TTLL1_MOUSE
ID TTLL1_MOUSE Reviewed; 423 AA.
AC Q91V51; Q3TGC8; Q543S4; Q8C0A2; Q91ZG1;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Polyglutamylase complex subunit TTLL1 {ECO:0000305};
DE EC=6.3.2.- {ECO:0000305|PubMed:15890843};
DE AltName: Full=Tubulin polyglutamylase TTLL1;
DE AltName: Full=Tubulin polyglutamylase complex subunit 3 {ECO:0000303|PubMed:15890843};
DE Short=PGs3 {ECO:0000303|PubMed:15890843};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 1 {ECO:0000303|PubMed:20498047};
DE AltName: Full=p49 {ECO:0000303|PubMed:15890843};
GN Name=Ttll1 {ECO:0000312|MGI:MGI:2443047};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Kidney, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY AS PART OF THE TUBULIN
RP POLYGLUTAMYLASE COMPLEX, AND 3D-STRUCTURE MODELING.
RX PubMed=15890843; DOI=10.1126/science.1113010;
RA Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S.,
RA Gaertig J., Edde B.;
RT "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT family.";
RL Science 308:1758-1762(2005).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=17499049; DOI=10.1016/j.molcel.2007.04.012;
RA van Dijk J., Rogowski K., Miro J., Lacroix B., Edde B., Janke C.;
RT "A targeted multienzyme mechanism for selective microtubule
RT polyglutamylation.";
RL Mol. Cell 26:437-448(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20498047; DOI=10.1073/pnas.1002128107;
RA Ikegami K., Sato S., Nakamura K., Ostrowski L.E., Setou M.;
RT "Tubulin polyglutamylation is essential for airway ciliary function through
RT the regulation of beating asymmetry.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10490-10495(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20442420; DOI=10.1177/0300985810363485;
RA Vogel P., Hansen G., Fontenot G., Read R.;
RT "Tubulin tyrosine ligase-like 1 deficiency results in chronic
RT rhinosinusitis and abnormal development of spermatid flagella in mice.";
RL Vet. Pathol. 47:703-712(2010).
RN [8]
RP FUNCTION.
RX PubMed=22170066; DOI=10.1074/jbc.m111.309138;
RA Berezniuk I., Vu H.T., Lyons P.J., Sironi J.J., Xiao H., Burd B., Setou M.,
RA Angeletti R.H., Ikegami K., Fricker L.D.;
RT "Cytosolic carboxypeptidase 1 is involved in processing alpha- and beta-
RT tubulin.";
RL J. Biol. Chem. 287:6503-6517(2012).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=23897886; DOI=10.1083/jcb.201305041;
RA Bosch Grau M., Gonzalez Curto G., Rocha C., Magiera M.M., Marques Sousa P.,
RA Giordano T., Spassky N., Janke C.;
RT "Tubulin glycylases and glutamylases have distinct functions in
RT stabilization and motility of ependymal cilia.";
RL J. Cell Biol. 202:441-451(2013).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29593216; DOI=10.1038/s41467-018-03008-2;
RA Ye B., Liu B., Hao L., Zhu X., Yang L., Wang S., Xia P., Du Y., Meng S.,
RA Huang G., Qin X., Wang Y., Yan X., Li C., Hao J., Zhu P., He L., Tian Y.,
RA Fan Z.;
RT "Klf4 glutamylation is required for cell reprogramming and early embryonic
RT development in mice.";
RL Nat. Commun. 9:1261-1261(2018).
RN [11]
RP FUNCTION.
RA Mahalingan K.K., Keith Keenan E., Strickland M., Li Y., Liu Y., Ball H.L.,
RA Tanner M.E., Tjandra N., Roll-Mecak A.;
RT "Structural basis for polyglutamate chain initiation and elongation by TTLL
RT family enzymes.";
RL Nat. Struct. Mol. Biol. 27:802-813(2020).
