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Database: UniProt
Entry: L7CDD3_RHOBT
LinkDB: L7CDD3_RHOBT
Original site: L7CDD3_RHOBT 
ID   L7CDD3_RHOBT            Unreviewed;       424 AA.
AC   L7CDD3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Di-heme cytochrome c peroxidase {ECO:0000313|EMBL:ELP31983.1};
DE            EC=1.-.-.- {ECO:0000313|EMBL:ELP31983.1};
GN   ORFNames=RBSWK_04138 {ECO:0000313|EMBL:ELP31983.1};
OS   Rhodopirellula baltica SWK14.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=993516 {ECO:0000313|EMBL:ELP31983.1, ECO:0000313|Proteomes:UP000010959};
RN   [1] {ECO:0000313|EMBL:ELP31983.1, ECO:0000313|Proteomes:UP000010959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SWK14 {ECO:0000313|EMBL:ELP31983.1,
RC   ECO:0000313|Proteomes:UP000010959};
RX   PubMed=23273849;
RA   Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA   Achstetter T., Glockner F.O., Harder J.;
RT   "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT   sulfatases in the genus Rhodopirellula.";
RL   Mar. Genomics 0:0-0(2012).
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:ELP31983.1}.
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DR   EMBL; AMWG01000117; ELP31983.1; -; Genomic_DNA.
DR   RefSeq; WP_007338925.1; NZ_AMWG01000117.1.
DR   AlphaFoldDB; L7CDD3; -.
DR   PATRIC; fig|993516.3.peg.4425; -.
DR   Proteomes; UP000010959; 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   Pfam; PF00034; Cytochrom_C; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 2.
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:ELP31983.1};
KW   Peroxidase {ECO:0000313|EMBL:ELP31983.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           39..424
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003972240"
FT   DOMAIN          103..230
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          285..408
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   424 AA;  46291 MW;  389A1A6AD5610DB8 CRC64;
     MLRFNDAFPN TLNFTMTIHR FLMCAAATLV AAGPTAFAAE TVSLGDPTLT AGIPGDGPLT
     LEQAQRFLAD DDNHTELNVE LPKGLDAASG NIYIPEDNPI TRAKIELGRQ LYFDPRLSAD
     GTISCATCHA PETGWGAPTQ FGEGIRGQTG NRNSPVSFNR ILSKHQFHDG RAASLEEQAV
     GPIANPIEMG NTHEVCVKTL ADNPVYKAQF DKVFDDGVTI DNIGKALATF ERAIVTGPAP
     YDYYAPLSAF EKTFAEDLEY LDEEPALAEQ YAKLKEEAAK NPMTESSIRG MELTFGKANC
     TACHAGANFT DEQFHNIGVG MDSENPDLGR FEVTKEEKDR GAFKTPTMRN VADTGPYMHD
     GSQATLEEVI EWYNKGGHPN PYLSDKMKPL NLTEQEKADL VEFMRQGLQS DFPVIEAGRL
     PAEG
//
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