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Conserved domains on  [gi|37999810|sp|Q9SM64|]
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RecName: Full=Superoxide dismutase [Mn], mitochondrial; Flags: Precursor

Protein Classification

PLN02471 family protein( domain architecture ID 11476866)

PLN02471 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02471 PLN02471
superoxide dismutase [Mn]
1-228 8.49e-163

superoxide dismutase [Mn]


:

Pssm-ID: 215262  Cd Length: 231  Bit Score: 448.59  E-value: 8.49e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810    1 MALRTLVSRRTLATGLG---FRQQLRGLQTFSLPDLPYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKALEQLHDAISK 77
Cdd:PLN02471   1 MALRTLASRKTLGGLKEtssRLLSFRGLQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   78 GDAPTVAKLHSAIKFNGGGHINHSIFWKNLAPVREGGGEPPKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLAL 157
Cdd:PLN02471  81 GDASAVVKLQSAIKFNGGGHVNHSIFWKNLAPVSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37999810  158 DKELKKLVVETTANQDPLVTKGPTLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVINWKYASEVYEKESP 228
Cdd:PLN02471 161 DKELKKLVVETTANQDPLVTKGPSLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKECN 231
 
Name Accession Description Interval E-value
PLN02471 PLN02471
superoxide dismutase [Mn]
1-228 8.49e-163

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 448.59  E-value: 8.49e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810    1 MALRTLVSRRTLATGLG---FRQQLRGLQTFSLPDLPYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKALEQLHDAISK 77
Cdd:PLN02471   1 MALRTLASRKTLGGLKEtssRLLSFRGLQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   78 GDAPTVAKLHSAIKFNGGGHINHSIFWKNLAPVREGGGEPPKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLAL 157
Cdd:PLN02471  81 GDASAVVKLQSAIKFNGGGHVNHSIFWKNLAPVSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37999810  158 DKELKKLVVETTANQDPLVTKGPTLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVINWKYASEVYEKESP 228
Cdd:PLN02471 161 DKELKKLVVETTANQDPLVTKGPSLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKECN 231
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
29-221 2.93e-93

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 271.23  E-value: 2.93e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810  29 SLPDLPYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKALEQLHDAISKGDAPTVAKLHSAIK----FNGGGHINHSIFW 104
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEIIKKLSEELKralrNNAGGHWNHTLFW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810 105 KNLAPvrEGGGEPPkGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLALDKElKKLVVETTANQDPLVTKGptLVP 184
Cdd:COG0605  81 ENLSP--NGGGEPT-GELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDNPLMAG--GTP 154
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 37999810 185 LLGIDVWEHAYYLQYKNVRPDYLKNIWKVINWKYASE 221
Cdd:COG0605 155 LLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEK 191
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
118-221 1.83e-53

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: 167.22  E-value: 1.83e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   118 PKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLALDKElKKLVVETTANQDPLVTKGptLVPLLGIDVWEHAYYL 197
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPD-GKLEIVTTPNQDNPLTDG--LTPLLGLDVWEHAYYL 77
                          90       100
                  ....*....|....*....|....
gi 37999810   198 QYKNVRPDYLKNIWKVINWKYASE 221
Cdd:pfam02777  78 DYQNRRADYVKAFWNVVNWDEVEK 101
 
Name Accession Description Interval E-value
PLN02471 PLN02471
superoxide dismutase [Mn]
1-228 8.49e-163

superoxide dismutase [Mn]


Pssm-ID: 215262  Cd Length: 231  Bit Score: 448.59  E-value: 8.49e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810    1 MALRTLVSRRTLATGLG---FRQQLRGLQTFSLPDLPYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKALEQLHDAISK 77
Cdd:PLN02471   1 MALRTLASRKTLGGLKEtssRLLSFRGLQTFTLPDLPYDYGALEPAISGEIMQLHHQKHHQTYVTNYNKALEQLDQAVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   78 GDAPTVAKLHSAIKFNGGGHINHSIFWKNLAPVREGGGEPPKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLAL 157
Cdd:PLN02471  81 GDASAVVKLQSAIKFNGGGHVNHSIFWKNLAPVSEGGGEPPHGSLGWAIDEHFGSLEALVKKMSAEGAAVQGSGWVWLGL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37999810  158 DKELKKLVVETTANQDPLVTKGPTLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVINWKYASEVYEKESP 228
Cdd:PLN02471 161 DKELKKLVVETTANQDPLVTKGPSLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYASEVYEKECN 231
SodA COG0605
Superoxide dismutase [Inorganic ion transport and metabolism];
29-221 2.93e-93

Superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 440370 [Multi-domain]  Cd Length: 192  Bit Score: 271.23  E-value: 2.93e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810  29 SLPDLPYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKALEQLHDAISKGDAPTVAKLHSAIK----FNGGGHINHSIFW 104
Cdd:COG0605   1 ELPPLPYAYDALEPHISAETMELHHDKHHQAYVNNLNAALEGLAELEDKSLEEIIKKLSEELKralrNNAGGHWNHTLFW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810 105 KNLAPvrEGGGEPPkGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLALDKElKKLVVETTANQDPLVTKGptLVP 184
Cdd:COG0605  81 ENLSP--NGGGEPT-GELAAAIEADFGSFDAFKEEFKAAAAGRFGSGWAWLVVDKD-GKLEIVSTPNQDNPLMAG--GTP 154
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 37999810 185 LLGIDVWEHAYYLQYKNVRPDYLKNIWKVINWKYASE 221
Cdd:COG0605 155 LLGLDVWEHAYYLDYQNRRPDYVDAFWNVVNWDFVEK 191
PRK10925 PRK10925
superoxide dismutase [Mn];
27-224 9.39e-59

superoxide dismutase [Mn];


Pssm-ID: 182843  Cd Length: 206  Bit Score: 184.36  E-value: 9.39e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   27 TFSLPDLPYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKALEQL--------HDAISKGDAPTVAKLhSAIKFNGGGHI 98
Cdd:PRK10925   2 SYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLpefanlpvEELITKLDQLPADKK-TVLRNNAGGHA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   99 NHSIFWKNLAPvreggGEPPKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLALDKElkKLVVETTANQD-PLVT 177
Cdd:PRK10925  81 NHSLFWKGLKK-----GTTLQGDLKAAIERDFGSVDNFKAEFEKAAATRFGSGWAWLVLKGD--KLAVVSTANQDsPLMG 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 37999810  178 K---GPTLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVINWKYASEVYE 224
Cdd:PRK10925 154 EaisGASGFPILGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFA 203
Sod_Fe_C pfam02777
Iron/manganese superoxide dismutases, C-terminal domain; superoxide dismutases (SODs) catalyze ...
118-221 1.83e-53

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: 167.22  E-value: 1.83e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   118 PKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLALDKElKKLVVETTANQDPLVTKGptLVPLLGIDVWEHAYYL 197
Cdd:pfam02777   1 PTGALAEAIEKDFGSFDAFKEEFNAAAAGVFGSGWAWLVYDPD-GKLEIVTTPNQDNPLTDG--LTPLLGLDVWEHAYYL 77
                          90       100
                  ....*....|....*....|....
gi 37999810   198 QYKNVRPDYLKNIWKVINWKYASE 221
Cdd:pfam02777  78 DYQNRRADYVKAFWNVVNWDEVEK 101
PRK10543 PRK10543
superoxide dismutase [Fe];
27-221 1.65e-43

superoxide dismutase [Fe];


Pssm-ID: 182534  Cd Length: 193  Bit Score: 145.09  E-value: 1.65e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   27 TFSLPDLPYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKALeqlhdaisKGDAPTVAKLHSAIK------FNGGGHI-N 99
Cdd:PRK10543   2 SFELPALPYAKDALAPHISAETLEYHYGKHHQTYVTNLNNLI--------KGTAFEGKSLEEIVRsseggvFNNAAQVwN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810  100 HSIFWKNLAPvrEGGGEPpKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLALDKELKKLVVETTANQDPLVTkg 179
Cdd:PRK10543  74 HTFYWNCLAP--NAGGEP-TGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNADGKLAIVSTSNAGTPLTT-- 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 37999810  180 pTLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVINWKYASE 221
Cdd:PRK10543 149 -DATPLLTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAK 189
PLN02685 PLN02685
iron superoxide dismutase
8-224 1.04e-38

iron superoxide dismutase


Pssm-ID: 215369  Cd Length: 299  Bit Score: 135.90  E-value: 1.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810    8 SRRTLATG---LGFRQQLRGLQT--FSLPDLPYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKALEQLH-DAISKGDAP 81
Cdd:PLN02685  22 SRRMQWKGkrrTCTRKAVSGVITakFELKPPPYPLDALEPHMSRETLEYHWGKHHRAYVDNLNKQIVGTElDGMSLEDVV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   82 TVA--KLHSAIKFNGGGHI-NHSIFWKNLAPvreGGGEPPKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLA-- 156
Cdd:PLN02685 102 LITynKGDMLPAFNNAAQAwNHEFFWESMKP---GGGGKPSGELLQLIERDFGSFERFVEEFKSAAATQFGSGWAWLAyk 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810  157 ---LD----------KELKKLVVETTANQ-DPLVTKgptLVPLLGIDVWEHAYYLQYKNVRPDYLKN-IWKVINWKYASE 221
Cdd:PLN02685 179 anrLDvgnavnpcpsEEDKKLVVVKSPNAvNPLVWD---YSPLLTIDVWEHAYYLDFQNRRPDYISTfMEKLVSWEAVSA 255

