ID   R7V9K7_CAPTE            Unreviewed;      1116 AA.
AC   R7V9K7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN   ORFNames=CAPTEDRAFT_190779 {ECO:0000313|EMBL:ELU15162.1};
OS   Capitella teleta (Polychaete worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Scolecida; Capitellidae; Capitella.
OX   NCBI_TaxID=283909 {ECO:0000313|EMBL:ELU15162.1};
RN   [1] {ECO:0000313|EMBL:ELU15162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELU15162.1};
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(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};
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DR   EMBL; KB293952; ELU15162.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7V9K7; -.
DR   STRING; 283909.R7V9K7; -.
DR   InParanoid; R7V9K7; -.
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;
FT   REGION          388..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1019..1044
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..607
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..632
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1116 AA;  125395 MW;  8DFD869E0A69C12F CRC64;
     MLANSKSPSS IVWTGYGKKT PVLVFKAGNI VNKSAEIKAI GEKHHLAFKI VKTECKLLRT
     VLYAHGFHEV AHPNSNDFNL LWTGSHLKPY VLRSLQEFQK INHFPRSYEI TRKDRLFKNI
     QRLQQTKGFK NFDFIPSSYI IPSEFQEFCS AFLKDKGPYI VKPIASSRGR GIFLINHPEQ
     VPLDETMIVS KYVPNPLVID GFKFDIRLYV AVTSYDPLII YLYEEGLTRF ATVKYEKSTK
     HIRNNCMHLT NYSVNKKSND YVKNDDPDVE DFGNKWSLGA MLRYLRSIGK DTTAMMMRIE
     DVLIKTLLAA EVPIATACKM FMPFRGNCFE LYGFDILVDE NLRPWVIEVN LSPSLACDSP
     LDLKIKSNMM ADLFSLVGFV CQDPMVRKTP STKLPDGKPS SRSQSSMSRP YSSHGQRRDL
     RWTAKKGRPS SASSNKGSGG TNVIRATGLT GEEIRVVRRA KEEYQRRGGW VRIFPSPESW
     ELYGSIHLHS AQNPQLQLSS QPDQALAAAL QRSSQYERKL SCLGDKRKAP KSNGFRIQNT
     VDTSTSGAPF AKGGTFKGTL VQGVLPDRAA PLNPPAPQLQ PKVTRKSKPA ELVIKLPEKR
     MPSPPSEKTD DCKVSPPPPL LQSPPPPTSA FQSKPEPRFD VVSLLETGKT LSKVQARFAF
     ATYLMRVQHR LMAQTSAGED DDVEAANEQM DLVLRFLKRA AGNLQQAFKV VVPSRKLVLN
     DRRRILAKQL GDFVHIYNKE TDVLRQKNHL DKRQSKRPPS FTQNEGLDDG RFHQFVNSAG
     ENDLEEVLTT YTKINKSASI FLGSKSDGSN SHQYHHLDTT LVRRKDSFDG SRNPVGAVEE
     VQVTRATDGD VALMDSSRPA TYLRAVTIYS NKSGLRGLHG GRPSSASMAR GNKVDPYDEE
     AINSALQRLA VRQQQRQYAA SSSLVALSQE DVAKMTRERK GANETFQSFV TELEHPSMNV
     SQHHQQLRQM RMGEQSRALL EHSKAKHQAM VAQAHAAKSH PPIIFHSVSR DSLLPLNQEE
     DESFSVEPNR APKPPIKPSS VRKPTSIHRM ARTNLLDNSG SDYYNKVKYD HHTGTSKPVY
     SSGHNIVQQD IPEQNGKFRV NLVEFPVQAI FGKAMH
//