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Database: UniProt
Entry: A0A1Y2K8S1_9PROT
LinkDB: A0A1Y2K8S1_9PROT
Original site: A0A1Y2K8S1_9PROT 
ID   A0A1Y2K8S1_9PROT        Unreviewed;       361 AA.
AC   A0A1Y2K8S1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Putative cytochrome c peroxidase {ECO:0000313|EMBL:OSM07138.1};
GN   ORFNames=MAIT1_03947 {ECO:0000313|EMBL:OSM07138.1};
OS   Magnetofaba australis IT-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetofaba.
OX   NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM07138.1, ECO:0000313|Proteomes:UP000194003};
RN   [1] {ECO:0000313|EMBL:OSM07138.1, ECO:0000313|Proteomes:UP000194003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IT-1 {ECO:0000313|EMBL:OSM07138.1,
RC   ECO:0000313|Proteomes:UP000194003};
RX   PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA   Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA   Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT   "Combined genomic and structural analyses of a cultured magnetotactic
RT   bacterium reveals its niche adaptation to a dynamic environment.";
RL   BMC Genomics 17:726-726(2016).
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:OSM07138.1}.
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DR   EMBL; LVJN01000015; OSM07138.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2K8S1; -.
DR   STRING; 1434232.MAIT1_03947; -.
DR   Proteomes; UP000194003; 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:SF12; BLL6722 PROTEIN; 1.
DR   PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR   Pfam; PF03150; CCP_MauG; 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:OSM07138.1};
KW   Peroxidase {ECO:0000313|EMBL:OSM07138.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194003}.
FT   DOMAIN          11..132
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          189..355
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   361 AA;  39577 MW;  C061B9C4E60214E0 CRC64;
     MSAANVHADD RMADLGRQLF FDVNLSQNRT QACATCHDPN HGFVDGRDNG VEGMASLGDD
     GKSLGDRNAP TASYAAFVPP FVHNAKGNYV GGLFHDGRAG SLADQAGGPP LNPIEMGLKD
     KAEAVARIQE NPDYVAAFKT LYGADVFSRP ERAYAAMSEA IQAYERTAEF APFDSKYDRY
     LRGEAQLSEQ EELGRTLFFS QQFTNCNLCH QLRTSPMGAQ ETFSNYEHHN IGVPVNTALR
     AKNGAQPEHV DRGLLENPAI DDPAQAGKFK TPTLRNIAVT GPYMHNGVFK DLRTVILFYN
     SYNTKSAKRK INPETGQPFA PPEVAENLSL KELQSGPALD DKRIDALVAF LKTLTDARYV
     E
//
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