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Database: UniProt
Entry: A0A250WWM1_9CHLO
LinkDB: A0A250WWM1_9CHLO
Original site: A0A250WWM1_9CHLO 
ID   A0A250WWM1_9CHLO        Unreviewed;       441 AA.
AC   A0A250WWM1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Tubulin--tyrosine ligase-like protein 9 {ECO:0000256|ARBA:ARBA00030445};
GN   ORFNames=CEUSTIGMA_g2639.t1 {ECO:0000313|EMBL:GAX75195.1};
OS   Chlamydomonas eustigma.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX75195.1, ECO:0000313|Proteomes:UP000232323};
RN   [1] {ECO:0000313|EMBL:GAX75195.1, ECO:0000313|Proteomes:UP000232323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX75195.1,
RC   ECO:0000313|Proteomes:UP000232323};
RA   Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA   Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT   "Acidophilic green algal genome provides insights into adaptation to an
RT   acidic environment.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAX75195.1}.
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DR   EMBL; BEGY01000011; GAX75195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A250WWM1; -.
DR   STRING; 1157962.A0A250WWM1; -.
DR   OrthoDB; 100598at2759; -.
DR   Proteomes; UP000232323; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR   PANTHER; PTHR12241:SF39; TUBULIN POLYGLUTAMYLASE TTLL9-RELATED; 1.
DR   Pfam; PF03133; TTL; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000232323}.
FT   DOMAIN          104..359
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          413..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          83..113
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        419..433
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  51375 MW;  DB5B4F1A3450B7F2 CRC64;
     MSSYARTGDR AERQRPPGPV RWKSSLRNTI YDVLQSKKDW QETDNETDWD FFWADKGWIH
     YELDKIHLND WQRINHFPNH YELTRKDLLI KNLKRAKRQL EKEDRLTEAA QYNFFPLTFV
     VPSEYRMFVE EFRRSGGVWI MKPIGAAQGK GIFLFNKLSQ ISDWRRDHTW RPDDEEAPET
     YLAQRYVDGP YLVGGKKFDL RIYALVTNYS PLRIYLYRSG FARFTNTRYS TKKEDITNTY
     MHLTNVAIQK HAPGFDAAKG MKWSIKSLRT YMMARHGADA TNELFHNIQN LIIRCLLAVQ
     PAMINDKHCF ELYGYDILID QALKPWVLEV NASPSLSASD KADWVLKTAM LEDMLDIVDM
     DGKRESGQQP DLKVGGFDLI WDGGPVLRFD KPTSLPTMLG AYNDRDKNQL RIYKESGPPA
     DNRPPPRPLR PPQPLTDNGL V
//
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