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Conserved domains on  [gi|13259333|gb|AAK16912|]
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methyl-coenzyme M reductase subunit A, partial [uncultured methanogen MRE-MCR1]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
McorA super family cl29840
Methyl coenzyme M reductase, alpha subunit [Coenzyme transport and metabolism];
1-156 1.86e-113

Methyl coenzyme M reductase, alpha subunit [Coenzyme transport and metabolism];


The actual alignment was detected with superfamily member COG4058:

Pssm-ID: 443235 [Multi-domain]  Cd Length: 554  Bit Score: 332.08  E-value: 1.86e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259333   1 GSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYIKGKY-GIAKAKATLDVVNDVASEVTMYGIEQYEKCPTTLEDHFGGS 79
Cdd:COG4058 324 GSYMSGGVGFTQYATAAYTDNILDDFVYYGVDYVEDKYgGLAKAKPTMDVVKDIATEVTLYGLEQYEKYPALLEDHFGGS 403
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13259333  80 QRATVLAAASGITTSLATGNGNAGLSGWYLSMYLHKEAWGRLGFFGYDLQDQCGATNVFSCRSDEGLLAELRGPNYP 156
Cdd:COG4058 404 QRAAVLAAAAGISTAFATGNANAGLNGWYLSMLLHKEGHGRLGFYGYDLQDQCGAANSLSYRSDEGLPLELRGPNYP 480
 
Name Accession Description Interval E-value
McorA COG4058
Methyl coenzyme M reductase, alpha subunit [Coenzyme transport and metabolism];
1-156 1.86e-113

Methyl coenzyme M reductase, alpha subunit [Coenzyme transport and metabolism];


Pssm-ID: 443235 [Multi-domain]  Cd Length: 554  Bit Score: 332.08  E-value: 1.86e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259333   1 GSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYIKGKY-GIAKAKATLDVVNDVASEVTMYGIEQYEKCPTTLEDHFGGS 79
Cdd:COG4058 324 GSYMSGGVGFTQYATAAYTDNILDDFVYYGVDYVEDKYgGLAKAKPTMDVVKDIATEVTLYGLEQYEKYPALLEDHFGGS 403
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13259333  80 QRATVLAAASGITTSLATGNGNAGLSGWYLSMYLHKEAWGRLGFFGYDLQDQCGATNVFSCRSDEGLLAELRGPNYP 156
Cdd:COG4058 404 QRAAVLAAAAGISTAFATGNANAGLNGWYLSMLLHKEGHGRLGFYGYDLQDQCGAANSLSYRSDEGLPLELRGPNYP 480
met_CoM_red_alp TIGR03256
methyl-coenzyme M reductase, alpha subunit; Members of this protein family are the alpha ...
1-156 6.29e-95

methyl-coenzyme M reductase, alpha subunit; Members of this protein family are the alpha subunit of methyl coenzyme M reductase, also called coenzyme-B sulfoethylthiotransferase (EC 2.8.4.1). This enzyme, with alpha, beta, and gamma subunits, catalyzes the last step in methanogenesis. Several methanogens have encode two such enzymes, designated I and II; this model does not separate the isozymes. [Energy metabolism, Methanogenesis]


Pssm-ID: 132300 [Multi-domain]  Cd Length: 548  Bit Score: 284.49  E-value: 6.29e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259333     1 GSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYIKGKYG-IAKAKATLDVVNDVASEVTMYGIEQYEKCPTTLEDHFGGS 79
Cdd:TIGR03256 319 GSYMSGGVGFTQYATAAYTDNILDDFTYYGKEYVEDKYGgLAEAPASMDVVKDVATEVTLYGLEQYEEYPTALEDHFGGS 398
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13259333    80 QRATVLAAASGITTSLATGNGNAGLSGWYLSMYLHKEAWGRLGFFGYDLQDQCGATNVFSCRSDEGLLAELRGPNYP 156
Cdd:TIGR03256 399 QRAAVLAAAAGCSTAFATGNAQAGLSGWYLSMYLHKEAHGRLGFYGYDLQDQCGAANVLSIRGDEGLPLELRGPNYP 475
MCR_alpha pfam02249
Methyl-coenzyme M reductase alpha subunit, C-terminal domain; Methyl-coenzyme M reductase (MCR) ...
1-121 2.46e-77

Methyl-coenzyme M reductase alpha subunit, C-terminal domain; Methyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (this family), 2 beta (pfam02241), and 2 gamma (pfam02240) subunits with two identical nickel porphinoid active sites. The C-terminal domain is comprised of an all-alpha multi-helical bundle.