                 ...
gi 37999810  222 VYE 224
Cdd:PLN02685 256 RLE 258
PTZ00078 PTZ00078
Superoxide dismutase [Fe]; Provisional
31-225 6.84e-37

Superoxide dismutase [Fe]; Provisional


Pssm-ID: 185432 [Multi-domain]  Cd Length: 193  Bit Score: 127.98  E-value: 6.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   31 PDLPYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKALEQlHDAISKGDAPTVAKLHSAIkFNGGGHI-NHSIFWKNLAP 109
Cdd:PTZ00078   1 PKLPYGLKELSPHLSEETLKFHYSKHHAGYVNKLNGLIKG-TPLENKTLEELIKEYSGAV-FNNAAQIwNHNFYWLSMGP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810  110 vrEGGGEPpKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLALDKELKKLVVETTANQDPLvtKGPTLVPLLGID 189
Cdd:PTZ00078  79 --NGGGEP-TGEIKEKIDEKFGSFDNFKNEFSNVLSGHFGSGWGWLVLKNDGKLEIVQTHDAGNPI--KDNTGKPLLTCD 153
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 37999810  190 VWEHAYYLQYKNVRPDYLKNIWKVINWKYASEVYEK 225
Cdd:PTZ00078 154 IWEHAYYIDYRNDRASYVNSWWNKVNWDFANKNLKK 189
Sod_Fe_N pfam00081
Iron/manganese superoxide dismutases, alpha-hairpin domain; superoxide dismutases (SODs) ...
27-108 1.86e-35

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: 120.49  E-value: 1.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810    27 TFSLPDLPYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKALEQLHDAISKGDAPTVAKLHSAIKFNGGGHINHSIFWKN 106
Cdd:pfam00081   1 SYELPDLPYAYDALEPHISKETMEIHHTKHHQTYVNNLNAALEGLEEARKPLEELIIKALLGGLFNNGGGHWNHSLFWKN 80

                  ..
gi 37999810   107 LA 108
Cdd:pfam00081  81 LS 82
PLN02622 PLN02622
iron superoxide dismutase
16-219 1.63e-34

iron superoxide dismutase


Pssm-ID: 166263 [Multi-domain]  Cd Length: 261  Bit Score: 123.97  E-value: 1.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   16 LGFRQQLRGLQT-------FSLPDLPYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKALEQlhDAISKGDapTVAKLHS 88
Cdd:PLN02622  29 LRNKQRRRSLQRaskvvayYGLKTPPYPLDALEPYMSRRTLEVHWGEHHRGYVEGLNKQLAK--DDILYGY--TMDELVK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   89 AI--------KFNGGGHI-NHSIFWKNLAPvreGGGEPPKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLALDK 159
Cdd:PLN02622 105 VTynngnplpEFNNAAQVwNHDFFWESMQP---GGGDMPELGVLEQIEKDFGSFTNFREKFTEAALTLFGSGWVWLVLKR 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37999810  160 ELKKLVVETTANQ-DPLVTKGptlVPLLGIDVWEHAYYLQYKNVRPDYLKNIWK-VINWKYA 219
Cdd:PLN02622 182 EERRLEVVKTSNAiNPLVWDD---IPIICLDVWEHAYYLDYKNDRGKYVNAFMNhLVSWNAA 240
PLN02184 PLN02184
superoxide dismutase [Fe]
34-224 1.12e-28

superoxide dismutase [Fe]


Pssm-ID: 177838  Cd Length: 212  Bit Score: 107.14  E-value: 1.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810   34 PYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKaleQLHDAISKGDaPTVAKLHSAIK-------FNGGGHI-NHSIFWK 105
Cdd:PLN02184  17 PFALDALEPHMSKQTLEFHWGKHHRAYVDNLKK---QVLGTELEGK-PLEHIIHSTYNngdllpaFNNAAQAwNHEFFWE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37999810  106 NLAPvreGGGEPPKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLALDKELKKlVVETTANQDPLVTKGptlVPL 185
Cdd:PLN02184  93 SMKP---GGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEKLK-VVKTPNAVNPLVLGS---FPL 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 37999810  186 LGIDVWEHAYYLQYKNVRPDYLKN-IWKVINWKYASEVYE 224
Cdd:PLN02184 166 LTIDVWEHAYYLDFQNRRPDYIKTfMTNLVSWEAVSARLE 205
 
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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