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Conserved domains on  [gi|81857754|sp|Q9K8Z7|]
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RecName: Full=ClpXP adapter protein SpxH

Protein Classification

ClpXP adapter SpxH family protein( domain architecture ID 10617855)

ClpXP adapter SpxH family protein may function as an adapter protein, similar to SpxH that is required for efficient degradation of Spx by ClpXP under non-stress conditions; belongs to the thioredoxin superfamily

CATH:  3.40.30.10
SCOP:  3000031

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Thioredoxin_5 pfam13743
Thioredoxin;
37-234 1.39e-100

Thioredoxin;


:

Pssm-ID: 404608 [Multi-domain]  Cd Length: 176  Bit Score: 292.60  E-value: 1.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754    37 YTFIDPLCPECWAFEPILKKLQVEYGQYFRIRFIVAGKLEAWNLCRGKykgaqsredlahvwrkitetfgMPCDGDVWLE 116
Cdd:pfam13743   1 YLFIDPLCPECWAIEPQIKKLKVEYGQKFDIRFIPLGNLQTLNYNMGR----------------------MPIDGDVLRN 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754   117 DPITSSYTPSLAIKAAELQGPQAGVRFLRKLREHLFLNKQNVTKEDILISCAQRAGLDVKEFKQDLHSKGAAKALRCDMQ 196
Cdd:pfam13743  59 DPFSSPYLASLAYKAAELQGKKKGRRFLRKLQEAVFLEKQNISDEELLLECAEKAGLDVEEFKEDLHSDLAKKAFQCDQK 138
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 81857754   197 TTKEMDVDLVPTFVFFNDNVDEEGIKVTGHYPYHIYVQ 234
Cdd:pfam13743 139 LAAEMGVTEHPTLVFFNSNVEEEGLKVEGCYPYDVYEQ 176
 
Name Accession Description Interval E-value
Thioredoxin_5 pfam13743
Thioredoxin;
37-234 1.39e-100

Thioredoxin;


Pssm-ID: 404608 [Multi-domain]  Cd Length: 176  Bit Score: 292.60  E-value: 1.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754    37 YTFIDPLCPECWAFEPILKKLQVEYGQYFRIRFIVAGKLEAWNLCRGKykgaqsredlahvwrkitetfgMPCDGDVWLE 116
Cdd:pfam13743   1 YLFIDPLCPECWAIEPQIKKLKVEYGQKFDIRFIPLGNLQTLNYNMGR----------------------MPIDGDVLRN 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754   117 DPITSSYTPSLAIKAAELQGPQAGVRFLRKLREHLFLNKQNVTKEDILISCAQRAGLDVKEFKQDLHSKGAAKALRCDMQ 196
Cdd:pfam13743  59 DPFSSPYLASLAYKAAELQGKKKGRRFLRKLQEAVFLEKQNISDEELLLECAEKAGLDVEEFKEDLHSDLAKKAFQCDQK 138
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 81857754   197 TTKEMDVDLVPTFVFFNDNVDEEGIKVTGHYPYHIYVQ 234
Cdd:pfam13743 139 LAAEMGVTEHPTLVFFNSNVEEEGLKVEGCYPYDVYEQ 176
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
34-231 2.22e-69

DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif with similarity to DsbA and FrnE. FrnE is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins.


Pssm-ID: 239323 [Multi-domain]  Cd Length: 193  Bit Score: 213.72  E-value: 2.22e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754  34 LEIYTFIDPLCPECWAFEPILKKLQVEYGQYFRIRFIVAGKLEAWNLCrgkykGAQSREDLAHVWRKITE-TFGMPCDGD 112
Cdd:cd03025   1 LELYYFIDPLCGWCYGFEPLLEKLKEEYGGGIEVELHLGGLLPGNNAR-----QITKQWRIYVHWHKARIaLTGQPFGED 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754 113 VWLEDPI-TSSYTPSLAIKAAELQGPQAGVRFLRKLREHLFLNKQNVTKEDILISCAQRAGLDVKEFKQDLHSKGAAKAL 191
Cdd:cd03025  76 YLELLLFdLDSAPASRAIKAARLQGPERLLEMLKAIQRAHYVEGRDLADTEVLRELAIELGLDVEEFLEDFQSDEAKQAI 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 81857754 192 RCDMQTTKEMDVDLVPTFVFFNDNvdEEGIKVTGHYPYHI 231
Cdd:cd03025 156 QEDQKLARELGINGFPTLVLEDDN--GEGILLTGYYPYEP 193
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
33-241 4.07e-50

