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Conserved domains on  [gi|17569479|ref|NP_510764|]
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Superoxide dismutase [Mn] 2, mitochondrial [Caenorhabditis elegans]

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

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List of domain hits

Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
27-212 4.27e-89

Superoxide dismutase [Inorganic ion transport and metabolism];


:

Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 260.45  E-value: 4.27e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479  27 TLPDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQIEEKLHEAVSKgNLKEAI-----ALQPALKFNGGGHINHSIF 101
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDK-SLEEIIkklseELKRALRNNAGGHWNHTLF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479 102 WTNLAKDGG-EPSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYCKKDKiLKIATCANQD-PL-EGMVPLFGI 178
Cdd:COG0605  80 WENLSPNGGgEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGK-LEIVSTPNQDnPLmAGGTPLLGL 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 17569479 179 DVWEHAYYLQYKNVRPDYVHAIWKIANWKNISER 212
Cdd:COG0605 159 DVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
27-212 4.27e-89

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 260.45  E-value: 4.27e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479  27 TLPDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQIEEKLHEAVSKgNLKEAI-----ALQPALKFNGGGHINHSIF 101
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDK-SLEEIIkklseELKRALRNNAGGHWNHTLF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479 102 WTNLAKDGG-EPSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYCKKDKiLKIATCANQD-PL-EGMVPLFGI 178
Cdd:COG0605  80 WENLSPNGGgEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGK-LEIVSTPNQDnPLmAGGTPLLGL 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 17569479 179 DVWEHAYYLQYKNVRPDYVHAIWKIANWKNISER 212
Cdd:COG0605 159 DVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PLN02471 PLN02471
superoxide dismutase [Mn]
5-216 2.74e-88

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 259.84  E-value: 2.74e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479    5 TARTASKLVQPVAGVLAVRSKHT--LPDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQIEEKLHEAVSKGNLKEAI 82
Cdd:PLN02471   8 SRKTLGGLKETSSRLLSFRGLQTftLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   83 ALQPALKFNGGGHINHSIFWTNLA---KDGGEPSK-ELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYCKKDKIL 158
Cdd:PLN02471  88 KLQSAIKFNGGGHVNHSIFWKNLApvsEGGGEPPHgSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKL 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17569479  159 KIATCANQDPL----EGMVPLFGIDVWEHAYYLQYKNVRPDYVHAIWKIANWKNISERFANA 216
Cdd:PLN02471 168 VVETTANQDPLvtkgPSLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKE 229
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
112-212 1.90e-50

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: 159.13  E-value: 1.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   112 PSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYCKKDKiLKIATCANQDPL--EGMVPLFGIDVWEHAYYLQY 189
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGK-LEIVTTPNQDNPltDGLTPLLGLDVWEHAYYLDY 79
                          90       100
                  ....*....|....*....|...
gi 17569479   190 KNVRPDYVHAIWKIANWKNISER 212
Cdd:pfam02777  80 QNRRADYVKAFWNVVNWDEVEKR 102
 
Name Accession Description Interval E-value
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
27-212 4.27e-89

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 260.45  E-value: 4.27e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479  27 TLPDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQIEEKLHEAVSKgNLKEAI-----ALQPALKFNGGGHINHSIF 101
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDK-SLEEIIkklseELKRALRNNAGGHWNHTLF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479 102 WTNLAKDGG-EPSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYCKKDKiLKIATCANQD-PL-EGMVPLFGI 178
Cdd:COG0605  80 WENLSPNGGgEPTGELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKDGK-LEIVSTPNQDnPLmAGGTPLLGL 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 17569479 179 DVWEHAYYLQYKNVRPDYVHAIWKIANWKNISER 212
Cdd:COG0605 159 DVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEKR 192
PLN02471 PLN02471
superoxide dismutase [Mn]
5-216 2.74e-88

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 259.84  E-value: 2.74e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479    5 TARTASKLVQPVAGVLAVRSKHT--LPDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQIEEKLHEAVSKGNLKEAI 82
Cdd:PLN02471   8 SRKTLGGLKETSSRLLSFRGLQTftLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEKGDASAVV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   83 ALQPALKFNGGGHINHSIFWTNLA---KDGGEPSK-ELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYCKKDKIL 158
Cdd:PLN02471  88 KLQSAIKFNGGGHVNHSIFWKNLApvsEGGGEPPHgSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGLDKELKKL 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17569479  159 KIATCANQDPL----EGMVPLFGIDVWEHAYYLQYKNVRPDYVHAIWKIANWKNISERFANA 216
Cdd:PLN02471 168 VVETTANQDPLvtkgPSLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKE 229
PRK10925 PRK10925
superoxide dismutase [Mn];
26-217 5.59e-54

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 171.64  E-value: 5.59e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   26 HTLPDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQIEEKLHE--AVSKGNLKEAIALQPA-----LKFNGGGHINH 98
Cdd:PRK10925   3 YTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEfaNLPVEELITKLDQLPAdkktvLRNNAGGHANH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   99 SIFWTNLaKDGGEPSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLgyCKKDKILKIATCANQD-PLEGMV---- 173
Cdd:PRK10925  83 SLFWKGL-KKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWL--VLKGDKLAVVSTANQDsPLMGEAisga 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 17569479  174 ---PLFGIDVWEHAYYLQYKNVRPDYVHAIWKIANWKNISERFANAR 217
Cdd:PRK10925 160 sgfPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK 206
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
112-212 1.90e-50

