ID A0A257W918_9BACT Unreviewed; 508 AA.
AC A0A257W918;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Redoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=B7Z55_10720 {ECO:0000313|EMBL:OYW18392.1};
OS Planctomycetales bacterium 12-60-4.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX NCBI_TaxID=1970541 {ECO:0000313|EMBL:OYW18392.1, ECO:0000313|Proteomes:UP000216774};
RN [1] {ECO:0000313|EMBL:OYW18392.1, ECO:0000313|Proteomes:UP000216774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-60-4 {ECO:0000313|EMBL:OYW18392.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926}.
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:OYW18392.1}.
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DR EMBL; NCBX01000701; OYW18392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257W918; -.
DR Proteomes; UP000216774; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd02966; TlpA_like_family; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF13905; Thioredoxin_8; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559}.
FT DOMAIN 1..157
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 159..318
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 385..408
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 434..469
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 319..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OYW18392.1"
SQ SEQUENCE 508 AA; 55969 MW; 014C8EF1CF233CA7 CRC64;
GDELHLAGPT LGNEDFDLSA YRGKVVVVDF WASWCGFCVE ETAYLQRLYE KYHDQGLEIV
GVSADESRAD LERFVTDNHL PWTQIYFDEE GQRGRDNPAL REHLIRVLPQ LYVLDREGKV
TARLARRHQV EAEVAKSLGV APTPVDEAEA EVKLLAQRLV RPEKAKSPDA PSVEVGSKLE
IAGKTLEGQD FDIRTWRGKP VLVVYWASWC PHCKKELPNI HEAYRRHHAD GLEIVGISVD
KKLDDLQKYL TAHPQPWPNL YRDEDGYRGF DNPLVGQHGV HGVPALFLLD GDGQVVHLKP
RGPQLEIEVA KLLGKEPVTS PDAAPSMQVA AKPPVPNSNL VPSTNPLDYE DTDLAKGVVE
RYDTNGDGVL QTEEWHKMPR QGAGFDKNGD GLVTVEEFAS IVKAAKNNPT ARNAVLPVEK
TQPTAPQTTS KAFSAKDFAA QVLKKFDKDS SGLLEQAEWS ELPGGKPELF DIDKNGTISL
TELTQSITAA RTPPQTAADG DAANAPTP
//
