ID A0A075A207_9TREM Unreviewed; 558 AA.
AC A0A075A207;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Tubulin-tyrosine ligase family protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=T265_10230 {ECO:0000313|EMBL:KER21439.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER21439.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER21439.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KL596967; KER21439.1; -; Genomic_DNA.
DR RefSeq; XP_009174808.1; XM_009176544.1.
DR AlphaFoldDB; A0A075A207; -.
DR STRING; 6198.A0A075A207; -.
DR GeneID; 20324398; -.
DR KEGG; ovi:T265_10230; -.
DR CTD; 20324398; -.
DR OrthoDB; 7265at2759; -.
DR Proteomes; UP000054324; 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: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 Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054324}.
SQ SEQUENCE 558 AA; 63971 MW; 0642DEED75E6186B CRC64;
MSLFLSVDTK IAAPIYKQFG ASRRLVLYGT VKAHVRYFTK VLYHSEFNFD VSNQPNSWPS
LSFIGTLAGD RAKGAVEYWK LGQMSRIKYA IDVEKSVISN NCEARGWQCT SPDDDWHFFW
ASVQSVRAIF NNDSGYRLSD NQLVNHFPNH FELTRKDLMA KNIKRYRKEL EKEGNPLAAK
DETGRYLYLD FIPVTYMLPQ DYNLFTEEFK RNPTLTWILK PSGKARGIGI FLINRLSQLK
KWSREGRMGM MLGSVPSYVR DSYVISRYID NPLLIGGKKF DLRLYILVTS FRPLKAYIYK
LGFCRFCTVK YNTDVTELDN MFVHLTNVSI QKHGAHYNSL HGGKWTIENF RLWLEGTKGK
TVSDKLFDEI HWIVLHSLKA VASVLINDRH CFECYGYDII IDDTFKPWLI EVNASPSLSA
TTASDRILKY KLVNDVINIV VPNGLIPDAK GSKTVSREQM GQFDLLYDEE KAMEEANPLM
WPVSGSPSRK TAVTSAAEFA GNGLHTSLPS HWLTASDSLP SFTWLCEKSP SRKSVDWHTQ
HVAKPAQPMK RDQFTYRG
//