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 165.06  E-value: 4.07e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754  33 PLEIYTFIDPLCPECWAFEPILKKLQVEYGQYFRIRFI---------VAGKLEAWNLCRgKYKGAQSREDLAHvWRKITE 103
Cdd:COG2761   1 PLKIDIFSDVVCPWCYIGKRRLEKALAEFGDDVEIRWRpfelnpdmpPEGEDRREYLLA-KGSPEQAEQMRAH-VEEAAA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754 104 TFGMPCDgdvWLEDPITSSYTPSLAIKAAELQGPQAgvRFLRKLREHLFLNKQNVTKEDILISCAQRAGLDVKEFKQDLH 183
Cdd:COG2761  79 EEGLPFD---FDRIKPPNTFDAHRLLKAAELQGKQD--ALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLE 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 81857754 184 SKGAAKALRCDMQTTKEMDVDLVPTFVFfndnvdEEGIKVTGHYPYHIYVQILEDMLG 241
Cdd:COG2761 154 SDEAAAAVRADEAEARELGVTGVPTFVF------DGKYAVSGAQPYEVFEQALRQALA 205
 
Name Accession Description Interval E-value
Thioredoxin_5 pfam13743
Thioredoxin;
37-234 1.39e-100

Thioredoxin;


Pssm-ID: 404608 [Multi-domain]  Cd Length: 176  Bit Score: 292.60  E-value: 1.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754    37 YTFIDPLCPECWAFEPILKKLQVEYGQYFRIRFIVAGKLEAWNLCRGKykgaqsredlahvwrkitetfgMPCDGDVWLE 116
Cdd:pfam13743   1 YLFIDPLCPECWAIEPQIKKLKVEYGQKFDIRFIPLGNLQTLNYNMGR----------------------MPIDGDVLRN 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754   117 DPITSSYTPSLAIKAAELQGPQAGVRFLRKLREHLFLNKQNVTKEDILISCAQRAGLDVKEFKQDLHSKGAAKALRCDMQ 196
Cdd:pfam13743  59 DPFSSPYLASLAYKAAELQGKKKGRRFLRKLQEAVFLEKQNISDEELLLECAEKAGLDVEEFKEDLHSDLAKKAFQCDQK 138
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 81857754   197 TTKEMDVDLVPTFVFFNDNVDEEGIKVTGHYPYHIYVQ 234
Cdd:pfam13743 139 LAAEMGVTEHPTLVFFNSNVEEEGLKVEGCYPYDVYEQ 176
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
34-231 2.22e-69

DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif with similarity to DsbA and FrnE. FrnE is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins.


Pssm-ID: 239323 [Multi-domain]  Cd Length: 193  Bit Score: 213.72  E-value: 2.22e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754  34 LEIYTFIDPLCPECWAFEPILKKLQVEYGQYFRIRFIVAGKLEAWNLCrgkykGAQSREDLAHVWRKITE-TFGMPCDGD 112
Cdd:cd03025   1 LELYYFIDPLCGWCYGFEPLLEKLKEEYGGGIEVELHLGGLLPGNNAR-----QITKQWRIYVHWHKARIaLTGQPFGED 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754 113 VWLEDPI-TSSYTPSLAIKAAELQGPQAGVRFLRKLREHLFLNKQNVTKEDILISCAQRAGLDVKEFKQDLHSKGAAKAL 191
Cdd:cd03025  76 YLELLLFdLDSAPASRAIKAARLQGPERLLEMLKAIQRAHYVEGRDLADTEVLRELAIELGLDVEEFLEDFQSDEAKQAI 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 81857754 192 RCDMQTTKEMDVDLVPTFVFFNDNvdEEGIKVTGHYPYHI 231
Cdd:cd03025 156 QEDQKLARELGINGFPTLVLEDDN--GEGILLTGYYPYEP 193
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
33-241 4.07e-50

