|
Name |
Accession |
Description |
Interval |
E-value |
| BluB |
TIGR02476 |
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ... |
6-208 |
3.78e-79 |
|
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in cobalamin biosynthesis, is EC 1.16.8.1 (cob(II)yrinic acid a,c-diamide reductase) is now contradicted by newer work ascribing a role in 5,6-dimethylbenzimidazole (DMB) biosynthesis. The BluB protein is related to the nitroreductase family (pfam0881). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 162875 Cd Length: 205 Bit Score: 235.41 E-value: 3.78e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 6 FSPEERAAVYRAIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMQAQVEEERVRTAEAL 85
Cdd:TIGR02476 1 FSDAERAAVYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQAAAAIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 86 -GERTDEFMKLKVEGINDCAEVLVAALMEGR-EQHIFGRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLFDPEALA 163
Cdd:TIGR02476 81 dGERASQYHRLKLEGIREAPVQLAVFCDDARgEGHGLGRHTMPEMLRYSVACAIQNLWLAARAEGLGVGWVSILDPDAVR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 639490374 164 ELLGMPDGAKPLAIICLGPVKEFYPAPMLVMEGWAQARPLHELLY 208
Cdd:TIGR02476 161 RLLGVPEGWRLVAYLCLGWPDAFYDEPELERAGWQERRPLEWRRY 205
|
|
| BluB |
cd02145 |
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ... |
15-206 |
2.88e-71 |
|
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5,6-dimethylbenzimidazole (DMB), a component of vitamin B12; is is a subfamily of the nitroreductase family; nitroreductases typically reduce their substrates by using NAD(P)H as electron donor and often use FMN as a cofactor.
Pssm-ID: 380321 Cd Length: 196 Bit Score: 215.30 E-value: 2.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 15 YRAIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMQAQVEEERVRTAEAL-GERTDEFM 93
Cdd:cd02145 1 YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEMYtGERAAQYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 94 KLKVEGINDCAEVLVAALMEGREQ-HIFGRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLFDPEALAELLGMPDGA 172
Cdd:cd02145 81 TLKLEGIEEAPLQLAVFCDRARAGgHGLGRTTMPEMDLYSSVCAVQNLWLAARAEGLGVGWVSILDPDEVKRLLGIPEHW 160
|
170 180 190
....*....|....*....|....*....|....
gi 639490374 173 KPLAIICLGPVKEFYPAPMLVMEGWAQARPLHEL 206
Cdd:cd02145 161 EPVAYLCIGYPEFFYDEPELEQAGWEQRRPLEWV 194
|
|
| NfnB |
COG0778 |
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ... |
14-190 |
5.46e-41 |
|
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 440541 [Multi-domain] Cd Length: 163 Bit Score: 136.91 E-value: 5.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 14 VYRAIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMqaqveeervrtAEALGERTDEFM 93
Cdd:COG0778 1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERL-----------AEALAEANQEWV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 94 KlkveginDCAEVLVAALMEGReqhifGRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLFDPEALAELLGMPDGAK 173
Cdd:COG0778 70 A-------DAPVLIVVCADPDR-----SEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEE 137
|
170
....*....|....*...
gi 639490374 174 PLAIICLG-PVKEFYPAP 190
Cdd:COG0778 138 PVALLALGyPAEELNPRP 155
|
|
| Nitroreductase |
pfam00881 |
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ... |
18-181 |
8.68e-31 |
|
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.
Pssm-ID: 425926 [Multi-domain] Cd Length: 168 Bit Score: 110.94 E-value: 8.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 18 IAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMQA----QVEEERVRTAEALGERTDEFM 93
Cdd:pfam00881 1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEaaleLLLVEPAAALLLLLRRDANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 94 KLKVEGINDCAEVLVAALMEGReQHIFGRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLFDPEALAELLGMPDGAK 173
Cdd:pfam00881 81 LLLQDFLRGAPVLIVITASLST-YLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDER 159
|
....*...
