ID A0A0N4ZP74_PARTI Unreviewed; 896 AA.
AC A0A0N4ZP74;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 13-SEP-2023, entry version 35.
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};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001033500.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0001033500.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
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DR AlphaFoldDB; A0A0N4ZP74; -.
DR STRING; 131310.A0A0N4ZP74; -.
DR WBParaSite; PTRK_0001033500.1; PTRK_0001033500.1; PTRK_0001033500.
DR Proteomes; UP000038045; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR CDD; cd02799; tRNA_bind_EMAP-II_like; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002547; tRNA-bd_dom.
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; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
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; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363039};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363039};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00209};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00209}.
FT DOMAIN 735..836
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT REGION 586..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 646..680
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 591..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 896 AA; 101622 MW; 5C1C70B5034DACEA CRC64;
MEDTFFSKPE IYEEPVKKLP VSGKKNYLVT SALPYVNNVP HLGNIIGCVL SADVFVRFCN
IKGINCLYIC GTDEYGTATE VKALQENMTP NEICSKYHEM HKQIYEWFNI KFDNFGRTST
KDQTEVTHEI FHKLNNNGFI ESQDVDQLHC SSCNMFLADR YVNGICPLCK YDDARGDQCD
SCGKLINAIE LKEPKCLLCK GTPLSKKSKH LFLCLDKLSS EVYDNLKKSL DKEDNHWSNN
AVAIAKSWLK TGLEKRCITR DLKWGVKVPL EGFEDKVFYV WFDAPIGYMS ITKQYLGDDY
LKWWKNSKDV ELFNFLGKDN VAFHSIMFPA TLIGTRDKYT IVNHISATEY FNYEDQKFSK
SRGVGVFGDA AAETGIPADV WRFYLLYMRP ESSDTYFSWD DFANKINSEL LSNLGNFCNR
ALSFLENNYN GVVQKITLNN EDNELLLGIA KDLEEYEKHL TDIKLRDGLL KILSLSRRGN
QYMQNNAPWV LKKGTDEEQR RAGSVIGLSV NLVYLISVAL YPYMPKISEE IRNQCNKREL
IMLPKNLICV LEPGHKINYS APLFAKLEAK DIASFKARFG SMTNLKTEGN GKIKKNNKED
NKKKGEKKMQ SNVQNTENFY PKAQGNVKNI ENGMTCLEEA FNIAGKAFEN QQLAKLAEDK
KSLTLEVEKL LNQLKEEEIK GGIKQIEIPS DVKVTVPEKV VKVAEKKVSL SKNEKKEKSA
NSGNKKPVTI DDTIDIGRLD LRVGKIIDCK RHPDADALYL ETIDLGEEKP RTVISGLVKF
VPIEEMQNRL VVCLCNLKPA KMRGIESQAM VMCASTPDKV EILEVDPSCK PGQRIICGSY
EPRPDAVLNP KKKIWEQIAP DLKVNSEGKA TYKGELILIN GENPMIAPTL RNVNVK
//
