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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//