ID   A0A2Y9NGV8_DELLE        Unreviewed;      1299 AA.
AC   A0A2Y9NGV8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN   Name=TTLL5 {ECO:0000313|RefSeq:XP_022432206.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022432206.1};
RN   [1] {ECO:0000313|RefSeq:XP_022432206.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022432206.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_022432206.1; XM_022576498.2.
DR   Proteomes; UP000248483; Unplaced.
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:UP000248483}.
FT   REGION          416..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          835..875
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1005..1044
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1103..1132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1221..1299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..618
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        835..850
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1005..1023
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1103..1128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1299 AA;  144720 MW;  9E2A47AB6B1BB95E CRC64;
     MPVVMARDLE ETAASSEDEE AVSQEDHPCI MWTGGCRRIP VLVFHAEAIL TKDNNVRVIG
     ERYHLSYKIV RTDSRLVRSI LTAHGFHEVH PSSTDYNLMW TGSHLKPFLL RTLSEAQKVN
     HFPRSYELTR KDRLYKNIIR MQHTHGFKAF HILPQTFLLP AEYAEFCNSY SKDRGPWIVK
     PVASSRGRGV YLINNPNQIS LEENILVSRY INNPLLIDDF KFDVRLYVLV TSYDPLVIYL
     YEEGLARFAT VRYDQGTKNI RNQFMHLTNY SVNKKSGDYV SCDDPEVEDY GNKWSMSAML
     RYLKQEGKDT TALMAHVEDL IIKTIISAEL AIATACKTFV PHRSSCFELY GFDVLIDSTL
     KPWLLEVNLS PSLACDAPLD LKIKASMISD MFTVVGFVCQ DPAQRASTRP IYPTFESSRR
     NPFQKPQRPV SAQFQSSSTK QRCRPLSASD AEMKNLVGSA REKVPGKLGG SVLGLSMEEI
     KVLRRVKEEN DRRGGFIRIF PTSETWEIYG SYLEHKTSMN YMLATRLFQD RVAVDGAPEL
     KVENMNLRAK LHAALYERKL LSLEVRKRRR RSGRLRAMRP KYPVITQPAE MNVKTETESE
     EEEEVALDSE DEEQEASQEE SAGSLGENRA KHTPSLTVMV ENSPKENAVK VPEWNDKGEH
     CCKTETQEPE PKFNLMQILQ DNGNLSKVQA RIAFSAYLQH VQIRLMKDSG GQTFSASWAA
     KEDEQMELVV RFLKRASSNL QHSLRMVLPS RRLALLERRR ILAHHLGDFI IVYNKETEQM
     AGKKSKKKLE EEEEDGVNTE NFQEFIRQAS EAELEEVLTF YTQKNKSASV FLGTHSKSSK
     NSNSFSDSGA KGDHPETMEE VKIKQPKQQQ ATEIHSDKLS RFTTSAEKEA KLVYTSSSST
     SFSGPTATLL QKIPNTHLSS VITTSDLSPG PGHHSLSQIP PAIRSMAHQP AILLSTVPGS
     ASPSIHPGTQ NVLSPAGLPR CRSGSYTIGP FSSFQGAAHI YSQKLSRPSS AKAGSCHPNK
     QHSGVAKTQK EGEDGSSYSR RYNPSTVTAE LQRLAEKQAA RQYSPSTHVS LLTQQVTHLN
     LASGVINGGS ASTPHTLWPV ISPSGPTWSI QSDPQAPESH SAPPGSRSLQ TGGFAWEGEV
     KNSAYSKATG VVPQHRCHST VGSYQLHFAL QQLEQQKLQS RQLLDQSRAR HQAIFGSQTL
     PNSNLWTINN GAACRISSAT ASGQKPTTLP QKVVPAPSSS SSLVPKPPSN HKQVLRKAAS
     QRASKASSTE GQLDGLQSSL NSAAFVPITS STDPAHTKR
//