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Database: UniProt
Entry: G8NY30_GRAMM
LinkDB: G8NY30_GRAMM
Original site: G8NY30_GRAMM 
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.
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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
//
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