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Conserved domains on  [gi|489849963|ref|WP_003753644|]
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iron uptake transporter deferrochelatase/peroxidase subunit [Neisseria polysaccharea]

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 ...
2-420 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: 675.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963    2 STNNPTQPTRRTLFKTAIAAGAVGAIGGYLGGKKQGETAERTAESQ--HSPQAYPCYGEHQAGIVTPQQAFSIMCAFDVT 79
Cdd:TIGR01412   1 SANAPTQPSRRRLLKTAGAAGLAGAAAAAGAGAVAVATAAKTAFSLpdDESEAVPFYGKHQAGITTPQQARGHFVAFDVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963   80 AQSAKQLENLFRTLTARIEFLTQGGEYQDG-DDKLPPAGSGILGKAFNPDGLTVTVGVGSSLFDgRFGLKDKKPVHLQEM 158
Cdd:TIGR01412  81 AKDRKAIEALFRRWTARARRLTAGGAVGEGaNNPLAPPDDTGEARDLGPSNLTVTFGFGHSLFD-RFGLADKRPVALADL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  159 RDFSNDKLQKNWCDGDLSLQICAFTPETCQAALRDIIKHTAQTAVIRWSIDGWQPKSEPGAMAARNLLGFRDGTGNPKVS 238
Cdd:TIGR01412 160 PDFPNDNLDKNRSGGDLCVQICADDPQVAFHALRNIIRHAGGTAVVRWSQNGFISGATKGKETPRNLLGFKDGTRNPKPG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  239 DPKTADEVLWTGVAanslDEPEWAKNGSYQAVRLIRHFVEFWDRTPLQEQTDIFGRRKYSGAPMDGKKEADQPDFAKDPE 318
Cdd:TIGR01412 240 EDDLLDRVVWVDEE----GEPAWMTGGSYQVVRRIRMHLETWDRTSLKEQEDVFGRRKSSGAPLGGAKESDEPDLAKDPE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  319 GNTTPKDSHIRLANPRDPeflKKHRLFRRAYSYSRGLASSGQLDVGLVFVCYQANLADGFIFVQNLLNGEPLEEYISPFG 398
Cdd:TIGR01412 316 GEVIPKDAHVRLAKPDQN---GGAAMLRRAFSYTDGTDATGQLDAGLLFVCYQADPLKGFIPVQRNLAGDALNEYIQHIG 392
                         410       420
                  ....*....|....*....|..
gi 489849963  399 GGYFFVLPGVEKGGFLGQGLLD 420
Cdd:TIGR01412 393 SGLFAVPPGVKKGEYLGQRLLE 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 ...
2-420 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: 675.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963    2 STNNPTQPTRRTLFKTAIAAGAVGAIGGYLGGKKQGETAERTAESQ--HSPQAYPCYGEHQAGIVTPQQAFSIMCAFDVT 79
Cdd:TIGR01412   1 SANAPTQPSRRRLLKTAGAAGLAGAAAAAGAGAVAVATAAKTAFSLpdDESEAVPFYGKHQAGITTPQQARGHFVAFDVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963   80 AQSAKQLENLFRTLTARIEFLTQGGEYQDG-DDKLPPAGSGILGKAFNPDGLTVTVGVGSSLFDgRFGLKDKKPVHLQEM 158
Cdd:TIGR01412  81 AKDRKAIEALFRRWTARARRLTAGGAVGEGaNNPLAPPDDTGEARDLGPSNLTVTFGFGHSLFD-RFGLADKRPVALADL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  159 RDFSNDKLQKNWCDGDLSLQICAFTPETCQAALRDIIKHTAQTAVIRWSIDGWQPKSEPGAMAARNLLGFRDGTGNPKVS 238
Cdd:TIGR01412 160 PDFPNDNLDKNRSGGDLCVQICADDPQVAFHALRNIIRHAGGTAVVRWSQNGFISGATKGKETPRNLLGFKDGTRNPKPG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  239 DPKTADEVLWTGVAanslDEPEWAKNGSYQAVRLIRHFVEFWDRTPLQEQTDIFGRRKYSGAPMDGKKEADQPDFAKDPE 318
Cdd:TIGR01412 240 EDDLLDRVVWVDEE----GEPAWMTGGSYQVVRRIRMHLETWDRTSLKEQEDVFGRRKSSGAPLGGAKESDEPDLAKDPE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  319 GNTTPKDSHIRLANPRDPeflKKHRLFRRAYSYSRGLASSGQLDVGLVFVCYQANLADGFIFVQNLLNGEPLEEYISPFG 398
Cdd:TIGR01412 316 GEVIPKDAHVRLAKPDQN---GGAAMLRRAFSYTDGTDATGQLDAGLLFVCYQADPLKGFIPVQRNLAGDALNEYIQHIG 392
                         410       420
                  ....*....|....*....|..
gi 489849963  399 GGYFFVLPGVEKGGFLGQGLLD 420
Cdd:TIGR01412 393 SGLFAVPPGVKKGEYLGQRLLE 414
Dyp_perox pfam04261
Dyp-type peroxidase family; This family of dye-decolourising peroxidases lack a typical ...
60-410 2.54e-140

