ID   A0A3M8GCE0_9FLAO        Unreviewed;       395 AA.
AC   A0A3M8GCE0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Cytochrome-c peroxidase {ECO:0000313|EMBL:RNC87189.1};
GN   ORFNames=ED556_07145 {ECO:0000313|EMBL:RNC87189.1};
OS   Winogradskyella sp.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=1883156 {ECO:0000313|EMBL:RNC87189.1, ECO:0000313|Proteomes:UP000278005};
RN   [1] {ECO:0000313|EMBL:RNC87189.1, ECO:0000313|Proteomes:UP000278005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bin3 {ECO:0000313|EMBL:RNC87189.1};
RA   Zheng Q., Wang Y., Jiao N.;
RT   "Metagenomics and metaproteomics analyze the interactions between
RT   Synechococcus and associated heterotrophic bacteria in one oligotrophic
RT   Synechococcus culture.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RNC87189.1}.
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DR   EMBL; RHLG01000002; RNC87189.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8GCE0; -.
DR   Proteomes; UP000278005; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR   PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR   PANTHER; PTHR30600:SF10; METHYLAMINE UTILIZATION PROTEIN; 1.
DR   Pfam; PF03150; CCP_MauG; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Oxidoreductase {ECO:0000313|EMBL:RNC87189.1};
KW   Peroxidase {ECO:0000313|EMBL:RNC87189.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000278005};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..395
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018257599"
FT   DOMAIN          74..183
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          240..379
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   395 AA;  43467 MW;  B377D5D39F6499EE CRC64;
     MKNVLPILLA IALCSCSSDS DNGLTPVDTN DPNQAFDFSQ YFTANFDVLP NYANQDIPNY
     ITRDNTGNNG ISDEGAMLGR VLFYDTNLSV NNSVSCASCH RQELAFSDDD QASLGVNGVT
     GRHSMRLVNA RFSDEARFFW DERANTLEIQ TTMPIQDHVE MGFSGENGDL DFNDLIERLE
     TIDYYPELFN RAFGNETITE ALIQDALAQF IRSIQSFDSR YDEGRENANN DGQPFTNFTD
     QENLGKQLFL QPPVFNNMGV RIAGGIGCAG CHQAPEFSID PNSLNNGVIG SIDNSGADLD
     VTRSPTLRDV VKADGSNNGP FMHLGASNTL TAVLNHYNNI NVAGNTNLDP RLRPNGVGQQ
     LNLTDQERAA VIAFLRTLAG NDIYSNEKWS NPFID
//