NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1871991848|ref|WP_180002169|]
View 

MULTISPECIES: superoxide dismutase [Acinetobacter]

Protein Classification

superoxide dismutase( domain architecture ID 11427369)

Mn/Fe superoxide dismutase eliminates superoxide radicals by catalyzing their conversion into hydrogen peroxide and oxygen

CATH:  1.10.287.990
EC:  1.15.1.1
Gene Ontology:  GO:0046872|GO:0004784|GO:0006801
PubMed:  3345848|3315461

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 COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-197 3.71e-123

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 345.96  E-value: 3.71e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848   4 TLPELPYAYDALEPHIDAKTMEIHHAKHHQTYINNINAGIEGT-EWEDLSVEELVSKANqvpEDLKNNVINNGGGHANHS 82
Cdd:COG0605     1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLaELEDKSLEEIIKKLS---EELKRALRNNAGGHWNHT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  83 LFWTVMSPSGGGNPQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWLSVAPDQTIIIESSANQDSPLMHGNTPILG 162
Cdd:COG0605    78 LFWENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLG 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1871991848 163 LDVWEHAYYLKYQNRRPEYIAAFFNVVNWKEVNRR 197
Cdd:COG0605   158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-197 3.71e-123

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 345.96  E-value: 3.71e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848   4 TLPELPYAYDALEPHIDAKTMEIHHAKHHQTYINNINAGIEGT-EWEDLSVEELVSKANqvpEDLKNNVINNGGGHANHS 82
Cdd:COG0605     1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLaELEDKSLEEIIKKLS---EELKRALRNNAGGHWNHT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  83 LFWTVMSPSGGGNPQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWLSVAPDQTIIIESSANQDSPLMHGNTPILG 162
Cdd:COG0605    78 LFWENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLG 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1871991848 163 LDVWEHAYYLKYQNRRPEYIAAFFNVVNWKEVNRR 197
Cdd:COG0605   158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PRK10925 PRK10925
superoxide dismutase [Mn];
1-201 5.24e-92

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 267.94  E-value: 5.24e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848   1 MSYTLPELPYAYDALEPHIDAKTMEIHHAKHHQTYINNINAGIEG-TEWEDLSVEELVSKANQVPEDLKNNVINNGGGHA 79
Cdd:PRK10925    1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESlPEFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  80 NHSLFWTVMSPsgGGNPQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWLSVAPDQTIIIeSSANQDSPLM----- 154
Cdd:PRK10925   81 NHSLFWKGLKK--GTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDKLAVV-STANQDSPLMgeais 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1871991848 155 -HGNTPILGLDVWEHAYYLKYQNRRPEYIAAFFNVVNWKEVNRRYLEA 201
Cdd:PRK10925  158 gASGFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAK 205
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 96-197 1.84e-63

Iron/manganese superoxide dismutases, C-terminal 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. C-terminal domain is a mixed alpha/beta fold.


Pssm-ID: 460691  Cd Length: 102  Bit Score: 191.49  E-value: 1.84e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  96 PQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWLSVAPDQTIIIESSANQDSPLMHGNTPILGLDVWEHAYYLKYQ 175
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQ 80

                          90       100
                  ....*....|....*....|..
gi 1871991848 176 NRRPEYIAAFFNVVNWKEVNRR 197
Cdd:pfam02777  81 NRRADYVKAFWNVVNWDEVEKR 102
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-197 3.71e-123

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 345.96  E-value: 3.71e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848   4 TLPELPYAYDALEPHIDAKTMEIHHAKHHQTYINNINAGIEGT-EWEDLSVEELVSKANqvpEDLKNNVINNGGGHANHS 82
Cdd:COG0605     1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLaELEDKSLEEIIKKLS---EELKRALRNNAGGHWNHT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  83 LFWTVMSPSGGGNPQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWLSVAPDQTIIIESSANQDSPLMHGNTPILG 162
Cdd:COG0605    78 LFWENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPLMAGGTPLLG 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1871991848 163 LDVWEHAYYLKYQNRRPEYIAAFFNVVNWKEVNRR 197
Cdd:COG0605   158 LDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PRK10925 PRK10925
superoxide dismutase [Mn];
1-201 5.24e-92

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 267.94  E-value: 5.24e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848   1 MSYTLPELPYAYDALEPHIDAKTMEIHHAKHHQTYINNINAGIEG-TEWEDLSVEELVSKANQVPEDLKNNVINNGGGHA 79
Cdd:PRK10925    1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESlPEFANLPVEELITKLDQLPADKKTVLRNNAGGHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  80 NHSLFWTVMSPsgGGNPQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWLSVAPDQTIIIeSSANQDSPLM----- 154
Cdd:PRK10925   81 NHSLFWKGLKK--GTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDKLAVV-STANQDSPLMgeais 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1871991848 155 -HGNTPILGLDVWEHAYYLKYQNRRPEYIAAFFNVVNWKEVNRRYLEA 201
Cdd:PRK10925  158 gASGFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAK 205
PRK10543 PRK10543
superoxide dismutase [Fe];
1-196 1.37e-67

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 205.57  E-value: 1.37e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848   1 MSYTLPELPYAYDALEPHIDAKTMEIHHAKHHQTYINNINAGIEGTEWEDLSVEELVSKANqvpedlkNNVINNGGGHAN 80
Cdd:PRK10543    1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIVRSSE-------GGVFNNAAQVWN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  81 HSLFWTVMSPSGGGNPQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWLSVAPDQTIIIESSANQDSPLMHGNTPI 160
Cdd:PRK10543   74 HTFYWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDATPL 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1871991848 161 LGLDVWEHAYYLKYQNRRPEYIAAFFNVVNWKEVNR 196
Cdd:PRK10543  154 LTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAK 189
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
 96-197 1.84e-63

Iron/manganese superoxide dismutases, C-terminal 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. C-terminal domain is a mixed alpha/beta fold.


