ID A0A368FNT9_ANCCA Unreviewed; 341 AA.
AC A0A368FNT9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN ORFNames=ANCCAN_22357 {ECO:0000313|EMBL:RCN31857.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN31857.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN31857.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN31857.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-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}.
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:RCN31857.1}.
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DR EMBL; JOJR01001203; RCN31857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368FNT9; -.
DR STRING; 29170.A0A368FNT9; -.
DR Proteomes; UP000252519; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000252519}.
SQ SEQUENCE 341 AA; 39116 MW; 07CF8B9CF5E3B63C CRC64;
MASEDFGHKW TLGALLRHIE KEGMDAKMLM LRIEDVVVKS LLSVQTRITS ACRTTTPHVG
TNFELFGFDI LVDEDLKPWL LEVNLSPSLS CDAPLDSLVK SRLICDLFNL ACVPLVNRKL
AGIQLIRPNK EDDCDSEDAE AEIERTKKIS PSKRGFNVKR RRVRTPFSSS PYAPDPSMRA
ICRRARAEMS RRGGFVRIFP REHSLQLYRG VMERIGSENR DERLYYKEYG FEEEEENAEQ
NENNLAKLYH DVMMDSSVYP TLESVPPELR EVLRGWYNDA NAYTQRITKD GEKYAVCESG
KYMLKPVAAK LPVVRPSARL RTKSCSEWYE VKKGDYSRGE A
//