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 165.06  E-value: 4.07e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754  33 PLEIYTFIDPLCPECWAFEPILKKLQVEYGQYFRIRFI---------VAGKLEAWNLCRgKYKGAQSREDLAHvWRKITE 103
Cdd:COG2761   1 PLKIDIFSDVVCPWCYIGKRRLEKALAEFGDDVEIRWRpfelnpdmpPEGEDRREYLLA-KGSPEQAEQMRAH-VEEAAA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754 104 TFGMPCDgdvWLEDPITSSYTPSLAIKAAELQGPQAgvRFLRKLREHLFLNKQNVTKEDILISCAQRAGLDVKEFKQDLH 183
Cdd:COG2761  79 EEGLPFD---FDRIKPPNTFDAHRLLKAAELQGKQD--ALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLE 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 81857754 184 SKGAAKALRCDMQTTKEMDVDLVPTFVFfndnvdEEGIKVTGHYPYHIYVQILEDMLG 241
Cdd:COG2761 154 SDEAAAAVRADEAEARELGVTGVPTFVF------DGKYAVSGAQPYEVFEQALRQALA 205
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
35-215 1.32e-26

Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 103.79  E-value: 1.32e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754  35 EIYTFIDPLCPECWAFEPILKKLQVEYGQYFRIRfIVAGKL------EAWNlcrgkykgAQSREDLAHVWRKITE----T 104
Cdd:COG3531   3 KLHYIYDPLCGWCYGFAPVIEALAEALGDRLDVE-LLSGGLfpgsnrRPMD--------PEMRAYIQPHWQRIAQltgqP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754 105 FGMPCDGDVWLEDPITSSYTPSLAIKAAELQGPQAGVRFLRKLREHLFLNKQNVTKEDILISCAQRAGLDVKEFKQDLHS 184
Cdd:COG3531  74 FGEAYNDLLRDGTFVLDSEPACRAVLAARELAPERELAMLHAIQRAFYVEGRDISDPEVLAELAAELGLDAEAFAAALAS 153
                       170       180       190
                ....*....|....*....|....*....|.
gi 81857754 185 KGAAKALRCDMQTTKEMDVDLVPTFVFFNDN 215
Cdd:COG3531 154 EETRQHIQQEFALARQLGVQGFPTLVLEQGG 184
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
33-240 4.45e-10

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 57.32  E-value: 4.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754  33 PLEIYTFIDPLCPECWAFEPILKKLQVEYGqYFRIRFivagkleawnlcrgkykgaqsredlahvwrkitetfgmpcdgd 112
Cdd:COG1651   1 KVTVVEFFDYQCPYCARFHPELPELLKKYV-DGKVRV------------------------------------------- 36
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754 113 VWLEDPI--TSSYTPSLAIKAAELQGpqagvRFLrKLREHLFLNKQNVTkEDILISCAQRAGLDVKEFKQDLHSKGAAKA 190
Cdd:COG1651  37 VYRPFPLlhPDSLRAARAALCAADQG-----KFW-AFHDALFANQPALT-DDDLREIAKEAGLDAAKFDACLNSGAVAAK 109
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 81857754 191 LRCDMQTTKEMDVDLVPTFvFFNdnvdeeGIKVTGHYPYHIYVQILEDML 240
Cdd:COG1651 110 VEADTALAQALGVTGTPTF-VVN------GKLVSGAVPYEELEAALDAAL 152
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
39-222 2.83e-09