Pssm-ID: 460691  Cd Length: 102  Bit Score: 191.49  E-value: 1.84e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  96 PQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWLSVAPDQTIIIESSANQDSPLMHGNTPILGLDVWEHAYYLKYQ 175
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTDGLTPLLGLDVWEHAYYLDYQ 80

                          90       100
                  ....*....|....*....|..
gi 1871991848 176 NRRPEYIAAFFNVVNWKEVNRR 197
Cdd:pfam02777  81 NRRADYVKAFWNVVNWDEVEKR 102
PLN02685 PLN02685
iron superoxide dismutase
 9-201 2.49e-61

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 192.91  E-value: 2.49e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848   9 PYAYDALEPHIDAKTMEIHHAKHHQTYINNINAGIEGTEWEDLSVEELV----SKANQVPedlknnVINNGGGHANHSLF 84
Cdd:PLN02685   53 PYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIVGTELDGMSLEDVVlityNKGDMLP------AFNNAAQAWNHEFF 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  85 WTVMSPSGGGNPQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWL-----------SVAP-----DQTIIIESSAN 148
Cdd:PLN02685  127 WESMKPGGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLaykanrldvgnAVNPcpseeDKKLVVVKSPN 206

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1871991848 149 QDSPLMHGNTPILGLDVWEHAYYLKYQNRRPEYIAAFFN-VVNWKEVNRRyLEA 201
Cdd:PLN02685  207 AVNPLVWDYSPLLTIDVWEHAYYLDFQNRRPDYISTFMEkLVSWEAVSAR-LES 259
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
 6-196 6.62e-58

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 180.75  E-value: 6.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848   6 PELPYAYDALEPHIDAKTMEIHHAKHHQTYINNINAGIEGTEWEDLSVEELVSKANqvpedlkNNVINNGGGHANHSLFW 85
Cdd:PTZ00078    1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEELIKEYS-------GAVFNNAAQIWNHNFYW 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  86 TVMSPSGGGNPQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWLSVAPDQTIIIESSANQDSPLMHGN-TPILGLD 164
Cdd:PTZ00078   74 LSMGPNGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPIKDNTgKPLLTCD 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1871991848 165 VWEHAYYLKYQNRRPEYIAAFFNVVNWKEVNR 196
Cdd:PTZ00078  154 IWEHAYYIDYRNDRASYVNSWWNKVNWDFANK 185
PLN02184 PLN02184
superoxide dismutase [Fe]
 2-201 5.49e-53

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 168.77  E-value: 5.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848   2 SYTLPELPYAYDALEPHIDAKTMEIHHAKHHQTYINNINAGIEGTEWEDLSVEELVSKANQVPEDLKnnVINNGGGHANH 81
Cdd:PLN02184   10 NYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTYNNGDLLP--AFNNAAQAWNH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  82 SLFWTVMSPSGGGNPQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWLSVAPDQTIIIEsSANQDSPLMHGNTPIL 161
Cdd:PLN02184   88 EFFWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEKLKVVK-TPNAVNPLVLGSFPLL 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1871991848 162 GLDVWEHAYYLKYQNRRPEYIAAFF-NVVNWKEVNRRyLEA 201
Cdd:PLN02184  167 TIDVWEHAYYLDFQNRRPDYIKTFMtNLVSWEAVSAR-LEA 206
PLN02471 PLN02471
superoxide dismutase [Mn]
 2-203 6.15e-53

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 169.32  E-value: 6.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848   2 SYTLPELPYAYDALEPHIDAKTMEIHHAKHHQTYINNINAGIEgtewedlSVEELVSKAN-QVPEDLKNNVINNGGGHAN 80
Cdd:PLN02471   30 TFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALE-------QLDQAVEKGDaSAVVKLQSAIKFNGGGHVN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  81 HSLFWTVMSPS---GGGNPQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWLSVAPD-QTIIIESSANQDSPLMHG 156
Cdd:PLN02471  103 HSIFWKNLAPVsegGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKElKKLVVETTANQDPLVTKG 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1871991848 157 NT--PILGLDVWEHAYYLKYQNRRPEYIAAFFNVVNWKEVNRRYLEALS 203
Cdd:PLN02471  183 PSlvPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKECN 231
PLN02622 PLN02622
iron superoxide dismutase
 3-201 3.50e-51

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 165.96  E-value: 3.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848   3 YTLPELPYAYDALEPHIDAKTMEIHHAKHHQTYINNINAGIE------GTEWEDLsVEELVSKANQVPEdlknnvINNGG 76
Cdd:PLN02622   48 YGLKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAkddilyGYTMDEL-VKVTYNNGNPLPE------FNNAA 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848  77 GHANHSLFWTVMSPSGGGNPQGEIAQAIDKELGGFEAFKEAFTKAALTRFGSGWAWLSVAPDQ-TIIIESSANQDSPLMH 155
Cdd:PLN02622  121 QVWNHDFFWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREErRLEVVKTSNAINPLVW 200

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1871991848 156 GNTPILGLDVWEHAYYLKYQNRRPEYIAAFFN-VVNWKEVNRRYLEA 201
Cdd:PLN02622  201 DDIPIICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMARMARA 247
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
 2-89 1.55e-37

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: 125.11  E-value: 1.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871991848   2 SYTLPELPYAYDALEPHIDAKTMEIHHAKHHQTYINNINAGIEGTEWEDLSVEELVSKANQvpedlkNNVINNGGGHANH 81
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIKALL------GGLFNNGGGHWNH 74


                  ....*...
gi 1871991848  82 SLFWTVMS 89
Cdd:pfam00081  75 SLFWKNLS 82
 
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