ID K9HPB9_9PROT Unreviewed; 342 AA.
AC K9HPB9;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Thioredoxin domain-containing protein EC-YbbN {ECO:0000313|EMBL:EKV32118.1};
GN ORFNames=C882_3182 {ECO:0000313|EMBL:EKV32118.1};
OS Caenispirillum salinarum AK4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=1238182 {ECO:0000313|EMBL:EKV32118.1, ECO:0000313|Proteomes:UP000009881};
RN [1] {ECO:0000313|EMBL:EKV32118.1, ECO:0000313|Proteomes:UP000009881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK4 {ECO:0000313|EMBL:EKV32118.1,
RC ECO:0000313|Proteomes:UP000009881};
RX PubMed=23409257;
RA Khatri I., Singh A., Korpole S., Pinnaka A.K., Subramanian S.;
RT "Draft Genome Sequence of an Alphaproteobacterium, Caenispirillum salinarum
RT AK4(T), Isolated from a Solar Saltern.";
RL Genome Announc. 1:E00199-12(2013).
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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:EKV32118.1}.
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DR EMBL; ANHY01000004; EKV32118.1; -; Genomic_DNA.
DR AlphaFoldDB; K9HPB9; -.
DR STRING; 1238182.C882_3182; -.
DR PATRIC; fig|1238182.3.peg.930; -.
DR eggNOG; COG3118; Bacteria.
DR Proteomes; UP000009881; Unassembled WGS sequence.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR CDD; cd02956; ybbN; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR Pfam; PF14559; TPR_19; 1.
DR Pfam; PF14561; TPR_20; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000009881};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 51..163
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 342 AA; 36841 MW; FB37BA8C4359F316 CRC64;
MPLERSVDDV NHRRVLDQQT IIQDTDEATM AIILDGAGNP AGGGNQGQGG GAGGDAVKDT
SAATFMADVI EQSQTVPVIV DFWAEWCGPC KSLGPMLEKL VRQSGGKVKM VKVDVDKDQE
LAAQFRIQSI PTVYAFKDGR PVDAFQGALP ESQLKQFIDK LAGGGANVID QALEQAKELL
DQGQADQAAG VYEQILGQDP QNAPAIAGII RCYVAMDEPD AAKELLSQLP ADILAHADVQ
AAKTALELAD TPPADSEEVV ALQKKVEADP ADLQARFDLA NAYYAANKRE EAVDQLLEIF
KRDRTWNEDA ARAQLVKFFE AFGPTDPATI KGRRKLSSMM FA
//
