ID V5AP79_TRYCR Unreviewed; 380 AA.
AC V5AP79;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Tubulin tyrosine ligase {ECO:0000313|EMBL:ESS62530.1};
GN ORFNames=TCDM_09805 {ECO:0000313|EMBL:ESS62530.1};
OS Trypanosoma cruzi Dm28c.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=1416333 {ECO:0000313|EMBL:ESS62530.1, ECO:0000313|Proteomes:UP000017861};
RN [1] {ECO:0000313|EMBL:ESS62530.1, ECO:0000313|Proteomes:UP000017861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dm28c {ECO:0000313|EMBL:ESS62530.1,
RC ECO:0000313|Proteomes:UP000017861};
RX PubMed=24482508;
RA Grisard E.C., Teixeira S.M., de Almeida L.G., Stoco P.H., Gerber A.L.,
RA Talavera-Lopez C., Lima O.C., Andersson B., de Vasconcelos A.T.;
RT "Trypanosoma cruzi Clone Dm28c Draft Genome Sequence.";
RL Genome Announc. 2:e01114-13(2014).
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:ESS62530.1}.
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DR EMBL; AYLP01000178; ESS62530.1; -; Genomic_DNA.
DR EnsemblProtists; ESS62530; ESS62530; TCDM_09805.
DR VEuPathDB; TriTrypDB:TCDM_09805; -.
DR Proteomes; UP000017861; 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:0016874; F:ligase activity; 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 Ligase {ECO:0000313|EMBL:ESS62530.1};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000017861}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 380 AA; 43320 MW; 2B4CF77439F98DC6 CRC64;
MQHKAAQSWN EYGSARHTET NGSSKAAQVM STKKTFTTSS VAAPAVATAG ATSTPLSLLE
DRAKGDDTPP LRYRTDLDKH VIHFAFQRFP HSIEILEDED VMSDDWHFFW MNVGRVRSIF
STAEYRLTDT QIINHFPNHY ELTRKDLMYK NIKKYIRDPN NAQLMVRYTP PCRGPYEWSE
KPSGWLRFVD CVPVTYNIPN DFQMFTQEFR RQPCSTWIVK PTSRSQGRGI FLINRITQLK
RWIKERKEAD EAEGLPASTF VVSKYVANPL LIGGKKFDLR LYVLVTSFKP LVAYLHEQGF
ARFCATPYVA NALKDDNLCS HLTNVALQKG EDAYNEVHGG KWSLANLCLF VQGRYGAVCA
DGLMRXXXPV VCVCIINFTG
//
