ID G8NY30_GRAMM Unreviewed; 739 AA.
AC G8NY30;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Redoxin domain protein {ECO:0000313|EMBL:AEU35618.1};
DE Flags: Precursor;
GN OrderedLocusNames=AciX8_1275 {ECO:0000313|EMBL:AEU35618.1};
OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU35618.1, ECO:0000313|Proteomes:UP000007113};
RN [1] {ECO:0000313|EMBL:AEU35618.1, ECO:0000313|Proteomes:UP000007113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC {ECO:0000313|Proteomes:UP000007113};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA Haggblom M., Woyke T.;
RT "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003130; AEU35618.1; -; Genomic_DNA.
DR RefSeq; WP_014264498.1; NC_016631.1.
DR AlphaFoldDB; G8NY30; -.
DR STRING; 682795.AciX8_1275; -.
DR KEGG; gma:AciX8_1275; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_375429_0_0_0; -.
DR OrthoDB; 102435at2; -.
DR Proteomes; UP000007113; Chromosome.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02966; TlpA_like_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
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 SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007113};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..739
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003513184"
FT DOMAIN 595..734
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 566..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 83645 MW; 408EC8F411A9EC0A CRC64;
MRSSASLLLI AIALGSVRVH GQTTSKPYGC EAPEVRAALD TTLSQDELVK LTITQRVARR
QQVLDALLAK YPHEYLLYRE QLYAIAGTGD WEAPLAALRE RWVSDAKSHP DDPMALMLAG
KVLADKDPLE AIRLLNAAQV KAPKFPWPSF ELSNIYWRGK YADDTKLKEN LERFYALCPS
WVEATYFGNQ IEGVKLRKDL PLLAKTSVAM RAELAKQTDP KRLEDYEILW QREFLTRPPS
EHEAERAQIR QDLDRLQKLV PHGDAHWRLF LISGYQLAGA SNEELARMQS QAAKDFPHEA
PAERLAKERW DKEHPLPDGQ KDADAWKAYE AAKVEKEKTD FQDFPDDPFL QRTEFFFTVQ
DDEYVSEADG LAAVDRYQKS IDEYGGYGIL SAGPADLAKF LLKHGWQPER ALELLKKTST
FKDGGHTKET WSSSLDADTV KRFHRQMVSM DLENLGLILK AAMLAGKPEE AMQFRAAIEE
PPPENKKDLG QYWTNRARFA TLDHHPEDAL VYYRTALDSR TQTPTYSHGI LRDDLTAEFH
TLWTRQGGTE TAWALWNPAA PVADADATQR DGASAAGKPA ATPKGVAATQ EGEWEKVGKE
MPSFELSDFS GKKWRQGDLA GKVVVVVSWA TWCGPCHLQD ALLQKFYDKV KDRKDLTIVS
FNVDENPGQV LPFMQKQGYT FPVLAAFSYE EAQSYVPRTW IIDKQGHWRW VKNGYDESKT
YAEFEKGLLG QIEKAEAGQ
//