ID V9DX90_PHYPR Unreviewed; 428 AA.
AC V9DX90;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Tubulin polyglutamylase TTLL1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=F443_21711 {ECO:0000313|EMBL:ETI31301.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI31301.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI31301.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI31301.1,
RC ECO:0000313|Proteomes:UP000018721};
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., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000256|ARBA:ARBA00004120}.
CC -!- SIMILARITY: Belongs to the tubulin polyglutamylase family.
CC {ECO:0000256|ARBA:ARBA00006118}.
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:ETI31301.1}.
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DR EMBL; ANIZ01003794; ETI31301.1; -; Genomic_DNA.
DR AlphaFoldDB; V9DX90; -.
DR EnsemblProtists; ETI31301; ETI31301; F443_21711.
DR eggNOG; KOG2157; Eukaryota.
DR HOGENOM; CLU_010131_0_0_1; -.
DR OrthoDB; 5487479at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR PANTHER; PTHR12241:SF31; POLYGLUTAMYLASE COMPLEX SUBUNIT TTLL1; 1.
DR PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR Pfam; PF03133; TTL; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS51221; TTL; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 48638 MW; 17B59EA6437AD9C5 CRC64;
MSRPTTPATA STSLSASGGS GKFRWRVDAE KNVVVWNFER RGWAKTEGDD WNIYWASKTT
IKNIFNPETG VRLVDGQYVN HFPNHYELTR KDLMVKNIKR YKKEMLAAQA TASEAGSSTA
YPIESLDFFP MTYTLPADYS LFVEEFRRNP NVMWIMKPCS KAQGKGIFII NKLSQTKKWA
NQRWTNMPIK EGYVVSRYIE NPLLVGGKKF DLRMYVLVLS YRPMQALVYR EGFARFCNVK
YSAAVDDMDN PFMHLTNVAV QKNNEDYNSN HGGKWSVANL CLYVEATRGH GAGEKLLRDI
HGVMLHALKA VQNVIINDPH CFECYGYDII VDDNLKPWLV EVNASPSLAT TTREDRSMKS
RLLRDVLELA VAADAGPDQR RAVLPPPTLS PTSGFSWLLN ETTQLEADRL RADALRKNAK
RASSAQWR
//