ID A0A061J6U0_TRYRA Unreviewed; 615 AA.
AC A0A061J6U0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN ORFNames=TRSC58_01131 {ECO:0000313|EMBL:ESL11128.1};
OS Trypanosoma rangeli SC58.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Herpetosoma.
OX NCBI_TaxID=429131 {ECO:0000313|EMBL:ESL11128.1, ECO:0000313|Proteomes:UP000031737};
RN [1] {ECO:0000313|EMBL:ESL11128.1, ECO:0000313|Proteomes:UP000031737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC58 {ECO:0000313|EMBL:ESL11128.1,
RC ECO:0000313|Proteomes:UP000031737};
RA Stoco P.H., Wagner G., Gerber A., Zaha A., Thompson C., Bartholomeu D.C.,
RA Luckemeyer D.D., Bahia D., Loreto E., Prestes E.B., Lima F.M.,
RA Rodrigues-Luiz G., Vallejo G.A., Filho J.F., Monteiro K.M., Tyler K.M.,
RA de Almeida L.G., Ortiz M.F., Siervo M.A., de Moraes M.H., Cunha O.L.,
RA Mendonca-Neto R., Silva R., Teixeira S.M., Murta S.M., Sincero T.C.,
RA Mendes T.A., Urmenyi T.P., Silva V.G., da Rocha W.D., Andersson B.,
RA Romanha A.J., Steindel M., de Vasconcelos A.T., Grisard E.C.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-
CC glutamyl-L-glutamyl-[protein] + H(+) + phosphate;
CC Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC Evidence={ECO:0000256|ARBA:ARBA00036640};
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:ESL11128.1}.
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DR EMBL; AUPL01001131; ESL11128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061J6U0; -.
DR EnsemblProtists; ESL11128; ESL11128; TRSC58_01131.
DR VEuPathDB; TriTrypDB:TRSC58_01131; -.
DR OrthoDB; 155190at2759; -.
DR Proteomes; UP000031737; Unassembled WGS sequence.
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; TUBULIN POLYGLUTAMYLASE; 1.
DR PANTHER; PTHR12241:SF145; TUBULIN POLYGLUTAMYLASE TTLL5; 1.
DR Pfam; PF03133; TTL; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS51221; TTL; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:ESL11128.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031737}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 68997 MW; 05EBFA17A0447074 CRC64;
MRKAEEKKHE GAQEGLTGAQ RQRNRRLAHG AVFIAAPPVR RYDESDGKVW RTTTKICTTV
RSAAADVRVT LSVSPFCGRQ PTIAFLPFDR PWDGDPHSGD TTAYVEPPLL AWLPPPHTGT
RAEVQRDRTY AALGFTISDN AVHFSSVMCA LERAGFTEVS LLSKSWSLKW CKRSVRSDFA
RLKSFQRVNH FPGTWRIGKK DELHKHLLAA RERWREEKGE GSFGDFFPEG WVLPEEQEAL
AQVLRSSKER GQLFIVKPTT SACGRGIYLV RADEGVQLAS ALRQPDECSE RDMRSRRLLV
QRYVADTLLV EGYKFDLRLY VVVTSYAPLR AYLYSEGLVR FATSPYPTAE SADADHAFDL
SLTAHLTNFT INKKSEDFVP PDELTVKEGG TSASKWTLAA LQKHFHMHGL DWNATMAHIH
DLLVKTLLAV EPHVILEQNA ISDTVGGGCF EVYGVDVLLR RPHSSENPVP MPVLMEVNIM
PSLSTHYSLL DQCVKGNFIA EMLTLVGITA ASGSKKRGNA AVTVPQMQEE DKLTFSYGHP
FLDALTDATE LEACLTAEEE FVRRMHFQRL CPTSHSYSRY RSLFTPCKSG TSHRSLNEVL
SLWEQAKLVD PPAYI
//