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


Pssm-ID: 461241  Cd Length: 315  Bit Score: 403.31  E-value: 2.54e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963   60 QAGIVTPQQAFSIMCAFDVTAQSAKQLENLFRTLTARIEFLTQGGEYqdgddklPPAGSGILGKAFNPDG-LTVTVGVGS 138
Cdd:pfam04261   1 QAGILTPHQAAAIFLAFDVTAGDKAALEALFRKWTARVRRLTAGGRA-------PPLDTGEAGGARFPDSrLTVTVGFGS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  139 SLFDgRFGLKDKKPVHLQEMRDFSNDKLQKNWCDGDLSLQICAFTPETCQAALRDIIKHTAQTAVIRWSIDGWQpksepg 218
Cdd:pfam04261  74 SLWD-RFGLGSKRPKELKPFPEFPNDNLDAPSTDGDLLIHICADRPDVAFHAARNIMRAFGDAVEVRWEIHGFR------ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  219 AMAARNLLGFRDGTGNPKVSDPKTAdeVLWTGvaanslDEPEWAKNGSYQAVRLIRHFVEFWDRTPLQEQTDIFGRRKYS 298
Cdd:pfam04261 147 YETPRNLLGFVDGTENPKGEEAKRA--VVWIK------DGPPWFAGGSYVVVQRIRHNLEAWDRLSLKEQEDVIGRRKES 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  299 GAPMDGKKeadqpdfakdpegnTTPKDSHIRLANPRDPefLKKHRLFRRAYSYSrglaSSGQLDVGLVFVCYQANLADGF 378
Cdd:pfam04261 219 GAELGGDK--------------VKPADSHVRLANPKEN--GKGLKILRRSLPYG----DVGQGDHGLLFIAYQRTLHNGE 278
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 489849963  379 IFVQNLL-----NGEPLEEYISPFGGGYFFVLPGVEK 410
Cdd:pfam04261 279 QMLQNMLggtdgKTDALLEFITAVTGGYFFAPSGVKL 315
EfeB COG2837
Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism];
59-416 2.46e-131

