NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|124803454|ref|XP_001347720|]
View 

FeS cluster assembly protein SufD [Plasmodium falciparum 3D7]

Protein Classification

SufD family Fe-S cluster assembly protein( domain architecture ID 10477762)

SufD family Fe-S cluster assembly protein similar to SufD, which is part of the SufBCD complex that acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS, and contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SUFBD pfam01458
SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors ...
 1205-1429 1.48e-51

SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S] and [4Fe-4S]. FeS cluster assembly is a complex process involving the mobilization of Fe and S atoms from storage sources, their assembly into [Fe-S] form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S] clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems. The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA, acting as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets. This entry represents SufB and SufD proteins, which are homologous, and form part of the SufBCD complex in the SUF system. SufB accepts sulfur transferred from SufE, whereas SufD may play a role in iron acquisition.


:

Pssm-ID: 460219 [Multi-domain]  Cd Length: 218  Bit Score: 181.11  E-value: 1.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454  1205 NPRLVVYVKGNSKINIYESHislnksnsgLVNGFSRICLEEKSNVKHTLSQELGNNVWHFHNVSVKNGLNANYKFVDVLL 1284
Cdd:pfam01458    3 FPRNLIVAEEGAEVTIIEEY---------EGCGVVEIYVGKGAKLRYVTVQNWGENAYNFVTTRAELGADARVEWVQVSL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454  1285 GSLSSRINL--QIEGEkGCKQESYGLSLLEDKQNISQYEMFHHEHPSMETNQLFKCLVSDKAHAVWRSRGRIERNAIKAK 1362
Cdd:pfam01458   74 GGKLTRNYPsvQLKGE-GAEAELNGVYLADGGQHADTGTKVIHNGPNTSSNILSKGVLKDRSRGVFRGLIKVRKGAQKTD 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124803454  1363 LNTLCKSILLNFGASAVCIPTLEIIPSDIECaNHGATISDLEKEPIFSLMTRGISERNAREIMMNSF 1429
Cdd:pfam01458  153 GHQECRNLLLSDKARADTIPELEIYADDVKC-SHGATVGKIDEEQLFYLMSRGLSEEEARRLIVRGF 218
 
Name Accession Description Interval E-value
SUFBD pfam01458
SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors ...
 1205-1429 1.48e-51

SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S] and [4Fe-4S]. FeS cluster assembly is a complex process involving the mobilization of Fe and S atoms from storage sources, their assembly into [Fe-S] form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S] clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems. The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA, acting as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets. This entry represents SufB and SufD proteins, which are homologous, and form part of the SufBCD complex in the SUF system. SufB accepts sulfur transferred from SufE, whereas SufD may play a role in iron acquisition.


Pssm-ID: 460219 [Multi-domain]  Cd Length: 218  Bit Score: 181.11  E-value: 1.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454  1205 NPRLVVYVKGNSKINIYESHislnksnsgLVNGFSRICLEEKSNVKHTLSQELGNNVWHFHNVSVKNGLNANYKFVDVLL 1284
Cdd:pfam01458    3 FPRNLIVAEEGAEVTIIEEY---------EGCGVVEIYVGKGAKLRYVTVQNWGENAYNFVTTRAELGADARVEWVQVSL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454  1285 GSLSSRINL--QIEGEkGCKQESYGLSLLEDKQNISQYEMFHHEHPSMETNQLFKCLVSDKAHAVWRSRGRIERNAIKAK 1362
Cdd:pfam01458   74 GGKLTRNYPsvQLKGE-GAEAELNGVYLADGGQHADTGTKVIHNGPNTSSNILSKGVLKDRSRGVFRGLIKVRKGAQKTD 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124803454  1363 LNTLCKSILLNFGASAVCIPTLEIIPSDIECaNHGATISDLEKEPIFSLMTRGISERNAREIMMNSF 1429
Cdd:pfam01458  153 GHQECRNLLLSDKARADTIPELEIYADDVKC-SHGATVGKIDEEQLFYLMSRGLSEEEARRLIVRGF 218
SufB COG0719
Fe-S cluster assembly scaffold protein SufB [Posttranslational modification, protein turnover, ...
 1197-1450 1.05e-47

