YFH7_YEAST
ID YFH7_YEAST Reviewed; 353 AA.
AC P43591; D6VTN7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ATP-dependent kinase YFH7;
DE EC=2.7.1.-;
DE AltName: Full=Altered inheritance of mitochondria protein 12;
GN Name=YFH7; Synonyms=AIM12; OrderedLocusNames=YFR007W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION.
RX PubMed=12868057; DOI=10.1002/yea.994;
RA Wright R., Parrish M.L., Cadera E., Larson L., Matson C.K.,
RA Garrett-Engele P., Armour C., Lum P.Y., Shoemaker D.D.;
RT "Parallel analysis of tagged deletion mutants efficiently identifies genes
RT involved in endoplasmic reticulum biogenesis.";
RL Yeast 20:881-892(2003).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=19300474; DOI=10.1371/journal.pgen.1000407;
RA Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J.,
RA Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M.,
RA Troyanskaya O.G., Caudy A.A.;
RT "Computationally driven, quantitative experiments discover genes required
RT for mitochondrial biogenesis.";
RL PLoS Genet. 5:E1000407-E1000407(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS), AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18004758; DOI=10.1002/prot.21740;
RA Gueguen-Chaignon V., Chaptal V., Lariviere L., Costa N., Lopes P.,
RA Morera S., Nessler S.;
RT "Crystal structure and functional analysis identify the P-loop containing
RT protein YFH7 of Saccharomyces cerevisiae as an ATP-dependent kinase.";
RL Proteins 71:804-812(2008).
CC -!- FUNCTION: ATP-dependent kinase that could be involved in endoplasmic
CC reticulum membrane assembly. {ECO:0000269|PubMed:12868057}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1178 uM for ATP {ECO:0000269|PubMed:18004758};
CC -!- DISRUPTION PHENOTYPE: Increases frequency of mitochondrial genome loss.
CC {ECO:0000269|PubMed:19300474}.
CC -!- MISCELLANEOUS: Present with 161 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the YFH7 family. {ECO:0000305}.
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DR EMBL; D50617; BAA09246.1; -; Genomic_DNA.
DR EMBL; AY558494; AAS56820.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12447.1; -; Genomic_DNA.
DR PIR; S56262; S56262.
DR RefSeq; NP_116662.1; NM_001179972.1.
DR PDB; 2GA8; X-ray; 1.77 A; A=1-353.
DR PDB; 2GAA; X-ray; 1.95 A; A=1-353.
DR PDBsum; 2GA8; -.
DR PDBsum; 2GAA; -.
DR AlphaFoldDB; P43591; -.
DR SMR; P43591; -.
DR BioGRID; 31156; 62.
DR DIP; DIP-5443N; -.
DR IntAct; P43591; 1.
DR STRING; 4932.YFR007W; -.
DR MaxQB; P43591; -.
DR PaxDb; P43591; -.
DR PRIDE; P43591; -.
DR EnsemblFungi; YFR007W_mRNA; YFR007W; YFR007W.
DR GeneID; 850558; -.
DR KEGG; sce:YFR007W; -.
DR SGD; S000001903; YFH7.
DR VEuPathDB; FungiDB:YFR007W; -.
DR eggNOG; KOG2702; Eukaryota.
DR HOGENOM; CLU_067202_1_0_1; -.
DR InParanoid; P43591; -.
DR OMA; LYDQENW; -.
DR BioCyc; YEAST:G3O-30460-MON; -.
DR SABIO-RK; P43591; -.
DR EvolutionaryTrace; P43591; -.
DR PRO; PR:P43591; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43591; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0016301; F:kinase activity; ISS:SGD.
DR GO; GO:0016310; P:phosphorylation; ISS:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF07728; AAA_5; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..353
FT /note="ATP-dependent kinase YFH7"
FT /id="PRO_0000202683"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:2GA8"
FT TURN 18..21
FT /evidence="ECO:0007829|PDB:2GA8"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 37..58
FT /evidence="ECO:0007829|PDB:2GA8"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:2GA8"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:2GA8"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:2GA8"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:2GA8"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2GA8"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:2GA8"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:2GA8"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 192..206
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:2GA8"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:2GA8"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:2GA8"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:2GA8"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:2GA8"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:2GA8"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 299..312
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 319..328
FT /evidence="ECO:0007829|PDB:2GA8"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:2GA8"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:2GA8"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:2GA8"
SQ SEQUENCE 353 AA; 39885 MW; 521A76D6E9C9F11D CRC64;
MVDTHKLADD VLQLLDNRIE DNYRVCVILV GSPGSGKSTI AEELCQIINE KYHTFLSEHP
NVIEVNDRLK PMVNLVDSLK TLQPNKVAEM IENQGLFKDH VEDVNFQPVK YSALTSNNEE
CTAVVARGGT ANAIRIAAVD NPVNVNKLAQ DSINIAQIVP MDGFHLSRRC LDLFKDPQTA
HKRRGSPSTF DSNNFLQLCK ILAKTSLCKV SSHHKFYSTS SVFEKLSKTF SQTIPDIFVP
GFNHALKDPT PDQYCISKFT RIVILEGLYL LYDQENWKKI YKTLADTGAL LVYKIDIDYE
ATEERVAKRH LQSGLVTTIA EGREKFRSND LLNGRDIDNH LIKVDNIVHI RND
