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Conserved domains on  [gi|996153203|emb|CXI36449|]
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Sec-independent exported protein [Staphylococcus aureus]

Protein Classification

deferrochelatase/peroxidase EfeB( domain architecture ID 10019045)

deferrochelatase/peroxidase EfeB is involved in the recovery of exogenous heme iron

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
tat_substr_1 TIGR01412
Tat-translocated enzyme; This model represents a small family of proteins with a typical Tat ...
6-409 0e+00

Tat-translocated enzyme; This model represents a small family of proteins with a typical Tat (twin-arginine translocation) signal sequence, suggesting that the family is exported in a folded state, perhaps with a bound redox cofactor. Members of this family show homology to Dyp, a dye-decolorizing peroxidase from Geotrichum candidum that lacks any typical heme-binding site.


:

Pssm-ID: 273606 [Multi-domain]  Cd Length: 414  Bit Score: 641.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203    6 QVNDSTQFSRRTFLKMLGIGGA---GVAIGASGVGSMWSFKSMFNTPeDPEKDAYEFYGKVQPGITTPTQKTCNFVALDL 82
Cdd:TIGR01412   1 SANAPTQPSRRRLLKTAGAAGLagaAAAAGAGAVAVATAAKTAFSLP-DDESEAVPFYGKHQAGITTPQQARGHFVAFDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203   83 KSKDRDAIKAMFKKWTVMADRMMDGDTVGKPSNNPLMPPVDTGESIGLGASKLTITFGISKSLMKKIGLSSKIPDAFKDL 162
Cdd:TIGR01412  80 TAKDRKAIEALFRRWTARARRLTAGGAVGEGANNPLAPPDDTGEARDLGPSNLTVTFGFGHSLFDRFGLADKRPVALADL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  163 PHFPNDQLIDDYSDGDIMIQACSNDSQVSFHAVHNLVRPFRDIVKVRWAQSGFIS--AKGKETPRNLMAFKDGTINPR-- 238
Cdd:TIGR01412 160 PDFPNDNLDKNRSGGDLCVQICADDPQVAFHALRNIIRHAGGTAVVRWSQNGFISgaTKGKETPRNLLGFKDGTRNPKpg 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  239 KNNQLKDYVFIDDG----WAKHGTYCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGKEFDEIDLkAKDSHGEy 314
Cdd:TIGR01412 240 EDDLLDRVVWVDEEgepaWMTGGSYQVVRRIRMHLETWDRTSLKEQEDVFGRRKSSGAPLGGAKESDEPDL-AKDPEGE- 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  315 IIDKDAHTRLAKEA---NTSILRRAFNYVDGTDDrTGNFETGLLFIAFQK-ATKQFIDIQNNLgSNDKLNEYITHRGSAS 390
Cdd:TIGR01412 318 VIPKDAHVRLAKPDqngGAAMLRRAFSYTDGTDA-TGQLDAGLLFVCYQAdPLKGFIPVQRNL-AGDALNEYIQHIGSGL 395
                         410
                  ....*....|....*....
gi 996153203  391 FLVLPGVSKGGYLGETLFD 409
Cdd:TIGR01412 396 FAVPPGVKKGEYLGQRLLE 414
 
Name Accession Description Interval E-value
tat_substr_1 TIGR01412
Tat-translocated enzyme; This model represents a small family of proteins with a typical Tat ...
6-409 0e+00

Tat-translocated enzyme; This model represents a small family of proteins with a typical Tat (twin-arginine translocation) signal sequence, suggesting that the family is exported in a folded state, perhaps with a bound redox cofactor. Members of this family show homology to Dyp, a dye-decolorizing peroxidase from Geotrichum candidum that lacks any typical heme-binding site.