gi 639490374 174 PLAIICLG 181
Cdd:pfam00881 160 LVGLIAVG 167
|
|
| PRK13294 |
PRK13294 |
F420-0--gamma-glutamyl ligase; Provisional |
2-189 |
4.35e-13 |
|
F420-0--gamma-glutamyl ligase; Provisional
Pssm-ID: 183957 [Multi-domain] Cd Length: 448 Bit Score: 67.35 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 2 TEQAFSPEERAAVYRaiaeRRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMQaqveeERVRT 81
Cdd:PRK13294 245 TAEALELGRREAVLL----RRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVRTRLL-----DAMRD 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 82 AEALGERTDEFMKLKVEG-------INDCAEVLVAAL-MEGREQHIFGRRTLPEMDM--ASLSCAIQNLWLASRAEGLGM 151
Cdd:PRK13294 316 AWRADLRADGLSEESIARrvrrgdiLYDAPELVVPFLvPDGAHSYPDARRTAAERTMftVAVGAAVQNLLVALAVEGLGS 395
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 639490374 152 GWVS--LFDPEALAELLGMPDGAKPLAIICLGpvkefYPA 189
Cdd:PRK13294 396 CWIGstIFAADVVRAVLDLPADWEPLGAVAIG-----HPA 430
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BluB |
TIGR02476 |
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ... |
6-208 |
3.78e-79 |
|
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in cobalamin biosynthesis, is EC 1.16.8.1 (cob(II)yrinic acid a,c-diamide reductase) is now contradicted by newer work ascribing a role in 5,6-dimethylbenzimidazole (DMB) biosynthesis. The BluB protein is related to the nitroreductase family (pfam0881). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 162875 Cd Length: 205 Bit Score: 235.41 E-value: 3.78e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 6 FSPEERAAVYRAIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMQAQVEEERVRTAEAL 85
Cdd:TIGR02476 1 FSDAERAAVYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQAAAAIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 86 -GERTDEFMKLKVEGINDCAEVLVAALMEGR-EQHIFGRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLFDPEALA 163
Cdd:TIGR02476 81 dGERASQYHRLKLEGIREAPVQLAVFCDDARgEGHGLGRHTMPEMLRYSVACAIQNLWLAARAEGLGVGWVSILDPDAVR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 639490374 164 ELLGMPDGAKPLAIICLGPVKEFYPAPMLVMEGWAQARPLHELLY 208
Cdd:TIGR02476 161 RLLGVPEGWRLVAYLCLGWPDAFYDEPELERAGWQERRPLEWRRY 205
|
|
| BluB |
cd02145 |
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ... |
15-206 |
2.88e-71 |
|
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5,6-dimethylbenzimidazole (DMB), a component of vitamin B12; is is a subfamily of the nitroreductase family; nitroreductases typically reduce their substrates by using NAD(P)H as electron donor and often use FMN as a cofactor.
Pssm-ID: 380321 Cd Length: 196 Bit Score: 215.30 E-value: 2.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 15 YRAIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMQAQVEEERVRTAEAL-GERTDEFM 93
Cdd:cd02145 1 YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEMYtGERAAQYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 94 KLKVEGINDCAEVLVAALMEGREQ-HIFGRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLFDPEALAELLGMPDGA 172
Cdd:cd02145 81 TLKLEGIEEAPLQLAVFCDRARAGgHGLGRTTMPEMDLYSSVCAVQNLWLAARAEGLGVGWVSILDPDEVKRLLGIPEHW 160
|
170 180 190
....*....|....*....|....*....|....
gi 639490374 173 KPLAIICLGPVKEFYPAPMLVMEGWAQARPLHEL 206
Cdd:cd02145 161 EPVAYLCIGYPEFFYDEPELEQAGWEQRRPLEWV 194
|
|
| NfnB |
COG0778 |
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ... |
14-190 |
5.46e-41 |
|
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 440541 [Multi-domain] Cd Length: 163 Bit Score: 136.91 E-value: 5.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 14 VYRAIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMqaqveeervrtAEALGERTDEFM 93
Cdd:COG0778 1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERL-----------AEALAEANQEWV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 94 KlkveginDCAEVLVAALMEGReqhifGRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLFDPEALAELLGMPDGAK 173
Cdd:COG0778 70 A-------DAPVLIVVCADPDR-----SEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEE 137
|
170
....*....|....*...
gi 639490374 174 PLAIICLG-PVKEFYPAP 190
Cdd:COG0778 138 PVALLALGyPAEELNPRP 155
|
|
| Nitroreductase |
pfam00881 |
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ... |
18-181 |
8.68e-31 |
|
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.
