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Database: UniProt
Entry: A0A0N1PDX5_LEPSE
LinkDB: A0A0N1PDX5_LEPSE
Original site: A0A0N1PDX5_LEPSE 
ID   A0A0N1PDX5_LEPSE        Unreviewed;       812 AA.
AC   A0A0N1PDX5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Putative tubulin tyrosine ligase {ECO:0000313|EMBL:KPI89312.1};
GN   ORFNames=ABL78_1541 {ECO:0000313|EMBL:KPI89312.1};
OS   Leptomonas seymouri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI89312.1, ECO:0000313|Proteomes:UP000038009};
RN   [1] {ECO:0000313|EMBL:KPI89312.1, ECO:0000313|Proteomes:UP000038009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI89312.1,
RC   ECO:0000313|Proteomes:UP000038009};
RX   PubMed=26317207;
RA   Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA   Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA   Yurchenko V.;
RT   "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT   Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT   donovani.";
RL   PLoS Pathog. 11:E1005127-E1005127(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:KPI89312.1}.
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DR   EMBL; LJSK01000026; KPI89312.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1PDX5; -.
DR   EnsemblProtists; KPI89312; KPI89312; ABL78_1541.
DR   VEuPathDB; TriTrypDB:Lsey_0026_0080; -.
DR   OMA; HFMFERY; -.
DR   OrthoDB; 124205at2759; -.
DR   Proteomes; UP000038009; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR   PANTHER; PTHR12241:SF31; TUBULIN POLYGLUTAMYLASE TTLL1-RELATED; 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   Ligase {ECO:0000313|EMBL:KPI89312.1};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          43..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   812 AA;  86731 MW;  4B9C2476515B633F CRC64;
     MPASAEPPAK VHGSFRRSKA PLKTEKIASK PLVTATVTVE AATAAGGSTA TAPSISTASS
     LSTRTKKKRV KKSISAARRR SVRSVSTSCC SSVSPKKHPQ QQQLQASADA VEGLTEAFHS
     LPSEDANNAC DGAYDVTSTS SVSDDSRDGV SRGGSVRHAP EQVTSLAGKR HTRVVMNPPS
     AACNGGSAPA NLAAVAGSSG AAGNRASGAS WRRGGLYGAT GSAGGANSGN YANDGALRYR
     TDLDKQVIHF MFERYHQEQI CPTADPTLLK DAERAEDSGA GEELSVELNS SGNGRNVKAA
     GAAAAGQLSS SAPPPCSQPR ARRIAVEEIY VPSNGEGDDK NIGLGDWHFF WMHVGRVRHT
     VCSGDFRWQD QQIINHFPDH AELTRKDLMY KNIKRYLREN QANNYARLTL HTATDWVSAA
     ANAASASSAA VAGGSESAAT VSLANPFFGP ESSEHVASTK AFCFADSVPI TYNIPNDMSM
     FKEECQKQRG TQWIMKPTAR SQGKGIFIID SARALQRWVK EKKDTENVVS LSTTGPAKRV
     SCAAGANNAV HSTGSPTSPS TGAAAAAASS SGGPSNPVAS LSTTAAGGGG HSSGGLGAYI
     VSRYISNPLL ICGKKFDLRL YVLVTSYRPL VAYLHEDGFA RFCATRYNGD SLAQEDLGSH
     LTNVALQKGD EHYNASHGGK WSFQNLFLYV QCRYGPYAAE GMMKNIQFLI YHSLKAVEPV
     MFNDKHAFEL YGYDILIDDQ INPHLIEVNA SPSMSTTTPS DRLLKEQVLT DMTKIVFPPG
     FPANSKSMPY WEYRQRTDLT TQQLTGFKLL QF
//
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