NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1679156713|dbj|BBK63568|]
View 

superoxide dismutase, partial [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SodA super family cl29407
Superoxide dismutase [Inorganic ion transport and metabolism];
25-69 6.42e-24

Superoxide dismutase [Inorganic ion transport and metabolism];


The actual alignment was detected with superfamily member COG0605:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 88.65  E-value: 6.42e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1679156713  25 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQE 69
Cdd:COG0605     1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAE 45
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
25-69 6.42e-24

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 88.65  E-value: 6.42e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1679156713  25 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQE 69
Cdd:COG0605     1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAE 45
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 23-69 2.49e-22

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: 81.20  E-value: 2.49e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 1679156713 23 KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQE 69
Cdd:pfam00081  1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEE 47
PLN02471 PLN02471
superoxide dismutase [Mn]
 22-69 1.57e-17

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 73.02  E-value: 1.57e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1679156713  22 QKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQE 69
Cdd:PLN02471   29 QTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQ 76
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
25-69 6.42e-24

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 88.65  E-value: 6.42e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1679156713  25 SLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQE 69
Cdd:COG0605     1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAE 45
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 23-69 2.49e-22

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: 81.20  E-value: 2.49e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 1679156713 23 KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQE 69
Cdd:pfam00081  1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEE 47
PLN02471 PLN02471
superoxide dismutase [Mn]
 22-69 1.57e-17

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 73.02  E-value: 1.57e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1679156713  22 QKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQE 69
Cdd:PLN02471   29 QTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQ 76
PRK10925 PRK10925
superoxide dismutase [Mn];
24-69 5.63e-16

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 68.41  E-value: 5.63e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1679156713  24 HSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQE 69
Cdd:PRK10925    3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPE 48
PRK10543 PRK10543
superoxide dismutase [Fe];
26-61 4.24e-11

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 55.34  E-value: 4.24e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1679156713  26 LPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLN 61
Cdd:PRK10543    5 LPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLN 40
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 27-61 5.64e-09

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 49.40  E-value: 5.64e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1679156713  27 PDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLN 61
Cdd:PTZ00078    1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLN 35
PLN02685 PLN02685
iron superoxide dismutase
 30-61 8.05e-08

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 46.92  E-value: 8.05e-08
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1679156713  30 PYDYGALEPHINAQIMQLHHSKHHAAYVNNLN 61
Cdd:PLN02685   53 PYPLDALEPHMSRETLEYHWGKHHRAYVDNLN 84
PLN02622 PLN02622
iron superoxide dismutase
 5-66 6.23e-07

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 44.62  E-value: 6.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1679156713   5 FSTSRQLAPVLGYLGsrqkhsLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEK 66
Cdd:PLN02622   35 RRSLQRASKVVAYYG------LKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAK 90
PLN02184 PLN02184
superoxide dismutase [Fe]
 30-60 6.82e-06

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 41.27  E-value: 6.82e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1679156713  30 PYDYGALEPHINAQIMQLHHSKHHAAYVNNL 60
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH