GenomeNet

Database: UniProt
Entry: F6PRC1_MONDO
LinkDB: F6PRC1_MONDO
Original site: F6PRC1_MONDO 
ID   F6PRC1_MONDO            Unreviewed;       605 AA.
AC   F6PRC1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Methionine--tRNA ligase, mitochondrial {ECO:0000256|ARBA:ARBA00026124};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE   AltName: Full=Methionyl-tRNA synthetase 2 {ECO:0000256|ARBA:ARBA00029831};
DE   AltName: Full=Mitochondrial methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030331};
GN   Name=MARS2 {ECO:0000313|Ensembl:ENSMODP00000034846.2};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000034846.2, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000034846.2, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000034846.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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   RefSeq; XP_007494628.1; XM_007494566.2.
DR   AlphaFoldDB; F6PRC1; -.
DR   STRING; 13616.ENSMODP00000034846; -.
DR   Ensembl; ENSMODT00000036434.2; ENSMODP00000034846.2; ENSMODG00000024604.2.
DR   GeneID; 100029705; -.
DR   KEGG; mdo:100029705; -.
DR   CTD; 92935; -.
DR   eggNOG; KOG0436; Eukaryota.
DR   GeneTree; ENSGT00550000075136; -.
DR   HOGENOM; CLU_009710_9_0_1; -.
DR   InParanoid; F6PRC1; -.
DR   OMA; SDMHGTP; -.
DR   OrthoDB; 166496at2759; -.
DR   TreeFam; TF105709; -.
DR   Proteomes; UP000002280; Chromosome 4.
DR   Bgee; ENSMODG00000024604; Expressed in forelimb bud and 18 other cell types or tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00398; metG; 1.
DR   PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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:UP000002280}.
FT   DOMAIN          52..422
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          454..556
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
SQ   SEQUENCE   605 AA;  68062 MW;  BF5BA024DA8EE0C1 CRC64;
     MFRVVFRGLK RSVLLGLHSR ASALGSRGWC NSSGDGEWRP GRPRAESGRV CFTTPIFYVN
     AAPHIGHLYS ALLADALARY CRLRAAAPPV TSPAAPLVRF STGTDEHGLK IQQAATAAGL
     TPSELCDRVS AQFRALFQEA GISITDFLRT TEARHRRAVH HFWEVLHARG LLYKGLYEGW
     YCASEECFLP DGKVTWRPGP NGQSHPVALD SGHPVCWMKE ENYIFRLSQF REPLRQWLQD
     DPQAITPDPF RSTVLKWLEE DLPDLSVSRS NSHLYWGLPV PGDPTQTIYV WVDALVNYLT
     VIGYPDSEQE AWWPATHHII GKDILKFHAI YWPALLLGAG MTPPHRIYVH SHWTVHGQKM
     SKSLGNVVDP LSCLDQFTVD GFRYFLLRQG VPNWDCDYYE KKVVKLLDAE LADALGGLLN
     RCTATSLNPT GIFPVFSTSC FPSMEDIMAA PTKAQPEDYA LVKAVSALPL QVENYYENFQ
     IYKALEAVST CVRQTNGFVQ RNAPWKLNRE NLADAQWLDT VLHVTLECLR VFGLLLQPVT
     PALADKLLSR LGISETERGL QNIYFLPRYY GQPCPFEGRR LGPDTGLLFP RLDKSKARVA
     KIHST
//
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