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Conserved domains on  [gi|13259303|gb|AAK16897|]
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methyl-coenzyme M reductase subunit A, partial [uncultured methanogen RS-ME32]

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];
1-239 3.42e-169

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: 477.69  E-value: 3.42e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303   1 FIDAYKMCAGEAAVADLAFAAKHASLVEMADILPARRARGPNEPGGLPFGYLADMVQTNRKYPDDPVKSSLEFVGAGCML 80
Cdd:COG4058 238 FISAYKMCAGEAAVADFAYAAKHAEVINMGTMLPARRARGPNEPGGIPFGFLADIVQTSRVYPDDPAKVSLEVVAAGAML 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303  81 YDQIWLGSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYAKGK-GKIGQTKPTMDVVNDLGTEVTLYGIEQYEKYPTTLE 159
Cdd:COG4058 318 YDQIWLGSYMSGGVGFTQYATAAYTDNILDDFVYYGVDYVEDKyGGLAKAKPTMDVVKDIATEVTLYGLEQYEKYPALLE 397
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303 160 DHFGGSQRATVLAAAAGVTTALATGNSNAGLSAWYLSMYLHKEAWGRLGFFGYDLQDQCGATNVFSCRSDEGAMGELRGP 239
Cdd:COG4058 398 DHFGGSQRAAVLAAAAGISTAFATGNANAGLNGWYLSMLLHKEGHGRLGFYGYDLQDQCGAANSLSYRSDEGLPLELRGP 477
 
Name Accession Description Interval E-value
McorA COG4058
Methyl coenzyme M reductase, alpha subunit [Coenzyme transport and metabolism];
1-239 3.42e-169

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


Pssm-ID: 443235 [Multi-domain]  Cd Length: 554  Bit Score: 477.69  E-value: 3.42e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303   1 FIDAYKMCAGEAAVADLAFAAKHASLVEMADILPARRARGPNEPGGLPFGYLADMVQTNRKYPDDPVKSSLEFVGAGCML 80
Cdd:COG4058 238 FISAYKMCAGEAAVADFAYAAKHAEVINMGTMLPARRARGPNEPGGIPFGFLADIVQTSRVYPDDPAKVSLEVVAAGAML 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303  81 YDQIWLGSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYAKGK-GKIGQTKPTMDVVNDLGTEVTLYGIEQYEKYPTTLE 159
Cdd:COG4058 318 YDQIWLGSYMSGGVGFTQYATAAYTDNILDDFVYYGVDYVEDKyGGLAKAKPTMDVVKDIATEVTLYGLEQYEKYPALLE 397
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303 160 DHFGGSQRATVLAAAAGVTTALATGNSNAGLSAWYLSMYLHKEAWGRLGFFGYDLQDQCGATNVFSCRSDEGAMGELRGP 239
Cdd:COG4058 398 DHFGGSQRAAVLAAAAGISTAFATGNANAGLNGWYLSMLLHKEGHGRLGFYGYDLQDQCGAANSLSYRSDEGLPLELRGP 477
met_CoM_red_alp TIGR03256
methyl-coenzyme M reductase, alpha subunit; Members of this protein family are the alpha ...
1-239 1.50e-138

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: 399.67  E-value: 1.50e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303     1 FIDAYKMCAGEAAVADLAFAAKHASLVEMADILPARRARGPNEPGGLPFGYLADMVQTNRKYPDDPVKSSLEFVGAGCML 80
Cdd:TIGR03256 233 FISAYKQAAGEAAVADFAFAAKHAEVIHMGEMLPARRARGENEPGGVPFGHLADIVQTSRVNYEDPAKVALEVVAAGAML 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303    81 YDQIWLGSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYAKGK-GKIGQTKPTMDVVNDLGTEVTLYGIEQYEKYPTTLE 159
Cdd:TIGR03256 313 YDQIWLGSYMSGGVGFTQYATAAYTDNILDDFTYYGKEYVEDKyGGLAEAPASMDVVKDVATEVTLYGLEQYEEYPTALE 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303   160 DHFGGSQRATVLAAAAGVTTALATGNSNAGLSAWYLSMYLHKEAWGRLGFFGYDLQDQCGATNVFSCRSDEGAMGELRGP 239
Cdd:TIGR03256 393 DHFGGSQRAAVLAAAAGCSTAFATGNAQAGLSGWYLSMYLHKEAHGRLGFYGYDLQDQCGAANVLSIRGDEGLPLELRGP 472
MCR_alpha pfam02249
Methyl-coenzyme M reductase alpha subunit, C-terminal domain; Methyl-coenzyme M reductase (MCR) ...
82-207 1.46e-84

