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Conserved domains on  [gi|16080877|ref|NP_391705|]
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peroxidase converting ferric iron into ferrous iron [Bacillus subtilis subsp. subtilis str. 168]

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 ...
4-415 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: 673.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877     4 EQKKPEQIHRRDILKWGAMAGAAVAIGASGlgGLAPLVQTAAKPSKKDEKEEEQIVPFYGKHQAGITTAHQTYVYFAALD 83
Cdd:TIGR01412   1 SANAPTQPSRRRLLKTAGAAGLAGAAAAAG--AGAVAVATAAKTAFSLPDDESEAVPFYGKHQAGITTPQQARGHFVAFD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877    84 VTAKDKSDIITLFRNWTSLTQMLTSGKKMSAEQRNQYLPPQDTGESADLSPSNLTVTFGFGPGFFekdgkDRFGLKSKKP 163
Cdd:TIGR01412  79 VTAKDRKAIEALFRRWTARARRLTAGGAVGEGANNPLAPPDDTGEARDLGPSNLTVTFGFGHSLF-----DRFGLADKRP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   164 KHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCEVRFVNKGFLSG-GKNGETPRNLFGFKDGT 242
Cdd:TIGR01412 154 VALADLPDFPNDNLDKNRSGGDLCVQICADDPQVAFHALRNIIRHAGGTAVVRWSQNGFISGaTKGKETPRNLLGFKDGT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   243 GNQSTKDDTLMNSIVWIQS-GEPDWMTGGTYMAFRKIKMFLEVWDRSSLKDQEDTFGRRKSSGAPFGQKKETDPVKL--- 318
Cdd:TIGR01412 234 RNPKPGEDDLLDRVVWVDEeGEPAWMTGGSYQVVRRIRMHLETWDRTSLKEQEDVFGRRKSSGAPLGGAKESDEPDLakd 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   319 ---NQIPSNSHVSLAKST---GKQILRRAFSYTEGLDPkTGYMDAGLLFISFQKNPDNQFIPMLKALsAKDALNEYTQTI 392
Cdd:TIGR01412 314 pegEVIPKDAHVRLAKPDqngGAAMLRRAFSYTDGTDA-TGQLDAGLLFVCYQADPLKGFIPVQRNL-AGDALNEYIQHI 391
                         410       420
                  ....*....|....*....|...
gi 16080877   393 GSALYACPGGCKKGEYIAQRLLE 415
Cdd:TIGR01412 392 GSGLFAVPPGVKKGEYLGQRLLE 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 ...
4-415 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: 673.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877     4 EQKKPEQIHRRDILKWGAMAGAAVAIGASGlgGLAPLVQTAAKPSKKDEKEEEQIVPFYGKHQAGITTAHQTYVYFAALD 83
Cdd:TIGR01412   1 SANAPTQPSRRRLLKTAGAAGLAGAAAAAG--AGAVAVATAAKTAFSLPDDESEAVPFYGKHQAGITTPQQARGHFVAFD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877    84 VTAKDKSDIITLFRNWTSLTQMLTSGKKMSAEQRNQYLPPQDTGESADLSPSNLTVTFGFGPGFFekdgkDRFGLKSKKP 163
Cdd:TIGR01412  79 VTAKDRKAIEALFRRWTARARRLTAGGAVGEGANNPLAPPDDTGEARDLGPSNLTVTFGFGHSLF-----DRFGLADKRP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   164 KHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCEVRFVNKGFLSG-GKNGETPRNLFGFKDGT 242
Cdd:TIGR01412 154 VALADLPDFPNDNLDKNRSGGDLCVQICADDPQVAFHALRNIIRHAGGTAVVRWSQNGFISGaTKGKETPRNLLGFKDGT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   243 GNQSTKDDTLMNSIVWIQS-GEPDWMTGGTYMAFRKIKMFLEVWDRSSLKDQEDTFGRRKSSGAPFGQKKETDPVKL--- 318
Cdd:TIGR01412 234 RNPKPGEDDLLDRVVWVDEeGEPAWMTGGSYQVVRRIRMHLETWDRTSLKEQEDVFGRRKSSGAPLGGAKESDEPDLakd 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   319 ---NQIPSNSHVSLAKST---GKQILRRAFSYTEGLDPkTGYMDAGLLFISFQKNPDNQFIPMLKALsAKDALNEYTQTI 392
Cdd:TIGR01412 314 pegEVIPKDAHVRLAKPDqngGAAMLRRAFSYTDGTDA-TGQLDAGLLFVCYQADPLKGFIPVQRNL-AGDALNEYIQHI 391
                         410       420
                  ....*....|....*....|...
gi 16080877   393 GSALYACPGGCKKGEYIAQRLLE 415
Cdd:TIGR01412 392 GSGLFAVPPGVKKGEYLGQRLLE 414
Dyp_perox pfam04261
Dyp-type peroxidase family; This family of dye-decolourising peroxidases lack a typical ...
66-405 1.43e-137

