ID A0A0L0DFL0_THETB Unreviewed; 445 AA.
AC A0A0L0DFL0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Tubulin-tyrosine ligase family protein {ECO:0000313|EMBL:KNC50951.1};
GN ORFNames=AMSG_07203 {ECO:0000313|EMBL:KNC50951.1};
OS Thecamonas trahens ATCC 50062.
OC Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC50951.1, ECO:0000313|Proteomes:UP000054408};
RN [1] {ECO:0000313|EMBL:KNC50951.1, ECO:0000313|Proteomes:UP000054408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC50951.1,
RC ECO:0000313|Proteomes:UP000054408};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL Submitted (MAY-2010) 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; GL349463; KNC50951.1; -; Genomic_DNA.
DR RefSeq; XP_013756647.1; XM_013901193.1.
DR AlphaFoldDB; A0A0L0DFL0; -.
DR STRING; 461836.A0A0L0DFL0; -.
DR EnsemblProtists; KNC50951; KNC50951; AMSG_07203.
DR GeneID; 25566177; -.
DR eggNOG; KOG2157; Eukaryota.
DR OMA; DWNFYWS; -.
DR OrthoDB; 7265at2759; -.
DR Proteomes; UP000054408; 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: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: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 Ligase {ECO:0000313|EMBL:KNC50951.1};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054408}.
FT REGION 381..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 50066 MW; 74DC3EB6E61B8397 CRC64;
MDSRVRCKVD HAKEVIVTNF RKRRWVIVDD DDDTWHFYWG TGSAARNTFN PEIGFRLADN
QFINHFPNHF ELTKKDLMVK NIKRYRKELA KEGRMAEYEA SDFLPTTYTL PADYHLFIEE
YKRRPATSWI VKPAGGSLGS GIFIMKKLSQ LRKWKAQKQA AGSSVKWVVS QYIDNPLLIG
GRKFDLRIYF LVLSYRPLRV YMHSMGFARF CTAKYDTEVL DPEDLMQHLT NVAIQKHGDE
YNSAHGGKFS LQNLRLFVEG THGRAAARKL FADIKAIAFH AFSAVKNVIN SDRHCFECYG
YDVLVDDTLK PWLVEVNASP SMSATTQTDR TVKHTVINDV INMVLPAGFP DLAACKLGVG
SNLDAPMGGF ELVVDELKDA ARPGSASPRP PPSSAAASTR VRRARARSRT RGSTAGRPSS
AAGTRTPRSR PASRTSSSRP ASRRR
//
