ID A0A3N4JVV7_9PEZI Unreviewed; 246 AA.
AC A0A3N4JVV7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=L873DRAFT_1809332 {ECO:0000313|EMBL:RPA97854.1};
OS Choiromyces venosus 120613-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Choiromyces.
OX NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPA97854.1, ECO:0000313|Proteomes:UP000276215};
RN [1] {ECO:0000313|EMBL:RPA97854.1, ECO:0000313|Proteomes:UP000276215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=120613-1 {ECO:0000313|EMBL:RPA97854.1,
RC ECO:0000313|Proteomes:UP000276215};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
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; ML120401; RPA97854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4JVV7; -.
DR STRING; 1336337.A0A3N4JVV7; -.
DR Proteomes; UP000276215; 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:UP000276215}.
FT DOMAIN 4..67
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 137..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 246 AA; 26030 MW; BE68066A8150425F CRC64;
MIDPFQTLFA VPLECDACVQ DISNSLKKLP GILSVDANLQ KQLVTVEGTA APSAIVSAIQ
DTGRDAILRG SGKSNSAAVA ILETHAKDTP SPVRGLVRMV QVSSKLTILD LTLQGLSPST
YYATIRTAGD ISRGAASTGD VWGRQESEKG EAVDVPPRGN FGSIGVGKSG TASVLLDKPI
QVWEIIGRSF VVSKERDGCF KPDDPDTVVG VIARSAGVWE NEKTVCSCSG KTIWDERKEN
IGRGMV
//
