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Database: UniProt
Entry: A0A1E4HXB6_9PROT
LinkDB: A0A1E4HXB6_9PROT
Original site: A0A1E4HXB6_9PROT 
ID   A0A1E4HXB6_9PROT        Unreviewed;       400 AA.
AC   A0A1E4HXB6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Cytochrome C {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ABS89_07310 {ECO:0000313|EMBL:ODU01482.1};
OS   Thiobacillus sp. SCN 63-1177.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=1660147 {ECO:0000313|EMBL:ODU01482.1, ECO:0000313|Proteomes:UP000094540};
RN   [1] {ECO:0000313|EMBL:ODU01482.1, ECO:0000313|Proteomes:UP000094540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA   Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA   Banfield J.F.;
RT   "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT   unravelled with genome-resolved metagenomics.";
RL   Environ. Microbiol. 17:4929-4941(2015).
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:ODU01482.1}.
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DR   EMBL; MEFI01000134; ODU01482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4HXB6; -.
DR   Proteomes; UP000094540; 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:0005506; F:iron ion binding; IEA:InterPro.
DR   CDD; cd00158; RHOD; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR008168; Cyt_C_IC.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   PANTHER; PTHR35008; BLL4482 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR35008:SF4; SOXD PROTEIN; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   PRINTS; PR00605; CYTCHROMECIC.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS51007; CYTC; 1.
DR   PROSITE; PS50206; RHODANESE_3; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..400
FT                   /note="Cytochrome C"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009152204"
FT   DOMAIN          192..275
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          311..393
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   400 AA;  44749 MW;  60CB95EC9BAA3345 CRC64;
     MKKFALTTLA AVMLPALAWS VGTPPSAASK PMMLAANAPA SKSAPLTPAE NLVLGTALLL
     EKERDAFEMS QVFRLALYLR PMRRVYDPNP NLVRAGDDPS AEKTYMERIR SVIKPELVAR
     IDRMALTRKD MEHYLQHHQP LYAVDWKKHP TFALMEYAVN DFHEQIAPPD TIAAKDKDDF
     YIPESVKRIS GKSAGDGKRL FDGICASCHG VDGQGRFPPI AMKSYLSLHS DHEHFEIIKA
     GPPQKPGAPI VMPTFGDKLT DDQIWAIAQY IRSWENHWAD PKNVRRGEAE AKEAGVKFYS
     TPDLHGIWKA KNGNVVILDV QSDIAYRIMG HIPGSKHIRP EELDTKMKTL PKDKEIIIVD
     MFGSQGLAPA TALAKAGYKT SYLANGMMDW HIVRDFQTEY
//
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