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Conserved domains on  [gi|6730558|pdb|1QT9|A]
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Chain A, FERREDOXIN I

Protein Classification

ferredoxin( domain architecture ID 10784691)

ferredoxin is an iron-sulfur protein transfering electrons in a wide variety of metabolic reactions

Gene Ontology:  GO:0051536
PubMed:  11734195

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
petF CHL00134
ferredoxin; Validated
 1-98 2.91e-58

ferredoxin; Validated


:

Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 173.75  E-value: 2.91e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A        1 ATFKVTLINEAEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCV 80
Cdd:CHL00134  2 ATYKVTLLSEEEGIDVTIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCV 81

                        90
                ....*....|....*...
1QT9_A       81 AYPTSDVVIQTHKEEDLY 98
Cdd:CHL00134 82 AYPTSDCTILTHQEEELY 99
 
Name Accession Description Interval E-value
petF CHL00134
ferredoxin; Validated
 1-98 2.91e-58

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 173.75  E-value: 2.91e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A        1 ATFKVTLINEAEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCV 80
Cdd:CHL00134  2 ATYKVTLLSEEEGIDVTIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCV 81

                        90
                ....*....|....*...
1QT9_A       81 AYPTSDVVIQTHKEEDLY 98
Cdd:CHL00134 82 AYPTSDCTILTHQEEELY 99
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 1-98 1.07e-56

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 169.94  E-value: 1.07e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A         1 ATFKVTLINEaEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCV 80
Cdd:TIGR02008  1 ATYKVTLVNP-DGGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCV 79

                         90
                 ....*....|....*...
1QT9_A        81 AYPTSDVVIQTHKEEDLY 98
Cdd:TIGR02008 80 AYPTSDCTIETHKEEDLY 97
Fdx COG0633
Ferredoxin [Energy production and conversion];
4-92 1.22e-35

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 116.10  E-value: 1.22e-35
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A       4 KVTLIneaeGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAYP 83
Cdd:COG0633  3 KVTFI----PEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARP 78


               ....*....
1QT9_A      84 TSDVVIQTH 92
Cdd:COG0633 79 TSDLVVELP 87
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 5-90 4.31e-33

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 109.79  E-value: 4.31e-33
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A       5 VTLINEaeGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAYPT 84
Cdd:cd00207  1 VTINVP--GSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVT 78


               ....*.
1QT9_A      85 SDVVIQ 90
Cdd:cd00207 79 DGLVIE 84
Frdxn_Halo NF041393
ferredoxin Fer;
18-88 5.17e-23

ferredoxin Fer;


Pssm-ID: 469284 [Multi-domain]  Cd Length: 128  Bit Score: 85.45  E-value: 5.17e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1QT9_A        18 IEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQI-EAGYVLTCVAYPTSDVV 88
Cdd:NF041393  40 FEVEEGEYILEAAEDAGYDWPFSCRAGACANCAAIVVEGEIEMDMQQILSDEEVeERNIRLTCVGTPATDEV 111
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
12-84 4.76e-22

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 81.80  E-value: 4.76e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1QT9_A        12 EGTKHEIEVPDDEY-ILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTvDQSDQSFLDDDQIEAGYV-LTCVAYPT 84
Cdd:pfam00111  4 NGKGVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGE-DQSDQSFLEDDELAAGYVvLACQTYPK 77
 
Name Accession Description Interval E-value
petF CHL00134
ferredoxin; Validated
 1-98 2.91e-58

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 173.75  E-value: 2.91e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A        1 ATFKVTLINEAEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCV 80
Cdd:CHL00134  2 ATYKVTLLSEEEGIDVTIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCV 81

                        90
                ....*....|....*...
1QT9_A       81 AYPTSDVVIQTHKEEDLY 98
Cdd:CHL00134 82 AYPTSDCTILTHQEEELY 99
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 1-98 1.07e-56

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 169.94  E-value: 1.07e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A         1 ATFKVTLINEaEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCV 80
Cdd:TIGR02008  1 ATYKVTLVNP-DGGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCV 79

                         90
                 ....*....|....*...
1QT9_A        81 AYPTSDVVIQTHKEEDLY 98
Cdd:TIGR02008 80 AYPTSDCTIETHKEEDLY 97
PTZ00038 PTZ00038
ferredoxin; Provisional
 3-98 1.39e-48

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 152.68  E-value: 1.39e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A         3 FKVTLINEaEGTKhEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAY 82
Cdd:PTZ00038  96 YNITLQTP-DGEK-VIECDEDEYILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGYCLLCTCY 173

                         90
                 ....*....|....*.
1QT9_A        83 PTSDVVIQTHKEEDLY 98
Cdd:PTZ00038 174 PKSDCTIETHKEDELH 189
PLN03136 PLN03136
Ferredoxin; Provisional
 1-97 7.37e-44

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 139.11  E-value: 7.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A         1 ATFKVTLINeAEGtKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCV 80
Cdd:PLN03136  53 ATYKVKFIT-PEG-EQEVECEEDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLTCV 130

                         90
                 ....*....|....*..
1QT9_A        81 AYPTSDVVIQTHKEEDL 97
Cdd:PLN03136 131 AYPTSDVVIETHKEEAI 147
Fdx COG0633
Ferredoxin [Energy production and conversion];
4-92 1.22e-35