CC -!- FUNCTION: Catalytic subunit of a polyglutamylase complex which modifies
CC tubulin, generating side chains of glutamate on the gamma-carboxyl
CC group of specific glutamate residues within the C-terminal tail of
CC tubulin (PubMed:15890843). Probably involved in the side-chain
CC elongation step of the polyglutamylation reaction rather than the
CC initiation step (Probable). Modifies both alpha- and beta-tubulins with
CC a preference for the alpha-tail (PubMed:15890843, PubMed:22170066).
CC Unlike most polyglutamylases of the tubulin--tyrosine ligase family,
CC only displays a catalytic activity when in complex with other proteins
CC as it is most likely lacking domains important for autonomous activity
CC (PubMed:15890843). Part of the neuronal tubulin polyglutamylase complex
CC (PubMed:15890843). Mediates cilia and flagella polyglutamylation which
CC is essential for their biogenesis and motility (PubMed:20498047,
CC PubMed:20442420, PubMed:23897886). Involved in respiratory motile cilia
CC function through the regulation of beating asymmetry (PubMed:20498047,
CC PubMed:20442420). Essential for sperm flagella biogenesis, motility and
CC male fertility (PubMed:20442420). Also mediates glutamylation of non-
CC tubulin proteins (PubMed:29593216). Involved in KLF4 glutamylation
CC which impedes its ubiquitination, thereby leading to somatic cell
CC reprogramming, pluripotency maintenance and embryogenesis
CC (PubMed:29593216). {ECO:0000269|PubMed:15890843,
CC ECO:0000269|PubMed:20442420, ECO:0000269|PubMed:20498047,
CC ECO:0000269|PubMed:22170066, ECO:0000269|PubMed:23897886,
CC ECO:0000269|PubMed:29593216, ECO:0000305|Ref.11}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP +
CC L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein]
CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519,
CC Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:15890843};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149;
CC Evidence={ECO:0000305|PubMed:15890843};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which
CC contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. Interacts with PCM1,
CC CSTPP1 and LRRC49 (By similarity). {ECO:0000250|UniProtKB:O95922,
CC ECO:0000269|PubMed:15890843}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:20498047}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305|PubMed:20498047}.
CC Cell projection, cilium, flagellum {ECO:0000305|PubMed:20442420}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart and kidney
CC (PubMed:17499049, PubMed:20442420). Expressed in liver, lung, muscle,
CC spleen, testis and trachea (PubMed:17499049, PubMed:20442420). In the
CC brain, expressed in ependymal cilia, cortex, corpus callosum and
CC striatum (PubMed:23897886). Expressed in blastomere (PubMed:29593216).
CC {ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:20442420,
CC ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:29593216}.
CC -!- DOMAIN: Gln-144 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}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice exhibit a loss of axonemal
CC curvature and beating asymmetry in tracheal epithelial cilia, resulting
CC in a reduction of cilia-generated fluid flow in trachea
CC (PubMed:20498047). Knockout mice exhibit accumulations of exudates in
CC the nasal passages and sinuses, rhinosinusitis and otitis media, and
CC also emitted frequent coughing- or sneezing-like noises
CC (PubMed:20498047, PubMed:20442420). Knockout male show abnormal sperm
CC morphology and function characterized by shortened or absent flagella
CC and immotility, and male infertility (PubMed:20498047,
CC PubMed:20442420). Partial loss of tubulin glutamylation, probably due
CC to redundancy with other polyglutamylases (PubMed:20498047).
CC {ECO:0000269|PubMed:20442420, ECO:0000269|PubMed:20498047}.
CC -!- SIMILARITY: Belongs to the tubulin polyglutamylase family.
CC {ECO:0000305}.
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DR EMBL; AK031917; BAC27603.1; -; mRNA.
DR EMBL; AK047046; BAC32947.1; -; mRNA.
DR EMBL; AK140472; BAE24404.1; -; mRNA.
DR EMBL; AK168786; BAE40620.1; -; mRNA.
DR EMBL; AK169150; BAE40929.1; -; mRNA.
DR EMBL; AL583887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010510; AAH10510.1; -; mRNA.
DR CCDS; CCDS27702.1; -.
DR RefSeq; NP_849200.2; NM_178869.4.
DR RefSeq; XP_006521141.1; XM_006521078.3.
