Basic Information
| Name | Leucine--tRNA ligase, mitochondrial (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) |
| Uniprot ID | P11325 |
| Systematic gene name | YLR382C |
| Standard gene name | NAM2 |
| Gene names | NAM2 MSL1 YLR382C L3502.6 |
| Description from SGD | YLR382C NAM2 SGDID:S000004374, Chr XII from 884751-882067, Genome Release 64-3-1, reverse complement, Verified ORF, "Mitochondrial leucyl-tRNA synthetase; also has direct role in splicing of several mitochondrial group I introns; indirectly required for mitochondrial genome maintenance; human homolog LARS2 can complement yeast null mutant, and is implicated in Perrault syndrome" |
| Protein length | 894 |
| Download | sequence (fasta, from Uniprot), modifications (csv format) |
| Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLSRPSSRFL STKRGPGPAV KKLIAIGEKW KQKTTRGLPK QDTLNSGSKY
ILCQFPYPSG ALHIGHLRVY VISDSLNRFY KQKGYNVIHP MGWDAFGLPA
ENAAIERSIN PAIWTRDNIA KMKQQMQSML ANFDWDREIT TCDPEYYKFT
QWIFLKLFEN GLAYRKEAEI NWDPVDMTVL ANEQVDAQGR SWRSGAIVEK
KQLKQWFLGI TKFAPKLKKH LNQLKDWPSN VKQMQKNWIG ESVGAELVFK
VADPKFENLI VFTTRPETLF AVQYVALALD HPIVQKYCEE MPDLKEFIQK
SDQLPNDTKE GFQLPNIKAV NPLTKEEVPI FAAPYVVSSY GSAPSAVMGC
PGHDNRDFEF WQTNCPGEHI KTCIAPFFDD ASKVTEQERQ RIIDTVPFTS
TDGVLTKECG EHSGVLTVVA RKSIMGMLNS EGLSKSVVRY KIRDWLISRQ
RYWGTPIPII HCDNCGPVPV PESDLPVKLP ELEGLDTKGN PLSTIDEFVN
VACPSCGSPA KRETDTMDTF IDSSWYYFRF LDPKNTSKPF DREIASKNMP
VDIYIGGVEH AILHLLYSRF IAKFLGSINA WSDPAGIFEP FKKLVTQGMV
QGKTYVDPDS GKFLKPDELT FVNDSPDGNT VIIKSNGKVP VVSYEKMSKS
KYNGADPNEC ILRHGPDATR AHILFQSPIA DALNWDESKI VGIERWLQKV
LHLTKNILSL EKDLAISKDY KTPTDLNDAE VKFHNDFQRF LKSITESFEV
NLSLNTVISD YMKLTNILES ALKKGEVRNE MIVQNLQKLV TVIYPAVPSI
SEEAAEMINS QMEWNQYRWP EVERTTESKF KKFQIVVNGR VKFMYTADKN
FLKLGRDAVI ETLMNLPEGR MYLMNKKIKK FVMKFNVISF LFHK
ILCQFPYPSG ALHIGHLRVY VISDSLNRFY KQKGYNVIHP MGWDAFGLPA
ENAAIERSIN PAIWTRDNIA KMKQQMQSML ANFDWDREIT TCDPEYYKFT
QWIFLKLFEN GLAYRKEAEI NWDPVDMTVL ANEQVDAQGR SWRSGAIVEK
KQLKQWFLGI TKFAPKLKKH LNQLKDWPSN VKQMQKNWIG ESVGAELVFK
VADPKFENLI VFTTRPETLF AVQYVALALD HPIVQKYCEE MPDLKEFIQK
SDQLPNDTKE GFQLPNIKAV NPLTKEEVPI FAAPYVVSSY GSAPSAVMGC
PGHDNRDFEF WQTNCPGEHI KTCIAPFFDD ASKVTEQERQ RIIDTVPFTS
TDGVLTKECG EHSGVLTVVA RKSIMGMLNS EGLSKSVVRY KIRDWLISRQ
RYWGTPIPII HCDNCGPVPV PESDLPVKLP ELEGLDTKGN PLSTIDEFVN
VACPSCGSPA KRETDTMDTF IDSSWYYFRF LDPKNTSKPF DREIASKNMP
VDIYIGGVEH AILHLLYSRF IAKFLGSINA WSDPAGIFEP FKKLVTQGMV
QGKTYVDPDS GKFLKPDELT FVNDSPDGNT VIIKSNGKVP VVSYEKMSKS
KYNGADPNEC ILRHGPDATR AHILFQSPIA DALNWDESKI VGIERWLQKV
LHLTKNILSL EKDLAISKDY KTPTDLNDAE VKFHNDFQRF LKSITESFEV
NLSLNTVISD YMKLTNILES ALKKGEVRNE MIVQNLQKLV TVIYPAVPSI
SEEAAEMINS QMEWNQYRWP EVERTTESKF KKFQIVVNGR VKFMYTADKN
FLKLGRDAVI ETLMNLPEGR MYLMNKKIKK FVMKFNVISF LFHK
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
| [48, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
| [48, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
| [324, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |