YLF2_YEAST
ID YLF2_YEAST Reviewed; 405 AA.
AC P38746; D3DKP8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Obg-like ATPase homolog;
DE Short=OLA1 homolog;
GN Name=YLF2; OrderedLocusNames=YHL014C;
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 [GENOMIC DNA].
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=8021936; DOI=10.1006/jmbi.1994.1412;
RA Hermann-Le Denmat S., Sipickzki M., Thuriaux P.;
RT "Suppression of yeast RNA polymerase III mutations by the URP2 gene
RT encoding a protein homologous to the mammalian ribosomal protein S20.";
RL J. Mol. Biol. 240:1-7(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
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 [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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower
CC efficiency. Has lower affinity for GTP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 2360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000255|PROSITE-ProRule:PRU01047}.
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DR EMBL; Z29089; CAA82332.1; -; Genomic_DNA.
DR EMBL; U11582; AAB65067.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06672.1; -; Genomic_DNA.
DR PIR; S46828; S46828.
DR RefSeq; NP_011849.1; NM_001179094.1.
DR AlphaFoldDB; P38746; -.
DR SMR; P38746; -.
DR BioGRID; 36409; 68.
DR IntAct; P38746; 1.
DR MINT; P38746; -.
DR STRING; 4932.YHL014C; -.
DR MaxQB; P38746; -.
DR PaxDb; P38746; -.
DR PRIDE; P38746; -.
DR EnsemblFungi; YHL014C_mRNA; YHL014C; YHL014C.
DR GeneID; 856372; -.
DR KEGG; sce:YHL014C; -.
DR SGD; S000001006; YLF2.
DR VEuPathDB; FungiDB:YHL014C; -.
DR eggNOG; KOG1491; Eukaryota.
DR GeneTree; ENSGT00390000000673; -.
DR HOGENOM; CLU_018395_1_1_1; -.
DR InParanoid; P38746; -.
DR OMA; DQIEKRM; -.
DR BioCyc; YEAST:G3O-31034-MON; -.
DR PRO; PR:P38746; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38746; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISS:SGD.
DR CDD; cd04867; TGS_YchF_OLA1; 1.
DR CDD; cd01900; YchF; 1.
DR Gene3D; 1.10.150.300; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004396; ATPase_YchF/OLA1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR023192; TGS-like_dom_sf.
DR InterPro; IPR013029; YchF_C.
DR InterPro; IPR041706; YchF_N.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF06071; YchF-GTPase_C; 1.
DR PIRSF; PIRSF006641; CHP00092; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00092; TIGR00092; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; GTP-binding; Mitochondrion; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..405
FT /note="Obg-like ATPase homolog"
FT /id="PRO_0000122455"
FT DOMAIN 17..283
FT /note="OBG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT DOMAIN 312..398
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT BINDING 26..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 63
FT /note="S -> T (in Ref. 1; CAA82332)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="L -> F (in Ref. 1; CAA82332)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="E -> A (in Ref. 1; CAA82332)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 45715 MW; DF25FBCB6BE80AEC CRC64;
MNIGGGKFLL GRISNNPTSG IVGLANVGKS TFFQAITNSK LGNPANYPFA TIDAECAKVN
IPSVPLSNLL RIYQSAKCVP GTLTIYDIAG LTRGASQGHG LGNKFLNDIR HVEGIFQVVR
GFLKEDITHI EGNVDPVRDL SVVQDELILK DLEFLENIRE RLSKKMRMVS KNSKEHQEMK
IETELLDALE EHLFNGKKIR HFKDHWNLDE VKILNKHNFL TSKPTLILLN VSPQDYVRNE
NKFVRNIIEW INEFSPGDKF LLFSAEFESQ LMECKGIASE YFDKIKEDTN VSDQQLVSAI
PQIILEMRKL LNLISFFTCG PQEVHQWNIR EGTTAQEAAG VIHSDLRETF ISADVIKYDD
LKKMEPPLNE SLLKSKGLIK RAGKQYIMQD NDIALFKAAG GKIKK
