ID H2AWT5_KAZAF Unreviewed; 312 AA.
AC H2AWT5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN Name=KAFR0F02380 {ECO:0000313|EMBL:CCF58835.1};
GN ORFNames=KAFR_0F02380 {ECO:0000313|EMBL:CCF58835.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF58835.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF58835.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; HE650826; CCF58835.1; -; Genomic_DNA.
DR RefSeq; XP_003957970.1; XM_003957921.1.
DR AlphaFoldDB; H2AWT5; -.
DR STRING; 1071382.H2AWT5; -.
DR GeneID; 13884303; -.
DR KEGG; kaf:KAFR_0F02380; -.
DR eggNOG; KOG2792; Eukaryota.
DR HOGENOM; CLU_050131_0_1_1; -.
DR InParanoid; H2AWT5; -.
DR OrthoDB; 169656at2759; -.
DR Proteomes; UP000005220; Chromosome 6.
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 InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220}.
FT DOMAIN 127..295
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 165
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 169
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 256
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 165..169
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 312 AA; 36312 MW; 21B88807DCB6476A CRC64;
MNKFSLRTVN YPLKLYSKFK DPVRPKFGLQ GKALFSSTRY RLDGSGDSNI EESILNDLKK
VRLDQIRVND GRSTDFRNLK TTDKKGGNGN KTRQWLGIGA FVTLCSGSYY YLLRKKSRLE
VEKIAESNRQ LLDGQFQLTD FNGQKFTQDD LLGKFSIIYF GFTHCPDVCP TELDRLTVWL
KKLEKKRGIK PNAIFVTCDP IRDTPDVLKR YLKDFHPSII GLTGTYDQIK DMCKNFKVFF
STPRNVSPQE DYIVDHSAFF YLLDPEGQFV EALGTIYEDK DGLERIEKHI DAYVPKAERE
RRMSKWYSFL YK
//
