ID E4V557_ARTGP Unreviewed; 257 AA.
AC E4V557;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Superoxide dismutase 1 copper chaperone {ECO:0000256|ARBA:ARBA00016103};
DE AltName: Full=Superoxide dismutase copper chaperone {ECO:0000256|ARBA:ARBA00032899};
GN ORFNames=MGYG_08143 {ECO:0000313|EMBL:EFR05131.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- SIMILARITY: Belongs to the CCS1 family.
CC {ECO:0000256|ARBA:ARBA00010636}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the Cu-Zn superoxide
CC dismutase family. {ECO:0000256|ARBA:ARBA00025798}.
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DR EMBL; DS989829; EFR05131.1; -; Genomic_DNA.
DR RefSeq; XP_003169966.1; XM_003169918.1.
DR AlphaFoldDB; E4V557; -.
DR STRING; 535722.E4V557; -.
DR GeneID; 10025201; -.
DR VEuPathDB; FungiDB:MGYG_08143; -.
DR eggNOG; KOG4656; Eukaryota.
DR HOGENOM; CLU_056632_0_0_1; -.
DR InParanoid; E4V557; -.
DR OMA; KNVWEER; -.
DR OrthoDB; 1693333at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003:SF86; COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669}.
FT DOMAIN 4..67
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 150..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 257 AA; 27972 MW; FAE63CE6B39CB9DD CRC64;
MIEPFQATFA VPLTCESCIK DVSKPLYELA GIKKVDANLA DQLIMVEGTA APSAIVAAIQ
GTGRDAILRG SGTSNNASVC ILETHREDVA NKIRGLVRMV QVSGNLTIFD LTINGLSPGR
YWATIRETGD ISRGPESTGG VWEAVKELKE QQQQSNHNDD KSRKDSEPRG VVGSVDVDEH
GKGSVFLDRP IAVWEMIGRS MVVSRQREGP FSVDDEDTIV GVVARSAGVW DNEKMVCSCS
GKNVWEERRE QLSRGIV
//
