ID F0YH87_AURAN Unreviewed; 1138 AA.
AC F0YH87;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin Q {ECO:0000256|ARBA:ARBA00042163};
GN ORFNames=AURANDRAFT_66290 {ECO:0000313|EMBL:EGB05629.1};
OS Aureococcus anophagefferens (Harmful bloom alga).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC Aureococcus.
OX NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN [1] {ECO:0000313|EMBL:EGB05629.1, ECO:0000313|Proteomes:UP000002729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT "Niche of harmful alga Aureococcus anophagefferens revealed through
RT ecogenomics.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000280};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000256|ARBA:ARBA00004456}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000256|ARBA:ARBA00038489}.
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DR EMBL; GL833140; EGB05629.1; -; Genomic_DNA.
DR RefSeq; XP_009039757.1; XM_009041509.1.
DR AlphaFoldDB; F0YH87; -.
DR EnsemblProtists; EGB05629; EGB05629; AURANDRAFT_66290.
DR GeneID; 20225731; -.
DR KEGG; aaf:AURANDRAFT_66290; -.
DR eggNOG; KOG0855; Eukaryota.
DR InParanoid; F0YH87; -.
DR OrthoDB; 53812at2759; -.
DR Proteomes; UP000002729; Unassembled WGS sequence.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42801:SF4; AHPC_TSA FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR42801; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Reference proteome {ECO:0000313|Proteomes:UP000002729};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT DOMAIN 149..184
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 189..224
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 849..985
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 249..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1138 AA; 121993 MW; 54EE0BC7D97CAB17 CRC64;
MARVMPRGRH RLSEAQHAEI RRHFRAAFMG STPHQVFLKF AGQHGPRGSA AARDMLRGVR
IHLRLTVQQL PDEDTAAGSE CLRASRARGA EQFGRREEDP ALGLGGVSHA ILHMICTRLK
ALSIQEYVWK HVAEHVEHVD KAKPWLGPSN RTVREAVFEH IDLNGDGQLS VQEFHDVIRH
NLKVSVFELN DEGIMHLVDA LDTDRSGFVN LDELNVLLEK GDAYDPAESA GDDAPGTPDL
SARLQLDKTW VGPRPPLPEG EVRRAERPAS RKSKKRPLFR GWGDRSKRAP RFDAAFLAAK
EAADIARAVA EPVMALLGRR AAALTPVSSH RLSDQTESPN VPGLNACPAT PPAKARSKRR
GRGGALEGAE GGERWAFAAC LAVGSGLWCA LLRLFLKRHK FPYHRHRTEA AALYGLPPLR
MRLAFALALA RAAGAAAPRN ATLAVDASAL PPLVIAGADK GGTSDAFELL LRHGFASKQK
FECEDPSSSP KVRDLCVARS KELGCLYRGG DAASHRDCYR RYAVRGALWM DATPNYLWGW
VNGEDAAARL SALSPNSAVA LLLREPVARL ASLFAHWRSR PIGDELGAAL EPHVLADLAY
LDAMRRDSVY EVVKGRKVVF ARNVSVPRLF GPGGAEVFSL LLRDYPRWAG RALDRATCEA
LVGDKQRTAG PFEAWRNYVS PPPSAAPRPC ARKKCPPRRP AKIPPCPVFV NFVLTSVRRW
VDAFPGRVAV VQSEYYFADR AAFLAAFGLA PRPAFAGPPA APDAAEKVNN RGAYAERGAT
ALTAATRAAL ARFYERPNAE LRALLAARRD LVVVPEPDVA GSWWTMENAL LALCLGVAGA
LRAPVSMSIA VGDKFPSASL SKLGCAGSNS VIYFYGADEA PSCTKQAEGF DASMGDFSGV
KVVGVRNDAG VKDGFSDKYA QSFYVDAGDA IRDEIGIPKD FFGFLGGRET YVVDKAGTVQ
MVFNGQLNPE KHVEAAKAAV AELGASSGGG GFDPSNLAFA PAFYLSPRPT APARAAVGDT
GARLPTRDAP GAPMAGSDDA PSATEAARRA KLERLRGKRR SSKSKAGDQA SSSSPPASAP
TSPDDLGGFP SFDAAAPPAE ASAPTMRGVA EAPPDFGSDA KALEDRWGTA ARATARST
//
