ID A0A151WF69_9HYME Unreviewed; 701 AA.
AC A0A151WF69;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Peroxiredoxin-5, mitochondrial {ECO:0000256|ARBA:ARBA00014329};
DE AltName: Full=Peroxiredoxin V {ECO:0000256|ARBA:ARBA00031861};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 5 {ECO:0000256|ARBA:ARBA00033191};
GN ORFNames=ALC60_14531 {ECO:0000313|EMBL:KYQ46435.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ46435.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ46435.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ46435.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ46435.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) 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. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events. {ECO:0000256|ARBA:ARBA00003330}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix
CC {ECO:0000256|ARBA:ARBA00004253}.
CC -!- SIMILARITY: Belongs to the importin alpha family.
CC {ECO:0000256|ARBA:ARBA00010394}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000256|ARBA:ARBA00010505}.
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DR EMBL; KQ983227; KYQ46435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151WF69; -.
DR STRING; 64791.A0A151WF69; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IEA:InterPro.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR GO; GO:0006606; P:protein import into nucleus; IEA:InterPro.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.20.5.690; Importin-alpha, importin-beta-binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032413; Arm_3.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR036975; Importin-a_IBB_sf.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR23316; IMPORTIN ALPHA; 1.
DR PANTHER; PTHR23316:SF71; IMPORTIN SUBUNIT ALPHA; 1.
DR Pfam; PF00514; Arm; 8.
DR Pfam; PF16186; Arm_3; 1.
DR Pfam; PF01749; IBB; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50176; ARM_REPEAT; 4.
DR PROSITE; PS51214; IBB; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Transport {ECO:0000256|PROSITE-ProRule:PRU00561}.
FT DOMAIN 33..198
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 159..222
FT /note="IBB"
FT /evidence="ECO:0000259|PROSITE:PS51214"
FT REPEAT 287..330
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 330..372
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 372..400
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 499..533
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 193..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 77
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 701 AA; 77092 MW; 4050C12CCB7E45B8 CRC64;
MSQLLSRVFI NGRQSTFSCL VRRFLISSQK MVIAVGDKLP SVDLFENTPA DMVNLAETTA
QKKIIVFGVP GAFTPGCSKT HLPGYVVKAD ELKSKGISEI FCISVNDPFV MAAWGKEHGA
TGKVRMLADP KAEFTDAMDL AVNLSVLGGK RSKRYSMVVE NGIVKEINMS TGPTHKHRYK
NVGLDSQELR RRREEEGVQL RKQKREQQLS KRRNVPNIVA DEDNVTSTDE YSLPIGTAQS
SPGIITSEMV DALYSPNIQD QLAATQKFRK LLSREPNPPI DEVIQTGIVP QFVEFLKNNT
NCTLQFEAAW ALTNIASGTS QQTRIVIDAG AVPTFISLLG SEYEDVQEQA VWALGNIAGD
SPECRDHVLA NGILTPLLQL LSKATRLSMT RNAVWALSNL CRGKNPAPAF AKVAPCLPVL
AHLLNHTDYD VLADACWALS YLSDGPNDKI QAVIDAGVCR RLVELLMHEQ NNVISAALRA
VGNIVTGDDV QTQVVLNCSA LPCLLHLLSS PRESVRKEAC WTVSNITAGN PQQIQAVIDA
NIFPVLIEIL SKAEFKTRKE AAWAITNATS GGTAEQIRYL AVQGCIPPLC DLLTVMDVKI
VQVALNGIEN ILRLGEQDAT MHNGLNPYAV LIEECYGLDK IEFLQSHQNM DIYQKAFDII
ERFFGSEEED TRLVPSIDSQ GQEYQFIAPD SSHLPVQGFE F
//
