ID A0A1F8SYZ3_9CHLR Unreviewed; 662 AA.
AC A0A1F8SYZ3;
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:0000259|PROSITE:PS51007};
GN ORFNames=A2030_02665 {ECO:0000313|EMBL:OGO65032.1};
OS Chloroflexi bacterium RBG_19FT_COMBO_50_10.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797668 {ECO:0000313|EMBL:OGO65032.1, ECO:0000313|Proteomes:UP000177637};
RN [1] {ECO:0000313|EMBL:OGO65032.1, ECO:0000313|Proteomes:UP000177637}
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:OGO65032.1}.
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DR EMBL; MGOJ01000072; OGO65032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8SYZ3; -.
DR Proteomes; UP000177637; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR PANTHER; PTHR33751; CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP; 1.
DR PANTHER; PTHR33751:SF13; CYTOCHROME BC1 COMPLEX CYTOCHROME C SUBUNIT; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 2.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
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|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..662
FT /note="Cytochrome c domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009538689"
FT TRANSMEM 570..589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..144
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 148..235
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 70740 MW; 1DF15A0B537EF05C CRC64;
MHKFSGTILL LGLVILLSAC SFSLAADITP PPGSEQEPAE PAIEPEVSSP VYPIVPPDLE
NGAVLYNQEC AQCHGTSGLG DGSQAAQLSV PVATLGLSDF ARLYNPAEWY TVVTQGNMEK
FMPPFGNLTD RQRWDVVAYA MSLSAPDELG TQGKTLYQEN CSTCHGQSGK GDGPDAATLS
TQPTNFTDQS LMAQRSAASL YQAILSGVAP DMPAYTSTQD DNERWALVSY LRSLTYAIPA
QADNSYPSPA VNAAAAPTIN AYPAPGAYPE PVVNQSPVLT STINISSTAP FLGTVVVQLI
NGSGGDAPSD APVILYGFDN MQNTYSETLS TGVGGVYTFT EVLMPEGRVF LAGTDFASGT
YGSDIVTVDP ATPDLQLQIT VFDSTTDVSL LTTDRVHIFF DFTEPQNTQV IEVFIISNPS
KQAVVAPVQD GTIVTFPLPQ GYTNLQFQDG ELGDRYVEVT QGFADKMTVN PGVGEYQVIF
AFQMPYNRKL DFVQPMFLPT NAVVVMVPES GVKVDSSQLQ DGGTRDFQGS TYHMYNGSSF
IAGSSLEFTV SGNIKQATAS AFSTGTVQNL AIGLGVFGVA LVVGGLWLFR RNQIRVAMQR
SSAGMDQAAT GALIDAIPED EETLMDTIIA LDDQYRAGNL PEEAYLERRA VLKGKLRDIE
QG
//
