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Conserved domains on  [gi|84997794|ref|XP_953618|]
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Fe/Mn superoxide dismutase (SOD), putative [Theileria annulata]

Protein Classification

superoxide dismutase( domain architecture ID 11487980)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
6-209 4.38e-119

Superoxide dismutase [Fe]; Provisional


:

Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 335.99  E-value: 4.38e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794    6 PPLPYGLKDLVPHLSEETLTYHYTKHHAGYVNKLNGLVNGTALENKSLEDivcnnylyvldLLKTESGAVFNNAAQVWNH 85
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEE-----------LIKEYSGAVFNNAAQIWNH 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   86 TFYWHSMSPSGGGEPRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLKSDGTPEVVQTHDAGNPLRyiygicc 165
Cdd:PTZ00078  70 NFYWLSMGPNGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPIK------- 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 84997794  166 sDNTGTPLLACDVWEHAYYVDYRNDRASYVNG--TPCFHSFPQRIL 209
Cdd:PTZ00078 143 -DNTGKPLLTCDIWEHAYYIDYRNDRASYVNSwwNKVNWDFANKNL 187
 
Name Accession Description Interval E-value
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
6-209 4.38e-119

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 335.99  E-value: 4.38e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794    6 PPLPYGLKDLVPHLSEETLTYHYTKHHAGYVNKLNGLVNGTALENKSLEDivcnnylyvldLLKTESGAVFNNAAQVWNH 85
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEE-----------LIKEYSGAVFNNAAQIWNH 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   86 TFYWHSMSPSGGGEPRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLKSDGTPEVVQTHDAGNPLRyiygicc 165
Cdd:PTZ00078  70 NFYWLSMGPNGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPIK------- 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 84997794  166 sDNTGTPLLACDVWEHAYYVDYRNDRASYVNG--TPCFHSFPQRIL 209
Cdd:PTZ00078 143 -DNTGKPLLTCDIWEHAYYIDYRNDRASYVNSwwNKVNWDFANKNL 187
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-196 5.42e-96

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 277.40  E-value: 5.42e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   4 KLPPLPYGLKDLVPHLSEETLTYHYTKHHAGYVNKLNGLVNGTA-LENKSLEDIVCNnylyvldLLKTESGAVFNNAAQV 82
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAeLEDKSLEEIIKK-------LSEELKRALRNNAGGH 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794  83 WNHTFYWHSMSPSGGGEPRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLKSDGTPEVVQTHDAGNPLryIYG 162
Cdd:COG0605  74 WNHTLFWENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPL--MAG 151
                       170       180       190
                ....*....|....*....|....*....|....
gi 84997794 163 iccsdntGTPLLACDVWEHAYYVDYRNDRASYVN 196
Cdd:COG0605 152 -------GTPLLGLDVWEHAYYLDYQNRRPDYVD 178
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
100-196 2.33e-44

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: 143.34  E-value: 2.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   100 PRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLKSDGTPEVVQTHDAGNPLRYiygiccsdnTGTPLLACDVW 179
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTD---------GLTPLLGLDVW 71
                          90
                  ....*....|....*..
gi 84997794   180 EHAYYVDYRNDRASYVN 196
Cdd:pfam02777  72 EHAYYLDYQNRRADYVK 88
 
Name Accession Description Interval E-value
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
6-209 4.38e-119

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 335.99  E-value: 4.38e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794    6 PPLPYGLKDLVPHLSEETLTYHYTKHHAGYVNKLNGLVNGTALENKSLEDivcnnylyvldLLKTESGAVFNNAAQVWNH 85
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKGTPLENKTLEE-----------LIKEYSGAVFNNAAQIWNH 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   86 TFYWHSMSPSGGGEPRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLKSDGTPEVVQTHDAGNPLRyiygicc 165
Cdd:PTZ00078  70 NFYWLSMGPNGGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPIK------- 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 84997794  166 sDNTGTPLLACDVWEHAYYVDYRNDRASYVNG--TPCFHSFPQRIL 209
Cdd:PTZ00078 143 -DNTGKPLLTCDIWEHAYYIDYRNDRASYVNSwwNKVNWDFANKNL 187
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
4-196 5.42e-96

