ID A0A010ZPZ5_9ACTN Unreviewed; 193 AA.
AC A0A010ZPZ5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Thiol-disulfide isomerase-like thioredoxin {ECO:0000313|EMBL:EXG79252.1};
GN ORFNames=CryarDRAFT_0283 {ECO:0000313|EMBL:EXG79252.1};
OS Cryptosporangium arvum DSM 44712.
OC Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC Cryptosporangiaceae; Cryptosporangium.
OX NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG79252.1, ECO:0000313|Proteomes:UP000021053};
RN [1] {ECO:0000313|EMBL:EXG79252.1, ECO:0000313|Proteomes:UP000021053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG79252.1,
RC ECO:0000313|Proteomes:UP000021053};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JUL-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:EXG79252.1}.
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DR EMBL; JFBT01000001; EXG79252.1; -; Genomic_DNA.
DR RefSeq; WP_035847779.1; NZ_KK073874.1.
DR AlphaFoldDB; A0A010ZPZ5; -.
DR HOGENOM; CLU_042529_11_1_11; -.
DR OrthoDB; 9796554at2; -.
DR Proteomes; UP000021053; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR CDD; cd02966; TlpA_like_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR013740; Redoxin.
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; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cytochrome c-type biogenesis {ECO:0000256|ARBA:ARBA00022748};
KW Isomerase {ECO:0000313|EMBL:EXG79252.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000021053};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..193
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039558894"
FT DOMAIN 29..189
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 193 AA; 19688 MW; 85ED4AED9E5CBC2A CRC64;
MKRLLAVALV VLLAGCSSSG PADVEPKPTK AAFASSKFAA CPAAAGSAPA DSPLRSVEPL
LCMDPSGKKV TIGAPTGHPV VLNLWGSWCP PCGKEMPAFV RLAASAGDRV SVVGVNTADD
ASRAVAAADE LDVRFANVFD RGEEVRKALG VNALPATAFV SAAGEVVHVH RGTPLTDATL
NALVRQHLGV TVE
//
