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Conserved domains on  [gi|1018191634|ref|NP_001309745|]
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superoxide dismutase [Mn], mitochondrial isoform D [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sod_Fe_N super family cl02809
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 25-76 2.79e-26

Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one. In humans, there is a cytoplasmic Cu/Zn SOD, and a mitochondrial Mn/Fe SOD. N-terminal domain is a long alpha antiparallel hairpin. A small fragment of YTRE_LEPBI matches well - sequencing error?


The actual alignment was detected with superfamily member pfam00081:

Pssm-ID: 425457  Cd Length: 82  Bit Score: 94.29  E-value: 2.79e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1018191634  25 KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKG 76
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPL 52
 
Name Accession Description Interval E-value
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 25-76 2.79e-26

Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one. In humans, there is a cytoplasmic Cu/Zn SOD, and a mitochondrial Mn/Fe SOD. N-terminal domain is a long alpha antiparallel hairpin. A small fragment of YTRE_LEPBI matches well - sequencing error?


Pssm-ID: 425457  Cd Length: 82  Bit Score: 94.29  E-value: 2.79e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1018191634  25 KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKG 76
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPL 52
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
27-75 2.24e-25

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 94.81  E-value: 2.24e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1018191634  27 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAK 75
Cdd:COG0605     1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDK 49
PLN02471 PLN02471
superoxide dismutase [Mn]
 1-76 3.26e-21

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 85.34  E-value: 3.26e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1018191634   1 MLSRAVCGTSRQLAPVLGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKG 76
Cdd:PLN02471    6 LASRKTLGGLKETSSRLLSFRGLQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKG 81
 
Name Accession Description Interval E-value
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 25-76 2.79e-26

Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one. In humans, there is a cytoplasmic Cu/Zn SOD, and a mitochondrial Mn/Fe SOD. N-terminal domain is a long alpha antiparallel hairpin. A small fragment of YTRE_LEPBI matches well - sequencing error?


Pssm-ID: 425457  Cd Length: 82  Bit Score: 94.29  E-value: 2.79e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1018191634  25 KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKG 76
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPL 52
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
27-75 2.24e-25

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 94.81  E-value: 2.24e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1018191634  27 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAK 75
Cdd:COG0605     1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDK 49
PLN02471 PLN02471
superoxide dismutase [Mn]
 1-76 3.26e-21

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 85.34  E-value: 3.26e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1018191634   1 MLSRAVCGTSRQLAPVLGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKG 76
Cdd:PLN02471    6 LASRKTLGGLKETSSRLLSFRGLQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKG 81
PRK10925 PRK10925
superoxide dismutase [Mn];
26-75 4.83e-16

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 71.11  E-value: 4.83e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1018191634  26 HSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEaLAK 75
Cdd:PRK10925    3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPE-FAN 51
PRK10543 PRK10543
superoxide dismutase [Fe];
28-63 1.09e-10

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 56.50  E-value: 1.09e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1018191634  28 LPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLN 63
Cdd:PRK10543    5 LPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLN 40
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 29-63 3.63e-09

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 52.48  E-value: 3.63e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1018191634  29 PDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLN 63
Cdd:PTZ00078    1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLN 35
PLN02685 PLN02685
iron superoxide dismutase
 32-63 6.39e-07

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 46.92  E-value: 6.39e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1018191634  32 PYDYGALEPHINAQIMQLHHSKHHAAYVNNLN 63
Cdd:PLN02685   53 PYPLDALEPHMSRETLEYHWGKHHRAYVDNLN 84
PLN02622 PLN02622
iron superoxide dismutase
 10-68 5.12e-06

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 44.23  E-value: 5.12e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1018191634  10 SRQLAPVLGYLGsrqkhsLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEK 68
Cdd:PLN02622   38 LQRASKVVAYYG------LKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAK 90
PLN02184 PLN02184
superoxide dismutase [Fe]
 32-62 1.28e-05

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 42.81  E-value: 1.28e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1018191634  32 PYDYGALEPHINAQIMQLHHSKHHAAYVNNL 62
Cdd:PLN02184   17 PFALDALEPHMSKQTLEFHWGKHHRAYVDNL 47
 
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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