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


Pssm-ID: 461241  Cd Length: 315  Bit Score: 395.99  E-value: 1.43e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877    66 QAGITTAHQTYVYFAALDVTAKDKSDIITLFRNWTSLTQMLTSGKKMsaeqrnqylPPQDTGESADLS--PSNLTVTFGF 143
Cdd:pfam04261   1 QAGILTPHQAAAIFLAFDVTAGDKAALEALFRKWTARVRRLTAGGRA---------PPLDTGEAGGARfpDSRLTVTVGF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   144 GPGFFekdgkDRFGLKSKKPKHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCEVRFVNKGFL 223
Cdd:pfam04261  72 GSSLW-----DRFGLGSKRPKELKPFPEFPNDNLDAPSTDGDLLIHICADRPDVAFHAARNIMRAFGDAVEVRWEIHGFR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   224 SggkngETPRNLFGFKDGTGNQSTKDDTLMNsiVWIQsGEPDWMTGGTYMAFRKIKMFLEVWDRSSLKDQEDTFGRRKSS 303
Cdd:pfam04261 147 Y-----ETPRNLLGFVDGTENPKGEEAKRAV--VWIK-DGPPWFAGGSYVVVQRIRHNLEAWDRLSLKEQEDVIGRRKES 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   304 GAPFGQKKetdpvklnQIPSNSHVSLAKST----GKQILRRAFSYTEgldpkTGYMDAGLLFISFQKNPDNQFIPMLKAL 379
Cdd:pfam04261 219 GAELGGDK--------VKPADSHVRLANPKengkGLKILRRSLPYGD-----VGQGDHGLLFIAYQRTLHNGEQMLQNML 285
                         330       340       350
                  ....*....|....*....|....*....|
gi 16080877   380 S----AKDALNEYTQTIGSALYACPGGCKK 405
Cdd:pfam04261 286 GgtdgKTDALLEFITAVTGGYFFAPSGVKL 315
EfeB COG2837
Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism];
65-411 2.59e-125

