ID   F1RXQ1_PIG              Unreviewed;       789 AA.
AC   F1RXQ1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2022, sequence version 5.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Tubulin tyrosine ligase like 8 {ECO:0000313|Ensembl:ENSSSCP00000001050.5};
GN   Name=TTLL8 {ECO:0000313|Ensembl:ENSSSCP00000001050.5,
GN   ECO:0000313|VGNC:VGNC:94572};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000001050.5, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000001050.5, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000001050.5,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000001050.5}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; F1RXQ1; -.
DR   STRING; 9823.ENSSSCP00000001050; -.
DR   Ensembl; ENSSSCT00000001072.5; ENSSSCP00000001050.5; ENSSSCG00000000982.5.
DR   VGNC; VGNC:94572; TTLL8.
DR   eggNOG; KOG2157; Eukaryota.
DR   GeneTree; ENSGT00940000162265; -.
DR   HOGENOM; CLU_010131_5_4_1; -.
DR   InParanoid; F1RXQ1; -.
DR   TreeFam; TF313087; -.
DR   Reactome; R-SSC-8955332; Carboxyterminal post-translational modifications of tubulin.
DR   Proteomes; UP000008227; Chromosome 5.
DR   Bgee; ENSSSCG00000000982; Expressed in testis and 6 other cell types or tissues.
DR   ExpressionAtlas; F1RXQ1; baseline and differential.
DR   GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0036126; C:sperm flagellum; IEA:Ensembl.
DR   GO; GO:0070736; F:protein-glycine ligase activity, initiating; IBA:GO_Central.
DR   GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR   GO; GO:0003341; P:cilium movement; IBA:GO_Central.
DR   GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
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:UP000008227}.
FT   REGION          220..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          764..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..789
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   789 AA;  89511 MW;  9E4BC4D7516D72D6 CRC64;
     RREVRAAARS VLISVCFSFA ELKRGLAQDL ISSPKLDRYK LARQLTDKAV KEKKIFSIYG
     HYPVVRAALR RKGWVEKLHL LPRVGPNVDD DENKQAEGKE SQEAALEKTD DIHAVMSRLV
     RNEVPYFLWT IRRDAVDHHS LRCEQTLNHY GKTASFTTKI GLCVNMRSLP WYVQANPDSF
     FPRCYGLCTE SEKQEFLDDF RRTVASSILK WVVSGQNHSR SKPRSRREEA GDTEPGREQA
     PEAAGPQLRG LSEQLVDAAC KVCEAYLGRL EHEDIDLPED ATKDLTEDEW KELTRQYYAL
     VHGEAFISNS RSHFSQCQAL LNKITSVNPQ TEIDGLRNIW ILKPAAKSRG RDIVCMNRVE
     EILELVAADR LEAREHKWVV QKYIETPLLI YDTKFDIRQW FLVTDWNPLT IWFYKESYLR
     FSTQRFSLDN LDSAIHLCNN SIQKHLKNDK DRSPLLPCHN MWTSTRFQEY LQKRGRGAVW
     GSVVYPSMKR AIANTMKVAQ DHVEPRKNSF ELYGADFVLG RDFKPWLIEI NSSPTMHAST
     PVTAQLCAQV QEDTLKVVVD RRLDRNCDIG NFELLWRQPA VELPPVQGSD LLVEGLALRK
     AQKQIPPMAN CGFASPLTNV QPLKERGPSA MPDLARGPPR RDLRLKDEKV FPCAFPVPLK
     RRAEGSARAQ HVYSEPGRKI ELPTWRVQHP DDKAPSTALA KAEPDKHLAP NLSNVCPLPA
     VLPRAKTMES ALFQPPRPPG NAWCLRPTSP GAACSASWRA GWGLRPGSNL SSEQRSGTQA
     PSGPARLSE
//