Pssm-ID: 273606 [Multi-domain]  Cd Length: 414  Bit Score: 641.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203    6 QVNDSTQFSRRTFLKMLGIGGA---GVAIGASGVGSMWSFKSMFNTPeDPEKDAYEFYGKVQPGITTPTQKTCNFVALDL 82
Cdd:TIGR01412   1 SANAPTQPSRRRLLKTAGAAGLagaAAAAGAGAVAVATAAKTAFSLP-DDESEAVPFYGKHQAGITTPQQARGHFVAFDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203   83 KSKDRDAIKAMFKKWTVMADRMMDGDTVGKPSNNPLMPPVDTGESIGLGASKLTITFGISKSLMKKIGLSSKIPDAFKDL 162
Cdd:TIGR01412  80 TAKDRKAIEALFRRWTARARRLTAGGAVGEGANNPLAPPDDTGEARDLGPSNLTVTFGFGHSLFDRFGLADKRPVALADL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  163 PHFPNDQLIDDYSDGDIMIQACSNDSQVSFHAVHNLVRPFRDIVKVRWAQSGFIS--AKGKETPRNLMAFKDGTINPR-- 238
Cdd:TIGR01412 160 PDFPNDNLDKNRSGGDLCVQICADDPQVAFHALRNIIRHAGGTAVVRWSQNGFISgaTKGKETPRNLLGFKDGTRNPKpg 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  239 KNNQLKDYVFIDDG----WAKHGTYCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGKEFDEIDLkAKDSHGEy 314
Cdd:TIGR01412 240 EDDLLDRVVWVDEEgepaWMTGGSYQVVRRIRMHLETWDRTSLKEQEDVFGRRKSSGAPLGGAKESDEPDL-AKDPEGE- 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  315 IIDKDAHTRLAKEA---NTSILRRAFNYVDGTDDrTGNFETGLLFIAFQK-ATKQFIDIQNNLgSNDKLNEYITHRGSAS 390
Cdd:TIGR01412 318 VIPKDAHVRLAKPDqngGAAMLRRAFSYTDGTDA-TGQLDAGLLFVCYQAdPLKGFIPVQRNL-AGDALNEYIQHIGSGL 395
                         410
                  ....*....|....*....
gi 996153203  391 FLVLPGVSKGGYLGETLFD 409
Cdd:TIGR01412 396 FAVPPGVKKGEYLGQRLLE 414
Dyp_perox pfam04261
Dyp-type peroxidase family; This family of dye-decolourising peroxidases lack a typical ...
64-399 6.12e-133

Dyp-type peroxidase family; This family of dye-decolourising peroxidases lack a typical heme-binding region.


Pssm-ID: 461241  Cd Length: 315  Bit Score: 384.05  E-value: 6.12e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203   64 QPGITTPTQKTCNFVALDLKSKDRDAIKAMFKKWTVMADRMMDGDTvgkpsnnplMPPVDTGESIGLG--ASKLTITFGI 141
Cdd:pfam04261   1 QAGILTPHQAAAIFLAFDVTAGDKAALEALFRKWTARVRRLTAGGR---------APPLDTGEAGGARfpDSRLTVTVGF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  142 SKSLMKKIGLSSKIPDAFKDLPHFPNDQLIDDYSDGDIMIQACSNDSQVSFHAVHNLVRPFRDIVKVRWAQSGFISakgk 221
Cdd:pfam04261  72 GSSLWDRFGLGSKRPKELKPFPEFPNDNLDAPSTDGDLLIHICADRPDVAFHAARNIMRAFGDAVEVRWEIHGFRY---- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  222 ETPRNLMAFKDGTINPRKNNQLKDYVFIDDG--WAKHGTYCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGke 299
Cdd:pfam04261 148 ETPRNLLGFVDGTENPKGEEAKRAVVWIKDGppWFAGGSYVVVQRIRHNLEAWDRLSLKEQEDVIGRRKESGAELGGD-- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  300 fdeidlkakdshgeYIIDKDAHTRLAKEA----NTSILRRAFNYVDgtddrTGNFETGLLFIAFQKATKQFIDI-QNNL- 373
Cdd:pfam04261 226 --------------KVKPADSHVRLANPKengkGLKILRRSLPYGD-----VGQGDHGLLFIAYQRTLHNGEQMlQNMLg 286
                         330       340
                  ....*....|....*....|....*....
gi 996153203  374 ---GSNDKLNEYITHRGSASFLVLPGVSK 399
Cdd:pfam04261 287 gtdGKTDALLEFITAVTGGYFFAPSGVKL 315
EfeB COG2837
Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism];
63-405 8.39e-117

Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism];


Pssm-ID: 442085  Cd Length: 334  Bit Score: 343.79  E-value: 8.39e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  63 VQPGITTPTQKTCNFVALDLK-SKDRDAIKAMFKKWTVMADRMMDGDTVGkpsnnplmppvdtgesiGLGASKLTITFGI 141
Cdd:COG2837    8 IQAGILTPPQAHAIFLAFDLKdGADRAALRALLRRLTALAARLTSGAPAL-----------------RLPPAGLTVTVGF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203 142 SKSLMKKIGLSSKiPDAFKDLPHFPNDQLIDDYSDGDIMIQACSNDSQVSFHAVHNLVRPFRDIVKVRWAQSGFISAKgk 221
Cdd:COG2837   71 GPSLWDRLGLAPR-PAELAPFPEFPGDGLDAPATGGDLLLQICADDPDVLFHAARQLLRALRGAATVRWEQDGFRYFP-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203 222 eTPRNLMAFKDGTINPRKNNQLKDYVFIDDG---WAKHGTYCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGK 298
Cdd:COG2837  148 -TGRNLFGFVDGTENPKGEDEADEVVLVGDEdpaWFAGGSYVVVRRIRHDLEAWDRLSLEEQEKVIGRTKDDGAPLDGGP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203 299 EFDEIDLKAkdshGEYIIDKDAHTRLA--KEANTS--ILRRAFNYVDGTDDrTGNFETGLLFIAFQK-ATKQFIDIQNNL 373
Cdd:COG2837  227 EFDDPDFAA----DAGVIPADSHVRRAnpRDDGNElrILRRGMPYGDGLDP-AGELDAGLLFIAYQAdPARQFEMLQRML 301
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 996153203 374 GSN-----DKLNEYITHRGSASFLVLPgvskGGYLGE 405
Cdd:COG2837  302 GGDpdgnyDRLLDFTTPVGGAYFFVPS----GDFLGQ 334
 
Name Accession Description Interval E-value
tat_substr_1 TIGR01412
Tat-translocated enzyme; This model represents a small family of proteins with a typical Tat ...
6-409 0e+00

Tat-translocated enzyme; This model represents a small family of proteins with a typical Tat (twin-arginine translocation) signal sequence, suggesting that the family is exported in a folded state, perhaps with a bound redox cofactor. Members of this family show homology to Dyp, a dye-decolorizing peroxidase from Geotrichum candidum that lacks any typical heme-binding site.


