Basic Information

NameATP-dependent DNA helicase HMI1, mitochondrial (EC 3.6.4.12)
Uniprot IDQ12039
Systematic gene nameYOL095C
Standard gene nameHMI1
Gene namesHMI1 YOL095C O0920
Description from SGDYOL095C HMI1 SGDID:S000005455, Chr XV from 141347-139227, Genome Release 64-3-1, reverse complement, Verified ORF, "Mitochondrial inner membrane localized ATP-dependent DNA helicase; required for the maintenance of the mitochondrial genome; not required for mitochondrial transcription; has homology to E. coli helicase uvrD"
Protein length706
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MDKLTPSQWK VINKSYEPAS TIKVIAGPGS GKTLTLLYKV LHLITVENIK
PEEILIFSLT NKAVDSIIEN LLSIFENSHT NKEIVHQIGC YTVHGLANRI
VVENEGMINI IEEIGWRGLM KLLPPSKRTP HHFRSYKELE KVVKDYKLNN
AKNNNPVIEK LVELMDNCKV MTNDDLIIRA KKYLELDSSD SDASSFTQDL
RNKYKVVLID EFQDLYPSLA PLITMICKGK QLIMFGDTNQ SIYGFLGSNN
EIMSQLDNLH PKNSTTVLKL FDNFRSTPEI ISLASKIINR PLAEKQIIDD
TDETPSELVR KLPSGVSPQI MTFDDLAAES EFIIDKITQL ICSSAKFSDI
AILSRTNSHL TAIASILKKY GIPYQKLKSQ PDWMDDLRIQ FLLDILKVCS
LASDEKHNRE FNTGDKWQSN FSILVTMSAL KGIGDASIQA LYKACSLKNL
SIWKYLTMVP NFEWPLGLSI KKKMENYTSN LYEMIENDQV HQLDDPMELL
EKVASITNNL NLNPTYFQSL SDAQSSLEFK THLQEMAQVM KVSKSNKPPG
ISFVKWFLET YFDQTMVFHQ SQQALQTTGP GTVKLSTIHS AKGLEFPIVF
LTNGSMSNFP MDTNALYVGI TRARNLLYMC NMKHERLVSK SSPYSRNIMS
NNLFWTYYNK DLKRSVCDVK VTHGYNVQRY NQLRKNFGFY RAYSSLRGCK
SVFRRI

Legend

  • X SUMOylation
  • 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

[471, SUMO]Paasch, F., den Brave, F., Psakhye, I., Pfander, B., Jentsch, S. (2018). Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins. J Biol Chem 293: 599-609. (Publication) (All modifications)
[472, SUMO]Paasch, F., den Brave, F., Psakhye, I., Pfander, B., Jentsch, S. (2018). Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins. J Biol Chem 293: 599-609. (Publication) (All modifications)
[665, 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)
[665, Phos]Holt, L.J.,  Tuch, B.B.,  Villén, J.,  Johnson, A.D.,  Gygi, S.P.,  Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications)
[665, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[675, 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)
[675, Phos]Holt, L.J.,  Tuch, B.B.,  Villén, J.,  Johnson, A.D.,  Gygi, S.P.,  Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications)
[675, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)