ID A0A413G8E3_9FIRM Unreviewed; 448 AA.
AC A0A413G8E3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cytochrome C biogenesis protein {ECO:0000313|EMBL:RGX56962.1};
GN ORFNames=DWV16_01200 {ECO:0000313|EMBL:RGX56962.1};
OS Anaerotruncus sp. AF02-27.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=2292191 {ECO:0000313|EMBL:RGX56962.1, ECO:0000313|Proteomes:UP000284135};
RN [1] {ECO:0000313|EMBL:RGX56962.1, ECO:0000313|Proteomes:UP000284135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF02-27 {ECO:0000313|EMBL:RGX56962.1,
RC ECO:0000313|Proteomes:UP000284135};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RGX56962.1}.
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DR EMBL; QSBX01000001; RGX56962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A413G8E3; -.
DR Proteomes; UP000284135; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd02966; TlpA_like_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR31272; CYTOCHROME C-TYPE BIOGENESIS PROTEIN HI_1454-RELATED; 1.
DR PANTHER; PTHR31272:SF4; CYTOCHROME C-TYPE BIOGENESIS PROTEIN HI_1454-RELATED; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF02683; DsbD; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000284135};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 292..442
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 250..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 48541 MW; A7B983887A24AF5B CRC64;
MANLVSTQNI SFLLVFAEGL LSFFSPCVIP LIPVYVSYLA GSAEKGPDGQ PVYARGRTLW
HTVCFVLGIS FAFFLLGMSF SALGQFLGGH KTLLTRIGGV IILLLGLVQI GFFELKFLQR
ERRFHLNLAG KKVSPVMAFV MGFTFSFAWT PCVGPALSSV LILASGAKSA LVGNLLVLVY
AAGFVIPFLL LGLFTAQALT FLERNRKLMK YTIKAGGVIL ILIGIMTFTG WMNGISSYLN
SFGGANVPQA SSSQAVEPPQ PAPSESAASS ESAEPVPASS GASGVAPASE PEPEAFPAFD
FTLTDQYGNT HTLSDYKGKV VFLNFWATWC PPCRQEMPHI EELYNELGMN QEDVVFLGVA
NPKTDSFPHN QDVTVEEVKQ FLTDNGYTFP TVMDETGKVF GDYMINAFPT TFMIDRDGNI
YGYVPGALSK EIMQNIIDQT LEAVPAQG
//