ID A0A0V0R4K6_PSEPJ Unreviewed; 578 AA.
AC A0A0V0R4K6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Tubulin-tyrosine ligase/Tubulin polyglutamylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PPERSA_04717 {ECO:0000313|EMBL:KRX09411.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX09411.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX09411.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX09411.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
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:KRX09411.1}.
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DR EMBL; LDAU01000051; KRX09411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0R4K6; -.
DR EnsemblProtists; KRX09411; KRX09411; PPERSA_04717.
DR InParanoid; A0A0V0R4K6; -.
DR OrthoDB; 7265at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
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:UP000054937}.
SQ SEQUENCE 578 AA; 67808 MW; C155929A9ED2B111 CRC64;
MTTAIYLGCK NSKDISYTLE SKIKAAITYS ILSVEKVLKA KQPQIIGFDF EINNNLEPFV
TQISIVDNPK LIKAIKEKQV CNLPENNKCE VLLDTLQNIN FIQSHQFQIR KWNVPKMNQV
KYHQLIDEFG QPLSNIKTFH SNRLQSFNVV SQHLKRRGLK NTQIKNNSSF KHGLVYTSTI
EFDNKKKYTN QLTYSINAAW PSFLSDKFKL IKSLKEFDKL QPYNNIYNSS FINPLQYQID
FRNLSQPLSK DETEVLNLEN KGMWILKSAQ GMKGIGIELI YDLNDIQEAI QLKRDHHQLT
DKLNIKNHKS YHRYFTLQKY IENPLLQDGK KFDSRQFILV VSSDPLIVVY QTGYTRKTLV
DYHRFSKSKY THLGNGDIQK ELPGYKQKVQ KNHNYLREEF KSKLIKEYPE YNQVNFDLME
EKTKAGITYA IKAALNQNPN VRKGDTEIIS VDMVIDENLN AFITEFNRNP YLGTSQKVLA
QFFPSLGQDF ADATLALHAM EHDEIIARSR EDPFFICDIM KKIYNCKDNV LINDAVGYSY
LDHVDIQSYK YPEYKIYEEK DREQYQKDRQ QRMRKILK
//
