ID A0A0V0QND1_PSEPJ Unreviewed; 584 AA.
AC A0A0V0QND1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Tubulin-tyrosine ligase/Tubulin polyglutamylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PPERSA_04223 {ECO:0000313|EMBL:KRX03671.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX03671.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX03671.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX03671.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
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:KRX03671.1}.
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DR EMBL; LDAU01000129; KRX03671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QND1; -.
DR EnsemblProtists; KRX03671; KRX03671; PPERSA_04223.
DR InParanoid; A0A0V0QND1; -.
DR OMA; HINISNC; -.
DR OrthoDB; 5487479at2759; -.
DR Proteomes; UP000054937; 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; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR PANTHER; PTHR12241:SF147; TUBULIN POLYGLUTAMYLASE TTLL7; 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:UP000054937}.
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 69672 MW; CD031561D16B8C0A CRC64;
MDNSKQNVEQ DQQDDQMILK NNEDQKQEQK NNDQSHQNQN VENHNKQEKP PFSIMTLQQL
VDKPRKIRQH KKITIDLTKC QYEILREVAQ LFNWNIIDNS ENYENEVKSD FNIKWYDSYI
QEDQLRALLP YQKINRFPGS NNLGRKNLLA KYLIKLQKVH PEDYSFFPRT WLLPNQLEEL
RSFTQKCNFS KYLIVKPENQ SQGKGIYLTK KIDKNLDSQD HFVIQEYITN PYLIDNLKFD
LRIYVLLKSV CPLKIFIYKE GLVRFATQEY AKPNKQNQQN LMMHLTNYAI NKKSDKFQFN
TNQDDDNKGH KRSLSSFLIE LQQKGINVEN LWDQIKQVVV KTFCSCIPNI QHIYKSCQPK
EENNEISFEL FGFDIFLDEK LKPYLLEVNH TPSFSTDTPL DHQIKKSLIL DTLILENIMW
KTRVRYFDQK NNANPSIKGG SNNRMSKEDI QIQKEKRITW EQNNIGGYEQ IYPELYDEEL
QKQYDKFKQS AQDQFDQFSG ANIQRAQKKE YKKELPPIKI NGANTNKFTQ NQQSNKTTNN
NQNAQKQYKS QLRYTASHYW QLEYIKKQTP HQQRQYISLI QICQ
//
