ID A0A2Y9D5V8_TRIMA Unreviewed; 903 AA.
AC A0A2Y9D5V8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=LOW QUALITY PROTEIN: tubulin monoglycylase TTLL3 {ECO:0000313|RefSeq:XP_004368368.1};
GN Name=LOC101349487 {ECO:0000313|RefSeq:XP_004368368.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004368368.1};
RN [1] {ECO:0000313|RefSeq:XP_004368368.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_004368368.1; XM_004368311.1.
DR STRING; 127582.A0A2Y9D5V8; -.
DR GeneID; 101349487; -.
DR KEGG; tmu:101349487; -.
DR InParanoid; A0A2Y9D5V8; -.
DR OrthoDB; 7265at2759; -.
DR Proteomes; UP000248480; Unplaced.
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:UP000248480}.
FT REGION 29..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 903 AA; 101166 MW; 4D30208B1482AFEB CRC64;
MQSPGAALLL AGVQVGAVRP GSATWYRQEG GPVCRWPQKP QPPEPRSRSP APWPWAHHSE
FRLPATLPWP GPASAGLHRA NAGGQSQVGG PAPARRLDCA FPTLARSAQA KGAADPHPLG
PTHTPALDDP QPQEGSFVLW RGFSKASHHM GRLGNAKIHV ERAVKQKKIF MIQGRYPVIR
CLLRRRGWVE KKMAHHTGTT LPPSQKDLDS SVMCDSDTTE DEDEDEDKEF RPPQLFDFDG
LLEFDDLDGT HALMVGLCLN LRNLPWFDEA DADSFFPRCY RLGAEDDKRA FIEDFWLTAA
RNVLKLVVKS EWRPCSIQEE EEETPGDKQH KKQEKKPVTV SPEFVDEALC ACEEHLSNLA
HMDIDKDLEA PLYLSPQGWS VFLQRYYQVV HEGAELKHLD TQVQRCEDIL QQLRAVVPQI
DMEGDRNIWI VKPGAKSRGR GIVCMDHLEE MLKLVNCNPM MMKDGKWVVQ KYIERPLLIF
GTKFDLRQWF LVTDWNPLTV WFYRDSYIRF STQPFSLKNL DNSVHLCNNS IQKHLENSCH
RHPQLPPDNM WSSQKFQAHL QEMGAPEAWS TIIVPGMKAA VIHALQTSQD TVQCRKASFE
LYGADFVFGE DFQPWLIEIN ASPTMAPSTA VTARLCAGVQ ADTLRVVIDR RQDHNCDTGA
FELIYKQPAV EVPQYVGIRL LVEGSTIKKP TAMCHRRMTI RPALPHLLTQ QDSREAPYRF
PSLHTKAWLP SPHVFRPQGR GLRLQHKLVG SQALSTTGKA LMTLPMAKVL IVLPPKPELR
PAASERPSQV GLQLAFVASI LEVPCGLCPL KLEHVLSPIG RSRPKASSRT GSKKPKAEAC
LKKGLSHLGP LRLIGEQQML EGMGDARLEK PLLRXPTTSI LDSEPNKMEQ VKSSGLGSIS
IGG
//