ID A0A1R3I5I3_COCAP Unreviewed; 1579 AA.
AC A0A1R3I5I3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=CCACVL1_14838 {ECO:0000313|EMBL:OMO77771.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO77771.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO77771.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO77771.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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:OMO77771.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWWV01010692; OMO77771.1; -; Genomic_DNA.
DR STRING; 210143.A0A1R3I5I3; -.
DR EnsemblPlants; OMO77771; OMO77771; CCACVL1_14838.
DR Gramene; OMO77771; OMO77771; CCACVL1_14838.
DR OMA; NERPCEE; -.
DR OrthoDB; 4271850at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
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 CDD; cd20147; PWWP_HULK; 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:UP000188268}.
FT DOMAIN 24..81
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 864..1005
FT /note="CID"
FT /evidence="ECO:0000259|PROSITE:PS51391"
FT DOMAIN 1414..1576
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 156..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1579 AA; 172680 MW; DA955C21306CF549 CRC64;
MAPSRRKGAS KAAAAAAARR QWKVGDLVLA KVKGFPAWPA TVSEPEKWGY SSDWKKVLVY
FFGTQQIAFC NPADVEAFTE EKKQSLLTKR QGKGADFIRA VQEIIDSYEK SKKQDEVVDY
NSADRVAEAK CGNSADSSAS KDLNETHEAT VELRIKTSNA DTNQSDPSVA TEVAPAEAKT
EALHEKEFIA EQPPDKVLVK ETPVLTTYSS RKRSGGLRSQ KSASQQKAPP VRRVRSSSRV
ESSRFQNFMT SNDVTSGADV SANGIHDVSL RKNKRVRKST DASESDDVDS SVLLSNGSTG
DNGSEIATID SDGVSLNDGS TMDSSCKPEH SETVVECSEG DVELCKGLDF QIKAVVIKKK
RKPLRKRVNH DSAEPSVRMD AEADVDLGAN SSRQNLRNMN ESSNERYAKD DGDEHLPLVK
RARVRMGKLL ATDEELTSSS PTEEKPVNEG AVNSFEQMSP SSSCRNDSPA DRDSLARGAL
VSASPSKVET QVHESRLEPW KVMRNQLGCL AGGEAALPPS KRLHRALEAM SANAAEEDQA
CAEHSPAMKL DDRCNGSPIR SCSHATVDDK DTNGLEQCNV DLPANSDSGI LSTSNPTPLE
ILAQSSLEPD ICNESAKIPT NQKHEFHKDV SECVNHFSHD TDEDQNLEHK NRAIFRPTCD
SSDEQLPSKD DSDAEPAGMS NFRAENPDEQ FNMSEHDMNS DPVAGTEKNG KISPQDVSNA
CQCTTEHTSR EKSDSAKSQT DESSLVNSMS EVPKELQPEQ NEKATSSLIC DANSEKDVVV
VRLSPSSADR VDSPARVSPS NASICHTSTS ESANIIRSNG YCSPNIHSSH NKSLYSSVAD
DEGKADTAAS ERPKSVSKCN NYTEAHAALA SFENMLGTLT RTKESIARAT RIAIDCAKFG
VSAKVLEIVS RSLERESSLH RRVDLFFLVD SIAQCSRGLK GDVCGIYPSA IQAALPRLLS
AAAPPGSSAQ ENRRQCLKVL RLWLERRILP DSVIRHHIRE LDSLSASSSG GAFSRRSART
SRTERSLDDP IRDMEGMHVD EYGSNSSFQL PGFCMPRMLK DEDEGSDSDG ESFEAVTPEH
CSRTPDEQET NTANEKRRHI LEDVDGELEM EDVAPEIEMS STGGIGINIA QTSHDQNPPL
SFAPPLPHDV PPSLPPLPSS PPPPAPPPPP PPPSIAPHCP ISDPFASGVD SAIHTNIHVR
SPCLQDATVP PSVAPRINST MCNNAVPYHG PESRDHPCPM QVSDCNTSFN GYPVHPVNNI
QQLDGPNFHH NSYPPRPPHP SQTSQFSYVN SGQHHMNSMR DAPPPPYPNR YYSPNVDGGN
YYNSHERMKL APNEPRESWR LPPPPFSGPR YDDKIKASYG HGSYGGPQCE PTRMPNQGWG
YHPPAMNHRN SFPVRPPPEG AVPVGSREMG ASESVPQKSI HEFTVKNSKG QDVDLSIYKG
KVLLVVNVAS KCGFTDVNYT QLTDLYSKYR NQGLEILAFP CNQFLKQEPG SSQEAEEFAC
TRYQAEYPIF RKVRVNGPNT EPVYKFLKSS KSGFLGSRVK WNFTKFLVDK DGHVIGRYGP
TTAPLAIETD IKKAMEADT
//