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


Pssm-ID: 442085  Cd Length: 334  Bit Score: 381.16  E-value: 2.46e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  59 HQAGIVTPQQAFSIMCAFDVT-AQSAKQLENLFRTLTARIEFLTQGGEYQdgddklppagsgilgkAFNPDGLTVTVGVG 137
Cdd:COG2837    8 IQAGILTPPQAHAIFLAFDLKdGADRAALRALLRRLTALAARLTSGAPAL----------------RLPPAGLTVTVGFG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963 138 SSLFDgRFGLkDKKPVHLQEMRDFSNDKLQKNWCDGDLSLQICAFTPETCQAALRDIIKHTAQTAVIRWSIDGWQPKSEP 217
Cdd:COG2837   72 PSLWD-RLGL-APRPAELAPFPEFPGDGLDAPATGGDLLLQICADDPDVLFHAARQLLRALRGAATVRWEQDGFRYFPTG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963 218 gamaaRNLLGFRDGTGNPKVSDpkTADEVLWTGvaanslDE-PEWAKNGSYQAVRLIRHFVEFWDRTPLQEQTDIFGRRK 296
Cdd:COG2837  150 -----RNLFGFVDGTENPKGED--EADEVVLVG------DEdPAWFAGGSYVVVRRIRHDLEAWDRLSLEEQEKVIGRTK 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963 297 YSGAPMDGKKEADQPDFAKDPEgnTTPKDSHIRLANPRDPEflKKHRLFRRAYSYSRGLASSGQLDVGLVFVCYQANLAD 376
Cdd:COG2837  217 DDGAPLDGGPEFDDPDFAADAG--VIPADSHVRRANPRDDG--NELRILRRGMPYGDGLDPAGELDAGLLFIAYQADPAR 292
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 489849963 377 GFIFVQNLLNG------EPLEEYISPFGGGYFFVLPgvekGGFLGQ 416
Cdd:COG2837  293 QFEMLQRMLGGdpdgnyDRLLDFTTPVGGAYFFVPS----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 ...
2-420 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: 675.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963    2 STNNPTQPTRRTLFKTAIAAGAVGAIGGYLGGKKQGETAERTAESQ--HSPQAYPCYGEHQAGIVTPQQAFSIMCAFDVT 79
Cdd:TIGR01412   1 SANAPTQPSRRRLLKTAGAAGLAGAAAAAGAGAVAVATAAKTAFSLpdDESEAVPFYGKHQAGITTPQQARGHFVAFDVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963   80 AQSAKQLENLFRTLTARIEFLTQGGEYQDG-DDKLPPAGSGILGKAFNPDGLTVTVGVGSSLFDgRFGLKDKKPVHLQEM 158
Cdd:TIGR01412  81 AKDRKAIEALFRRWTARARRLTAGGAVGEGaNNPLAPPDDTGEARDLGPSNLTVTFGFGHSLFD-RFGLADKRPVALADL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  159 RDFSNDKLQKNWCDGDLSLQICAFTPETCQAALRDIIKHTAQTAVIRWSIDGWQPKSEPGAMAARNLLGFRDGTGNPKVS 238
Cdd:TIGR01412 160 PDFPNDNLDKNRSGGDLCVQICADDPQVAFHALRNIIRHAGGTAVVRWSQNGFISGATKGKETPRNLLGFKDGTRNPKPG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  239 DPKTADEVLWTGVAanslDEPEWAKNGSYQAVRLIRHFVEFWDRTPLQEQTDIFGRRKYSGAPMDGKKEADQPDFAKDPE 318
Cdd:TIGR01412 240 EDDLLDRVVWVDEE----GEPAWMTGGSYQVVRRIRMHLETWDRTSLKEQEDVFGRRKSSGAPLGGAKESDEPDLAKDPE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  319 GNTTPKDSHIRLANPRDPeflKKHRLFRRAYSYSRGLASSGQLDVGLVFVCYQANLADGFIFVQNLLNGEPLEEYISPFG 398
Cdd:TIGR01412 316 GEVIPKDAHVRLAKPDQN---GGAAMLRRAFSYTDGTDATGQLDAGLLFVCYQADPLKGFIPVQRNLAGDALNEYIQHIG 392
                         410       420
                  ....*....|....*....|..
gi 489849963  399 GGYFFVLPGVEKGGFLGQGLLD 420
Cdd:TIGR01412 393 SGLFAVPPGVKKGEYLGQRLLE 414
Dyp_perox pfam04261
Dyp-type peroxidase family; This family of dye-decolourising peroxidases lack a typical ...
60-410 2.54e-140

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


Pssm-ID: 461241  Cd Length: 315  Bit Score: 403.31  E-value: 2.54e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963   60 QAGIVTPQQAFSIMCAFDVTAQSAKQLENLFRTLTARIEFLTQGGEYqdgddklPPAGSGILGKAFNPDG-LTVTVGVGS 138
Cdd:pfam04261   1 QAGILTPHQAAAIFLAFDVTAGDKAALEALFRKWTARVRRLTAGGRA-------PPLDTGEAGGARFPDSrLTVTVGFGS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  139 SLFDgRFGLKDKKPVHLQEMRDFSNDKLQKNWCDGDLSLQICAFTPETCQAALRDIIKHTAQTAVIRWSIDGWQpksepg 218
Cdd:pfam04261  74 SLWD-RFGLGSKRPKELKPFPEFPNDNLDAPSTDGDLLIHICADRPDVAFHAARNIMRAFGDAVEVRWEIHGFR------ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  219 AMAARNLLGFRDGTGNPKVSDPKTAdeVLWTGvaanslDEPEWAKNGSYQAVRLIRHFVEFWDRTPLQEQTDIFGRRKYS 298
Cdd:pfam04261 147 YETPRNLLGFVDGTENPKGEEAKRA--VVWIK------DGPPWFAGGSYVVVQRIRHNLEAWDRLSLKEQEDVIGRRKES 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  299 GAPMDGKKeadqpdfakdpegnTTPKDSHIRLANPRDPefLKKHRLFRRAYSYSrglaSSGQLDVGLVFVCYQANLADGF 378
Cdd:pfam04261 219 GAELGGDK--------------VKPADSHVRLANPKEN--GKGLKILRRSLPYG----DVGQGDHGLLFIAYQRTLHNGE 278
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 489849963  379 IFVQNLL-----NGEPLEEYISPFGGGYFFVLPGVEK 410
Cdd:pfam04261 279 QMLQNMLggtdgKTDALLEFITAVTGGYFFAPSGVKL 315
EfeB COG2837
Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism];
59-416 2.46e-131

