     MNSDRQAARL KRRAERLGPP SRAHSSSVGS RHSYAVSSDA SSSRTRGSSV PTDSSDSLRR
     PPVMSTSATA VAMSARRGSS ARSPRDINVL VDKLLAKVHG APSAITTRRT VVRLHDAVSN
     APQTDAFSIL EKIKRKIAAD APQFYTDSQE TVTRLNEVYS RFVKFKNLDK KTEALLLLYG
     LMDTAPPPVH SEEIHSRPGF PARSVNNCPA SSTPDSLDSS ASEKNGEHHR SHSMPVVSLN
     LGAQNAAPME QSMTDLDSLE DSFKFAVGIA PTHKPSRGKG SSPRTYPGAL VSDAMGASRA
     TGRSSFDVPE EVLLRDVLYA LQAIESRYLY FDDAADRFQI TRSVGVPTPM RELIHMLCDL
     GWIFRKISEY IKQHREELAF GLVGQSFCHV LNTELAGYFR LIAVLAAQID EDAETRQPHE
     RGVSSLTLRT LIVWLQDPLD RMRLMTRLID SVEGLRGGAL ASGIHSHVLH GDPDVSQSVQ
     RVLKQIAAPI VRMIKRWVFE GELEDVHGEF FVVADPTVSD DQFWAKKYTL NLKMLPPFIS
     IELAKKILVI GKSINFIRQC CGNADWVMDA AQETAVIGMD TENEGAYFAE LKRLETVIAN
     VSNSTNEYLI RTLTQKYRLL DHCQALKRYL LLGQGDFIQY LMDLLGPELS KRGAQVYRHT
     LTNVLETALN ASNAKFESPD ILGRLDVELL QGSSADTGWD IFCLHYNLQA PVNSVIPASS
     MLQYQQIFDF LWRMKRVEHS LSASWTKDMN LGHEVQGCVP GIRPVLHRSQ LVRSEMIHFI
     TNLLNYMMFE VLETAWHKLV KDLNAANDLD GLIESHAAYI ASIKKNGFMM KDSRDLLKQL
     KLIFATIIRF CKAQENLYTT AMHEKHVEER HQQLMQQQEL GSSWGIPEED EYTMRTERDT
     FGSNSKILRQ IEEISEDFST QFLELLEIVK KNSIRGSQSL SFLMSRFDFN EFYLKKTNPP
     MDADE
//
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