ID A0A2S4L4E9_9HYPO Unreviewed; 861 AA.
AC A0A2S4L4E9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Protein SCO1, mitochondrial {ECO:0000313|EMBL:POR37287.1};
GN ORFNames=TPAR_02511 {ECO:0000313|EMBL:POR37287.1};
OS Tolypocladium paradoxum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=94208 {ECO:0000313|EMBL:POR37287.1, ECO:0000313|Proteomes:UP000237481};
RN [1] {ECO:0000313|EMBL:POR37287.1, ECO:0000313|Proteomes:UP000237481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRBC 100945 {ECO:0000313|EMBL:POR37287.1,
RC ECO:0000313|Proteomes:UP000237481};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:POR37287.1}.
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DR EMBL; PKSG01000265; POR37287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4L4E9; -.
DR STRING; 94208.A0A2S4L4E9; -.
DR OrthoDB; 2876640at2759; -.
DR Proteomes; UP000237481; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02968; SCO; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR006353; HAD-SF_hydro_IIA_CECR5.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR01456; CECR5; 1.
DR NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR PANTHER; PTHR12151:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR Pfam; PF13344; Hydrolase_6; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237481}.
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 241
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 245
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 332
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 241..245
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 861 AA; 94569 MW; 6FD721E867BE2FB3 CRC64;
MDDGRCRALA ASSAGATGRW RRLTKRKQRC PRPRQIFGGD SATAASAPIK RASAPINLPS
STSNDDSPRR LRGRHVAFGR IIKGSAGRIQ QALCSPMPAL FLEQRAAAEA APSDASARPG
TVETTDYAEA DQVQDGRRGQ EPAQHRGILF VATCAGLVWY FEFEKGRMQR KRIADAAKGV
GRPKVGGEFE LVDQDGKPFT SQMMKGKYSL VCPWSEAASP NPSRRLADVR LRQVYFGFTR
CPDICPEELD KMARMLDVVE DKAPGSLLPI FVTCDPERDD PKALKSYLAE FHPAFIGLTG
TYDQIKDLCK KYRVYFSTPQ DVKPGQDYLV DHSIYFYLMD PEGDFVEALG RQHSPDQGAQ
LILDHMKDWK GRTYRPLTSP MPILVSRAIA EARCLSGLAS GASPVALGTQ RPGPALVRLA
LRSRVAYAGG RRFGNSAVLS ERNVGPRSEV PGSPVGEAKS GWGQDASHSA FSDIAFAFDI
DGVLYQGQQG IPGAREMLRS IRSRGIRYVF LTNGGGAHED AKVASLTKRL QMSADEDVIR
NRVIVSHTPM RGWDDAVKSQ TVLITGAHPE AAREIANEYG FSRAVTPADL IHANGTLYPF
DNLKDSVHAR FRELPDGKSA SRITDSYSRD IAADALKIDQ MLVWNDPRDW SLDIQIIHDL
LVSHRGYLGT VSDKNGDASL PNSGWQQDGQ PELWISNLDL FWKTEYPVNR FGTGAFVEAL
RGVWSAVSGG AELRFKALGK PSKLTYDYAH DRLLHYYADM LAAEQGGGAA AERTGHPLRR
VYMIGDNPES DIRGANEFEP ADGTEWVSIL VRTGVWRQTA AEREPRHRPA AVVDDVVDAI
VWALRNEGVA ATREALTGMD G
//