ID Q8PYG6_METMA Unreviewed; 105 AA.
AC Q8PYG6;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 111.
DE SubName: Full=Conserved protein {ECO:0000313|EMBL:AAM30592.1};
GN OrderedLocusNames=MM_0896 {ECO:0000313|EMBL:AAM30592.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM30592.1, ECO:0000313|Proteomes:UP000000595};
RN [1] {ECO:0000313|EMBL:AAM30592.1, ECO:0000313|Proteomes:UP000000595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC {ECO:0000313|Proteomes:UP000000595};
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA Bruggemann H., Lienard T., Christmann A., Bomeke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.P., Gunsalus R.P.,
RA Fritz H.J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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DR EMBL; AE008384; AAM30592.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8PYG6; -.
DR KEGG; mma:MM_0896; -.
DR PATRIC; fig|192952.21.peg.1056; -.
DR eggNOG; arCOG01068; Archaea.
DR HOGENOM; CLU_2230403_0_0_2; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
FT DOMAIN 7..98
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 105 AA; 12013 MW; 74930977AF63FB45 CRC64;
MQYLPIPVLA SVGISEEKES DKYRVIFRDR STWSTTRRAG MEFAASKIIL DEENDHIMGA
HILGPNAEEV INIFAMAMRL GLRTSDIRKV VFTYPTICSD IRYML
//
