ID A0A0F8CXW2_CERFI Unreviewed; 554 AA.
AC A0A0F8CXW2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Protein SCO1 mitochondrial {ECO:0000313|EMBL:KKF95492.1};
GN Name=SCO1 {ECO:0000313|EMBL:KKF95492.1};
GN ORFNames=CFO_g2138 {ECO:0000313|EMBL:KKF95492.1};
OS Ceratocystis fimbriata f. sp. platani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF95492.1, ECO:0000313|Proteomes:UP000034841};
RN [1] {ECO:0000313|EMBL:KKF95492.1, ECO:0000313|Proteomes:UP000034841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFO {ECO:0000313|EMBL:KKF95492.1,
RC ECO:0000313|Proteomes:UP000034841};
RA Belbahri L.;
RT "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT trees.";
RL Submitted (APR-2015) 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:KKF95492.1}.
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DR EMBL; LBBL01000092; KKF95492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8CXW2; -.
DR Proteomes; UP000034841; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034841};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 111
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 115
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 202
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 111..115
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 554 AA; 61469 MW; E11141EF6091E2AF CRC64;
MSSALPLRAA ARCTSLVRGA KTIGEAKSRM RFGPFSWQAG VLCLVTLGGL MIYFENEKKR
MHQKRIAEAN KQIGRPKIGG PFELLDQNGK LFSSEDLKGR YSLVYFGFTH CPDICPEELD
KMAEMMNIVN KKIPGSVKPV FITCDPARDG PAELKTYLAE FDSNLVGLTG TYEQIKAVCK
SYRVYFSTPS KVKPGEDYLV DHSIYFYLMD PNGDFVEALG RQHSPQAAAD IIQGHPQTCY
RARFDPPHFV FTPQACYCFN IDGVLLHVAK PIPGAAESLQ YLTNNKIPFI LLTNGGGKHE
SDRVSDLASK LGVRLSTENF VQSHTPFQDL VDNSEGLREK TILVTGADAH KCRQIAEAYG
FQSVVTPADI LAAQPNIYPF QTLMTEVYAN TWRPLPKPLY NPDQPTADAL KIDAVFVFND
PRDWSLDIQI ITDILQSHNG IIGTYSPKNG KSSLPNNGWQ GDGQPRVYFS NPDLLWAAHF
HQPRLGQGAF QASLDGVWRA ITGGHSLQRG KPGDTVDSLH NVYMVGDNPE SDIRGANEFR
SLLFQMCARQ LDGP
//
