OXR1_DEBHA
ID OXR1_DEBHA Reviewed; 323 AA.
AC Q6BJM5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Oxidation resistance protein 1;
GN Name=OXR1; OrderedLocusNames=DEHA2G01320g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: May be involved in protection from oxidative damage.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OXR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG90043.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR382139; CAG90043.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_461596.2; XM_461596.2.
DR AlphaFoldDB; Q6BJM5; -.
DR SMR; Q6BJM5; -.
DR STRING; 4959.XP_461596.2; -.
DR EnsemblFungi; CAG90043; CAG90043; DEHA2G01320g.
DR GeneID; 2904458; -.
DR KEGG; dha:DEHA2G01320g; -.
DR eggNOG; KOG2372; Eukaryota.
DR HOGENOM; CLU_029204_0_0_1; -.
DR InParanoid; Q6BJM5; -.
DR OrthoDB; 1133465at2759; -.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR InterPro; IPR006571; TLDc_dom.
DR Pfam; PF07534; TLD; 1.
DR SMART; SM00584; TLDc; 1.
DR PROSITE; PS51886; TLDC; 1.
PE 3: Inferred from homology;
KW Mitochondrion; Reference proteome.
FT CHAIN 1..323
FT /note="Oxidation resistance protein 1"
FT /id="PRO_0000058114"
FT DOMAIN 91..320
FT /note="TLDc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 36705 MW; 91B068D863CFB7AD CRC64;
MVTDKTNASS SSLVDTPADE TEVQPPINRR PTFLDRLMRR QTSPSSMEYS ESDKKKDGPM
ENEQSKGVRE SSLPPLSQLS LKGYKSSTKR RLLDDELASN IRNLLPARLQ LFDEWDLVYS
LEQHGVSLNT LYQRSNPDYQ LSQLRKNKPE VGYGDSVISS MMSGNVNSMR ERRRPQGYVL
IIKDENNSKF GCFVNEHLRP MDQKRYYGNG ECFLWKSELF TPSPSNSNSE EDISSHLATP
QIRFKAFMYT GINDNIIYSN HDFIAIGSSK GQNGLWIDRS LYNGVSYSCD TFGNEILNSN
SGDAKIGKFK IMGLELWRVG TLE