Basic Information
Name | Protein adenylyltransferase SelO, mitochondrial (EC 2.7.7.-) (Selenoprotein O) (SelO) |
Uniprot ID | Q08968 |
Systematic gene name | YPL222W |
Standard gene name | FMP40 |
Gene names | FMP40 YPL222W |
Description from SGD | YPL222W FMP40 SGDID:S000006143, Chr XVI from 130162-132228, Genome Release 64-3-1, Uncharacterized ORF, "Putative protein of unknown function; proposed to be involved in responding to environmental stresses; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies" |
Protein length | 688 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MGEKRTIIKA LKNSAASHFI KKLTADTSLS SIQEAINVVQ QYNATDPVRL
KLFHTPRMVS QGAHFAFCLP TKKPHYKPLL LSQNALDEFN LVQDQDLEKI
LSGEKVYYSD SIFPYSTVYS GFQFGSFAAQ LGDGRVVNLF DLKDKCSGQW
QTFQLKGAGM TPFSRFADGK AVLRSSIREF IMSEALHSIG IPSTRAMQLT
LLPGTKAQRR NQEPCAVVCR FAPSWIRLGN FNLFRWRHDL KGLIQLSDYC
IEELFAGGTQ FEGKPDFNIF KRDFFPDTET KIDEQVEKDE TEVSTMTGDN
ISTLSKYDEF FRHVVSLNAN TVAHWQAYGF ANGVLNTDNT SIMGLTIDYG
PFAFLDKFEP SFTPNHDDTA KRYSFANQPS IIWWNLQQFA KDLACLLGPE
ARDLELLLKG ELNSVDDALE KTMIERVQKL VELSANEYKY VFTTRYAQIM
SQRLGVDLDL EKCMSSTNLK DIEHAAEKAK EFCDVIVEPL LDILQATKVD
YNNFFIHLQN YKGPFFIKDK SDTATLFGAF DEEYLGMFFN SKQLQQMAET
EEAFAAGEKV FDANGELRLL NEKLQEIRNW TQDYLTLVPP TETAARASLA
KKANPLFVPR SWVLEEVVDD LMYSQRDGLQ DPSSELDTSA LKKLYLMSVN
PYDRTKWDVT LRPELETKWA DLSHQDDAKF MMQASCSS
KLFHTPRMVS QGAHFAFCLP TKKPHYKPLL LSQNALDEFN LVQDQDLEKI
LSGEKVYYSD SIFPYSTVYS GFQFGSFAAQ LGDGRVVNLF DLKDKCSGQW
QTFQLKGAGM TPFSRFADGK AVLRSSIREF IMSEALHSIG IPSTRAMQLT
LLPGTKAQRR NQEPCAVVCR FAPSWIRLGN FNLFRWRHDL KGLIQLSDYC
IEELFAGGTQ FEGKPDFNIF KRDFFPDTET KIDEQVEKDE TEVSTMTGDN
ISTLSKYDEF FRHVVSLNAN TVAHWQAYGF ANGVLNTDNT SIMGLTIDYG
PFAFLDKFEP SFTPNHDDTA KRYSFANQPS IIWWNLQQFA KDLACLLGPE
ARDLELLLKG ELNSVDDALE KTMIERVQKL VELSANEYKY VFTTRYAQIM
SQRLGVDLDL EKCMSSTNLK DIEHAAEKAK EFCDVIVEPL LDILQATKVD
YNNFFIHLQN YKGPFFIKDK SDTATLFGAF DEEYLGMFFN SKQLQQMAET
EEAFAAGEKV FDANGELRLL NEKLQEIRNW TQDYLTLVPP TETAARASLA
KKANPLFVPR SWVLEEVVDD LMYSQRDGLQ DPSSELDTSA LKKLYLMSVN
PYDRTKWDVT LRPELETKWA DLSHQDDAKF MMQASCSS
Legend
- X K-Succinylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[12, 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) |
[21, 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) |
[143, K-succ] | Weinert, B.T., Schölz, C., Wagner, S.A., et al. (2013). Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Reports, 4(4), 842-851. (Publication) (All modifications) |
[170, 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) |
[573, 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) |