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Database: UniProt
Entry: J9HR69_9SPIT
LinkDB: J9HR69_9SPIT
Original site: J9HR69_9SPIT 
ID   J9HR69_9SPIT            Unreviewed;       710 AA.
AC   J9HR69;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Tubulintyrosine ligase family putative {ECO:0000313|EMBL:EJY68372.1};
GN   ORFNames=OXYTRI_11014 {ECO:0000313|EMBL:EJY68372.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY68372.1};
RN   [1] {ECO:0000313|EMBL:EJY68372.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY68372.1};
RX   PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA   Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA   Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA   Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA   Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA   Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT   with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
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:EJY68372.1}.
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DR   EMBL; AMCR01018878; EJY68372.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9HR69; -.
DR   EnsemblProtists; EJY68372; EJY68372; OXYTRI_11014.
DR   OrthoDB; 7265at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0070735; F:protein-glycine ligase activity; IEA:UniProt.
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; PTHR45870; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR   PANTHER; PTHR45870:SF2; TUBULIN MONOGLYCYLASE TTLL3; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000313|EMBL:EJY68372.1}.
FT   REGION          39..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          202..229
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          425..457
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   710 AA;  83657 MW;  DE60B713CB11BA36 CRC64;
     MTKFRIKRLK LSQKSNQQLI KAKINLKLNQ VNKHYRLNAH QQSKKKEIRQ QAQLSRTQAK
     RNQKMLKDHL KKLEEKKYQD NSLKELERKR FQEAKIRLRN YVIYHSIPSA SLIQNYSTIP
     DYDYEEERQL ERVRLLNYFK HRYFTFIQIM KDSIRARKVQ SKSSNVEIPF LGRQSSTINH
     EEQKKIFSLA SQGQQKIQSV QNLTAKQAQE AAEEEIQKYL RNNNLASDTK LFTICGHYDD
     VRQELLRRGW VEHVRQADEK FNSLAFHFLY ATKSKDIFRI HNISSIQHTN HFEGAKSLTT
     KVGLTHNMKN LVLKHNIDID SSFPQSFDLS DLTGDEVKDW KEDFKYCQVI SYLKQAINFN
     KQSLAKNIDK IVIAISICEQ RLKANNDSIF QITEWGEENK PISDDIHEIM SDMKLLPNFG
     TQPWFRKLQK QYKEINEENA KATIKQLLEQ VSQLHGRQYH LIGNKNAWIL KPGGKSRGRG
     ITIHNKIESI LQAVQSSSDS IWVIMKYIEN PLIIHNKKFD IRQWVVVTSW DKLKIWYFDE
     CYLRFTSDDY DPNRLHDKFM HLTNNCVASQ SENFNNSVIE GNMWDSTSFR DHLCSQYSNI
     DEDIYKNRLQ PQIKQGVIAS MLAARAMVIH KENTHEMFGY DFMVDTDFNV WLIEVNSSPS
     MEHSTKVTQR LVKSILTEIP HLVIDCQNGT RFSDEMHQKC GKFELIFSEE
//
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