HMI1_YEAST
ID HMI1_YEAST Reviewed; 706 AA.
AC Q12039; D6W1X3; Q05379;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=ATP-dependent DNA helicase HMI1, mitochondrial;
DE EC=3.6.4.12;
DE Flags: Precursor;
GN Name=HMI1; OrderedLocusNames=YOL095C; ORFNames=O0920;
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 204508 / S288c;
RX PubMed=1346062; DOI=10.1128/mcb.12.1.155-163.1992;
RA Fien K., Stillman B.;
RT "Identification of replication factor C from Saccharomyces cerevisiae: a
RT component of the leading-strand DNA replication complex.";
RL Mol. Cell. Biol. 12:155-163(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7502582; DOI=10.1002/yea.320111108;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including
RT the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for
RT tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.";
RL Yeast 11:1069-1075(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8533473; DOI=10.1002/yea.320111009;
RA Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
RT "A 29.425 kb segment on the left arm of yeast chromosome XV contains more
RT than twice as many unknown as known open reading frames.";
RL Yeast 11:975-986(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-704 AND
RP ARG-705.
RX PubMed=10669756; DOI=10.1128/mcb.20.5.1816-1824.2000;
RA Sedman T., Kuusk S., Kivi S., Sedman J.;
RT "A DNA helicase required for maintenance of the functional mitochondrial
RT genome in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 20:1816-1824(2000).
RN [7]
RP C-TERMINAL TARGETING DOMAIN.
RX PubMed=10409639; DOI=10.1074/jbc.274.30.20937;
RA Lee C.M., Sedman J., Neupert W., Stuart R.A.;
RT "The DNA helicase, Hmi1p, is transported into mitochondria by a C-terminal
RT cleavable targeting signal.";
RL J. Biol. Chem. 274:20937-20942(1999).
CC -!- FUNCTION: Required for mitochondrial genome maintenance and
CC mitochondrial DNA inheritance. {ECO:0000269|PubMed:10669756}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10669756};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:10669756}; Peripheral membrane protein
CC {ECO:0000305|PubMed:10669756}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA88166.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U26030; AAC49064.1; -; Genomic_DNA.
DR EMBL; Z48149; CAA88166.1; ALT_INIT; Genomic_DNA.
DR EMBL; X83121; CAA58184.1; -; Genomic_DNA.
DR EMBL; Z74837; CAA99107.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10689.1; -; Genomic_DNA.
DR PIR; S57374; S57374.
DR RefSeq; NP_014546.1; NM_001183349.1.
DR AlphaFoldDB; Q12039; -.
DR SMR; Q12039; -.
DR BioGRID; 34307; 318.
DR DIP; DIP-4225N; -.
DR MINT; Q12039; -.
DR STRING; 4932.YOL095C; -.
DR iPTMnet; Q12039; -.
DR MaxQB; Q12039; -.
DR PaxDb; Q12039; -.
DR PRIDE; Q12039; -.
DR EnsemblFungi; YOL095C_mRNA; YOL095C; YOL095C.
DR GeneID; 854058; -.
DR KEGG; sce:YOL095C; -.
DR SGD; S000005455; HMI1.
DR VEuPathDB; FungiDB:YOL095C; -.
DR eggNOG; KOG2108; Eukaryota.
DR GeneTree; ENSGT00390000011669; -.
DR HOGENOM; CLU_004585_7_0_1; -.
DR InParanoid; Q12039; -.
DR OMA; VTLMSLH; -.
DR BioCyc; YEAST:G3O-33495-MON; -.
DR BRENDA; 3.6.4.12; 984.
DR PRO; PR:Q12039; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12039; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032042; P:mitochondrial DNA metabolic process; IMP:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Magnesium; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..692
FT /note="ATP-dependent DNA helicase HMI1, mitochondrial"
FT /id="PRO_0000013297"
FT PROPEP 693..706
FT /note="Cleaved upon import into mitochondrion"
FT /id="PRO_0000013298"
FT DOMAIN 5..277
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 278..593
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT BINDING 29..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 704
FT /note="R->D: Impaired import into mitochondrion."
FT /evidence="ECO:0000269|PubMed:10669756"
FT MUTAGEN 705
FT /note="R->D: Impaired import into mitochondrion."
FT /evidence="ECO:0000269|PubMed:10669756"
SQ SEQUENCE 706 AA; 80576 MW; 626FD0FB2A5520F5 CRC64;
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
