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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//