Pssm-ID: 273606 [Multi-domain]  Cd Length: 414  Bit Score: 641.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203    6 QVNDSTQFSRRTFLKMLGIGGA---GVAIGASGVGSMWSFKSMFNTPeDPEKDAYEFYGKVQPGITTPTQKTCNFVALDL 82
Cdd:TIGR01412   1 SANAPTQPSRRRLLKTAGAAGLagaAAAAGAGAVAVATAAKTAFSLP-DDESEAVPFYGKHQAGITTPQQARGHFVAFDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203   83 KSKDRDAIKAMFKKWTVMADRMMDGDTVGKPSNNPLMPPVDTGESIGLGASKLTITFGISKSLMKKIGLSSKIPDAFKDL 162
Cdd:TIGR01412  80 TAKDRKAIEALFRRWTARARRLTAGGAVGEGANNPLAPPDDTGEARDLGPSNLTVTFGFGHSLFDRFGLADKRPVALADL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  163 PHFPNDQLIDDYSDGDIMIQACSNDSQVSFHAVHNLVRPFRDIVKVRWAQSGFIS--AKGKETPRNLMAFKDGTINPR-- 238
Cdd:TIGR01412 160 PDFPNDNLDKNRSGGDLCVQICADDPQVAFHALRNIIRHAGGTAVVRWSQNGFISgaTKGKETPRNLLGFKDGTRNPKpg 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  239 KNNQLKDYVFIDDG----WAKHGTYCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGKEFDEIDLkAKDSHGEy 314
Cdd:TIGR01412 240 EDDLLDRVVWVDEEgepaWMTGGSYQVVRRIRMHLETWDRTSLKEQEDVFGRRKSSGAPLGGAKESDEPDL-AKDPEGE- 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  315 IIDKDAHTRLAKEA---NTSILRRAFNYVDGTDDrTGNFETGLLFIAFQK-ATKQFIDIQNNLgSNDKLNEYITHRGSAS 390
Cdd:TIGR01412 318 VIPKDAHVRLAKPDqngGAAMLRRAFSYTDGTDA-TGQLDAGLLFVCYQAdPLKGFIPVQRNL-AGDALNEYIQHIGSGL 395
                         410
                  ....*....|....*....
gi 996153203  391 FLVLPGVSKGGYLGETLFD 409
Cdd:TIGR01412 396 FAVPPGVKKGEYLGQRLLE 414
Dyp_perox pfam04261
Dyp-type peroxidase family; This family of dye-decolourising peroxidases lack a typical ...
64-399 6.12e-133

Dyp-type peroxidase family; This family of dye-decolourising peroxidases lack a typical heme-binding region.


Pssm-ID: 461241  Cd Length: 315  Bit Score: 384.05  E-value: 6.12e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203   64 QPGITTPTQKTCNFVALDLKSKDRDAIKAMFKKWTVMADRMMDGDTvgkpsnnplMPPVDTGESIGLG--ASKLTITFGI 141
Cdd:pfam04261   1 QAGILTPHQAAAIFLAFDVTAGDKAALEALFRKWTARVRRLTAGGR---------APPLDTGEAGGARfpDSRLTVTVGF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  142 SKSLMKKIGLSSKIPDAFKDLPHFPNDQLIDDYSDGDIMIQACSNDSQVSFHAVHNLVRPFRDIVKVRWAQSGFISakgk 221
Cdd:pfam04261  72 GSSLWDRFGLGSKRPKELKPFPEFPNDNLDAPSTDGDLLIHICADRPDVAFHAARNIMRAFGDAVEVRWEIHGFRY---- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  222 ETPRNLMAFKDGTINPRKNNQLKDYVFIDDG--WAKHGTYCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGke 299
Cdd:pfam04261 148 ETPRNLLGFVDGTENPKGEEAKRAVVWIKDGppWFAGGSYVVVQRIRHNLEAWDRLSLKEQEDVIGRRKESGAELGGD-- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  300 fdeidlkakdshgeYIIDKDAHTRLAKEA----NTSILRRAFNYVDgtddrTGNFETGLLFIAFQKATKQFIDI-QNNL- 373
Cdd:pfam04261 226 --------------KVKPADSHVRLANPKengkGLKILRRSLPYGD-----VGQGDHGLLFIAYQRTLHNGEQMlQNMLg 286
                         330       340
                  ....*....|....*....|....*....
gi 996153203  374 ---GSNDKLNEYITHRGSASFLVLPGVSK 399
Cdd:pfam04261 287 gtdGKTDALLEFITAVTGGYFFAPSGVKL 315
EfeB COG2837
Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism];
63-405 8.39e-117

Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism];


