ID   A0A151JR50_9HYME        Unreviewed;      1598 AA.
AC   A0A151JR50;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Tubulin glycylase 3A {ECO:0000313|EMBL:KYN29843.1};
GN   ORFNames=ALC57_00725 {ECO:0000313|EMBL:KYN29843.1};
OS   Trachymyrmex cornetzi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN29843.1, ECO:0000313|Proteomes:UP000078492};
RN   [1] {ECO:0000313|EMBL:KYN29843.1, ECO:0000313|Proteomes:UP000078492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN29843.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN29843.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex cornetzi WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ978615; KYN29843.1; -; Genomic_DNA.
DR   STRING; 471704.A0A151JR50; -.
DR   Proteomes; UP000078492; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0070735; F:protein-glycine ligase activity; IEA:UniProt.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR45870; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR   PANTHER; PTHR45870:SF2; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR   Pfam; PF03133; TTL; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078492}.
FT   DOMAIN          319..576
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..735
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1598 AA;  183909 MW;  B82A5620596D5858 CRC64;
     MNAKDGSSSN LESSSEDKKD KKENIENEDE NPGEEVVTKT DATDCDIKCL KEEPDCLENK
     CESSLELPLE PTLHERFLRI KQTVKDAIAA HHTFMIYGKS RVIRDCMLKR GWCEKFYRRN
     SGGDQHFNVD SNPVLLLAGI GDLKDQQSER LLMSRMLANH TVDFLWNTGS DWPGWPAQDN
     KTTVFNRYCR AGFTSKVGLC SSVRQMHWYY EAGVANTLFP RCYNICQSDQ MHAFVEDFRL
     TGCLSLLKWL VDKVNAEDED VVRSPTGTVP LKALDFAIKR CSDYISAQSH EDIDQEGEKV
     WSHQWDQFIN WYYQIVRDQA LFVRTNVPFN KYILASKHVL KKMRKYWPQI DMDGVMNMWI
     LKPGNKSRGR GIVLMNKLED VVAKVNPTGK PDTRYVVQKY IERPLLIHHT KFDIRQWFIV
     TCAQPLTLWM YKESYLRFCS QKFSLDDFHE SIHLCNHAIQ CKYNNCGDRD SALPADNMWD
     ATTFKEFLSS QGHADAWDEQ IYPGIKQGLV GSLLASQEAM DRRKNSFELY GADFMIMEDF
     SVWLIEINSH PDMSYSTSVT TRLCRQVMED TIKVVVDFRE DKNADTGDFE LAYKQRTPSC
     QPYLGAALSL QGTRITTCEK KSSLYQDSKS NLVARSPMTK KKSVVQSNIG PVIVDLIEEL
     EIQLDQELYS YYNTDLLKSR PALPATAPTK PLKAISDEKA ETMTKSTSAG TTSINKTKSP
     IPSKTNVQNH AKSSNNGKRS SHKPARKLRM SINTAGSKLD TSPRQTLISK IMALQEESSN
     EAPKSEKSLR KNEDKIIKTA IRDAVKKYKR NVTIRPEVPP LPSLLTPPIM KVTPVSTTKS
     KSRSFPKKQT HYKKNKMLTD ISDMYAVDLQ AIEINSLQSR LQSFKLHCLQ KISSPIILRC
     SHKKIKVLPM LAHSIVEETI QEIRQKKHVR NKYVKKKIEE FTRSKNKNNE KVFPPKGQSE
     CPDFKHPQLE ECKEQKRKLF ATFPKDQKYE IDEIQKPVFQ NPAVDNSVVC IDSQSKWQII
     LSSKNCTIKK HFEGWQICPK DVNTDEKNLQ FILTVPKLKI NSQCAVETIK TADAEICCNR
     EDLKELLRAD KESDRENGNI ILTDYLKLVT NDEARINLLL KILMKAMDEH KCYVICGTFP
     VLRKPLTDRG WIDKKAIRKM ISIPPNAYED GLQQLEKLLR TPADFIWYTN KRPAIRTDDK
     TIVNKFAGSY FTSKVDMCNN LEKAYWFYET GVSNIQFPRC YNFYQSAQME EFIQDYYITA
     CFGILKWFTL LANLVGPKNT WSPNGTIPIN AISFALERCE EYIRFIQIHE DIDRTDCEYT
     PPAWDQFLDW HHDIIYKRVE FVVSVHDVMK AMIKYRPQSI IDGIRNIWIL KPGDDSLGRG
     IVLKSSLVDI IAKVNQAAKE NIEDILIRFA SKDFTLSDFH ESIHLCNTTV QLKYRQLPRC
     NSDLPEQRHW NLQDFKDYLQ SRGQKLAWEK IIRPGIKQNL IGALLASQDN MVNRKNSFQL
     YGADFVVADD FSVWLLEINT NPRLHPPSSE VTAKLYPEVI EDAMKIILDR RKNKKTSQGK
     FECIYKQRNP FYGVNILGQG ASLGIRGKGL FVTPKSST
//