Fe-S cluster assembly scaffold protein SufB [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440483 [Multi-domain]  Cd Length: 393  Bit Score: 176.10  E-value: 1.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454 1197 YHTHNP---ITNPRLVVYVKGNSKINIYESHISLNKSNSgLVNGFSRICLEEKSNVKHTLSQELGNNVWHFHNVSVKNGL 1273
Cdd:COG0719   130 YFRINAegtGQFERTLIVAEEGAEVTYIEGCTAPGDEAS-LHNAVVEIVVGDNARLRYSTVQNWSGNAYHFVTKRARVGR 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454 1274 NANYKFVDVLLGSLSSRINLQIE--GEkGCKQESYGLSLLEDKQNISQYEMFHHEHPSMETNQLFKCLVSDKAHAVWRSR 1351
Cdd:COG0719   209 DARYEWTTGSLGSKLTRNYPSVIlnGE-GAEAELNGVALAGGGQHADTGTKVIHAAPNTTSRILSKGILDDRARGVFRGK 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454 1352 GRIERNAIKAKLNTLCKSILLNFGASAVCIPTLEIIPSDIECAnHGATISDLEKEPIFSLMTRGISERNAREIMMNSFVK 1431
Cdd:COG0719   288 IKVAKGAQKTDAYQSNRNLLLSDKARADTKPELEIYADDVKCS-HGATVGQIDEEQLFYLRSRGISEEEARALLVNGFAA 366

                         250
                  ....*....|....*....
gi 124803454 1432 EILDHISDENLKNRVYQKV 1450
Cdd:COG0719   367 EVIEELPDEELREELNRLI 385
sufD TIGR01981
FeS assembly protein SufD; This protein, SufD, forms a cytosolic complex SufBCD. This complex ...
 1199-1446 4.75e-47

FeS assembly protein SufD; This protein, SufD, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. SufB and SufD are homologous. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273908  Cd Length: 275  Bit Score: 170.11  E-value: 4.75e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454  1199 THNPITNPRLVVYVKGNSKINIYESHISLnkSNSGLVNGFSRICLEEKSNVKHTLSQELGNNVWHFHNVSVKNGLNANYK 1278
Cdd:TIGR01981   30 SENRVLAPRLLIVVEEGAKATVLERHDSG--EGDAFLNGLVEINVGENASVEFIKVQFLSATSFHFSTVRITLERDARVR 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454  1279 FVDVLLGSLSSRINLQIE-GEKGCKQESYGLSLLEDKQNISQYEMFHHEHPSMETNQLFKCLVSDKAHAVWRSRGRIERN 1357
Cdd:TIGR01981  108 LSDVNLGGKLSRHDTDVDlNGEGSKAEIKGLYFGDGSQHIDVHTNVIHNGPHTVSNILHRGVLDDRAHGVFNGNIDIPKG 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454  1358 AIKAKLNTLCKSILLNFGASAVCIPTLEIIPSDIECAnHGATISDLEKEPIFSLMTRGISERNAREIMMNSFVKEILDHI 1437
Cdd:TIGR01981  188 AQGTDARQSNRTLLLSDKARADTKPELEIDADDVKAS-HGATVGQLDEEQLFYLRSRGIDEAEAKRLLIEGFFGEVIEEI 266


                   ....*....
gi 124803454  1438 SDENLKNRV 1446
Cdd:TIGR01981  267 PDESLKEEL 275
PRK10948 PRK10948
Fe-S cluster assembly protein SufD;
1259-1450 1.37e-13

Fe-S cluster assembly protein SufD;