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: 159.13  E-value: 1.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   112 PSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYCKKDKiLKIATCANQDPL--EGMVPLFGIDVWEHAYYLQY 189
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPDGK-LEIVTTPNQDNPltDGLTPLLGLDVWEHAYYLDY 79
                          90       100
                  ....*....|....*....|...
gi 17569479   190 KNVRPDYVHAIWKIANWKNISER 212
Cdd:pfam02777  80 QNRRADYVKAFWNVVNWDEVEKR 102
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
29-213 2.24e-40

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 136.46  E-value: 2.24e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   29 PDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQIEEKlhEAVSKGNLKEAIALQPALKFNGGGHI-NHSIFWTNLAK 107
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKG--TPLENKTLEELIKEYSGAVFNNAAQIwNHNFYWLSMGP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479  108 D-GGEPSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYcKKDKILKIATCANQD-PLEGMV--PLFGIDVWEH 183
Cdd:PTZ00078  79 NgGGEPTGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVL-KNDGKLEIVQTHDAGnPIKDNTgkPLLTCDIWEH 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 17569479  184 AYYLQYKNVRPDYVHAIWKIANW----KNISERF 213
Cdd:PTZ00078 158 AYYIDYRNDRASYVNSWWNKVNWdfanKNLKKLM 191
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
25-106 2.68e-40

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: 132.81  E-value: 2.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479    25 KHTLPDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQIEEKLHEAVSKGNLKEAIALQPALKFNGGGHINHSIFWTN 104
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIKALLGGLFNNGGGHWNHSLFWKN 80

                  ..
gi 17569479   105 LA 106
Cdd:pfam00081  81 LS 82
PRK10543 PRK10543
superoxide dismutase [Fe];
28-214 3.14e-40

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 136.24  E-value: 3.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   28 LPDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQ-IEEKLHEAVSkgnLKEAIALQPALKFNGGGHI-NHSIFWTNL 105
Cdd:PRK10543   5 LPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNlIKGTAFEGKS---LEEIVRSSEGGVFNNAAQVwNHTFYWNCL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479  106 AKD-GGEPSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYCKKDKILKIATCANQDPLEGM-VPLFGIDVWEH 183
Cdd:PRK10543  82 APNaGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTTDaTPLLTVDVWEH 161
                        170       180       190
                 ....*....|....*....|....*....|.
gi 17569479  184 AYYLQYKNVRPDYVHAIWKIANWKNISERFA 214
Cdd:PRK10543 162 AYYIDYRNARPGYLEHFWALVNWEFVAKNLA 192
PLN02685 PLN02685
iron superoxide dismutase
7-217 6.17e-37

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 130.89  E-value: 6.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479    7 RTASKlvQPVAGVLAVRSKHTLPDLPFDyaDLEPVISHEIMQLHHQKHHATYVNNLNQ-----------IEEKLHEAVSK 75
Cdd:PLN02685  32 RTCTR--KAVSGVITAKFELKPPPYPLD--ALEPHMSRETLEYHWGKHHRAYVDNLNKqivgteldgmsLEDVVLITYNK 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   76 GNLKEAialqpalkFNGGGHI-NHSIFWTNLAKDGG-EPSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGY-- 151
Cdd:PLN02685 108 GDMLPA--------FNNAAQAwNHEFFWESMKPGGGgKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAYka 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479  152 -------------CKKDKILKIATCANQ-DPLE-GMVPLFGIDVWEHAYYLQYKNVRPDYVHA-IWKIANWKNISERFAN 215
Cdd:PLN02685 180 nrldvgnavnpcpSEEDKKLVVVKSPNAvNPLVwDYSPLLTIDVWEHAYYLDFQNRRPDYISTfMEKLVSWEAVSARLES 259

                 ..
gi 17569479  216 AR 217
Cdd:PLN02685 260 AK 261
PLN02622 PLN02622
iron superoxide dismutase
22-216 3.00e-32

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 117.42  E-value: 3.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   22 VRSKHTLPDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQ------------IEEKLHEAVSKGNlkeaialqPALK 89
Cdd:PLN02622  44 VVAYYGLKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKqlakddilygytMDELVKVTYNNGN--------PLPE 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   90 FNGGGHI-NHSIFWTNLAKDGGE-PSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYCKKDKILKIATCANQ- 166
Cdd:PLN02622 116 FNNAAQVwNHDFFWESMQPGGGDmPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKREERRLEVVKTSNAi 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17569479  167 DPLE-GMVPLFGIDVWEHAYYLQYKNVRPDYVHAIWK-IANWKNISERFANA 216
Cdd:PLN02622 196 NPLVwDDIPIICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAAMARMARA 247
PLN02184 PLN02184
superoxide dismutase [Fe]
16-217 1.69e-31

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 114.46  E-value: 1.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   16 VAGVLAVRSKHTLPDLPFDYADLEPVISHEIMQLHHQKHHATYVNNLNQ-----------IEEKLHEAVSKGNLkeaial 84
Cdd:PLN02184   1 MAASSAVTANYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKqvlgtelegkpLEHIIHSTYNNGDL------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569479   85 QPALKfNGGGHINHSIFWTNLAKDGG-EPSKELMDTIKRDFGSLDNLQKRLSDITIAVQGSGWGWLGYCKkDKILKIATC 163
Cdd:PLN02184  75 LPAFN-NAAQAWNHEFFWESMKPGGGgKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSN-EKLKVVKTP 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17569479  164 ANQDPLE-GMVPLFGIDVWEHAYYLQYKNVRPDYVHA-IWKIANWKNISERFANAR 217
Cdd:PLN02184 153 NAVNPLVlGSFPLLTIDVWEHAYYLDFQNRRPDYIKTfMTNLVSWEAVSARLEAAK 208
 
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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