ID A0A1F8SZ15_9CHLR Unreviewed; 332 AA.
AC A0A1F8SZ15;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Cytochrome c domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2029_16985 {ECO:0000313|EMBL:OGO65155.1};
OS Chloroflexi bacterium RBG_19FT_COMBO_47_9.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797665 {ECO:0000313|EMBL:OGO65155.1, ECO:0000313|Proteomes:UP000178740};
RN [1] {ECO:0000313|EMBL:OGO65155.1, ECO:0000313|Proteomes:UP000178740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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:OGO65155.1}.
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; MGOG01000078; OGO65155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8SZ15; -.
DR Proteomes; UP000178740; Unassembled WGS sequence.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR PANTHER; PTHR42838; CYTOCHROME C OXIDASE SUBUNIT II; 1.
DR PANTHER; PTHR42838:SF1; NITROUS-OXIDE REDUCTASE; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 4: Predicted;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..134
FT /note="Cytochrome oxidase subunit II copper A binding"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT DOMAIN 221..325
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 253..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 36762 MW; 41CC5EECDDC659F5 CRC64;
MKKEWLARGI VVLGLAIAVV IPTVGWWEQK QGMVVHAHMA ETGGWSPEYL TAEVGKPLHL
QLTSDDVTHG FAVGQLDQPA VDVVPGEMTD VTLVFDKPGK YTFYCTRWCS VNHWRMRGTI
EVTGPEAANE LVKPPLYVTL GLDIDADHQA SVIPEEKPAA WRGALLDREI PDKYWDGEYY
LSQTPVDLWL ALRSEPSLDD LSDQEVWDLM AWVWKSNTTP EELQTGQEIF SANCAACHGE
NGAGDGVFAG QLADSSGDSE SRHITGTQTQ RPANFTDPTH MLSTSPAHLQ GKIIRGGMGT
GMPYWGAIFT EDQVWALVAY LWTFQFDMEA QP
//