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


Pssm-ID: 442085  Cd Length: 334  Bit Score: 365.75  E-value: 2.59e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877  65 HQAGITTAHQTYVYFAALDVT-AKDKSDIITLFRNWTSLTQMLTSGKkmsaeqrnqylppqdtgESADLSPSNLTVTFGF 143
Cdd:COG2837   8 IQAGILTPPQAHAIFLAFDLKdGADRAALRALLRRLTALAARLTSGA-----------------PALRLPPAGLTVTVGF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877 144 GPGFFekdgkDRFGLKsKKPKHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCEVRFVNKGFL 223
Cdd:COG2837  71 GPSLW-----DRLGLA-PRPAELAPFPEFPGDGLDAPATGGDLLLQICADDPDVLFHAARQLLRALRGAATVRWEQDGFR 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877 224 SGgkngETPRNLFGFKDGTGNQSTKDDtlMNSIVWIQSGEPDWMTGGTYMAFRKIKMFLEVWDRSSLKDQEDTFGRRKSS 303
Cdd:COG2837 145 YF----PTGRNLFGFVDGTENPKGEDE--ADEVVLVGDEDPAWFAGGSYVVVRRIRHDLEAWDRLSLEEQEKVIGRTKDD 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877 304 GAPFGQKKETDPVKLNQ----IPSNSHVSLA--KSTGK--QILRRAFSYTEGLDPkTGYMDAGLLFISFQKNPDNQFIPM 375
Cdd:COG2837 219 GAPLDGGPEFDDPDFAAdagvIPADSHVRRAnpRDDGNelRILRRGMPYGDGLDP-AGELDAGLLFIAYQADPARQFEML 297
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 16080877 376 LKALS-----AKDALNEYTQTIGSALYACPGgckkGEYIAQ 411
Cdd:COG2837 298 QRMLGgdpdgNYDRLLDFTTPVGGAYFFVPS----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 ...
4-415 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: 673.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877     4 EQKKPEQIHRRDILKWGAMAGAAVAIGASGlgGLAPLVQTAAKPSKKDEKEEEQIVPFYGKHQAGITTAHQTYVYFAALD 83
Cdd:TIGR01412   1 SANAPTQPSRRRLLKTAGAAGLAGAAAAAG--AGAVAVATAAKTAFSLPDDESEAVPFYGKHQAGITTPQQARGHFVAFD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877    84 VTAKDKSDIITLFRNWTSLTQMLTSGKKMSAEQRNQYLPPQDTGESADLSPSNLTVTFGFGPGFFekdgkDRFGLKSKKP 163
Cdd:TIGR01412  79 VTAKDRKAIEALFRRWTARARRLTAGGAVGEGANNPLAPPDDTGEARDLGPSNLTVTFGFGHSLF-----DRFGLADKRP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   164 KHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCEVRFVNKGFLSG-GKNGETPRNLFGFKDGT 242
Cdd:TIGR01412 154 VALADLPDFPNDNLDKNRSGGDLCVQICADDPQVAFHALRNIIRHAGGTAVVRWSQNGFISGaTKGKETPRNLLGFKDGT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   243 GNQSTKDDTLMNSIVWIQS-GEPDWMTGGTYMAFRKIKMFLEVWDRSSLKDQEDTFGRRKSSGAPFGQKKETDPVKL--- 318
Cdd:TIGR01412 234 RNPKPGEDDLLDRVVWVDEeGEPAWMTGGSYQVVRRIRMHLETWDRTSLKEQEDVFGRRKSSGAPLGGAKESDEPDLakd 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   319 ---NQIPSNSHVSLAKST---GKQILRRAFSYTEGLDPkTGYMDAGLLFISFQKNPDNQFIPMLKALsAKDALNEYTQTI 392
Cdd:TIGR01412 314 pegEVIPKDAHVRLAKPDqngGAAMLRRAFSYTDGTDA-TGQLDAGLLFVCYQADPLKGFIPVQRNL-AGDALNEYIQHI 391
                         410       420
                  ....*....|....*....|...
gi 16080877   393 GSALYACPGGCKKGEYIAQRLLE 415
Cdd:TIGR01412 392 GSGLFAVPPGVKKGEYLGQRLLE 414
Dyp_perox pfam04261
Dyp-type peroxidase family; This family of dye-decolourising peroxidases lack a typical ...
66-405 1.43e-137

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


Pssm-ID: 461241  Cd Length: 315  Bit Score: 395.99  E-value: 1.43e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877    66 QAGITTAHQTYVYFAALDVTAKDKSDIITLFRNWTSLTQMLTSGKKMsaeqrnqylPPQDTGESADLS--PSNLTVTFGF 143
Cdd:pfam04261   1 QAGILTPHQAAAIFLAFDVTAGDKAALEALFRKWTARVRRLTAGGRA---------PPLDTGEAGGARfpDSRLTVTVGF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   144 GPGFFekdgkDRFGLKSKKPKHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCEVRFVNKGFL 223
Cdd:pfam04261  72 GSSLW-----DRFGLGSKRPKELKPFPEFPNDNLDAPSTDGDLLIHICADRPDVAFHAARNIMRAFGDAVEVRWEIHGFR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   224 SggkngETPRNLFGFKDGTGNQSTKDDTLMNsiVWIQsGEPDWMTGGTYMAFRKIKMFLEVWDRSSLKDQEDTFGRRKSS 303
Cdd:pfam04261 147 Y-----ETPRNLLGFVDGTENPKGEEAKRAV--VWIK-DGPPWFAGGSYVVVQRIRHNLEAWDRLSLKEQEDVIGRRKES 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   304 GAPFGQKKetdpvklnQIPSNSHVSLAKST----GKQILRRAFSYTEgldpkTGYMDAGLLFISFQKNPDNQFIPMLKAL 379
Cdd:pfam04261 219 GAELGGDK--------VKPADSHVRLANPKengkGLKILRRSLPYGD-----VGQGDHGLLFIAYQRTLHNGEQMLQNML 285
                         330       340       350
                  ....*....|....*....|....*....|
gi 16080877   380 S----AKDALNEYTQTIGSALYACPGGCKK 405
Cdd:pfam04261 286 GgtdgKTDALLEFITAVTGGYFFAPSGVKL 315
EfeB COG2837
Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism];
65-411 2.59e-125

