TTL10_MACFA
ID TTL10_MACFA Reviewed; 618 AA.
AC Q4R7H0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein polyglycylase TTLL10 {ECO:0000250|UniProtKB:A4Q9F3};
DE EC=6.3.2.- {ECO:0000250|UniProtKB:A4Q9F3};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 10;
GN Name=TTLL10; ORFNames=QtsA-15349;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Polyglycylase which modifies both tubulin and non-tubulin
CC proteins, generating polyglycine side chains of variable lengths on the
CC gamma-carboxyl groups of specific glutamate residues of target
CC proteins. Involved in the elongation step rather than the initiation
CC step of the polyglycylation reaction. Polyglycylates alpha-tubulin and
CC beta-tubulin. Polyglycylates non-tubulin proteins such as nucleosome
CC assembly protein NAP1. {ECO:0000250|UniProtKB:A4Q9F3}.
CC -!- CATALYTIC ACTIVITY: [Protein polyglycylase TTLL10]:
CC Reaction=(glycyl)(n)-glycyl-L-glutamyl-[protein] + ATP + glycine =
CC (glycyl)(n+1)-glycyl-L-glutamyl-[protein] + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:67184, Rhea:RHEA-COMP:17208, Rhea:RHEA-COMP:17209,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:167891, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:A4Q9F3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67185;
CC Evidence={ECO:0000250|UniProtKB:A4Q9F3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:A4Q9F3}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:A4Q9F3}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:A4Q9F3}.
CC -!- DOMAIN: Gln-246 is the main determinant for regioselectivity, which
CC segregates between initiases and elongases in all tubulin--tyrosine
CC ligase family. A glutamine residue at this position is found in
CC elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-
CC chain elongation, whereas an arginine residue is found in initiases
CC TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
CC {ECO:0000250|UniProtKB:A4Q9E8}.
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DR EMBL; AB168848; BAE00952.1; -; mRNA.
DR AlphaFoldDB; Q4R7H0; -.
DR SMR; Q4R7H0; -.
DR STRING; 9541.XP_005545183.1; -.
DR eggNOG; KOG2157; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070735; F:protein-glycine ligase activity; ISS:UniProtKB.
DR GO; GO:0070737; F:protein-glycine ligase activity, elongating; ISS:UniProtKB.
DR GO; GO:0018094; P:protein polyglycylation; ISS:UniProtKB.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027752; TTLL10.
DR PANTHER; PTHR46810; PTHR46810; 1.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Ligase;
KW Magnesium; Metal-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..618
FT /note="Protein polyglycylase TTLL10"
FT /id="PRO_0000324521"
FT DOMAIN 82..479
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 246..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 246
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_part="L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:29973"
FT /ligand_part_note="L-glutamate acceptor residue in protein
FT target"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 289..292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 302..304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 345..346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 425
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 440
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 246
FT /note="Essential for specifying elongation versus
FT initiation step of the polyglycylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
SQ SEQUENCE 618 AA; 68941 MW; 67120433FFBDF583 CRC64;
MGSSQEEGLP CQPSQPDHDT GGHGGPDLEG AGRVSTTPGP PGLLTSHPPA DSDDTDATGP
PAALLEGLLL GDGKPSPHST RPGPFFYIGG NNGAAIISSY CKSKGWRRIQ DSRREDYVLK
WCEVKSRDSY GSFREGEQLL YQLPNNKLLT TKIGLLSTLR GRAWAMSKAS KAPGGTQARL
GKDATAPTLE DLPWTSPGHL RPQRVLRMEE FFPETYRLDL KHEREAFFTL FDETQIWICK
PTASNQGKGI FLLRNQEEVA ALQAKTRRAE DDPIHHKSPF RGPQARVVQR YIQNPLLLDG
RKFDVRSYLL IACTTPYMIF FSHGYARLTL SLYDPHSSDL SGHLTNQFMQ KKSPLYVLLK
EDTVWSMERL NRYINTTFWK ARGLPKDWVF TTLTKRMQQI MAHCFLAAKS KLECKLGYFD
LIGCDFLIDD NFKVWLLEMN SNPALHTNCE VLKEVIPGVV IETLDLALET FQKSLRGQKM
LPLLSQRRFV LLHNGEADVW PRLGGSCSLR RRLPPPTRQA KSSGPPTPRA PDQPGTRRPV
PPPLAPQRPQ LPGPSPDPDS AHDGQPQAPG TGDRHPEQEP SPGTAKEERE EPENARPWGG
HPRPTPHAPA TLPAFRDL