Pssm-ID: 236804 [Multi-domain]  Cd Length: 424  Bit Score: 74.68  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454 1259 NNVWHF-HNvSVKNGLNANYKFVDVLLGS--LSSRINLQIEGEKGckqesyGLSL----LEDKQNISQYEMF-HHEHPSM 1330
Cdd:PRK10948  224 PSSYHFaHN-DLLLGRDARAFSHSFLLGAavLRHNTSTQLNGENS------TLRLnslaMPVKNEVCDTRTWlEHNKGYC 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454 1331 ETNQLFKCLVSDKAHAVWRSRGRIERNAIKAKLNTLCKSILLNFGASAVCIPTLEIIPSDIECaNHGATISDLEKEPIFS 1410
Cdd:PRK10948  297 NSRQLHKTIVSDKGRAVFNGLIKVAQHAIKTDGQMTNNNLLLGKLAEVDTKPQLEIYADDVKC-SHGATVGRIDDEQLFY 375

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 124803454 1411 LMTRGISERNAREIMMNSFVKEILDHISDENLKNRVYQKV 1450
Cdd:PRK10948  376 LRSRGINQQDAQQMIIYAFAAELTEAIRDEALKQQVLARI 415
 
Name Accession Description Interval E-value
SUFBD pfam01458
SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors ...
 1205-1429 1.48e-51

SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S] and [4Fe-4S]. FeS cluster assembly is a complex process involving the mobilization of Fe and S atoms from storage sources, their assembly into [Fe-S] form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S] clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems. The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA, acting as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets. This entry represents SufB and SufD proteins, which are homologous, and form part of the SufBCD complex in the SUF system. SufB accepts sulfur transferred from SufE, whereas SufD may play a role in iron acquisition.


Pssm-ID: 460219 [Multi-domain]  Cd Length: 218  Bit Score: 181.11  E-value: 1.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454  1205 NPRLVVYVKGNSKINIYESHislnksnsgLVNGFSRICLEEKSNVKHTLSQELGNNVWHFHNVSVKNGLNANYKFVDVLL 1284
Cdd:pfam01458    3 FPRNLIVAEEGAEVTIIEEY---------EGCGVVEIYVGKGAKLRYVTVQNWGENAYNFVTTRAELGADARVEWVQVSL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454  1285 GSLSSRINL--QIEGEkGCKQESYGLSLLEDKQNISQYEMFHHEHPSMETNQLFKCLVSDKAHAVWRSRGRIERNAIKAK 1362
Cdd:pfam01458   74 GGKLTRNYPsvQLKGE-GAEAELNGVYLADGGQHADTGTKVIHNGPNTSSNILSKGVLKDRSRGVFRGLIKVRKGAQKTD 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124803454  1363 LNTLCKSILLNFGASAVCIPTLEIIPSDIECaNHGATISDLEKEPIFSLMTRGISERNAREIMMNSF 1429
Cdd:pfam01458  153 GHQECRNLLLSDKARADTIPELEIYADDVKC-SHGATVGKIDEEQLFYLMSRGLSEEEARRLIVRGF 218
SufB COG0719
Fe-S cluster assembly scaffold protein SufB [Posttranslational modification, protein turnover, ...
 1197-1450 1.05e-47

Fe-S cluster assembly scaffold protein SufB [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440483 [Multi-domain]  Cd Length: 393  Bit Score: 176.10  E-value: 1.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454 1197 YHTHNP---ITNPRLVVYVKGNSKINIYESHISLNKSNSgLVNGFSRICLEEKSNVKHTLSQELGNNVWHFHNVSVKNGL 1273
Cdd:COG0719   130 YFRINAegtGQFERTLIVAEEGAEVTYIEGCTAPGDEAS-LHNAVVEIVVGDNARLRYSTVQNWSGNAYHFVTKRARVGR 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454 1274 NANYKFVDVLLGSLSSRINLQIE--GEkGCKQESYGLSLLEDKQNISQYEMFHHEHPSMETNQLFKCLVSDKAHAVWRSR 1351
Cdd:COG0719   209 DARYEWTTGSLGSKLTRNYPSVIlnGE-GAEAELNGVALAGGGQHADTGTKVIHAAPNTTSRILSKGILDDRARGVFRGK 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454 1352 GRIERNAIKAKLNTLCKSILLNFGASAVCIPTLEIIPSDIECAnHGATISDLEKEPIFSLMTRGISERNAREIMMNSFVK 1431
Cdd:COG0719   288 IKVAKGAQKTDAYQSNRNLLLSDKARADTKPELEIYADDVKCS-HGATVGQIDEEQLFYLRSRGISEEEARALLVNGFAA 366

