OXR1_EMENI
ID OXR1_EMENI Reviewed; 393 AA.
AC Q5B8X6; C8VIW9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Oxidation resistance protein 1;
GN Name=oxr1; ORFNames=AN3004;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
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DR EMBL; AACD01000051; EAA63575.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF83582.1; -; Genomic_DNA.
DR RefSeq; XP_660608.1; XM_655516.1.
DR AlphaFoldDB; Q5B8X6; -.
DR SMR; Q5B8X6; -.
DR STRING; 162425.CADANIAP00010075; -.
DR EnsemblFungi; CBF83582; CBF83582; ANIA_03004.
DR EnsemblFungi; EAA63575; EAA63575; AN3004.2.
DR GeneID; 2874381; -.
DR KEGG; ani:AN3004.2; -.
DR eggNOG; KOG2372; Eukaryota.
DR HOGENOM; CLU_029204_0_1_1; -.
DR InParanoid; Q5B8X6; -.
DR OMA; ASYFSYP; -.
DR OrthoDB; 767847at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
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..393
FT /note="Oxidation resistance protein 1"
FT /id="PRO_0000058115"
FT DOMAIN 147..393
FT /note="TLDc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 393 AA; 42104 MW; 391E011F10953164 CRC64;
MSSASQPDLS TPTTPATSTS SSGTDPPHLN SNDKKSSSST SLHQSAASYF TYPVTHVVSG
LYRRLTDPPT TNSANSTSNN MMSRLRRQNP NPNPNPSSSS SSISSSSQHP VFTPVRTVSP
FQPPPLTPLT LLANEETTPI PLAPQNQLLS RALAEEIRLL VPPRLQLVNS WRLAYSLDRD
GASLSTLYEN CRSVSARSPR AGYVLVVRDA SPSASTIFGA YMTDPPHPDS HYFGTGECFL
WRASVLRPPP ASLSMADGDG GVYSEEALER AGLPPPPSAD TTNVGRSTTL RGEKAQPKSL
APHTHGLAQG GATNSGTTTP DRIRFKAFPY SGVNDYMMFC ETGFLSLGGG STVLGFTSAH
HRFGYLISNA LGRYGEMEAN ISKDDMLPRG IHY
