ID   A0A0B1SQ09_OESDE        Unreviewed;       531 AA.
AC   A0A0B1SQ09;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
DE   Flags: Fragment;
GN   ORFNames=OESDEN_14281 {ECO:0000313|EMBL:KHJ85981.1};
OS   Oesophagostomum dentatum (Nodular worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX   NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ85981.1, ECO:0000313|Proteomes:UP000053660};
RN   [1] {ECO:0000313|EMBL:KHJ85981.1, ECO:0000313|Proteomes:UP000053660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ85981.1,
RC   ECO:0000313|Proteomes:UP000053660};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Oesophagostomum dentatum.";
RL   Submitted (MAR-2014) 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   -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC       {ECO:0000256|ARBA:ARBA00006820}.
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DR   EMBL; KN561954; KHJ85981.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B1SQ09; -.
DR   Proteomes; UP000053660; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   GO; GO:0019098; P:reproductive behavior; IEA:UniProt.
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   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:KHJ85981.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053660}.
FT   REGION          473..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         531
FT                   /evidence="ECO:0000313|EMBL:KHJ85981.1"
SQ   SEQUENCE   531 AA;  60353 MW;  BC3369203D02AA11 CRC64;
     MRSTSLRSPF LQLAARYPTE YRRALADFDS EEEEELVVEL ESLEIRVYNR DTSMRPDANR
     LQLTGEEENI VDEIPVCGDA GTLIIGAENK PRKIEYLTFT PDSLKHIGRQ AAGELREKYT
     QTGENYNLAF KMINSDTKLV KTVLHSHGFT QCSRKNPSFN ILWCGSSVRA THMRSIQPWQ
     RINQFPRSTE LTRKDKLYDN LARSAALFGD AYSFIPDYFV TPRDVSMMET AMEQSMSDLT
     FIVKPVGSSQ GKGIFFANKP QEVPQTEPLL VSRYIENPLL IDGHKFDLRI YVAVTSIYPL
     VAYVFSEGLT RVASEKYSSD VDTQDAFVHL TNYSINKNNS NFIRNESMAS EDFGHKWTLG
     ALLRHLEKEG IDAKLLMIRI EDIVVKSLLS VQNRITSACR TTTPHVGTNF ELFGFDILVD
     EQLKPWLLEV NLSPSLSCDA PLDSLVKSRL ICDLFNLACV PLVNRKLAGI QPIRPKKDDD
     SESDNAEIET EKNKRSSPTK RGFNIKRRRV VRTAFATSPY APDPCMRAIY R
//