Pssm-ID: 396704 [Multi-domain]  Cd Length: 127  Bit Score: 225.78  E-value: 2.46e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259333     1 GSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYIKGKYG-IAKAKATLDVVNDVASEVTMYGIEQYEKCPTTLEDHFGGS 79
Cdd:pfam02249   6 GSYMSGGVGFTQYATAAYTDNILDDFVYYGVDYIKDKYGgLCKVKATMDVVKDIATEVTLYGLEQYEKYPTLLEDHFGGS 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 13259333    80 QRATVLAAASGITTSLATGNGNAGLSGWYLSMYLHKEAWGRL 121
Cdd:pfam02249  86 QRAAVLAAAAGISTAIATGNSNAGLNGWYLSMLLHKEGHGRL 127
 
Name Accession Description Interval E-value
McorA COG4058
Methyl coenzyme M reductase, alpha subunit [Coenzyme transport and metabolism];
1-156 1.86e-113

Methyl coenzyme M reductase, alpha subunit [Coenzyme transport and metabolism];


Pssm-ID: 443235 [Multi-domain]  Cd Length: 554  Bit Score: 332.08  E-value: 1.86e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259333   1 GSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYIKGKY-GIAKAKATLDVVNDVASEVTMYGIEQYEKCPTTLEDHFGGS 79
Cdd:COG4058 324 GSYMSGGVGFTQYATAAYTDNILDDFVYYGVDYVEDKYgGLAKAKPTMDVVKDIATEVTLYGLEQYEKYPALLEDHFGGS 403
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13259333  80 QRATVLAAASGITTSLATGNGNAGLSGWYLSMYLHKEAWGRLGFFGYDLQDQCGATNVFSCRSDEGLLAELRGPNYP 156
Cdd:COG4058 404 QRAAVLAAAAGISTAFATGNANAGLNGWYLSMLLHKEGHGRLGFYGYDLQDQCGAANSLSYRSDEGLPLELRGPNYP 480
met_CoM_red_alp TIGR03256
methyl-coenzyme M reductase, alpha subunit; Members of this protein family are the alpha ...
1-156 6.29e-95

methyl-coenzyme M reductase, alpha subunit; Members of this protein family are the alpha subunit of methyl coenzyme M reductase, also called coenzyme-B sulfoethylthiotransferase (EC 2.8.4.1). This enzyme, with alpha, beta, and gamma subunits, catalyzes the last step in methanogenesis. Several methanogens have encode two such enzymes, designated I and II; this model does not separate the isozymes. [Energy metabolism, Methanogenesis]


Pssm-ID: 132300 [Multi-domain]  Cd Length: 548  Bit Score: 284.49  E-value: 6.29e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259333     1 GSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYIKGKYG-IAKAKATLDVVNDVASEVTMYGIEQYEKCPTTLEDHFGGS 79
Cdd:TIGR03256 319 GSYMSGGVGFTQYATAAYTDNILDDFTYYGKEYVEDKYGgLAEAPASMDVVKDVATEVTLYGLEQYEEYPTALEDHFGGS 398
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13259333    80 QRATVLAAASGITTSLATGNGNAGLSGWYLSMYLHKEAWGRLGFFGYDLQDQCGATNVFSCRSDEGLLAELRGPNYP 156
Cdd:TIGR03256 399 QRAAVLAAAAGCSTAFATGNAQAGLSGWYLSMYLHKEAHGRLGFYGYDLQDQCGAANVLSIRGDEGLPLELRGPNYP 475
MCR_alpha pfam02249
Methyl-coenzyme M reductase alpha subunit, C-terminal domain; Methyl-coenzyme M reductase (MCR) ...
1-121 2.46e-77

Methyl-coenzyme M reductase alpha subunit, C-terminal domain; Methyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (this family), 2 beta (pfam02241), and 2 gamma (pfam02240) subunits with two identical nickel porphinoid active sites. The C-terminal domain is comprised of an all-alpha multi-helical bundle.


Pssm-ID: 396704 [Multi-domain]  Cd Length: 127  Bit Score: 225.78  E-value: 2.46e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259333     1 GSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYIKGKYG-IAKAKATLDVVNDVASEVTMYGIEQYEKCPTTLEDHFGGS 79
Cdd:pfam02249   6 GSYMSGGVGFTQYATAAYTDNILDDFVYYGVDYIKDKYGgLCKVKATMDVVKDIATEVTLYGLEQYEKYPTLLEDHFGGS 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 13259333    80 QRATVLAAASGITTSLATGNGNAGLSGWYLSMYLHKEAWGRL 121
Cdd:pfam02249  86 QRAAVLAAAAGISTAIATGNSNAGLNGWYLSMLLHKEGHGRL 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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