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: 247.35  E-value: 1.46e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303    82 DQIWLGSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYAKGK-GKIGQTKPTMDVVNDLGTEVTLYGIEQYEKYPTTLED 160
Cdd:pfam02249   1 DQIWLGSYMSGGVGFTQYATAAYTDNILDDFVYYGVDYIKDKyGGLCKVKATMDVVKDIATEVTLYGLEQYEKYPTLLED 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 13259303   161 HFGGSQRATVLAAAAGVTTALATGNSNAGLSAWYLSMYLHKEAWGRL 207
Cdd:pfam02249  81 HFGGSQRAAVLAAAAGISTAIATGNSNAGLNGWYLSMLLHKEGHGRL 127
 
Name Accession Description Interval E-value
McorA COG4058
Methyl coenzyme M reductase, alpha subunit [Coenzyme transport and metabolism];
1-239 3.42e-169

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


Pssm-ID: 443235 [Multi-domain]  Cd Length: 554  Bit Score: 477.69  E-value: 3.42e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303   1 FIDAYKMCAGEAAVADLAFAAKHASLVEMADILPARRARGPNEPGGLPFGYLADMVQTNRKYPDDPVKSSLEFVGAGCML 80
Cdd:COG4058 238 FISAYKMCAGEAAVADFAYAAKHAEVINMGTMLPARRARGPNEPGGIPFGFLADIVQTSRVYPDDPAKVSLEVVAAGAML 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303  81 YDQIWLGSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYAKGK-GKIGQTKPTMDVVNDLGTEVTLYGIEQYEKYPTTLE 159
Cdd:COG4058 318 YDQIWLGSYMSGGVGFTQYATAAYTDNILDDFVYYGVDYVEDKyGGLAKAKPTMDVVKDIATEVTLYGLEQYEKYPALLE 397
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303 160 DHFGGSQRATVLAAAAGVTTALATGNSNAGLSAWYLSMYLHKEAWGRLGFFGYDLQDQCGATNVFSCRSDEGAMGELRGP 239
Cdd:COG4058 398 DHFGGSQRAAVLAAAAGISTAFATGNANAGLNGWYLSMLLHKEGHGRLGFYGYDLQDQCGAANSLSYRSDEGLPLELRGP 477
met_CoM_red_alp TIGR03256
methyl-coenzyme M reductase, alpha subunit; Members of this protein family are the alpha ...
1-239 1.50e-138

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: 399.67  E-value: 1.50e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303     1 FIDAYKMCAGEAAVADLAFAAKHASLVEMADILPARRARGPNEPGGLPFGYLADMVQTNRKYPDDPVKSSLEFVGAGCML 80
Cdd:TIGR03256 233 FISAYKQAAGEAAVADFAFAAKHAEVIHMGEMLPARRARGENEPGGVPFGHLADIVQTSRVNYEDPAKVALEVVAAGAML 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303    81 YDQIWLGSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYAKGK-GKIGQTKPTMDVVNDLGTEVTLYGIEQYEKYPTTLE 159
Cdd:TIGR03256 313 YDQIWLGSYMSGGVGFTQYATAAYTDNILDDFTYYGKEYVEDKyGGLAEAPASMDVVKDVATEVTLYGLEQYEEYPTALE 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303   160 DHFGGSQRATVLAAAAGVTTALATGNSNAGLSAWYLSMYLHKEAWGRLGFFGYDLQDQCGATNVFSCRSDEGAMGELRGP 239
Cdd:TIGR03256 393 DHFGGSQRAAVLAAAAGCSTAFATGNAQAGLSGWYLSMYLHKEAHGRLGFYGYDLQDQCGAANVLSIRGDEGLPLELRGP 472
MCR_alpha pfam02249
Methyl-coenzyme M reductase alpha subunit, C-terminal domain; Methyl-coenzyme M reductase (MCR) ...
82-207 1.46e-84

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: 247.35  E-value: 1.46e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259303    82 DQIWLGSYMSGGVGFTQYATAAYTDDILDDFCYYGYDYAKGK-GKIGQTKPTMDVVNDLGTEVTLYGIEQYEKYPTTLED 160
Cdd:pfam02249   1 DQIWLGSYMSGGVGFTQYATAAYTDNILDDFVYYGVDYIKDKyGGLCKVKATMDVVKDIATEVTLYGLEQYEKYPTLLED 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 13259303   161 HFGGSQRATVLAAAAGVTTALATGNSNAGLSAWYLSMYLHKEAWGRL 207
Cdd:pfam02249  81 HFGGSQRAAVLAAAAGISTAIATGNSNAGLNGWYLSMLLHKEGHGRL 127
MCR_alpha_N pfam02745
Methyl-coenzyme M reductase alpha subunit, N-terminal domain; Methyl-coenzyme M reductase (MCR) ...
1-34 5.16e-07

Methyl-coenzyme M reductase alpha subunit, N-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 N-terminal domain has a ferredoxin-like fold.


Pssm-ID: 397045  Cd Length: 269  Bit Score: 49.36  E-value: 5.16e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 13259303     1 FIDAYKMCAGEAAVADLAFAAKHASLVEMADILP 34
Cdd:pfam02745 236 FISAYKMCAGEAAVADLAYAAKHASVIQMGEMLP 269
 
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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