ID A0A183ADJ4_9TREM Unreviewed; 784 AA.
AC A0A183ADJ4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN ORFNames=ECPE_LOCUS5029 {ECO:0000313|EMBL:VDP74353.1};
OS Echinostoma caproni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC Echinostoma.
OX NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0000504101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ECPE_0000504101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP74353.1, ECO:0000313|Proteomes:UP000272942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Egypt {ECO:0000313|EMBL:VDP74353.1,
RC ECO:0000313|Proteomes:UP000272942};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; UZAN01041876; VDP74353.1; -; Genomic_DNA.
DR WBParaSite; ECPE_0000504101-mRNA-1; ECPE_0000504101-mRNA-1; ECPE_0000504101.
DR Proteomes; UP000050740; Unplaced.
DR Proteomes; UP000272942; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000272942}.
FT REGION 481..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 88146 MW; 663791EE81C8077B CRC64;
MLTDFHKVNH FPRSYELTRK DRLAKNVQRM QQIKGLRQFD FVPQTYILPE EFRDFCKGFM
QDKGPYIVKP IASSRGRGIH IVSHPEEIPY EEPVIVSRYI SNPFLLDGFK FDVRIYAAVT
SYEPLVVYIY EEGLVRFATV RYQVGNKHLK TQCMHLTNYS VNKKNFEFVQ NDDANVEDFG
NKWSLGALLR FLKSEGADVT GLMVRIEEII IKSFLCVVSP IASACAMFQA CRSKCFELYG
FDIIVDEDFR PWLLEVNLSP SLACDSPLDF KVKSHMITDL FNLVGIVCHD PTRKTQGGMN
SLHMKADGHA AVPPKQPTYF VSAEEQINER GNSAANSKHD SFGHSVARSN SCCSTSDGVA
IGLAGVAISH LLPKGVSVDE TRLMRRLQEE SARAGGWIRL IPNPEVWEQY ASIWPNDSTP
WYMSHDRRSY GYAMDGSRTS LTDTGHGERR FPPNSLLASA FTASMAVTTL YGLVTTVYSH
EASDSSDGDS DADSDSWSQS SNTTSSPRTR IPCAGQLKFL HPNSSTISID LTTYLHHLAN
HRGSGDFQPA LVHGPRVPSR NAVTRPRLAL HNMPHGQMQG CLNSLLMGEL ESTEIPREQC
QRVIVCYTHT LGHMPFFLRK LGEPPVHLPG VCLRPGCKHD RARHTTPCGI YQGTRYPESN
PPTHIDPARS GLNPEDLIPS NKLDSPGPLH KAPNRHSRMD GAHRNTQEHE SLDSKSGTFD
LDPAKLSATQ ARHAFAAYLS RIQSRMLFES KQPMSQLIHS RTALQKEHKQ VDLMVRHYLL
QRWL
//
