Basic Information

NameMitochondrial respiratory chain complexes assembly protein AFG3 (EC 3.4.24.-) (ATPase family gene 3 protein) (Tat-binding homolog 10)
Uniprot IDP39925
Systematic gene nameYER017C
Standard gene nameAFG3
Gene namesAFG3 YTA10 YER017C
Description from SGDYER017C AFG3 SGDID:S000000819, Chr V from 191788-189503, Genome Release 64-3-1, reverse complement, Verified ORF, "Mitochondrial inner membrane m-AAA protease component; mediates degradation of misfolded or unassembled proteins; also required for correct assembly of mitochondrial enzyme complexes; involved in cytoplasmic mRNA translation and aging; expression of human homolog AFG3L2 can complement yeast yta12 afg3 double mutant"
Protein length761
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MMMWQRYARG APRSLTSLSF GKASRISTVK PVLRSRMPVH QRLQTLSGLA
TRNTIHRSTQ IRSFHISWTR LNENRPNKEG EGKNNGNKDN NSNKEDGKDK
RNEFGSLSEY FRSKEFANTM FLTIGFTIIF TLLTPSSNNS GDDSNRVLTF
QDFKTKYLEK GLVSKIYVVN KFLVEAELVN TKQVVSFTIG SVDIFEEQMD
QIQDLLNIPP RDRIPIKYIE RSSPFTFLFP FLPTIILLGG LYFITRKINS
SPPNANGGGG GGLGGMFNVG KSRAKLFNKE TDIKISFKNV AGCDEAKQEI
MEFVHFLKNP GKYTKLGAKI PRGAILSGPP GTGKTLLAKA TAGEANVPFL
SVSGSEFVEM FVGVGASRVR DLFTQARSMA PSIIFIDEID AIGKERGKGG
ALGGANDERE ATLNQLLVEM DGFTTSDQVV VLAGTNRPDV LDNALMRPGR
FDRHIQIDSP DVNGRQQIYL VHLKRLNLDP LLTDDMNNLS GKLATLTPGF
TGADIANACN EAALIAARHN DPYITIHHFE QAIERVIAGL EKKTRVLSKE
EKRSVAYHEA GHAVCGWFLK YADPLLKVSI IPRGQGALGY AQYLPPDQYL
ISEEQFRHRM IMALGGRVSE ELHFPSVTSG AHDDFKKVTQ MANAMVTSLG
MSPKIGYLSF DQNDGNFKVN KPFSNKTART IDLEVKSIVD DAHRACTELL
TKNLDKVDLV AKELLRKEAI TREDMIRLLG PRPFKERNEA FEKYLDPKSN
TEPPEAPAAT N

Legend

  • X K-Succinylation
  • 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

[279, K-succ]Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications)
[286, 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)
[286, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[313, 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)
[314, 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)
[549, K-succ]Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications)