ID   RTAI1_ARTBC             Reviewed;         331 AA.
AC   P0DN30; D4B1J8;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Probable zinc-binding oxidoreductase, mitochondrial {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_02327-2;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8WWV3}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE30837.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: ARB_02327-1 and ARB_02327-2.; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000026; EFE30837.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003011477.1; XM_003011431.1.
DR   AlphaFoldDB; P0DN30; -.
DR   SMR; P0DN30; -.
DR   STRING; 663331.P0DN30; -.
DR   EnsemblFungi; EFE30837; EFE30837; ARB_02327.
DR   GeneID; 9523245; -.
DR   KEGG; abe:ARB_02327; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   3: Inferred from homology;
KW   Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..331
FT                   /note="Probable zinc-binding oxidoreductase, mitochondrial"
FT                   /id="PRO_0000434427"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   331 AA;  35838 MW;  24D48CDB0A4B24E0 CRC64;
     MASVTSVPKT GRSVNQDVPA TTLTLQTRPT PAPNFDEGEH LIRVHATALC AGELYWHTYV
     TFTKEETVPG PDVAGTVVLA PPSSPFKPGD DVYCRIPYSR AGGARDHTIA LTSELARKPK
     NLTWEEAATV PLSALTAWQA LFDQSGLWEG PEDERVKGKR VAVTAASGAV GMWILQFARI
     AGFDAVIGTC GDGNEDFVKS MGATDAVNYK TTSLTAWAAE KQGRKADLVI DCFGGKSLAD
     AWGCVKDGGV LISMVGYPEQ EKPAGLEVKD VKSHFFIMEP RGDQLQKVTE LVEQGKCSFL
     MDSVYPLEQF QEATDKVESR RVRGKVVLKV L