ID A0A1S3BT48_CUCME Unreviewed; 1644 AA.
AC A0A1S3BT48;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN Name=LOC103492878 {ECO:0000313|RefSeq:XP_008451646.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008451646.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|RefSeq:XP_008451646.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR RefSeq; XP_008451646.1; XM_008453424.2.
DR GeneID; 103492878; -.
DR KEGG; cmo:103492878; -.
DR eggNOG; KOG1651; Eukaryota.
DR eggNOG; KOG1904; Eukaryota.
DR InParanoid; A0A1S3BT48; -.
DR OrthoDB; 4271850at2759; -.
DR Proteomes; UP000089565; Unplaced.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12550; HEPATOMA-DERIVED GROWTH FACTOR-RELATED; 1.
DR PANTHER; PTHR12550:SF49; JIL-1 ANCHORING AND STABILIZING PROTEIN, ISOFORM A; 1.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF00255; GSHPx; 1.
DR Pfam; PF00855; PWWP; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SMART; SM00293; PWWP; 1.
DR SMART; SM00582; RPR; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000499};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW Reference proteome {ECO:0000313|Proteomes:UP000089565}.
FT DOMAIN 24..81
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 865..1006
FT /note="CID"
FT /evidence="ECO:0000259|PROSITE:PS51391"
FT DOMAIN 1474..1636
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 134..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1644 AA; 181934 MW; F0D726CD9F7B7897 CRC64;
MAPSRRKGAG KAAIAAASRR QWKVGDLVLA KVKGFPAWPA TVSEPEKWGY STDWKKVLVY
FFGTQQIAFC NPADVEAFTE EKKQSLLVKR QGKGADFVRA VQEIIDCHEK LKECDNNDEI
ISSDDLARVN GGSVVDSSAN VGSKDETEAP VANNDNLQSN NSLSSRDTSE PALPLKFVLA
GAQGNSLLDN MARRDQSTDA DASEQPFPAC TSSRKRSGGT RLKSSVTKRN VSVQRSRSSS
RMESRRLQHL AIPFSSGDIV ANNIPEVLLR RNKRNRKSPD GSDCDDATSE ALISNVSIED
NASEIVTADS DTYSLNECST IDSGCKFEHS ETAVECLERD VEFGKGLDLH IKAVVIKKKR
KPMRKRVIND ASEDNGGAQD KEEILEAVVD NSNQCLQNGC ENKTERCSKE NGDEHLPLVK
RARVRMSEVS SSEDCKRHSD TEEQNQKKAV PFNLSGKVSC YSNSADGSND RVLDTANGVP
NYTSPSKVCT QFSANWSQLC NYKKDQSFCC SVDGESVLPP SKRLHRALEA MSANVAEEDQ
AAAETAVSTR TSTNGCPISS TCSSSHVQIE IKDGNCLGLQ GRTFHDDPSE LKDERFSTNV
NQTITEENGK TPLIVDFDHQ ADQNSQNQQH DFKDDVILEG GGKHIVVADH IDSQLGCHSD
RTVVHMNSVK KESPRELADI RSICGEMDQL LPLEGKSNTD IAGPLIVVSA NPDKDLECSE
NSRMDCELVA GSHDIGKLSH QNGSDEVKGC ADDIMIAKSP KPAVAENCEE NILDVKEVNG
RSPFSVEHII QKDVSEVRCS LSVAGTDDSL TMDSVDPVSI SDRRSLLQNN ISFSPNFHKK
SLGTLLEEVK LESPVSLKLK PKDVEARAAL SSFEAMLGNL TRTKDSIGRA TRVAIECAKF
GFGPKVVEVL TRTLDTESSL HKKLDLFFLI DSITQSSQNL KGNVADIYPP AIQLVLSRLL
AAVAPPGSNA QENRKQCIKV LRLWSQRGVL PEPIVRHHMR ELESLSGSSS VGAYSRRSSR
TERSLDDPLR EMEGMLVDEY GSNSSFQIPG FSMPRMLKDE DEGSDSDGGS FEAVTPEHTS
QACEEFESVP VMEKRRHILE DVDGELEMED VAPPCEVEIS SSNSVVVNAI EAVDNKFEQH
FPPPMAPPLP QDVPPSCPPL PSSPPPQPPP LPPSFSRSDS CVSDFELDRS FRETNSVQDN
LMQPVAQSSN ASGTTQRTAD TVHYPASSNA SGITQRTSDA GQYPASERRD LQMQMPESTS
RSYSNMPGRV LNNGQRDDST ALHNKGYPLR PPHPPPPQDH FTYVHGDHRM KPRWEDPPAS
YSSRFRYADD PDGECFYNDH ERMRHYSYEP HDNWRVPRPF YGSRYHDRGR TSYGPVSCGG
TPCEPTSHSQ RWRFPSRDMN SRNSMPYRQP YEGPVRVSNR GRNDFLAYSL RRWHGSTKVQ
TVSESMCANS VHRTPIFFFL LLLQNLKGMG ASQSVSEKSI HEFTVKDFRG KDVNLNVYKG
KVLLVVNVAS KCGFTDSNYT QLTELYNRYK DQDFEILAFP CNQFLKQEPG TSEDAQEFAC
TRYKAEYPIF QKVRVNGPDT VPVYKFLKAT SNGFLGSRIK WNFTKFLVDK EGVVINRYGP
TTNPLAIEVD VKKALGIASV PADL
//