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


Pssm-ID: 442085  Cd Length: 334  Bit Score: 365.75  E-value: 2.59e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877  65 HQAGITTAHQTYVYFAALDVT-AKDKSDIITLFRNWTSLTQMLTSGKkmsaeqrnqylppqdtgESADLSPSNLTVTFGF 143
Cdd:COG2837   8 IQAGILTPPQAHAIFLAFDLKdGADRAALRALLRRLTALAARLTSGA-----------------PALRLPPAGLTVTVGF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877 144 GPGFFekdgkDRFGLKsKKPKHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCEVRFVNKGFL 223
Cdd:COG2837  71 GPSLW-----DRLGLA-PRPAELAPFPEFPGDGLDAPATGGDLLLQICADDPDVLFHAARQLLRALRGAATVRWEQDGFR 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877 224 SGgkngETPRNLFGFKDGTGNQSTKDDtlMNSIVWIQSGEPDWMTGGTYMAFRKIKMFLEVWDRSSLKDQEDTFGRRKSS 303
Cdd:COG2837 145 YF----PTGRNLFGFVDGTENPKGEDE--ADEVVLVGDEDPAWFAGGSYVVVRRIRHDLEAWDRLSLEEQEKVIGRTKDD 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877 304 GAPFGQKKETDPVKLNQ----IPSNSHVSLA--KSTGK--QILRRAFSYTEGLDPkTGYMDAGLLFISFQKNPDNQFIPM 375
Cdd:COG2837 219 GAPLDGGPEFDDPDFAAdagvIPADSHVRRAnpRDDGNelRILRRGMPYGDGLDP-AGELDAGLLFIAYQADPARQFEML 297
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 16080877 376 LKALS-----AKDALNEYTQTIGSALYACPGgckkGEYIAQ 411
Cdd:COG2837 298 QRMLGgdpdgNYDRLLDFTTPVGGAYFFVPS----GDFLGQ 334
Dyp_perox_fam TIGR01413
Dyp-type peroxidase family; A defined member of this superfamily is Dyp, a dye-decolorizing ...
66-405 9.05e-119

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: 347.81  E-value: 9.05e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877    66 QAGITTAHQTYVYFAALDVTAkDKSDIITLFRNWTSLTQMLTSGKKMSAeqrnqylppqdtgesadlsPSNLTVTFGFGP 145
Cdd:TIGR01413   1 QPGILTPHQAAAIFLAFDVTA-DRAALEALLRALTALADLLTAGGAAGP-------------------PSRLTVTVGFGS 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   146 GFFekdgkDRFGLKSKKPKHLAALPAMPNDNLDEKQGGGDICIQVCADDEQVAFHALRNLLNQAVGTCEVRFVNKGFLSG 225
Cdd:TIGR01413  61 SLW-----DRLGLADKRPKELKDFPELGGDSLDAPSTGGDLLFHIRADDPDVVFHAARALLRRFGDAVTVRDEVHGFRYP 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   226 GKngETPRNLFGFKDGTGNQSTKDdtLMNSIVWIQSgEPDWMTGGTYMAFRKIKMFLEVWDRSSLKDQEDTFGRRKSSGA 305
Cdd:TIGR01413 136 GA--ETGRDLLGFVDGTENPKGPE--ALEAVLVIGE-DPAWAAGGSYVVVQRIQHDLEEWDRLPLAEQEDVIGRRKSSGA 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080877   306 PFGQKketdpvklNQIPSNSHVSLAK----STGKQILRRAFSYTEGLDPKTGymDAGLLFISFQKNPDNQFIPMLKAL-- 379
Cdd:TIGR01413 211 ELDGK--------ERAPADSHVRLTNpredGKGLKILRRGLPYGDGSDDTGQ--DAGLLFIAYQRSLENGEVQLQRMLgg 280
                         330       340
                  ....*....|....*....|....*...
gi 16080877   380 --SAKDALNEYTQTIGSALYACPGGCKK 405
Cdd:TIGR01413 281 tdGATDRLLEFIRPVGGGYFFAPSGVAL 308
TAT_signal pfam10518
TAT (twin-arginine translocation) pathway signal sequence;
10-35 1.56e-04

TAT (twin-arginine translocation) pathway signal sequence;


Pssm-ID: 463131 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.56e-04
                          10        20
                  ....*....|....*....|....*.
gi 16080877    10 QIHRRDILKWGAMAGAAVAIGASGLG 35
Cdd:pfam10518   1 KLSRRDFLKGSAAAAAAAALGGCAAA 26
 
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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