TTL3A_DROME
ID TTL3A_DROME Reviewed; 992 AA.
AC Q9VM91;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Tubulin glycylase 3A;
DE Short=dmTTLL3A;
DE EC=6.3.2.-;
GN Name=TTLL3A; ORFNames=CG11323;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N.,
RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
CC -!- FUNCTION: Polylycylase which modifies alpha- and beta-tubulin,
CC generating side chains of glycine on the gamma-carboxyl groups of
CC specific glutamate residues within the C-terminal tail of alpha- and
CC beta-tubulin. Involved both in the side-chain initiation and elongation
CC steps of the polyglycylation reaction by adding a single glycine chain
CC to generate monoglycine side chains and by elongating monoglycine side
CC chains to polyglycine side chains. {ECO:0000269|PubMed:19524510}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19524510}.
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DR EMBL; AE014134; AAF52432.1; -; Genomic_DNA.
DR RefSeq; NP_609069.1; NM_135225.2.
DR AlphaFoldDB; Q9VM91; -.
DR SMR; Q9VM91; -.
DR STRING; 7227.FBpp0078935; -.
DR PaxDb; Q9VM91; -.
DR PRIDE; Q9VM91; -.
DR EnsemblMetazoa; FBtr0079305; FBpp0078935; FBgn0031854.
DR GeneID; 33947; -.
DR KEGG; dme:Dmel_CG11323; -.
DR UCSC; CG11323-RA; d. melanogaster.
DR CTD; 33947; -.
DR FlyBase; FBgn0031854; TTLL3A.
DR VEuPathDB; VectorBase:FBgn0031854; -.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000168830; -.
DR HOGENOM; CLU_294449_0_0_1; -.
DR InParanoid; Q9VM91; -.
DR OMA; RIHRAMP; -.
DR OrthoDB; 143220at2759; -.
DR PhylomeDB; Q9VM91; -.
DR BioGRID-ORCS; 33947; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33947; -.
DR PRO; PR:Q9VM91; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031854; Expressed in organismal segment and 1 other tissue.
DR Genevisible; Q9VM91; DM.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070735; F:protein-glycine ligase activity; IDA:UniProtKB.
DR GO; GO:0070737; F:protein-glycine ligase activity, elongating; IDA:UniProtKB.
DR GO; GO:0070736; F:protein-glycine ligase activity, initiating; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0003341; P:cilium movement; IBA:GO_Central.
DR GO; GO:0018094; P:protein polyglycylation; IDA:UniProtKB.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Ligase; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..992
FT /note="Tubulin glycylase 3A"
FT /id="PRO_0000381795"
FT DOMAIN 295..645
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 457..460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 472
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ SEQUENCE 992 AA; 112256 MW; 0FC34674C15BDAAD CRC64;
MQTRPSSEPH RSRDQVTDGD RNRDQPQKCA SATLAKKPVT PPAAPPPTPS NRVVAPLTVP
VIQLTPAQSD SPVKLARPAT PKETAISVPD HSNKENQPAR TPPPSKSCPL GAPTNYVARR
TWITTERMNE LRRKAQEAAK QNKIFTIRGC FNSVRNALLM RGWVEKLDVH RKVMPAGQMT
YEDLTQRLPK RKAGETRRQY VQKCERNIMS RFLEHMPVDF LWTNRKEKCD YIDQAKNPGM
TINKFHRAPF TSKEGLCSQL RDFHWFFEEG TAEMYFPRCY NVWSPEELGE FIENFKLTAC
VAFLRAMLCK YHKQGSDAVF SCSGKIPYSA IDFAYKRLVE YIDSCQHNDI DFEDPPKIWE
HDWDAFLFQH QQLVNEDGRI QHDGGQRLEP MVKSCLSLVD KMKVHWPQYS LDGYQNMWIV
KPANKCRGRG IILMDNLKKI LGVVNLSIAS KSRYVVQKYI ERPLILFQTK FDIRQWFLIT
NTQPLVVWFY RESYLRFSSQ EYSLSNHHES VHLTNYAIQK KYTNGKRDKR LPSENMWDCY
SFQAYLRQIG KYNMWLERIF PGMRKAIVGC MLASQENMDR RPNTFELFGA DFMICENFYP
WLIEINSSPD LGATTSVTAR MCPQCLEDVV KVVIDRRTDP KAELGNFELA YRQVVPPTPA
YMGLNLFVKG KQVLQKANHG GGHGHYYYQQ QRKERSLATS SVYRQRSAII HPATSISRIH
RAMPTFNATE YMEKYMVEPL SSSRSSLCSQ LPQKSPSAAP ALTATPSGAT SSYILKQAGR
SITQLLSATH KRNTGGSLSG EQVQSTALPP KRQRSCGPRL SSTNPVESTE KKFKILIKNY
SSNGNENMQD ARPEVANSAT ATAISERKWR SLRNIAATAG GSSNLAARSK GPPLIAPPSL
PTRRLTRTKS EIDSTGMHAI GRTFGRKSNG PRLPISISVQ ALHRGEPIVA ALKQATSELQ
LSQAQMMSPR TALANKLNGS TLMVPASALP VG