DR RefSeq; XP_011243961.1; XM_011245659.2.
DR AlphaFoldDB; Q91V51; -.
DR SMR; Q91V51; -.
DR CORUM; Q91V51; -.
DR STRING; 10090.ENSMUSP00000016897; -.
DR PhosphoSitePlus; Q91V51; -.
DR MaxQB; Q91V51; -.
DR PaxDb; Q91V51; -.
DR PeptideAtlas; Q91V51; -.
DR PRIDE; Q91V51; -.
DR ProteomicsDB; 297752; -.
DR Antibodypedia; 27458; 42 antibodies from 19 providers.
DR DNASU; 319953; -.
DR Ensembl; ENSMUST00000016897; ENSMUSP00000016897; ENSMUSG00000022442.
DR Ensembl; ENSMUST00000109480; ENSMUSP00000105106; ENSMUSG00000022442.
DR GeneID; 319953; -.
DR KEGG; mmu:319953; -.
DR UCSC; uc007xbc.2; mouse.
DR CTD; 25809; -.
DR MGI; MGI:2443047; Ttll1.
DR VEuPathDB; HostDB:ENSMUSG00000022442; -.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000156720; -.
DR InParanoid; Q91V51; -.
DR OMA; TMYGRLP; -.
DR OrthoDB; 584228at2759; -.
DR PhylomeDB; Q91V51; -.
DR TreeFam; TF313087; -.
DR BRENDA; 6.3.2.B3; 3474.
DR BioGRID-ORCS; 319953; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ttll1; mouse.
DR PRO; PR:Q91V51; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q91V51; protein.
DR Bgee; ENSMUSG00000022442; Expressed in myocardium of ventricle and 243 other tissues.
DR ExpressionAtlas; Q91V51; baseline and differential.
DR Genevisible; Q91V51; MM.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IDA:MGI.
DR GO; GO:0035082; P:axoneme assembly; IMP:MGI.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IGI:MGI.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0002395; P:immune response in nasopharyngeal-associated lymphoid tissue; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0120197; P:mucociliary clearance; IMP:MGI.
DR GO; GO:0018095; P:protein polyglutamylation; IDA:MGI.
DR GO; GO:0120222; P:regulation of blastocyst development; IMP:MGI.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP:MGI.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027750; TTLL1.
DR PANTHER; PTHR12241:SF31; PTHR12241:SF31; 1.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Flagellum;
KW Ligase; Magnesium; Metal-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..423
FT /note="Polyglutamylase complex subunit TTLL1"
FT /id="PRO_0000212439"
FT DOMAIN 1..367
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 243..244
FT /note="L-glutamate"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT REGION 390..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 144..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 144
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 181..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 181..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 194..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 220
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 241..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 259
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 344
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 144
FT /note="Essential for specifying alpha-elongation versus
FT initiation step of the polyglutamylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT CONFLICT 80
FT /note="N -> K (in Ref. 1; BAC27603)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="E -> K (in Ref. 1; BAE40620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 49110 MW; A36F115FF6B7B8A8 CRC64;
MAGRVKWVTD IEKSVLINNF EKRGWIQVTE NEDWNFYWMS VQTIRNVFSV ETGYRLSDDQ
IVNHFPNHYE LTRKDLMVKN IKRYRKELEK EGSPLAEKDE NGKYLYLDFV PVTYMLPADY
NLFVEEFRKS PSSTWIMKPC GKAQGKGIFL INKLSQIKKW SRDSKTSSFV SQSTKEAYVI
SVYINNPLLI GGRKFDLRLY VLVSTYRPLR CYMYKLGFCR FCTVKYTPST SELDNMFVHL
TNVAIQKHGE DYNHIHGGKW TVNNLRLYLE STRGREVTSK LFDEIHWIIV QSLKAVAPVM
NNDKHCFECY GYDIIIDDKL KPWLIEVNAS PSLTSSTAND RILKYNLIND TLNIAVPNGE
IPDCKWNKSP PKEVLGNYEI LYDEELAQGD GAERELRNRP GQPVGPRAGR SRDSGRSVLT
TWK