Pssm-ID: 425926 [Multi-domain] Cd Length: 168 Bit Score: 110.94 E-value: 8.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 18 IAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMQA----QVEEERVRTAEALGERTDEFM 93
Cdd:pfam00881 1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEaaleLLLVEPAAALLLLLRRDANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 94 KLKVEGINDCAEVLVAALMEGReQHIFGRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLFDPEALAELLGMPDGAK 173
Cdd:pfam00881 81 LLLQDFLRGAPVLIVITASLST-YLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDER 159
|
....*...
gi 639490374 174 PLAIICLG 181
Cdd:pfam00881 160 LVGLIAVG 167
|
|
| Nitro_FMN_reductase |
cd02062 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
18-181 |
8.80e-24 |
|
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.
Pssm-ID: 380311 [Multi-domain] Cd Length: 139 Bit Score: 91.97 E-value: 8.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 18 IAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPllrgrmqaqveeERVRTAEALGERTDEFMKlkv 97
Cdd:cd02062 1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDR------------EKKEKLAKLAAPNQKFIA--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 98 egindCAEVLVAALMEgreqhifgRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLFD--PEALAELLGMPDGAKPL 175
Cdd:cd02062 66 -----GAPVVIVVVAD--------PDKSRPWALEDAGAAAQNLLLAAAALGLGSCWIGGFDfrEDKVRELLGIPENLRPV 132
|
....*.
gi 639490374 176 AIICLG 181
Cdd:cd02062 133 ALIAIG 138
|
|
| YdjA-like |
cd02135 |
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ... |
17-181 |
5.00e-23 |
|
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to nitroreductase YdjA from Escherichia coli. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer. Members of this family are also called NADH dehydrogenase, oxygen-insensitive NAD(P)H nitrogenase or dihydropteridine reductase.
Pssm-ID: 380312 [Multi-domain] Cd Length: 162 Bit Score: 90.74 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 17 AIAERRDMRHFI-GGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDP----LLRGRMQAQVEEERVRTAEALGERTDE 91
Cdd:cd02135 3 LIKTRRSIRKFKlTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGEgrerLAELLAAAAAARAPGADPEKLEKAREK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 92 FMKlkvegindcAEVLVAALMEGREQHifgrrTLPEM-DMASLSCAIQNLWLASRAEGLGMGWVS---LFDPEaLAELLG 167
Cdd:cd02135 83 ALR---------APVVIAVVAKPDEDP-----KVPEWeQYAAVGAAVQNLLLAAHALGLGAVWRTgpvTYDPA-VREALG 147
|
170
....*....|....
gi 639490374 168 MPDGAKPLAIICLG 181
Cdd:cd02135 148 LPEDERIVGFLYLG 161
|
|
| nitroreductase |
cd02139 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
14-189 |
2.40e-21 |
|
nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.
Pssm-ID: 380316 [Multi-domain] Cd Length: 165 Bit Score: 86.37 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 14 VYRAIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMQaqveeERVRTAEALGErtdefm 93
Cdd:cd02139 1 VYEAIKKRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLA-----EAANGQKFIAE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 94 klkvegindcAEVLVAALMEGREqhiFGRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLFDPEALAELLGMPDGAK 173
Cdd:cd02139 70 ----------APVVIVACADPSE---SGMGCGKPYYLVDVAIAMEHLVLAATEEGLGTCWIGAFDEDKVKEILGIPEEYR 136
|
170
....*....|....*.
gi 639490374 174 PLAIICLGpvkefYPA 189
Cdd:cd02139 137 VVALTPLG-----YPA 147
|
|
| nitroreductase |
cd20608 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
17-181 |
2.01e-19 |
|
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.