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 116.10  E-value: 1.22e-35
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A       4 KVTLIneaeGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAYP 83
Cdd:COG0633  3 KVTFI----PEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARP 78


               ....*....
1QT9_A      84 TSDVVIQTH 92
Cdd:COG0633 79 TSDLVVELP 87
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 5-90 4.31e-33

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 109.79  E-value: 4.31e-33
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A       5 VTLINEaeGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAYPT 84
Cdd:cd00207  1 VTINVP--GSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVT 78


               ....*.
1QT9_A      85 SDVVIQ 90
Cdd:cd00207 79 DGLVIE 84
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 1-89 1.60e-25

CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 96.86  E-value: 1.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A         1 ATFKVTLineaEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSD--QSFLDDDQIEAGYVLT 78
Cdd:PRK07609   1 MSFQVTL----QPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGPhqASALSGEERAAGEALT 76

                         90
                 ....*....|.
1QT9_A        79 CVAYPTSDVVI 89
Cdd:PRK07609  77 CCAKPLSDLVL 87
Frdxn_Halo NF041393
ferredoxin Fer;
18-88 5.17e-23

ferredoxin Fer;


Pssm-ID: 469284 [Multi-domain]  Cd Length: 128  Bit Score: 85.45  E-value: 5.17e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1QT9_A        18 IEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQI-EAGYVLTCVAYPTSDVV 88
Cdd:NF041393  40 FEVEEGEYILEAAEDAGYDWPFSCRAGACANCAAIVVEGEIEMDMQQILSDEEVeERNIRLTCVGTPATDEV 111
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
12-84 4.76e-22

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 81.80  E-value: 4.76e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1QT9_A        12 EGTKHEIEVPDDEY-ILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTvDQSDQSFLDDDQIEAGYV-LTCVAYPT 84
Cdd:pfam00111  4 NGKGVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGE-DQSDQSFLEDDELAAGYVvLACQTYPK 77
PA_CoA_Oxy5 TIGR02160
phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised ...
 4-89 5.90e-20

phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other]


Pssm-ID: 131215 [Multi-domain]  Cd Length: 352  Bit Score: 81.79  E-value: 5.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A          4 KVTLIneAEGTKHEIEV-PDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAY 82
Cdd:TIGR02160 264 KVTVT--LDGRSTETSSlSRDESVLDAALRARPDLPFACKGGVCGTCRAKVLEGKVDMERNYALEPDEVDAGYVLTCQAY 341


                  ....*..
1QT9_A         83 PTSDVVI 89
Cdd:TIGR02160 342 PLSDKLV 348
COG3894 COG3894
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ...
 2-97 3.57e-15

Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain [Function unknown];


Pssm-ID: 443101 [Multi-domain]  Cd Length: 621  Bit Score: 69.06  E-value: 3.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A        2 TFKVTLineaEGTKHEIEVPDDEYILDAAEEQGYDLPFSCR-AGACSTCAGKLVSGT---VDQSDQSFLDDDQIEAGYVL 77
Cdd:COG3894   3 KVKVTF----LPSGKRVEVEAGTTLLDAAREAGVDIDAPCGgRGTCGKCKVKVEEGEfspVTEEERRLLSPEELAEGYRL 78

                        90       100
                ....*....|....*....|
1QT9_A       78 TCVAYPTSDVVIQTHKEEDL 97
Cdd:COG3894  79 ACQARVLGDLVVEVPPESRL 98
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
2-86 1.34e-09

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 53.21  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QT9_A         2 TFKVTLiNEAEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSG--TVDQSDQSFLDDDQIEAGYVLTC 79
Cdd:PRK11872   2 NHKVAL-SFADGKTLFFPVGKDELLLDAALRNGINLPLDCREGVCGTCQGRCESGiySQDYVDEDALSERDLAQRKMLAC 80


                 ....*..
1QT9_A        80 VAYPTSD 86
Cdd:PRK11872  81 QTRVKSD 87
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 17-89 1.99e-09

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 52.79  E-value: 1.99e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1QT9_A        17 EIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAYPTSDVVI 89
Cdd:PRK10684 259 EFYAPVGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLACSCHPQGDLVL 331
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
20-91 4.19e-09

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 51.65  E-value: 4.19e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1QT9_A        20 VPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAYPTSDVVIQT 91
Cdd:PRK05713  13 VPAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEKREQGWRLACQCRVVGDLRVEV 84
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
17-90 6.39e-06

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 40.48  E-value: 6.39e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1QT9_A       17 EIEVPDDE-YILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQ--SFLDDDQIeagyvLTCVAYPTSDVVIQ 90
Cdd:PRK10713 12 QLLCQDEHpSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEplAFIQPGEI-----LPCCCRAKGDIEIE 83
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
 17-54 3.08e-04

NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440657 [Multi-domain]  Cd Length: 453  Bit Score: 37.90  E-value: 3.08e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
1QT9_A       17 EIEVPDDEYILDAAEEQGYDLPFSC------RAGACSTC------AGKLV 54
Cdd:COG1034  10 EVEVPKGTTVLQAAEKAGIEIPRFCyhpklsIAGACRMClvevegAPKPV 59
 
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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