ID   A0A078B592_STYLE        Unreviewed;      1099 AA.
AC   A0A078B592;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Ttl domain containing protein {ECO:0000313|EMBL:CDW88442.1};
GN   Name=Contig9025.g9650 {ECO:0000313|EMBL:CDW88442.1};
GN   ORFNames=STYLEM_17563 {ECO:0000313|EMBL:CDW88442.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW88442.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW88442.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW88442.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CCKQ01016569; CDW88442.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078B592; -.
DR   EnsemblProtists; CDW88442; CDW88442; STYLEM_17563.
DR   InParanoid; A0A078B592; -.
DR   OrthoDB; 180115at2759; -.
DR   Proteomes; UP000039865; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000039865}.
FT   REGION          40..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1099 AA;  127447 MW;  DC377B325CEF3E0F CRC64;
     MSIMSSTNNL QTKTKQQIDG VAFSFSEEKV QAQERAFIIR NPSKPRDQTV NNNINHNFNN
     STSGNYDNIS SLLKRQSIAT QDDTTNNKTQ FPSHQKQQLI KEEYQMGLQQ QTVLGYQHQH
     SLPSKFILKK DSVSSINYQN RNNYSLINQV LKNIQQQDSK NQSYYHTEED EKLPQLRKGK
     QQTSQSKEFQ KFQSDLNYQM HHSGGKQEAE NGYTNAEKRS IGQTKIRKAA KSVNPISKGH
     QQLIYTQGSQ TLKQATQRQN TYTELVMNNH SQVTVIDDNY MMSKGRLPPQ KLRQIDEELN
     NTGNLTPNNK TDNSQSLIKQ EGSSRQNKLE RLKIDQDMIN FQMGQQQYTV NTPNSKGQVK
     NVEKKIKLKK QNELKQYKTK LKNQYKRSID EISDLGSMGA AYIGSAFSNT STLPFSKQSQ
     LTSTNASGMK KILGFSQLTS TRNLIGDGFK FQVLKGNNAK LVQRVLSNRY WWTEMSTYSK
     PPQFKWSPCS IKADFPKMNS YKQIINHFEN HREITRKDEL LINLTHYFSN QNLNVFDYVP
     VTFQIIIPEG KSQNLELSLK KFQLCYDTLD RNKYTVLDIL RSSKNQIASQ NFADIEKSLQ
     IKYQLRNHFQ KYNPLQIVMP VCHFVGGNMW VLKTTSQNRG RGIHVFKSYK QLKQLIRQYI
     FQSNDESSYQ NKGSVPGGTQ SNGFHYIPKT LNFVIQKYIE RPMLINKRKF DIRVWVLVNQ
     DMDVFFFKEG YLRTTCAEYK LDNVEDQYIH LTNNAVQRNA SQYGQFEDGN QLSFQDLQRY
     IQEHYKGQVK IDVYEDLVED MKYQVVKTLE SIKKKLNSEN RKFCFEIFGF DFIIDQDFNV
     WLIECNTNPC LDESSGLLRI LLPRMLDDAF KLTIDKIFPN PKDVYLQNSN NISLKITSKN
     NALAQKDPLQ RRDTDYKFSK SQSNWKNLKT SYADQANYIG SQDSSIYPIE GYSDYANLWD
     KLMNLTSGSN YLKVNERRIR SDTVLYSPEG VEFFATSFKS YKEHQSMKAQ QLKSVTNRLS
     PNFLILQTSS QINNSIIDKN DQSHNESKIA GGGRNNLVTA DSNMLLISGK NTEIQIDEKY
     KKYVKLTQSS EFKNQSQLD
//