                         250
                  ....*....|....*....
gi 124803454 1432 EILDHISDENLKNRVYQKV 1450
Cdd:COG0719   367 EVIEELPDEELREELNRLI 385
sufD TIGR01981
FeS assembly protein SufD; This protein, SufD, forms a cytosolic complex SufBCD. This complex ...
 1199-1446 4.75e-47

FeS assembly protein SufD; This protein, SufD, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. SufB and SufD are homologous. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273908  Cd Length: 275  Bit Score: 170.11  E-value: 4.75e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454  1199 THNPITNPRLVVYVKGNSKINIYESHISLnkSNSGLVNGFSRICLEEKSNVKHTLSQELGNNVWHFHNVSVKNGLNANYK 1278
Cdd:TIGR01981   30 SENRVLAPRLLIVVEEGAKATVLERHDSG--EGDAFLNGLVEINVGENASVEFIKVQFLSATSFHFSTVRITLERDARVR 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454  1279 FVDVLLGSLSSRINLQIE-GEKGCKQESYGLSLLEDKQNISQYEMFHHEHPSMETNQLFKCLVSDKAHAVWRSRGRIERN 1357
Cdd:TIGR01981  108 LSDVNLGGKLSRHDTDVDlNGEGSKAEIKGLYFGDGSQHIDVHTNVIHNGPHTVSNILHRGVLDDRAHGVFNGNIDIPKG 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454  1358 AIKAKLNTLCKSILLNFGASAVCIPTLEIIPSDIECAnHGATISDLEKEPIFSLMTRGISERNAREIMMNSFVKEILDHI 1437
Cdd:TIGR01981  188 AQGTDARQSNRTLLLSDKARADTKPELEIDADDVKAS-HGATVGQLDEEQLFYLRSRGIDEAEAKRLLIEGFFGEVIEEI 266


                   ....*....
gi 124803454  1438 SDENLKNRV 1446
Cdd:TIGR01981  267 PDESLKEEL 275
PRK10948 PRK10948
Fe-S cluster assembly protein SufD;
1259-1450 1.37e-13

Fe-S cluster assembly protein SufD;


Pssm-ID: 236804 [Multi-domain]  Cd Length: 424  Bit Score: 74.68  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454 1259 NNVWHF-HNvSVKNGLNANYKFVDVLLGS--LSSRINLQIEGEKGckqesyGLSL----LEDKQNISQYEMF-HHEHPSM 1330
Cdd:PRK10948  224 PSSYHFaHN-DLLLGRDARAFSHSFLLGAavLRHNTSTQLNGENS------TLRLnslaMPVKNEVCDTRTWlEHNKGYC 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124803454 1331 ETNQLFKCLVSDKAHAVWRSRGRIERNAIKAKLNTLCKSILLNFGASAVCIPTLEIIPSDIECaNHGATISDLEKEPIFS 1410
Cdd:PRK10948  297 NSRQLHKTIVSDKGRAVFNGLIKVAQHAIKTDGQMTNNNLLLGKLAEVDTKPQLEIYADDVKC-SHGATVGRIDDEQLFY 375

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 124803454 1411 LMTRGISERNAREIMMNSFVKEILDHISDENLKNRVYQKV 1450
Cdd:PRK10948  376 LRSRGINQQDAQQMIIYAFAAELTEAIRDEALKQQVLARI 415
 
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