ID A0A026X1B2_OOCBI Unreviewed; 223 AA.
AC A0A026X1B2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Peroxiredoxin-6 {ECO:0000313|EMBL:EZA61154.1};
GN ORFNames=DMN91_004855 {ECO:0000313|EMBL:RLU22577.1}, X777_08366
GN {ECO:0000313|EMBL:EZA61154.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA61154.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA61154.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
RN [2] {ECO:0000313|EMBL:RLU22577.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU22577.1};
RX PubMed=30249741; DOI=10.1101/gr.237123.118;
RA McKenzie S.K., Kronauer D.J.C.;
RT "The genomic architecture and molecular evolution of ant odorant
RT receptors.";
RL Genome Res. 28:1757-1765(2018).
RN [3] {ECO:0000313|EMBL:RLU22577.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU22577.1};
RA Mckenzie S.K., Kronauer D.J.C.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. {ECO:0000256|PIRNR:PIRNR000239}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000256|ARBA:ARBA00025719}.
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DR EMBL; KK107063; EZA61154.1; -; Genomic_DNA.
DR EMBL; QOIP01000005; RLU22577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026X1B2; -.
DR STRING; 2015173.A0A026X1B2; -.
DR EnsemblMetazoa; XM_011353324.2; XP_011351626.1; LOC105287654.
DR OMA; HGPMNIP; -.
DR OrthoDB; 103042at2759; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
DR Proteomes; UP000279307; Chromosome 5.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR CDD; cd03016; PRX_1cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR43503; MCG48959-RELATED; 1.
DR PANTHER; PTHR43503:SF4; PEROXIREDOXIN-6; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|PIRNR:PIRNR000239};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000239};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR000239};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRNR:PIRNR000239};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097}.
FT DOMAIN 2..166
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 44
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 223 AA; 25123 MW; 71034221ACB73C76 CRC64;
MVLLGEVFPD FTAETQMGTI KFHEWLGDSW GILFSHPNDF TPVCTTELAR VAKLMPEFKR
LGVKVIALSC NSVESHRKWI KDIKSYGGLT DDEFPYPIIE DQMRKLATAL GMLDPMEVDN
QTGLPMSARA VFIIDPTKKM RLSILYPATT GRNFDEIIRV IESLQLTEKY QVATPVDWKK
GDDVMIDPRV SDSEAKSSYS NIKTVPLPSG KPYLRIVPQP IDA
//
