ID A0A5A7QS49_STRAF Unreviewed; 1650 AA. AC A0A5A7QS49; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 26-FEB-2020, entry version 3. DE RecName: Full=Peroxidase {ECO:0000256|SAAS:SAAS01215714}; DE EC=1.11.1.7 {ECO:0000256|SAAS:SAAS01215714}; GN ORFNames=STAS_23809 {ECO:0000313|EMBL:GER46751.1}; OS Striga asiatica (Asiatic witchweed) (Buchnera asiatica). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Orobanchaceae; Buchnereae; Striga. OX NCBI_TaxID=4170 {ECO:0000313|EMBL:GER46751.1, ECO:0000313|Proteomes:UP000325081}; RN [1] {ECO:0000313|EMBL:GER46751.1, ECO:0000313|Proteomes:UP000325081} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UVA1 {ECO:0000313|EMBL:GER46751.1, RC ECO:0000313|Proteomes:UP000325081}; RA Yoshida S., Kim S., Wafula E.K., Tanskanen J., Kim Y., Honaas L., Yang Z., RA Spallek T., Conn C.E., Ichihashi Y., Cheong K., Cui S., Der J.P., RA Gundlach H., Jiao Y., Hori C., Ishida J.K., Kasahara H., Kiba T., Kim M., RA Koo N., Laohavisit A., Lee Y., Lumba S., Mccourt P., Mortimer J.C., RA Mutuku J.M., Nomura T., Sasaki-sekimoto Y., Seto Y., Wang Y., Wakatake T., RA Sakakibara H., Demura T., Yamaguchi S., Yoneyama K., Manabe R., RA Nelson D.C., Schulman A.H., Timko M.P., Depamphilis C.W., Choi D., RA Shirasu K.; RT "Genome Sequence of Striga asiatica Provides Insight into the Evolution of RT Plant Parasitism."; RL Curr. Biol. 0:0-0(2019). CC -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, CC biosynthesis and degradation of lignin, suberization, auxin catabolism, CC response to environmental stresses such as wounding, pathogen attack CC and oxidative stress. These functions might be dependent on each CC isozyme/isoform in each plant tissue. {ECO:0000256|SAAS:SAAS01215719}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; CC Evidence={ECO:0000256|SAAS:SAAS01215718}; CC -!- SIMILARITY: Belongs to the peroxidase family. CC {ECO:0000256|RuleBase:RU004241}. 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:GER46751.1}. 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; BKCP01007626; GER46751.1; -; Genomic_DNA. DR Proteomes; UP000325081; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR CDD; cd00693; secretory_peroxidase; 2. DR InterPro; IPR002016; Haem_peroxidase. DR InterPro; IPR010255; Haem_peroxidase_sf. DR InterPro; IPR000823; Peroxidase_pln. DR InterPro; IPR019794; Peroxidases_AS. DR InterPro; IPR033905; Secretory_peroxidase. DR Pfam; PF00141; peroxidase; 3. DR PRINTS; PR00458; PEROXIDASE. DR PRINTS; PR00461; PLPEROXIDASE. DR SUPFAM; SSF48113; SSF48113; 3. DR PROSITE; PS00436; PEROXIDASE_2; 2. DR PROSITE; PS50873; PEROXIDASE_4; 2. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR600823-3}; KW Disulfide bond {ECO:0000256|SAAS:SAAS01215711}; KW Heme {ECO:0000256|SAAS:SAAS01215736}; KW Iron {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|SAAS:SAAS01215715}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3, KW ECO:0000256|SAAS:SAAS01215733}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS01215720}; KW Peroxidase {ECO:0000256|SAAS:SAAS01215725, ECO:0000313|EMBL:GER46751.1}. FT DOMAIN 953..1216 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|PROSITE:PS50873" FT DOMAIN 1303..1616 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|PROSITE:PS50873" FT REGION 1..