Pssm-ID: 380329 [Multi-domain] Cd Length: 145 Bit Score: 80.84 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 17 AIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPllrgrmqaqveeervRTAEALGERTDEFMKLK 96
Cdd:cd20608 3 AIKTRRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDK---------------ETLSELAKKESPSNGWL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 97 VEG---INDCAEVLVAALMEGREQHIFgrrtlpemdmaSLSCAIQNLWLASRAEGLGMGWVSLFDPEALAELLGMPDGAK 173
Cdd:cd20608 68 KDApviIVVCADPKDSGWLNGQNYYLV-----------DAAIAMQNLMLAATDLGLGTCWIGAFDEKKVKEILGIPENIR 136
|
....*...
gi 639490374 174 PLAIICLG 181
Cdd:cd20608 137 VVALTPLG 144
|
|
| nitroreductase |
cd20610 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
18-181 |
2.18e-15 |
|
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.
Pssm-ID: 380331 [Multi-domain] Cd Length: 167 Bit Score: 70.77 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 18 IAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDpllrGRMQAQVEEERVRTAEALGERTDEFMKLKV 97
Cdd:cd20610 1 IKKRRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKG----GEKIEKIGISIKKKNEEIARLLEKVFAEKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 98 EGI---------NDCAEVLVAALMEgREQHIFGRRTlpemDMASLSCAIQNLWLASRAEGLGMGWVS--LFDPEALAELL 166
Cdd:cd20610 77 IRFrkfrrfftlFGGAPVLVVVYTE-PYKPPEERKP----DLQSVSAAIQNLLLAAHALGLGTCWMTgpLYAEDEIEEIL 151
|
170
....*....|....*
gi 639490374 167 GMPDGAKPLAIICLG 181
Cdd:cd20610 152 EIPDDKELVAVTPLG 166
|
|
| PnbA_NfnB-like |
cd02136 |
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ... |
17-190 |
4.00e-15 |
|
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as a cofactor and catalyze reduction of a variety of nitroaromatic compounds, including nitrofurans, nitrobenzens, nitrophenol, nitrobenzoate and quinones by using either NADH or NADPH as a source of reducing equivalents in an obligatory two-election transfer mechanism. The enzyme is typically a homodimer. Mycobacterium smegmatis nitroreductase NfnB plays a role in resistance to benzothiazinone.
Pssm-ID: 380313 [Multi-domain] Cd Length: 152 Bit Score: 69.54 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 17 AIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLrgrmqaqveeERVRTAealgertdEFMklk 96
Cdd:cd02136 1 AIKSRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTGKAR----------ERLKKA--------FFG--- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 97 vegindcAEVLVAalmegreqhIFGRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLF--DPEALAELLGMPDGAKP 174
Cdd:cd02136 60 -------APVALF---------LTMDKVLGPWSWFDLGAFLQNLMLAAHALGLGTCPQGALagYPDVVRKELGIPDDEEL 123
|
170
....*....|....*.
gi 639490374 175 LAIICLGpvkefYPAP 190
Cdd:cd02136 124 VCGIALG-----YPDP 134
|
|
| nitroreductase |
cd20609 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
18-181 |
7.91e-15 |
|
nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers.
Pssm-ID: 380330 [Multi-domain] Cd Length: 145 Bit Score: 68.57 E-value: 7.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 18 IAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIrisdpllrgrmqaqVeeerVRTAEALgertdefmklkv 97
Cdd:cd20609 6 AKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRIL--------------V----VRSEEAL------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 98 EGINDCAE--------VLVAALMEGREQHIFGRRTLPEMDmasLSCAIQNLWLASRAEGLGMGWVSLFDPEALAELLGMP 169
Cdd:cd20609 56 EKLAKATPrffgaplvIVVCYDKDESWKRPYDGKDSGDID---AAIVATHMMLAATELGLGTCWVGNFDPEKVREAFNLP 132
|
170
....*....|..
gi 639490374 170 DGAKPLAIICLG 181
Cdd:cd20609 133 ENLEPVAILPLG 144
|
|
| nitroreductase |
cd02150 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
18-189 |
2.21e-14 |
|
nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers.
