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Database: UniProt
Entry: S2W2J5_9ACTO
LinkDB: S2W2J5_9ACTO
Original site: S2W2J5_9ACTO 
ID   S2W2J5_9ACTO            Unreviewed;       271 AA.
AC   S2W2J5;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Thioredoxin-like fold domain-containing protein {ECO:0000259|Pfam:PF13462};
GN   ORFNames=HMPREF9237_00706 {ECO:0000313|EMBL:EPD26777.1};
OS   Actinotignum schaalii FB123-CNA-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinotignum.
OX   NCBI_TaxID=883067 {ECO:0000313|EMBL:EPD26777.1, ECO:0000313|Proteomes:UP000014393};
RN   [1] {ECO:0000313|EMBL:EPD26777.1, ECO:0000313|Proteomes:UP000014393}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB123-CNA-2 {ECO:0000313|EMBL:EPD26777.1,
RC   ECO:0000313|Proteomes:UP000014393};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Actinobaculum schaalii FB123-CNA2.";
RL   Submitted (MAY-2013) 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:EPD26777.1}.
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DR   EMBL; AGWM01000010; EPD26777.1; -; Genomic_DNA.
DR   RefSeq; WP_016442337.1; NZ_KE150262.1.
DR   AlphaFoldDB; S2W2J5; -.
DR   STRING; 59505.FB03_09005; -.
DR   PATRIC; fig|883067.3.peg.692; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_000288_47_3_11; -.
DR   OrthoDB; 117402at2; -.
DR   Proteomes; UP000014393; Unassembled WGS sequence.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000014393};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..271
FT                   /note="Thioredoxin-like fold domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038682194"
FT   DOMAIN          100..260
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13462"
FT   REGION          26..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   271 AA;  29459 MW;  1608829088F43364 CRC64;
     MRRRSAFAFL GVLAFGLAAC TDTSDAPGVK PTVAATTDST TAPSGPTASA TPSASKEPAH
     LVPIQRGANV VTEKIPAPLD QWGGISIGAD GVAGSVNEGK PVVRVYSDYW CPWCNDLVRD
     HGEELIQMAK DGKITLVYHP NMRFEESPYS VKGEQAEVWF AVNAPDKYLD FHELLYKEGS
     IPVVKHADRA ERQQPDPALI EQFATRVGLD AAQLESLRAT LAADEYLPLL KQLREQFLAD
     GMKYIPAVVI DEKLVSDPNN GNLDQFLAPL K
//
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