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Database: UniProt
Entry: A0A2K3E3I9_CHLRE
LinkDB: A0A2K3E3I9_CHLRE
Original site: A0A2K3E3I9_CHLRE 
ID   A0A2K3E3I9_CHLRE        Unreviewed;       564 AA.
AC   A0A2K3E3I9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Tubulin--tyrosine ligase-like protein 9 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CHLRE_02g117350v5 {ECO:0000313|EMBL:PNW87307.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055 {ECO:0000313|EMBL:PNW87307.1, ECO:0000313|Proteomes:UP000006906};
RN   [1] {ECO:0000313|EMBL:PNW87307.1, ECO:0000313|Proteomes:UP000006906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906};
RX   PubMed=17932292; DOI=10.1126/science.1143609;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA   Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA   Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA   Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA   Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA   Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA   Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA   Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA   Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA   Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.,
RA   Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA   Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA   Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA   Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA   Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA   Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA   Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA   Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA   Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA   Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT   "The Chlamydomonas genome reveals the evolution of key animal and plant
RT   functions.";
RL   Science 318:245-250(2007).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000256|ARBA:ARBA00004120}.
CC   -!- SIMILARITY: Belongs to the tubulin polyglutamylase family.
CC       {ECO:0000256|ARBA:ARBA00006118}.
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DR   EMBL; CM008963; PNW87307.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3E3I9; -.
DR   STRING; 3055.A0A2K3E3I9; -.
DR   EnsemblPlants; PNW87307; PNW87307; CHLRE_02g117350v5.
DR   Gramene; PNW87307; PNW87307; CHLRE_02g117350v5.
DR   InParanoid; A0A2K3E3I9; -.
DR   OMA; DWNFYWS; -.
DR   OrthoDB; 100598at2759; -.
DR   Proteomes; UP000006906; Chromosome 2.
DR   ExpressionAtlas; A0A2K3E3I9; baseline and differential.
DR   GO; GO:0005929; C:cilium; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR   GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
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; PTHR12241:SF31; POLYGLUTAMYLASE COMPLEX SUBUNIT TTLL1; 1.
DR   PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR   Pfam; PF03133; TTL; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006906}.
FT   REGION          129..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  61931 MW;  5B0A300D45E2F1EC CRC64;
     MGIRWRCDLD KPVLIQNFKR RGWIDVSAEL EDDSWDLWWA NVQSVKQLFG DSMTRLHPHQ
     RINHFPNHYE LTRKDLMVKN IKRYQKQVKR EGGTAAELDI IPATYVLPQD YMLFAEEFRR
     CWQLQQKEQQ REQQEQQQGQ QGGSSSGGGA AGGSSSGSGG TTWIMKPSSK SQGKGIFLIN
     KLSQIKQWSV GSLPPALRSG TDSYVVSRYI DNPLLIGGKK FDMRIYVVVT SFKPLRVHVS
     NLGFCRFCNV KYSAEVGELE NEFMHLTNVA IQQHGQDYNE HHGNKWPLAD MRLLLEATRG
     PEAAERLFAD IDGVILKSLR ACQNIIVNDR HCFELYGYDI IIDDTLKPWL IEVNASPSLS
     TTTQADRLLK HRVISDTLNL VSPPDWLAAT DPAALPPDVR GLDPAEYPFR EQVGSLRLIC
     DESEEYARWR EERERQAARA ARAAAGAGAG TREGGGGSGG AGGGGDWSWG TAEQSGQQGR
     RMERHHSARA YGAGAQYGVR GAGGGGGAAA GEGGRQGPGG SAQQQTQQQA GGGEQRWEPA
     RAFRNTGAAG AKTGGGGSRP RSAV
//
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