Pssm-ID: 380325 [Multi-domain] Cd Length: 156 Bit Score: 67.63 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 18 IAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMqaqveeervrtAEALgertdEFMKLkv 97
Cdd:cd02150 1 ILTRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKI-----------AEAH-----PYGKM-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 98 egindCAEVLVAALMEGREQhifgRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLF----DPEALAELLGMPDGAK 173
Cdd:cd02150 63 -----LKEAPLAIVVCGDPS----KEKAPGYWVQDCSAATENILLAAHALGLGAVWLGVYpfeeRVKAIREILNIPENII 133
|
170
....*....|....*.
gi 639490374 174 PLAIICLGpvkefYPA 189
Cdd:cd02150 134 PFCVIALG-----YPA 144
|
|
| NfsA-like |
cd02146 |
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ... |
21-212 |
2.33e-13 |
|
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin reductase and oxygen-insensitive nitroreductase. These enzymes are homodimeric flavoproteins that contain one FMN per monomer as a cofactor. Flavin reductase catalyzes the reduction of flavin by using NADPH as an electron donor. Oxygen-insensitive nitroreductase, such as NfsA protein in Escherichia coli, catalyzes reduction of nitrocompounds using NADPH as electron donor.
Pssm-ID: 380322 [Multi-domain] Cd Length: 229 Bit Score: 66.49 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 21 RRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGR------MQAQVEEERV---------RTAEAL 85
Cdd:cd02146 8 HRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKlaelagNQPYVAQAPVflvfcadlyRHQKIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 86 GERtdefmKLKVEGINDCAEVLVAAlmegreqhifgrrtlpeMDmASLscAIQNLWLAsrAEGLGMGWVSL----FDPEA 161
Cdd:cd02146 88 EEA-----GGKDVGLDYLESFLVGV-----------------VD-AAL--AAQNALVA--AESLGLGIVYIggirNNPEE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 639490374 162 LAELLGMPDGAKPLAIICLGpvkefYPAPMlvmegwAQARP---LHELLYENQW 212
Cdd:cd02146 141 VIELLGLPEYVFPLFGLTVG-----HPDPT------PEVKPrlpLEAVVHEETY 183
|
|
| PRK13294 |
PRK13294 |
F420-0--gamma-glutamyl ligase; Provisional |
2-189 |
4.35e-13 |
|
F420-0--gamma-glutamyl ligase; Provisional
Pssm-ID: 183957 [Multi-domain] Cd Length: 448 Bit Score: 67.35 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 2 TEQAFSPEERAAVYRaiaeRRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMQaqveeERVRT 81
Cdd:PRK13294 245 TAEALELGRREAVLL----RRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVRTRLL-----DAMRD 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 82 AEALGERTDEFMKLKVEG-------INDCAEVLVAAL-MEGREQHIFGRRTLPEMDM--ASLSCAIQNLWLASRAEGLGM 151
Cdd:PRK13294 316 AWRADLRADGLSEESIARrvrrgdiLYDAPELVVPFLvPDGAHSYPDARRTAAERTMftVAVGAAVQNLLVALAVEGLGS 395
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 639490374 152 GWVS--LFDPEALAELLGMPDGAKPLAIICLGpvkefYPA 189
Cdd:PRK13294 396 CWIGstIFAADVVRAVLDLPADWEPLGAVAIG-----HPA 430
|
|
| MhqN-like |
cd02137 |
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ... |
17-181 |
2.01e-12 |
|
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily of the nitroreductase family containing uncharacterized proteins; includes nitroreductases MhqN, YodC, YdgI, DrgA. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.
Pssm-ID: 380314 [Multi-domain] Cd Length: 147 Bit Score: 62.26 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 17 AIAERRDMRHFIGGAVAP-ELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRM------QAQVEeervrTAEALgert 89
Cdd:cd02137 3 VIKSRRSVRNFDPDHKIPkEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLaeaaynQPQVT-----TASAV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 90 defmklkvegindcaeVLVAALMegreqhifgrrtlpemdmaSLSCAIQNLWLASRAEGLGMGWVSLFDPEALAELLGMP 169
Cdd:cd02137 74 ----------------ILVLGDL-------------------NAGLAAMNLMLAAKAKGYDTCPMGGFDKEKVAELLNLP 118
|
170
....*....|..
gi 639490374 170 DGAKPLAIICLG 181
Cdd:cd02137 119 DRYVPVLLIAIG 130
|
|
| nitroreductase |
cd03370 |
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ... |
17-188 |
5.02e-11 |
|
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus thermophilus NADH oxidase and other, uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.