Pssm-ID: 442085  Cd Length: 334  Bit Score: 343.79  E-value: 8.39e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  63 VQPGITTPTQKTCNFVALDLK-SKDRDAIKAMFKKWTVMADRMMDGDTVGkpsnnplmppvdtgesiGLGASKLTITFGI 141
Cdd:COG2837    8 IQAGILTPPQAHAIFLAFDLKdGADRAALRALLRRLTALAARLTSGAPAL-----------------RLPPAGLTVTVGF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203 142 SKSLMKKIGLSSKiPDAFKDLPHFPNDQLIDDYSDGDIMIQACSNDSQVSFHAVHNLVRPFRDIVKVRWAQSGFISAKgk 221
Cdd:COG2837   71 GPSLWDRLGLAPR-PAELAPFPEFPGDGLDAPATGGDLLLQICADDPDVLFHAARQLLRALRGAATVRWEQDGFRYFP-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203 222 eTPRNLMAFKDGTINPRKNNQLKDYVFIDDG---WAKHGTYCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGK 298
Cdd:COG2837  148 -TGRNLFGFVDGTENPKGEDEADEVVLVGDEdpaWFAGGSYVVVRRIRHDLEAWDRLSLEEQEKVIGRTKDDGAPLDGGP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203 299 EFDEIDLKAkdshGEYIIDKDAHTRLA--KEANTS--ILRRAFNYVDGTDDrTGNFETGLLFIAFQK-ATKQFIDIQNNL 373
Cdd:COG2837  227 EFDDPDFAA----DAGVIPADSHVRRAnpRDDGNElrILRRGMPYGDGLDP-AGELDAGLLFIAYQAdPARQFEMLQRML 301
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 996153203 374 GSN-----DKLNEYITHRGSASFLVLPgvskGGYLGE 405
Cdd:COG2837  302 GGDpdgnyDRLLDFTTPVGGAYFFVPS----GDFLGQ 334
Dyp_perox_fam TIGR01413
Dyp-type peroxidase family; A defined member of this superfamily is Dyp, a dye-decolorizing ...
64-399 2.32e-115

Dyp-type peroxidase family; A defined member of this superfamily is Dyp, a dye-decolorizing peroxidase that lacks a typical heme-binding region. A distinct, uncharacterized branch (TIGR01412) of this superfamily has a typical twin-arginine dependent signal sequence characteristic of exported proteins with bound redox cofactors.


Pssm-ID: 273607  Cd Length: 308  Bit Score: 338.95  E-value: 2.32e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203   64 QPGITTPTQKTCNFVALDLKSkDRDAIKAMFKKWTVMADRMMDGDTVGKPSNnplmppvdtgesiglgaskLTITFGISK 143
Cdd:TIGR01413   1 QPGILTPHQAAAIFLAFDVTA-DRAALEALLRALTALADLLTAGGAAGPPSR-------------------LTVTVGFGS 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  144 SLMKKIGLSSKIPDAFKDLPHFPNDQLIDDYSDGDIMIQACSNDSQVSFHAVHNLVRPFRDIVKVRWAQSGFISaKGKET 223
Cdd:TIGR01413  61 SLWDRLGLADKRPKELKDFPELGGDSLDAPSTGGDLLFHIRADDPDVVFHAARALLRRFGDAVTVRDEVHGFRY-PGAET 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  224 PRNLMAFKDGTINPRKNNQLKDYVFIDD--GWAKHGTYCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLtGGKEfd 301
Cdd:TIGR01413 140 GRDLLGFVDGTENPKGPEALEAVLVIGEdpAWAAGGSYVVVQRIQHDLEEWDRLPLAEQEDVIGRRKSSGAEL-DGKE-- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996153203  302 eidlkakdshgeyIIDKDAHTRLAK----EANTSILRRAFNYVDGTDDRTGnfETGLLFIAFQK-ATKQFIDIQNNLGSN 376
Cdd:TIGR01413 217 -------------RAPADSHVRLTNpredGKGLKILRRGLPYGDGSDDTGQ--DAGLLFIAYQRsLENGEVQLQRMLGGT 281
                         330       340
                  ....*....|....*....|....*..
gi 996153203  377 ----DKLNEYITHRGSASFLVLPGVSK 399
Cdd:TIGR01413 282 dgatDRLLEFIRPVGGGYFFAPSGVAL 308
 
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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