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Database: UniProt
Entry: A0A2S4L4E9_9HYPO
LinkDB: A0A2S4L4E9_9HYPO
Original site: A0A2S4L4E9_9HYPO 
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
//
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