ID   J9I7H1_9SPIT            Unreviewed;      1129 AA.
AC   J9I7H1;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN   ORFNames=OXYTRI_13051 {ECO:0000313|EMBL:EJY66660.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY66660.1};
RN   [1] {ECO:0000313|EMBL:EJY66660.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY66660.1};
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   -!- 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   -!- 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:EJY66660.1}.
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DR   EMBL; AMCR01020467; EJY66660.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9I7H1; -.
DR   EnsemblProtists; EJY66660; EJY66660; OXYTRI_13051.
DR   OrthoDB; 1937423at2759; -.
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; 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   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:EJY66660.1}.
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1034..1064
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1129 AA;  130202 MW;  45CBB0E2A5E85F71 CRC64;
     MENNYQQNSN FLQKESSLKL SSTSPTNNVL NQRSKTNPLI TGQSTSDTNI SQATNQANNH
     NISNKTNNIN GQSSGNTTTY LESSALERLK NIQNFVKRSW QGVQVDHSGR PGTASIVNKK
     RYNPISENQL EDEERFRLIL KLAIKLKEID DERQNHNQHQ NSSTQQNFFN TESRADTYKQ
     SYGQQLEFLQ FKGVAMNQLL SNNIPQQGYA KSYQVESGEL LYKIFRGETR LVRSVLEING
     FKYTESHEWN ILWANSHCKS YLYEGLNEYQ KINHFPSSNE ITRKDKLCLN LVKMQEKHGK
     HNFDFIPDTY VLPDEFGDFY AHYQKVKQND PKHNIWIVKP ANLSRGRGIY LIDDIAEVSV
     DDISVISRYI QNPLLINGHK FDLRIYVAVT SFDPLRIYVY KEGLARFASE QYSNKVNKDN
     KYQHLTNYSV NKNNENFIQN ENLDNDDFGF KWSLGAFCKH LESIGIDMNL FWSRIYDVII
     KSIISGENQI FNAVKKTCIH KTNCFELFGY DILIDSDLKP WLIEINLSPS LACESPLDIT
     IKSSLISELM TLVGVKKFDR RIESQNKMKN RMKSYMNRGK SMNSRYANIF NPLKERNKYS
     GGVVFSLNGG SSLSSQQDNF YQQPNSSTLQ MIERLAESDL DISENIELVK RLAGIKHKEI
     LRETIAEYQR KGNFVRIFPS NGCNSYDQYF QQQSLIKKSY KVSQNQGFSS LKEEVYPPHT
     PLESTYQANI RSQNDMTRPV DLDQSLGQIN QNTNNKVMIT GDDILIEYCE RLMFALKSIN
     DGLLRIQWKQ ALDKFLNHQV WQSQNSRPDS ALQNTKWQRL ECRIVEMQER RKRLIKSNYK
     KEGRLSDFEQ GYKNMLNKKN LIVKKFSNIQ LENLLKTSTK NVAQEIVMCL IPNSIGLNQP
     CGILVEMDQQ FNLSLKARQE ERKKISTDTE NSMANAETED EDLSFINQKN RPNRGNKLSK
     KIIIGGQGQQ DSMLIKEARS NNFFKEQIIS PKSIVGVNGL LNQRPMSNSV ASRGSVQPKS
     AQKFLRLKQP HNNRGPESIL NNHKSSSKQL QRDNQSTDRV NKNTIPGLQN FTYFGQSNYL
     NRMINQHQLE NPNAAYQNLE INNLNRIMSG NSLNNGLSTT LSQLKINKH
//