ID   A0A0G4IMR8_PLABS        Unreviewed;       560 AA.
AC   A0A0G4IMR8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN   ORFNames=PBRA_005069 {ECO:0000313|EMBL:CEO96397.1};
OS   Plasmodiophora brassicae (Clubroot disease agent).
OC   Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC   Plasmodiophoridae; Plasmodiophora.
OX   NCBI_TaxID=37360 {ECO:0000313|EMBL:CEO96397.1, ECO:0000313|Proteomes:UP000039324};
RN   [1] {ECO:0000313|EMBL:CEO96397.1, ECO:0000313|Proteomes:UP000039324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:CEO96397.1};
RA   Chooi Y.-H.;
RL   Submitted (FEB-2015) 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};
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DR   EMBL; CDSF01000057; CEO96397.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4IMR8; -.
DR   STRING; 37360.A0A0G4IMR8; -.
DR   EnsemblProtists; CEO96397; CEO96397; PBRA_005069.
DR   OMA; VRECAPK; -.
DR   OrthoDB; 5487479at2759; -.
DR   Proteomes; UP000039324; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000039324}.
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..29
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  63407 MW;  7C553906CEF0044A CRC64;
     MIIPPSYEID LDDALVEDDE EEDDDDDEIF SDRSRSSTPP PRGHTNEYVI KRRGPGEPRP
     KMPATAKATV PPYRTLSCTV AFPYPAYMTI RRPRHDVGRR PVQYVGVSGR LRYRIDSDVP
     DYYVVSRVAR GAGLRPTNST ARCNLFWGRP LSPEKWELLT SLQRVNHFPG MTALSRKDNL
     ARHLRHCPFL PKTFVLPADR LAFQEAAASE PNRLWIVKPW ASSCGRGIRL IDRIGQLGAK
     CKAVVSRYIE RPYLIDGYKF DIRLYFVVTC MDPLRIYTLD DGLVRFATQR YSVDKSSLKQ
     KCVHLTNFSV NRHSKAFVKA TDGAQGSKWS FKALLAYLAH QTPPVDVEKL VERINDIAVR
     SIIAVEPVVA GKMEAYRCPR TACFEVLGFD ILLDQELNPW LLEINSMPSL SSSSSLDKFI
     KTKLIADVFH TIGMVPAEND LKVIRRVQTR RLKRVIGLRR NGSGSASASA PAGRQTGTPI
     SWQTLSNQDL AILREVQAEY ERSGHLIRIY PTRTNAASYR SAFKYERYNN KLVCDWLALD
     ADYALTLLAD DDPDSDDGEY
//