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


Pssm-ID: 442085  Cd Length: 334  Bit Score: 381.16  E-value: 2.46e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  59 HQAGIVTPQQAFSIMCAFDVT-AQSAKQLENLFRTLTARIEFLTQGGEYQdgddklppagsgilgkAFNPDGLTVTVGVG 137
Cdd:COG2837    8 IQAGILTPPQAHAIFLAFDLKdGADRAALRALLRRLTALAARLTSGAPAL----------------RLPPAGLTVTVGFG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963 138 SSLFDgRFGLkDKKPVHLQEMRDFSNDKLQKNWCDGDLSLQICAFTPETCQAALRDIIKHTAQTAVIRWSIDGWQPKSEP 217
Cdd:COG2837   72 PSLWD-RLGL-APRPAELAPFPEFPGDGLDAPATGGDLLLQICADDPDVLFHAARQLLRALRGAATVRWEQDGFRYFPTG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963 218 gamaaRNLLGFRDGTGNPKVSDpkTADEVLWTGvaanslDE-PEWAKNGSYQAVRLIRHFVEFWDRTPLQEQTDIFGRRK 296
Cdd:COG2837  150 -----RNLFGFVDGTENPKGED--EADEVVLVG------DEdPAWFAGGSYVVVRRIRHDLEAWDRLSLEEQEKVIGRTK 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963 297 YSGAPMDGKKEADQPDFAKDPEgnTTPKDSHIRLANPRDPEflKKHRLFRRAYSYSRGLASSGQLDVGLVFVCYQANLAD 376
Cdd:COG2837  217 DDGAPLDGGPEFDDPDFAADAG--VIPADSHVRRANPRDDG--NELRILRRGMPYGDGLDPAGELDAGLLFIAYQADPAR 292
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 489849963 377 GFIFVQNLLNG------EPLEEYISPFGGGYFFVLPgvekGGFLGQ 416
Cdd:COG2837  293 QFEMLQRMLGGdpdgnyDRLLDFTTPVGGAYFFVPS----GDFLGQ 334
Dyp_perox_fam TIGR01413
Dyp-type peroxidase family; A defined member of this superfamily is Dyp, a dye-decolorizing ...
60-410 1.87e-123

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: 360.13  E-value: 1.87e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963   60 QAGIVTPQQAFSIMCAFDVTAQsAKQLENLFRTLTARIEFLTQGGeyqdgddklppagsgilgKAFNPDGLTVTVGVGSS 139
Cdd:TIGR01413   1 QPGILTPHQAAAIFLAFDVTAD-RAALEALLRALTALADLLTAGG------------------AAGPPSRLTVTVGFGSS 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  140 LFDgRFGLKDKKPVHLQEMRDFSNDKLQKNWCDGDLSLQICAFTPETCQAALRDIIKHTAQTAVIRWSIDGWQPksePGA 219
Cdd:TIGR01413  62 LWD-RLGLADKRPKELKDFPELGGDSLDAPSTGGDLLFHIRADDPDVVFHAARALLRRFGDAVTVRDEVHGFRY---PGA 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  220 MAARNLLGFRDGTGNPKVsdPKTADEVLWTGvaanslDEPEWAKNGSYQAVRLIRHFVEFWDRTPLQEQTDIFGRRKYSG 299
Cdd:TIGR01413 138 ETGRDLLGFVDGTENPKG--PEALEAVLVIG------EDPAWAAGGSYVVVQRIQHDLEEWDRLPLAEQEDVIGRRKSSG 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489849963  300 APMDGKkeadqpdfakdpegNTTPKDSHIRLANPRdpEFLKKHRLFRRAYSYSRGLASSGQlDVGLVFVCYQANLADGFI 379
Cdd:TIGR01413 210 AELDGK--------------ERAPADSHVRLTNPR--EDGKGLKILRRGLPYGDGSDDTGQ-DAGLLFIAYQRSLENGEV 272
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 489849963  380 FVQNLL-----NGEPLEEYISPFGGGYFFVLPGVEK 410
Cdd:TIGR01413 273 QLQRMLggtdgATDRLLEFIRPVGGGYFFAPSGVAL 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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