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 55.90  E-value: 2.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754    39 FIDPLCPECWAFEPILKKLQVEYGQyFRIRFIvagkleAWNLCRGKYKGAQSREDLAH----VWRKITETFGMPCDGDVW 114
Cdd:pfam01323   5 FFDFLCPFCYLAKERLEKLAARYGD-VKVVYR------PFPLAGAKKIGNVGPSNLPVklkyMMADLERWAALYGIPLRF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754   115 LEDPITSSYTPSLAIKAAELQGPQAGVrfLRKLREHLFLNKQNVTKEDILISCAQRAGLDVKEFKQDLHSKGAAKALRCD 194
Cdd:pfam01323  78 PANFLGNSTRANRLALAAGAEGLAEKV--VRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVREN 155
                         170       180       190
                  ....*....|....*....|....*....|..
gi 81857754   195 MQTTKEMDVDLVPTFV----FFNDNVDEEGIK 222
Cdd:pfam01323 156 TAAAISLGVFGVPTFVvggkMVFGADRLDTLA 187
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
36-70 5.06e-06

DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins.


Pssm-ID: 239270 [Multi-domain]  Cd Length: 98  Bit Score: 44.32  E-value: 5.06e-06
                        10        20        30
                ....*....|....*....|....*....|....*
gi 81857754  36 IYTFIDPLCPECWAFEPILKKLQVEYGQYFRIRFI 70
Cdd:cd02972   1 IVEFFDPLCPYCYLFEPELEKLLYADDGGVRVVYR 35
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
129-237 1.42e-03

DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins.


Pssm-ID: 239322 [Multi-domain]  Cd Length: 201  Bit Score: 39.10  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754 129 IKAAELQGPQAgvRFLRKLREHLFLNKQNVTKEDILISCAQRAGLDVKEFKQDLHSKGAAKALRCDMQTTKEMDVDLVPT 208
Cdd:cd03024 101 IHLAKEQGKQD--ALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYADEVRADEARARQLGISGVPF 178
                        90       100
                ....*....|....*....|....*....
gi 81857754 209 FVFfndnvdEEGIKVTGHYPYHIYVQILE 237
Cdd:cd03024 179 FVF------NGKYAVSGAQPPEVFLQALR 201
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
49-219 1.80e-03

DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a glutathione (GSH) dependent enzyme involved in the naphthalene catabolic pathway. It converts HCCA, a hemiketal formed spontaneously after ring cleavage of 1,2-dihydroxynapthalene by a dioxygenase, into cis-o-hydroxybenzylidenepyruvate (cHBPA). This is the fourth reaction in a six-step pathway that converts napthalene into salicylate. HCCA isomerase is unique to bacteria that degrade polycyclic aromatic compounds. It is closely related to the eukaryotic protein, GSH transferase kappa (GSTK).


Pssm-ID: 239320 [Multi-domain]  Cd Length: 192  Bit Score: 38.76  E-value: 1.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754  49 AFEPILKKLQvEYGQYFRIRFIVAGKL--EAWNL---CRGKYKGAQSREDLAHVWRKITETFGMPCDgdvwleDPItSSY 123
Cdd:cd03022  15 AHERLPALAA-RHGATVRYRPILLGGVfkATGNVppaNRPPAKGRYRLRDLERWARRYGIPLRFPPR------FPP-NTL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81857754 124 TPSLAIKAAELQGpQAGVRFLRKLREHLFLNKQNVTKEDILISCAQRAGLDVKEFKQDLHSKGAAKALRcdmQTTKEM-- 201
Cdd:cd03022  87 RAMRAALAAQAEG-DAAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAADDPAVKAALR---ANTEEAia 162
                       170
                ....*....|....*....
gi 81857754 202 -DVDLVPTFVffndnVDEE 219
Cdd:cd03022 163 rGVFGVPTFV-----VDGE 176
 
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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