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Database: UniProt
Entry: A0A1Q3QNK8_9BACT
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Original site: A0A1Q3QNK8_9BACT 
ID   A0A1Q3QNK8_9BACT        Unreviewed;      1280 AA.
AC   A0A1Q3QNK8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=BGO25_15295 {ECO:0000313|EMBL:OJV41121.1};
OS   Acidobacteriales bacterium 59-55.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales.
OX   NCBI_TaxID=1895690 {ECO:0000313|EMBL:OJV41121.1, ECO:0000313|Proteomes:UP000186822};
RN   [1] {ECO:0000313|EMBL:OJV41121.1, ECO:0000313|Proteomes:UP000186822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=59-55 {ECO:0000313|EMBL:OJV41121.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJV41121.1}.
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DR   EMBL; MKSV01000007; OJV41121.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3QNK8; -.
DR   STRING; 1895690.BGO25_15295; -.
DR   Proteomes; UP000186822; Unassembled WGS sequence.
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   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR027039; Crtac1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR006597; Sel1-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR011519; UnbV_ASPIC.
DR   PANTHER; PTHR16026; CARTILAGE ACIDIC PROTEIN 1; 1.
DR   PANTHER; PTHR16026:SF0; CARTILAGE ACIDIC PROTEIN 1; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   Pfam; PF13517; FG-GAP_3; 3.
DR   Pfam; PF13432; TPR_16; 3.
DR   Pfam; PF07593; UnbV_ASPIC; 1.
DR   SMART; SM00671; SEL1; 5.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   PROSITE; PS50005; TPR; 6.
DR   PROSITE; PS50293; TPR_REGION; 4.
PE   4: Predicted;
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   DOMAIN          860..1010
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REPEAT          1032..1065
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          1066..1099
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          1100..1133
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          1134..1167
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          1168..1201
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          1202..1235
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   1280 AA;  142987 MW;  D2D195B07B5096D2 CRC64;
     MSDQSNEKSL LSRRALLKSI GFAPLLLRSA PLFGSSFLFA SSRGLSAEQS TFLYNDIRFK
     PHYPAQSSLA DVLRLVAPGS DSYQTEKYAF EIDSLLSQWS QSLRRSAHDH SDLSKLVSTT
     LEASSLRPVK EVPVRSGYGI DVTKRQFGAA TPSGVEQFLK EFQTWLGPVS KVETAEFEIY
     AINEIASTPL TVELQIRYDI VALRSDARRE ERVGSWRTEW TRKEKESENW KVQRWEASEE
     ILSVGDQTTF LDVTAQALGG TESYKSQMLR GVDYWRTVLD GACGMDVYGN NGVAAGDYDN
     DGFDDFYVCQ PAGLPNRLYR NRGDGTFEDV TEKAGVGALD NAACALFADF DNRGLQDLLV
     VCGSGPLLFV NQGDGTFSLK RDAFKFARAP QGTFTHAAIA DYDGDGRLDI FFCTYMYYLG
     LDQYHYPVPY YDARNGPPNC LLHNEGNGHF VEKTDAAGLN VENDRYSFAC AWGDSNSNGH
     PDLTIANDFG SSQLYRNNGD GTFTVASKES RIEDVGAGMS ACWSDFNNDG RQDIYITSMW
     EAAGQRVSEQ AQFHQAAPQN IRALYQRHAR GNALYRNDGN GKFQNIGQQA GVAMGRWSWS
     ADFWDFDHDG YSDLYVTNGY ISAVDRNDIA SFFWRQVVAK SPEDGTASLA YEHGWNAINE
     LIRSDSSWNA YERNVMLANN RDGTFSEVSG VTGLDFLEDS RSFALADIDH DGRLEVILKS
     RNAPQLRILH NAMKHLGDSI AFRLRGHKSN RDAIGAAITV EAGTLRQTKY LQAGSGFLAQ
     HSKEVFFGLG KPEGTLKATV RWPSGLTQQF ESLPANHRIE IEEGNHLFVA KAFASAPKSY
     AQAEPPPTLD PLPAHAETWL IAPLKAPDFS LPDLAGNTRE LRQFKGGFVL LNFWATTAPL
     CREQLRQLHQ HRSAFTAGYL DIVAVNIDDP ADIAAARSMA TGERLSFPVV FATEEIAGIY
     NIIYRYLFDR RRDLALPTSL LLDKDGMIVK IYQGSIDPAR VLEDVRTAPT TVAERVQRAI
     PFKGQLYQGS FQRNDFTYGV ALFQHGYLDQ AAESFQQVIA SKPDDPEGYY NLGTLNLRRN
     DLEQARRYLE QTLKLRPNYP EAWNNLGMIS AQEGHPDQAV ENFQRALQLR PGYEIALLNL
     GNVYRRKGDF TKAEECLSQA LGIQPDDPEV NYSLGMLYAQ QNQLPRAAGY LQKAIELRPA
     YSEALNNLGI VYVRLQNYEK AEEQFKTGIR LVPNNDQAYL NLARLYAIQG NKDKARGVLV
     GLLRVQPQNL RAKQAMDILR
//
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