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Database: UniProt
Entry: A0A0P6XAL9_9SPHN
LinkDB: A0A0P6XAL9_9SPHN
Original site: A0A0P6XAL9_9SPHN 
ID   A0A0P6XAL9_9SPHN        Unreviewed;       133 AA.
AC   A0A0P6XAL9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Cytochrome c domain-containing protein {ECO:0000259|PROSITE:PS51007};
GN   ORFNames=SZ64_09555 {ECO:0000313|EMBL:KPL68344.1};
OS   Erythrobacter sp. SG61-1L.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL68344.1, ECO:0000313|Proteomes:UP000049978};
RN   [1] {ECO:0000313|EMBL:KPL68344.1, ECO:0000313|Proteomes:UP000049978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG61-1L {ECO:0000313|EMBL:KPL68344.1,
RC   ECO:0000313|Proteomes:UP000049978};
RA   Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA   Pandey G.;
RT   "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT   from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT   of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL   Appl. Environ. Microbiol. 0:0-0(2015).
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:KPL68344.1}.
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DR   EMBL; JXQC01000003; KPL68344.1; -; Genomic_DNA.
DR   RefSeq; WP_054530607.1; NZ_JXQC01000003.1.
DR   AlphaFoldDB; A0A0P6XAL9; -.
DR   STRING; 1603897.SZ64_09555; -.
DR   PATRIC; fig|1603897.4.peg.1830; -.
DR   OrthoDB; 7427921at2; -.
DR   Proteomes; UP000049978; 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   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000049978};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..133
FT                   /note="Cytochrome c domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006132956"
FT   DOMAIN          46..131
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   133 AA;  14523 MW;  FC5746D8DBE8F7AF CRC64;
     MKNDRKFLAL AAMALIAACS AKSDAGEEKP RPALPSQIEA VTFGQKSADP GERLYGKECA
     FCHVGRNTGT IMLQKRLPED VPAQLHQRTD LSADYVKAVV RNGLMNMPVF SRAELSDAEL
     EQIAAYLAKD KSK
//
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