ID A0A1H3VR17_9FIRM Unreviewed; 517 AA.
AC A0A1H3VR17;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Cytochrome c-type biogenesis protein {ECO:0000313|EMBL:SDZ76562.1};
GN ORFNames=SAMN02745687_00328 {ECO:0000313|EMBL:SDZ76562.1};
OS Lachnospiraceae bacterium NK3A20.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=877406 {ECO:0000313|EMBL:SDZ76562.1, ECO:0000313|Proteomes:UP000199449};
RN [1] {ECO:0000313|EMBL:SDZ76562.1, ECO:0000313|Proteomes:UP000199449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NK3A20 {ECO:0000313|EMBL:SDZ76562.1,
RC ECO:0000313|Proteomes:UP000199449};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FNQX01000006; SDZ76562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3VR17; -.
DR OrthoDB; 9809733at2; -.
DR Proteomes; UP000199449; 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; 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; 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:UP000199449};
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..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 356..510
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 281..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 55673 MW; 12BCBBE41758AE07 CRC64;
MGFDIQTNLN ALTVFLAGIV SFFSPCVLPL LPMYFGYLSG GTKRDADGTV HYDRLRVFVN
TIFFVFGIGF AFSVLGLGMT ALGRFLRGNT AVFTRVGGVL VLLFGIWQLL SWLRDTGILH
TEESTVSYDV PGANTGRLQI MVARLRTFLA TERRLPIHFE NISMSPLSAL LFGFVFSFAW
TPCIGPTLSS VLVMAATAGS NMHGFLYIAL YTLGFVLPFL AVGLFTQAIL EKLKRHRNIA
RIAMALGALL LILMGIGMLT GGVNHLSSYL AQRSGSIETT EQAAGENSVA SAGAADGSSA
DGSAAATTGQ AASAGTENAS GTDSSTSTES PAIGDVIASH EENEGEVTVE DPETAKVQLL
PAVDFTLHDQ YGETHSLSGY RGKTVFLNFW ATWCNPCVAE MPDIQKLYEE FESGVNADDD
PDNDVVILGI AAPDYGAETS EEGIKAFLED HDITYPVLMD PAADEDLYLD YYITAFPTTY
MIDRDGNVFG YITGSMSEDV MRQIIDQTQK GRGGAIH
//
