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Database: UniProt
Entry: J9IDB1_9SPIT
LinkDB: J9IDB1_9SPIT
Original site: J9IDB1_9SPIT 
ID   J9IDB1_9SPIT            Unreviewed;       784 AA.
AC   J9IDB1;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Tubulin-tyrosine ligase family protein {ECO:0000313|EMBL:EJY72198.1};
GN   ORFNames=OXYTRI_06805 {ECO:0000313|EMBL:EJY72198.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY72198.1};
RN   [1] {ECO:0000313|EMBL:EJY72198.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY72198.1};
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:EJY72198.1}.
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DR   EMBL; AMCR01015341; EJY72198.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9IDB1; -.
DR   EnsemblProtists; EJY72198; EJY72198; OXYTRI_06805.
DR   OrthoDB; 100598at2759; -.
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; PTHR46069:SF1; LIGASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR46069; TUBULIN TYROSINE LIGASE; 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:EJY72198.1}.
FT   REGION          48..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  91779 MW;  2824A126E9621275 CRC64;
     MQQLQNQIIQ LNGLKSNIYE EAGMRFSQNI QHRKQLSRIN IKGIQINSQL TRQPQTSSQS
     QSDINRQNSS NQKRTSTANH QSSNKYLRYS NRQQLQDTNA IPNSGLQITH NKTNKTQDLV
     NLNNPQTSYK DNISSNTVSV PTSANTAVNS ENKSGVIKQI EIKPKSSLLQ SRMSKKNSKE
     KKGNGQAKNQ HYDHIINQVI RYSNDFIVET FIRPNDQPAN IEKIKSICNF FGFKLPKNII
     ADVQQVKSKD FQIFSKEKIL QHLYLTLNAS NQADLTQIQQ QQAQQTRKFH IGRGNNYQLV
     RSIFKQRWWW QINQDGEEFE TANFIWTSWR KNELLNSLKP SGDATNQQSH QHWEDGKMRI
     YSKLEDNFHL SNKKALFFNM TQYYKLIGKE PFEFLPLTFH IEHGIEDPEY EKFKQYFNQI
     EQDKIDKKRL LEEKKRKYAQ EHPDDEYDSE EEVDEEQFYG VKIPKNIWIM KPGENSNRGT
     GIFVCNTIRE IQLEINSAAK KAHTHIIQKY IERPLLIHNR KFDIRVFGMM TSINGSMKGY
     FYEDGYIRTS CKEFSLDNLQ NRFIHLTNDA VQKKSDDYGK FENGNKLSYQ NFQKYLDTNM
     PLENINFHKQ ILPQIRDIIS DTFKATFMKI DPHRRVSSFE IFGYDFMIDD DFRVYLIEAN
     TNPCLELSCP LLARIIPAML DSAFRLSVDP LFPPPDFNMA RKNTLHEIMP INKFELVFDE
     SIEGQKLREI LKYQEIMTLK IDQNDEFEEE SNTSQNNDAA SNDGGNDHDI VQIEDTGLEF
     NDEE
//
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