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 277.40  E-value: 5.42e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   4 KLPPLPYGLKDLVPHLSEETLTYHYTKHHAGYVNKLNGLVNGTA-LENKSLEDIVCNnylyvldLLKTESGAVFNNAAQV 82
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAeLEDKSLEEIIKK-------LSEELKRALRNNAGGH 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794  83 WNHTFYWHSMSPSGGGEPRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLKSDGTPEVVQTHDAGNPLryIYG 162
Cdd:COG0605  74 WNHTLFWENLSPNGGGEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGKLEIVSTPNQDNPL--MAG 151
                       170       180       190
                ....*....|....*....|....*....|....
gi 84997794 163 iccsdntGTPLLACDVWEHAYYVDYRNDRASYVN 196
Cdd:COG0605 152 -------GTPLLGLDVWEHAYYLDYQNRRPDYVD 178
PRK10543 PRK10543
superoxide dismutase [Fe];
1-195 3.79e-77

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 229.84  E-value: 3.79e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794    1 MSFKLPPLPYGLKDLVPHLSEETLTYHYTKHHAGYVNKLNGLVNGTALENKSLEDIVcnnylyvldllKTESGAVFNNAA 80
Cdd:PRK10543   1 MSFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIV-----------RSSEGGVFNNAA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   81 QVWNHTFYWHSMSPSGGGEPRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLKSDGTPEVVQTHDAGNPLryi 160
Cdd:PRK10543  70 QVWNHTFYWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPL--- 146
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 84997794  161 ygiccsDNTGTPLLACDVWEHAYYVDYRNDRASYV 195
Cdd:PRK10543 147 ------TTDATPLLTVDVWEHAYYIDYRNARPGYL 175
PLN02685 PLN02685
iron superoxide dismutase
3-196 2.18e-64

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 201.00  E-value: 2.18e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794    3 FKLPPLPYGLKDLVPHLSEETLTYHYTKHHAGYVNKLNGLVNGTALENKSLEDIVCNNYLyvldllKTESGAVFNNAAQV 82
Cdd:PLN02685  47 FELKPPPYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIVGTELDGMSLEDVVLITYN------KGDMLPAFNNAAQA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   83 WNHTFYWHSMSPSGGGEPRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLKS----------------DGTPE 146
Cdd:PLN02685 121 WNHEFFWESMKPGGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAYKAnrldvgnavnpcpseeDKKLV 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 84997794  147 VVQTHDAGNPLRYIYgiccsdntgTPLLACDVWEHAYYVDYRNDRASYVN 196
Cdd:PLN02685 201 VVKSPNAVNPLVWDY---------SPLLTIDVWEHAYYLDFQNRRPDYIS 241
PLN02622 PLN02622
iron superoxide dismutase
9-196 6.99e-52

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 167.88  E-value: 6.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794    9 PYGLKDLVPHLSEETLTYHYTKHHAGYVNKLNglvngtalenKSLE--DIVcnnYLYVLD-LLKTESG-----AVFNNAA 80
Cdd:PLN02622  54 PYPLDALEPYMSRRTLEVHWGEHHRGYVEGLN----------KQLAkdDIL---YGYTMDeLVKVTYNngnplPEFNNAA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   81 QVWNHTFYWHSMSPSGGGEPRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLK-SDGTPEVVQTHDAGNPLRY 159
Cdd:PLN02622 121 QVWNHDFFWESMQPGGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKrEERRLEVVKTSNAINPLVW 200
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 84997794  160 iygiccsdnTGTPLLACDVWEHAYYVDYRNDRASYVN 196
Cdd:PLN02622 201 ---------DDIPIICLDVWEHAYYLDYKNDRGKYVN 228
PLN02184 PLN02184
superoxide dismutase [Fe]
2-195 4.01e-51

