ID   TTL12_CAEBR             Reviewed;         672 AA.
AC   A8XXC0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Tubulin--tyrosine ligase-like protein 12 {ECO:0000250|UniProtKB:Q09512};
DE   AltName: Full=Inactive tubulin--tyrosine ligase-like protein 12 {ECO:0000305};
GN   Name=ttll-12 {ECO:0000312|WormBase:CBG20224};
GN   ORFNames=CBG20224 {ECO:0000312|WormBase:CBG20224};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Regulates microtubule dynamics in uterine muscle cells.
CC       {ECO:0000250|UniProtKB:Q09512}.
CC   -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Although it belongs to the tubulin--tyrosine ligase family,
CC       the TTL domain lacks some of the ATP binding sites predicted to be
CC       essential for TTL activity (By similarity). Lacks tyrosine ligase
CC       activity in vitro (By similarity). Lacks glutamylation activity in
CC       vitro (By similarity). {ECO:0000250|UniProtKB:Q14166,
CC       ECO:0000250|UniProtKB:Q3UDE2}.
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DR   EMBL; HE601386; CAP37289.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XXC0; -.
DR   SMR; A8XXC0; -.
DR   STRING; 6238.CBG20224; -.
DR   WormBase; CBG20224; CBP39795; WBGene00039260; Cbr-ttll-12.
DR   eggNOG; KOG2155; Eukaryota.
DR   HOGENOM; CLU_018324_0_0_1; -.
DR   InParanoid; A8XXC0; -.
DR   OMA; CKRACDY; -.
DR   OrthoDB; 611643at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019098; P:reproductive behavior; IEA:UniProt.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   InterPro; IPR027749; TTLL12.
DR   PANTHER; PTHR46088; PTHR46088; 1.
DR   Pfam; PF03133; TTL; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..672
FT                   /note="Tubulin--tyrosine ligase-like protein 12"
FT                   /id="PRO_0000358602"
FT   DOMAIN          332..670
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT   BINDING         480..483
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         499
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT   BINDING         501
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZT98"
SQ   SEQUENCE   672 AA;  77790 MW;  320ACE2CD2FFEF93 CRC64;
     MSPSSSDRLG YPFSTFLDQH SAQLNASAVP PELWHSLYRK LSDQTFDAGD HFQIICEMDE
     NDEKKTLFVR ALEDMHNNDE ENIFLIDHFI SFPAESARKC VESNEKLPER LAALFGIDDD
     DCSSDGDETV EKIETSCEKE EEEHARRLSE PGLPRHESVD ARLSSYSVDD PKKTMTERVM
     RNLWKFAQTY TVSYQLENGE MEKKHVWYVM DDFGSRIRHS GCPNVRIVPL MFLPQNCAYS
     IMFLTKPVKI DDEITMDWAA NVITAKNPEW RQYLEMPWAE KDFSSESMVP GPPTLEYFTS
     GRNPDFLADE KDKKTCESAI FSALSVLKKQ GKIKIFLQIF ADDTQLTEHL KSRQIEYVDD
     WKAADVIWMI KHFHDYSNLA QENPCAQINQ FPFESCITVK DLLAACAMRD PSKNDWYQLT
     YNLNTQLPEF VARFQNRQKN GEHNVWIVKP WNLARGMEMA VTDDLNQIIR MVETGPKIVC
     EYIARPLLFP RPDNGNKVKF DLRYIVFVNA IGPVTAYVYN RFWIRFAINQ FQLGAYDDLE
     THFTVFNYLD KEKVLQMKCE KFVEIIEKTY PKLKWTQIQA DINSTIRKAI EVAASEPSPR
     GVAPNTQSRA MYGVDIMLQE SPESPDVIKP TLLEINFMPD TTRACQYYPD FADTVFDTMF
     LDEIDPTKVT PI