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Database: UniProt
Entry: A0A3B4GUU6_9CICH
LinkDB: A0A3B4GUU6_9CICH
Original site: A0A3B4GUU6_9CICH 
ID   A0A3B4GUU6_9CICH        Unreviewed;       470 AA.
AC   A0A3B4GUU6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Tubulin tyrosine ligase-like family, member 3 {ECO:0008006|Google:ProtNLM};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000027027.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000027027.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-
CC         glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180,
CC         Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036933};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67181;
CC         Evidence={ECO:0000256|ARBA:ARBA00036933};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC       {ECO:0000256|ARBA:ARBA00004611}.
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DR   AlphaFoldDB; A0A3B4GUU6; -.
DR   STRING; 303518.ENSPNYP00000027027; -.
DR   Ensembl; ENSPNYT00000027688.1; ENSPNYP00000027027.1; ENSPNYG00000020367.1.
DR   GeneTree; ENSGT00940000154857; -.
DR   Proteomes; UP000261460; Unplaced.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0070735; F:protein-glycine ligase activity; IEA:UniProt.
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; PTHR45870; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR   PANTHER; PTHR45870:SF2; TUBULIN MONOGLYCYLASE TTLL3; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490}.
FT   REGION          449..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  54504 MW;  626E72E1A87EB86E CRC64;
     SLNHEGTRPH RIETGLCLNL RKLHWFDSAD PDTFFPRCYR LAALDERHAF IDDYRRTACT
     SLLKYIVEKD QYCILLCSKK KRESDRCFSF FPSGKKKPSK RQSSPDFLQS LEHSDIDTNL
     ETQQTPGQEW AEFLDSYYLV VHGGAEIDSS DYLVIHCKAM LQRMKIVNPQ LEIEGIHNIW
     IIKPGAKSRG RGIKCANRLD QILDLVKGDP KLIKENKWVV QKYLERPFLI HDTKFDVRQW
     FLVTDWNPLT VWFYKKCYLR FSTQPYTLDS MDSSMHLCNN SIQKSLRPLL QRHGSIPVDN
     MWSVDQFKTF LCTKDREAQW DTVVVPGMKR ALIYALQTAQ DLIESHKNTF ELYGADFMLD
     RDLHPWLLEI NSSPTMAPST PVTAHLCAAV QEDTLRVVLD RRVKRTANTG DFQLIYKKAA
     VKVPQYVPQH LHVEGFLVKC PYSLPPLKSS SCAVPKHRSP SKTRVPQQKK
//
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