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Database: UniProt
Entry: A0A2R8ZNP9_PANPA
LinkDB: A0A2R8ZNP9_PANPA
Original site: A0A2R8ZNP9_PANPA 
ID   A0A2R8ZNP9_PANPA        Unreviewed;       901 AA.
AC   A0A2R8ZNP9;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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   Name=MARS1 {ECO:0000313|Ensembl:ENSPPAP00000006580.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000006580.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000006580.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000006580.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) 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   EMBL; AJFE02087625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02087626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02087627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02087628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02087629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02087630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02087631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02087632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02087633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8ZNP9; -.
DR   STRING; 9597.ENSPPAP00000006580; -.
DR   Ensembl; ENSPPAT00000028025.1; ENSPPAP00000006580.1; ENSPPAG00000025147.1.
DR   GeneTree; ENSGT00550000075017; -.
DR   OMA; HLNTTEY; -.
DR   Proteomes; UP000240080; Chromosome 12.
DR   Bgee; ENSPPAG00000025147; Expressed in testis and 6 other cell types or tissues.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
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:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:Ensembl.
DR   GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; IEA:Ensembl.
DR   GO; GO:0009303; P:rRNA transcription; IEA:Ensembl.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd10307; GST_C_MetRS_N; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   CDD; cd00939; MetRS_RNA; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 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; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR041598; MARS_N.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR   InterPro; IPR000738; WHEP-TRS_dom.
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; PF00043; GST_C; 1.
DR   Pfam; PF18485; GST_N_5; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   Pfam; PF00458; WHEP-TRS; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SMART; SM00991; WHEP-TRS; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS00762; WHEP_TRS_1; 1.
DR   PROSITE; PS51185; WHEP_TRS_2; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000240080}.
FT   DOMAIN          74..191
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   DOMAIN          842..898
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
SQ   SEQUENCE   901 AA;  101477 MW;  0D447C3FCA733EBD CRC64;
     MRLFVSEGVP GCLPVLAAAG RARGRAEVLI STVGPEDCVV PFLTRPKVPV LQLDSGNYLF
     STSAICRYFF LLSGWEQDDL TNQWLEWEAT ELQPALSAAL QEGEDVLGSV RRALTHIDHS
     LSRQNCPFLA GETESLADIV LWGALYPLLQ DPAYLPEELS ALHSWFQTLS TQEPCQRAAE
     TVLKQQGVLA LRPYLQKQPQ PSPTEGRAVT NEPEEEELAT LSEEEIAMAV TAWEKGLESL
     PPLRPQQNPV LPVAGERNVL ITSALPYVNN VPHLGNIIGC VLSADVFARY SRLRQWNTLY
     LCGTDEYGTA TETKALEEGL TPQEICDKYH IIHADIYRWF NISFDIFGRT TTPQQTKITQ
     DIFQQLLKRG FVWQDTVEQL RCEHCARFLA DRFVEGMCPF CGYEEARGDQ CDKCGKLINA
     VELKKPQCKV CRSCPVVQST QHLFLDLPKL EKRLEEWLGR TLPGSDWTPN AQFITRSWLR
     DGLKPRCITR DLKWGTPVPL EGFEDKVFYV WFDATIGYLS ITANYTDQWE RWWKNPEQVD
     LYQFMAKDNV PFHSLVFPCS ALGAEDNYTL VSHLIATEYL NYEDGKFSKS RGVGVFGDMA
     QDTGIPADIW RFYLLYIRPE GQDSAFSWTD LLLKNNSELL NNLGNFINRA GMFVSKFFGG
     YVPEMVLTPD DQRLLAHVTL ELQHYHQLLE KVRIRDALRS ILTISRHGNQ YIQVNEPWKR
     IKGSEADRQR AGTVTGLAVN IAALLSVMLQ PYMPTVSATI QAQLQLPPPA CSILLTNFLC
     TLPAGHQIGT VSPLFQKLEN DQIESLRQRF GGGQLEETFD LKAKTSLKPA VVETVTTARP
     QQIQALMDEV TKQGNIVREL KAQKADKNEV AAEVAKLLDL KKQLAVAEGK PPEAPKGKKK
     K
//
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