ID   A0A452HMS2_9SAUR        Unreviewed;       274 AA.
AC   A0A452HMS2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Tubulin tyrosine ligase like 8 {ECO:0008006|Google:ProtNLM};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000016231.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000016231.1}
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; A0A452HMS2; -.
DR   STRING; 38772.ENSGAGP00000016231; -.
DR   Ensembl; ENSGAGT00000018531.1; ENSGAGP00000016231.1; ENSGAGG00000012179.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:SF3; PROTEIN MONOGLYCYLASE TTLL8; 1.
DR   PANTHER; PTHR45870; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020}.
SQ   SEQUENCE   274 AA;  32550 MW;  A8145165C02C7974 CRC64;
     MHKQDIDGDH NIWIIKPGAK SRGREIVCKN RLDDILKLVE ATDQFPVKDH KWVVQKYIET
     PLLIYDTKFD IRQWFLVTDW NPLTIWFYKE SYLRFSTQRF SLDNLDSSIH LCNNSIQKHY
     KNAADRNPLL PWHNMWTSTK FQEYLQKRGR GNMWRNVIYP SMKKAITYTM RMAQESVEAR
     KSSFELYGAD FILGEDFKPW LIEINTSPTM LPSTPVTAEL CAQVQEDTIK VVIGKKRDKN
     WDTGKFELLW RQVRIILHHS LIRYQRGSHV SLDL
//