ID L5K8M3_PTEAL Unreviewed; 590 AA.
AC L5K8M3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Tubulin monoglycylase TTLL3 {ECO:0000313|EMBL:ELK07860.1};
GN ORFNames=PAL_GLEAN10022266 {ECO:0000313|EMBL:ELK07860.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK07860.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-
CC glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180,
CC Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036933};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67181;
CC Evidence={ECO:0000256|ARBA:ARBA00036933};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000256|ARBA:ARBA00004611}.
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DR EMBL; KB030947; ELK07860.1; -; Genomic_DNA.
DR AlphaFoldDB; L5K8M3; -.
DR STRING; 9402.L5K8M3; -.
DR InParanoid; L5K8M3; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; PTHR45870; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR PANTHER; PTHR45870:SF1; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR Pfam; PF03133; TTL; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS51221; TTL; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552}.
FT REGION 458..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 66225 MW; 1B2667817B623808 CRC64;
MGQVMIRFRN QNKLGARGLS SVFPALGAED FWLTAARNVL KLVVKSEWKS YSIQAEEEEA
PGDKLPKKQE KKPVMVSPEF VDEALCACEE HLSNLAHLDI DKDLEAPLYL SPEGWSLFLQ
RYYQVVQPSP AQDPSSPYSN GAELRHLDTQ VQRCEDILQQ LRAVVPQMDM EGDRNVWIVK
PGAKSRGRGI MCMDHLEEML KLVDSNPMMI KDGKWVVQKY IERPLLIFGT KFDLRQWFLV
TDWNPLTVWF YRDSYIRFST QPFSLKNLDN SVHLCNNSIQ KHLENSCHRH PQLPSDNMWS
SQKFQAHLQD MGAPNAWSTV IVPGMKAAVI HALQTSQDTV QCRKASFELY GADFVFGEDF
QPWLIEINAS PTMAPSTSVT ARLCAGVQAD TLRVVIDRRL DRNCDTGAFE LIYKQPAVEV
PQYVGIRLLV EGSTIKKPMA MCHRRTGVRT ALPHLQTQRG FGEGKDSGIL THRSAPRKVP
GARSLGHTEK PDSTAATSSS GKGKKGKAKT HYHFPSLYTK ARLPSPHVLR PQGRVLRLQH
SKLVGSKALS TTGKALMTLP TAKVLISLPP NPELKQAPTI LKPRKVGLKL
//
