ID A0A0R3VWG1_TAEAS Unreviewed; 1258 AA.
AC A0A0R3VWG1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 08-NOV-2023, entry version 45.
DE RecName: Full=Methionine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00018335};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN ORFNames=TASK_LOCUS1756 {ECO:0000313|EMBL:VDK23617.1};
OS Taenia asiatica (Asian tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000175501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TASK_0000175501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK23617.1, ECO:0000313|Proteomes:UP000282613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10;
CC Evidence={ECO:0000256|ARBA:ARBA00001234};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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DR EMBL; UYRS01000570; VDK23617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3VWG1; -.
DR STRING; 60517.A0A0R3VWG1; -.
DR WBParaSite; TASK_0000175501-mRNA-1; TASK_0000175501-mRNA-1; TASK_0000175501.
DR Proteomes; UP000046400; Unplaced.
DR Proteomes; UP000282613; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016409; F:palmitoyltransferase activity; IEA:InterPro.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR029038; MetRS_Zn.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF01529; DHHC; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000282613};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1132..1155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1167..1188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 253..649
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 655..758
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
FT REPEAT 880..912
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1089..1203
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 172..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 141069 MW; 367E649EBAC9663C CRC64;
MWRLFIDPRN RGSLAALAAV HKTKKAEIIK HGAERVSDGV VLETDSGLIS SVNAIVSFIL
GADALSPKLN AFLLWESTIL KPALNRISGS ISGDATDLLV DLQNRLQDLE KGASESDRLA
ANLIVWADIS HLLPSIVPDH LEYLRKLVKD CDAEEHCLHA LRDLPLKVHS QESSTVASKI
PQRKQGQDKV TQPNEKSTQN GDDELRRLQV EVSTDQMLKA QWTFSSTAPL AAFIHFNQRT
ILPMKKGEGV RNILISSALP YVNNVPHLGN LIGSLLSANI FALYCQTAGY NVLSICGTDE
YGTATEARAQ AEGLTPQQLT DKYHKLHCQV YDWFDIHFDY FGRTSTPVHT EITQEIFLNL
YNNGFITEAS VEQLFCEKCE RFLADRFVEG VCPFCKAEGA RGDQCDACGK LINAIELIKP
QCIACRGSPT VRSSDHLFLD LPKLEEKVDV FFSESVEDPN CKWTQVAQSI ARTWLRDGFK
KRCITRDLKW GVPVPLPNFK NKVFYVWFDA PIGYISITAN YTKEWRQWWL PSEDVEPVEY
FQFMAKDNVL FHSAIFPACL LGSNKKFTLV KHIIATEYLN YEGKKFSKSR GVGVFGNNAK
DSGIESNIWR FYLAYIRPET QDSTFSWEDF ALKNNGELLN NLGNFINRQF FNSTVPSMKN
LQPEDVTFLA RVNGILQEYI NNMERCCLRE GIRSVLGISR LGNGYLQAQK PWVLYKSSDT
TQRAGVVTGV SCNIAALLGI LLRPFMPTFA EEIFAQCKLP PEHRSLAPMV TNGGHIICLL
PEGHVIGELN ARKLKKLKKY LEGCPELLTI TDAFKDTLLH HAAFGDAFKT AAYLDSFDSS
LNSPNAIGQC PFMTSCLSGS FETAALLVCR SEDVNRADKT RLSATHLACR SNNTALVSML
IFCGADLEAV DSDNSLPLHF AAQSGGPNVC SLLLRFFPEA VEYQDTRKNT PLHVACASGN
MATASSILRA TLYPPPTHFK ETDAGTLCAV SVKRDYNVTI RNEEGQTPEH VAGRHGYYEL
AALIQNELYQ SGNARHISTP PGRLPLILRL QKRTSLLSVE GEAPQTELLP LQIQALRRSI
RIVKRRLSSL CHTCGCIKPI RAKHCSLCNR CVRIMDHHCP VTDNCVGQDN RVWFLLTSAV
VSIVSSWIGS LAVRYWQQTE STSLYEIVTL ILLSIGWMFG LNACFMTLSC ALFNMTTNEL
TNWRRYEHFG SAKTGFRNPF NQGYWGNVVE FFRPRYYETE RELYKYRGTD GGRHPFVV
//
