ID A0A3P8R409_ASTCA Unreviewed; 894 AA.
AC A0A3P8R409;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000036209.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000036209.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000036209.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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};
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DR AlphaFoldDB; A0A3P8R409; -.
DR STRING; 8154.ENSACLP00000036209; -.
DR Ensembl; ENSACLT00000037071.1; ENSACLP00000036209.1; ENSACLG00000024537.1.
DR GeneTree; ENSGT00940000162910; -.
DR OMA; TRLFQDX; -.
DR Proteomes; UP000265100; Chromosome 19.
DR Bgee; ENSACLG00000024537; Expressed in testis and 5 other cell types or tissues.
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 204..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 99563 MW; 94FAD1EA4834AFB9 CRC64;
MTENILVSRY INNPLLIDGF KFDVRLYVLV TSYDPLLIYV YEEGLARFAT VKYDRTSKNI
KNTFMHLTNY SVNKKSSDYV SCDDPEVEDY GNKWSMSAVL RYLKQEGKDT TSLMKQVEDL
IVKAVLSAEL QIATACKTFV PHKTNCFELY GFDVLIDSNL KPWLLEVNLS PSLACDAPLD
LKIKASMIAD MFSLVGFVCQ DPLSRQPRSD QRTQRPTSTN ISETEDLKDK RGAKHGQGDS
TLNLTVEEIR VLRSIKEEYE RRGGFIRIFP TADTWELYGG YLESKTSMNF VLANRLFHGR
NVNGNVQLQV DVVHGCHVVQ YERKLLSLEA RKRRQRHLTH GSAARKKKSG KESKASLTEN
SSQEGEECAQ EEVKQALEPV SHKALVAEQR KQVATPLERC HSKAQSSSEA AVHNASPTVN
LLNILQQGWE LSKVQARIAF SSYLQRVQQR LLAESRDNTI SAWPDNGNDQ MELVIRFLRK
AASNLQQNIK VVLPSRQLPL QDRRRILSHQ LGEFIHCYNK ETEHMVKKQE ISKEERCVNP
KVFQEYISAA SENDLEEVLT FYTQKNKSAT VFLGTKVRGI KKDVREANAS RDSGNCDNSK
SLAVEADSEL SLLTGKVSSD SDNKATDGQP SFCLLPEDIR AEVRMVKTQP EVQSSQHRSS
FPVTLDCVHN HVQHCSPASL PLHCPPPPPP PQPPSYAQSL AKSHLCHSES ISDPPAYTSA
HVVTQPPRVL WTAAPTGSNA ATTGPSTQVL RRIQSFTSSM AGSAAASSVP SATHIYSQKL
SRPTSAGQVI RRSTSSKLKS NSVGAFRELS TLTAQAQSNQ QAFISALQKL ADKQVAHHYA
SSSHINLLTQ HLTNLNLANK MLSRESFTLN PKAATIQGPV RAVHPETDLP NSTG
//