Pssm-ID: 380327 [Multi-domain] Cd Length: 191 Bit Score: 59.25 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 17 AIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRM------QAQVEEERVrtaeALGERTD 90
Cdd:cd03370 4 AIESRRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLqaaaygQAQVTSAPA----VIVIYSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 91 efMKlkvEGINDCAEVLVAALMEGREQHIFG--RRTLPEMDMASLS--------CAIQNLWLASRAEGLGMGWVSLFDPE 160
Cdd:cd03370 80 --ME---DALANLEETIHPGLSEERRQREAAglRGAFGKMSVEQRGqwglaqanIALGFLLLAAQSLGYDTSPMLGFDPE 154
|
170 180
....*....|....*....|....*....
gi 639490374 161 ALAELLGMPDGAKPLAIICLG-PVKEFYP 188
Cdd:cd03370 155 KVKALLGLPEHVTIAALVALGkPAEEGYP 183
|
|
| TdsD-like |
cd02138 |
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ... |
17-181 |
3.23e-10 |
|
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to Burkholderia pseudomallei TdsD, may be involved in the processing of organosulfur compounds. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.
Pssm-ID: 380315 [Multi-domain] Cd Length: 174 Bit Score: 56.78 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 17 AIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIrisdpllrgrmqaqveeervrtaeaLGERTDEFMKLK 96
Cdd:cd02138 1 LIAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFV-------------------------VARRDTEAFEKL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 97 VEGINDC-------AEVLVAAL-MEGREQHIFGRRTlpemdmASLSC--AIQNLWLASRAEGL---GMGwvsLFDPEALA 163
Cdd:cd02138 56 LDLLAEGnqswaknAPVLIVVLaKTEFDHNGKPNRY------ALFDTgaAVANLALQATALGLvvhQMA---GFDPEKAK 126
|
170
....*....|....*...
gi 639490374 164 ELLGMPDGAKPLAIICLG 181
Cdd:cd02138 127 EALGIPDEYEPITMIAIG 144
|
|
| PRK10765 |
PRK10765 |
oxygen-insensitive NADPH nitroreductase; |
18-203 |
4.67e-10 |
|
oxygen-insensitive NADPH nitroreductase;
Pssm-ID: 182710 Cd Length: 240 Bit Score: 57.29 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 18 IAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRM------QAQVEEervrtaealgertde 91
Cdd:PRK10765 8 ILSHRSIRHFTDEPISEAQREAIINAARAASSSSFLQCSSIIRITDKALREALveltggQKYVAQ--------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 92 fmklkvegindCAEVLVAALMEGREQHIFgrrtlPE--MDMASLS------CAI--QNLWLAsrAEGLGMGWVSL----F 157
Cdd:PRK10765 73 -----------AAEFWVFCADFNRHLQIC-----PDaqLGLAEQLligavdTAImaQNALLA--AESLGLGGVYIgglrN 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 639490374 158 DPEALAELLGMPDGAKPLAIICLG------PVKEFYPAPMLVMEGwaQARPL 203
Cdd:PRK10765 135 NIEAVTELLKLPQHVLPLFGLCLGwpaqnpDLKPRLPASLLVHEN--QYQPL 184
|
|
| iodotyrosine_dehalogenase |
cd02144 |
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ... |
14-190 |
1.11e-09 |
|
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the 3, 5 positions of L-tyosine in thyroid, liver and kidney, using NADPH as electron donor. This enzyme is a homolog of the nitroreductase family. These enzymes are usually homodimers.
Pssm-ID: 380320 Cd Length: 192 Bit Score: 55.62 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 14 VYRAIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPLLRGRMQAQVE-EERVRTAEALGE--RTD 90
Cdd:cd02144 1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAAEeEEKEFYEKRMGEewVWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 91 efmkLKVEGIN------DCAEVLVAalmegreqhIFGRRTLPEMDM-----------ASLSCAIqnLWLASRAEGLgmgw 153
Cdd:cd02144 81 ----LKPLGTNwekpylTEAPYLIV---------VFKQKYGVLPDGkkkkhyyneesVGIAVGI--LLAALHNAGL---- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 639490374 154 VSL----FDPEALAELLGMPDGAKPLAIICLGpvkefYPAP 190
Cdd:cd02144 142 VTLthtpSPMPFLRDLLGRPKNEKPLLLLPVG-----YPAE 177
|
|
| nitroreductase |
cd02151 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
17-189 |
3.05e-09 |
|
nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers..