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 164.54  E-value: 4.01e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794    2 SFKLPPLPYGLKDLVPHLSEETLTYHYTKHHAGYVNKLNGLVNGTALENKSLEDIVCNNYLyvldllKTESGAVFNNAAQ 81
Cdd:PLN02184  10 NYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTYN------NGDLLPAFNNAAQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   82 VWNHTFYWHSMSPSGGGEPRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLKSDGTpEVVQTHDAGNPLryIY 161
Cdd:PLN02184  84 AWNHEFFWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEKL-KVVKTPNAVNPL--VL 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 84997794  162 GiccsdntGTPLLACDVWEHAYYVDYRNDRASYV 195
Cdd:PLN02184 161 G-------SFPLLTIDVWEHAYYLDFQNRRPDYI 187
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
100-196 2.33e-44

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: 143.34  E-value: 2.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   100 PRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLKSDGTPEVVQTHDAGNPLRYiygiccsdnTGTPLLACDVW 179
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGKLEIVTTPNQDNPLTD---------GLTPLLGLDVW 71
                          90
                  ....*....|....*..
gi 84997794   180 EHAYYVDYRNDRASYVN 196
Cdd:pfam02777  72 EHAYYLDYQNRRADYVK 88
PRK10925 PRK10925
superoxide dismutase [Mn];
1-195 1.77e-42

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 141.98  E-value: 1.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794    1 MSFKLPPLPYGLKDLVPHLSEETLTYHYTKHHAGYVNKLNG-LVNGTALENKSLEDIVCNnylyvLDLLKTESGAVF-NN 78
Cdd:PRK10925   1 MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAaLESLPEFANLPVEELITK-----LDQLPADKKTVLrNN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   79 AAQVWNHTFYWHSMSPsgGGEPRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLKSDGTPeVVQTHDAGNPLr 158
Cdd:PRK10925  76 AGGHANHSLFWKGLKK--GTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGDKLA-VVSTANQDSPL- 151
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 84997794  159 yiYGICCSDNTGTPLLACDVWEHAYYVDYRNDRASYV 195
Cdd:PRK10925 152 --MGEAISGASGFPILGLDVWEHAYYLKFQNRRPDYI 186
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
2-93 7.00e-32

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: 110.86  E-value: 7.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794     2 SFKLPPLPYGLKDLVPHLSEETLTYHYTKHHAGYVNKLNGLVNGTALENKSLEDIVCNNYLyvldllktesGAVFNNAAQ 81
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIKALL----------GGLFNNGGG 70
                          90
                  ....*....|..
gi 84997794    82 VWNHTFYWHSMS 93
Cdd:pfam00081  71 HWNHSLFWKNLS 82
PLN02471 PLN02471
superoxide dismutase [Mn]
2-196 2.96e-30

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 111.15  E-value: 2.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794    2 SFKLPPLPYGLKDLVPHLSEETLTYHYTKHHAGYVNKLNglvngtalenKSLEDIvcNNYLYVLD---LLKTESGAVFNN 78
Cdd:PLN02471  30 TFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYN----------KALEQL--DQAVEKGDasaVVKLQSAIKFNG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84997794   79 AAQVwNHTFYWHSMSPS--GGGE-PRGTVRKLLDEKFGSFDNFKKEFSSVLVGHFGSGWGWLVLKSDGTPEVVQTHDAGN 155
Cdd:PLN02471  98 GGHV-NHSIFWKNLAPVseGGGEpPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKLVVETTANQD 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 84997794  156 PLryiygiCCSDNTGTPLLACDVWEHAYYVDYRNDRASYVN 196
Cdd:PLN02471 177 PL------VTKGPSLVPLLGIDVWEHAYYLQYKNVRPDYLK 211
 
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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