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 813..848 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1199..1221 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 9..47 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1350 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1" FT METAL 1351 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 1354 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 1356 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 1358 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 1360 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 1372 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 1479 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 1480 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 1511 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 1516 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 1449 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2" FT SITE 1346 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4" SQ SEQUENCE 1650 AA; 181199 MW; EC2011477A5E28AE CRC64; MMGFSPMGSG AGANSSSSTS NLSALAPPFT VDRSNPKLNS NPNLPYHDSP YTAEPYSHGW EYSIPSAPIV LESTGLASVP LPDDHRFSAA TTVSPTITHW STFSRVDKAS TSASYGDVKP YYSPYVPRLV GDESPLVEVD VTCYNKGPTS QIDYTRGVWD VDYEAGWAGN LGLNDGKRAN RVEIEGSFFE KSNIGDLQSY GHQLNQGWLD TEKNEKVSKE GSYGISNQIF NQVPDTGIHC GNSVVTQTKD NLCHEQNLGF FPYDSNKSLT SAYKSTYRES QELAVHKNSL DDQNSSTKCR KTVDKPFIGH VSSNMRSSAG VIRLPPANNG YIKQCTFARK STQCDSDESV RIANFGSISD SQLKEGSSET SLFGISNEGN FLTPLKELSI PLQSSDSLDR TCRAGFGSQS HDESIYGGFN MAGGNSVQTV KSNENSLDFV VDSPCWKGTS CSQFSTFDIE AGNSNNFKKK LDGYYESNHE AQQKNLDSVI DIDRTFFGKA SESNSNIGKN ESDTHCSSKD NSLLGDGKCR GWVAKENETL NEPNMPRKQS VLAKDLAGEF DAKTPDAKHL IDKVAKTISL NDVTEGGFVA VHAAEKVLAS PASQEDANER IKETDWKLHV PTVLKAMHNL SELLMFHLSG ESCSLEKENI ETLENTISNL NSCLHSKITE ASKKPKLNNP VRNSSGKLLE SRNMHTLEHE GNNSYFGKKD EKSPILSPLM DGIDMSSDDS MTKAIKKVLE ENFLLNEEIH SEALLFKNLW LDAEAKLCSI SYKARFDRMK IQMEQIRIKG SQDNEDCEGI SSDEVSISPA DITASEVGPK GPHDDQIVPK PALQDIPASS TGGPTDDVDA SVLARFNILK SREENAKPNK GFSGEQNEDP IVASLKLREE NFGKLMGMEE YENQPRSSEM NDACENTSLH EFHHSVTNND PTVHSCRNNL GRRDSSSSDW EHVLKDDFSC RTCVNVVSIV KEEVTSEYNN KDQFIASALL RLHFHDCFVR GCDGSILLDS TPGKLAEKDA PPNNPSLRKK AFALIDRIKG RLESLCPGVV SCADILAFAA RESVLLAGGP VYYLEGGRND GRISNATEAT QNLPKPQSNY KTLTEAFNGT ADPSLNKSSA DFLRGYCKRV PQPLVNMDDT PNAFDTKYYE YVLEGKVVLS SDNALLNNKD SRSRVKQYNE SSNKWFQDFA KAMEKMAKLS DTDPNNPDNE DCEGISSDEV SISPADITAS EVGPEGPHDD QIIPKPAMVP FVSINNEDCE GISSDEVSIS PADITASEVD PKGPHDDQIV PKPAFEDITS SRALQKDYYK NKCFGHGKQY NVEALVSDEV KSAYRSDKSI APALLRLHFH DCFVRGCDAS ILLDSTRGKP AEKVAPPNNP SIKQSTLDRI NYIKGQLESL CKGVVSCADI IAFAARDSVV LTGGKSYEVL GGRMDGRISN ASEAKSMVPS PQSNYKTLSD AFKKKNLTEV HMIALSGAHT IGQTNCSSVT KRPAPASCSR NPQKLVDMEN TPQKFDNGYY NRVLQRQALF SSDNALLNNK ISQTIVKRYN GSFDQWFHDF AIAMQKMGEI LDTDKSNHGE IRSDCRKFAE AMVKMGSIEV LTGSQGEVRA NCRVINGDCH EESSGKDILR MCAVDEDNLG MLPAARKGRR //