Pssm-ID: 380326 [Multi-domain] Cd Length: 157 Bit Score: 53.69 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 17 AIAERRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPllrgrmqaqveeervRTAEALGErTDEFMKLK 96
Cdd:cd02151 2 LLKKRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDK---------------ETLKKLSE-CKPHGSAF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 97 VEGindcAEVLVAalmegreqhIFGRRTLPEMDMASLSCAIQNLWLASRAEGLGMGWVSLFD---------PEALAELLG 167
Cdd:cd02151 66 LKG----APAAIV---------VLADTEKSDTWIEDASIAATYIQLAAESLGLGSCWIQIRNretqdgktaEEYVRELLG 132
|
170 180
....*....|....*....|..
gi 639490374 168 MPDGAKPLAIICLGpvkefYPA 189
Cdd:cd02151 133 IPENYRVLCIIALG-----YPD 149
|
|
| FbiB_C-like |
cd20607 |
nitroreductase family domain similar to the C-terminal domain of F420:gamma-glutamyl ligase ... |
54-189 |
5.83e-09 |
|
nitroreductase family domain similar to the C-terminal domain of F420:gamma-glutamyl ligase FbiB; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Mycobacterium tuberculosis FbiB, is a two-domain protein and produces F420 with predominantly 5 to 7 L-glutamate residues in the poly-gamma-glutamate tail, its C-terminal domain is homologous to FMN-dependent nitroreductases.
Pssm-ID: 380328 [Multi-domain] Cd Length: 155 Bit Score: 53.24 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 54 QPWRFIRISDPLLRGRMQAQVEEERVR-------TAEALGERTDEFMKLKveginDCAEVLVAALM-EGREQHIFGRRTL 125
Cdd:cd20607 5 RPWRFVWLQDPAIRKELLDRMADRWEAdltgdglTPEAIARRVSRGQILY-----DAPEVVIPFLVpDGAHTYPDARRTD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639490374 126 PEMDMASLS--CAIQNLWLASRAEGLGMGWVS--LFDPEALAELLGMPDGAKPLAIICLGpvkefYPA 189
Cdd:cd20607 80 AEHTMFTVAvgAAVQALLVALAVRGLGSCWIGstIFAPDVVRDELDLPDDWEPLGAIAIG-----YPL 142
|
|
| nitroreductase_FeS-like |
cd02143 |
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ... |
21-189 |
1.41e-07 |
|
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family utilize FMN as a cofactor. This family may be involved in the reduction of flavin or nitroaromatic compounds via an obligatory two-electron transfer. Nitroreductase is homodimer. Each subunit contains one FMN molecule.
Pssm-ID: 380319 [Multi-domain] Cd Length: 187 Bit Score: 49.78 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 21 RRDMRHFIGGAVAPELLARVLEAAHQAPSVGLMQPWRFIRISDPllrgrmqaqveeERVRtaeALGERTDEFMKLKVEGI 100
Cdd:cd02143 5 RRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDP------------EKVR---RLAELVIDWMRELIKED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639490374 101 NDCA-----EVLVAALMEGREqHIFgrRTLP---------EMDMASLSCAI--QNLWLASRAEGLGMGWVSLF------D 158
Cdd:cd02143 70 PELAgklflDGIVAAWEKGID-VIL--RGAPhlvvahapkDAPTPPVDCAIalTYLELAAPSLGLGTCWAGFFtaaannY 146
|
170 180 190
....*....|....*....|....*....|.
gi 639490374 159 PEaLAELLGMPDGAKPLAIICLGpvkefYPA 189
Cdd:cd02143 147 PP-LREALGLPEGHKVGGAMMLG-----YPK 171
|
|
| |
