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Conserved domains on  [gi|1277238141|gb|PIS31181|]
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MAG: nitroreductase [Candidatus Marinimicrobia bacterium CG08_land_8_20_14_0_20_45_22]

Protein Classification

NfnB family protein( domain architecture ID 10002498)

NfnB family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 2-154 7.72e-42

Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation


:

Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 138.06  E-value: 7.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   2 IELIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIFPLLQWAGyiqptgNPKPGKMPTA 81
Cdd:COG0778     2 LELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEAN------QEWVADAPVL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238141  82 YFVIAV---DQNVTDSSAEKDVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPERLVIDSIVACGYPDETP 154
Cdd:COG0778    76 IVVCADpdrSEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEEPVALLALGYPAEEL 151
 
Name Accession Description Interval E-value
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 2-154 7.72e-42

Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 138.06  E-value: 7.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   2 IELIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIFPLLQWAGyiqptgNPKPGKMPTA 81
Cdd:COG0778     2 LELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEAN------QEWVADAPVL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238141  82 YFVIAV---DQNVTDSSAEKDVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPERLVIDSIVACGYPDETP 154
Cdd:COG0778    76 IVVCADpdrSEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEEPVALLALGYPAEEL 151
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 5-149 2.45e-34

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: 118.17  E-value: 2.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   5 IRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIFPLLQWagyiqptgNPKPGKMPTAYFV 84
Cdd:cd02062     1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAKLAAP--------NQKFIAGAPVVIV 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238141  85 IAVDQNVTDSSAEKDVGAAIENFILSAWSLGIGTCWIVSIDR--EKLRQLLQIPERLVIDSIVACGY 149
Cdd:cd02062    73 VVADPDKSRPWALEDAGAAAQNLLLAAAALGLGSCWIGGFDFreDKVRELLGIPENLRPVALIAIGY 139
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 5-149 5.78e-32

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: 113.26  E-value: 5.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   5 IRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIFPLL--------QWAGYIQPT------ 70
Cdd:pfam00881   1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAAlelllvepAAALLLLLRrdanlk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  71 --GNPKPGKMPTAYFVIAVDQNVTDSSAEK-------DVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPERLVI 141
Cdd:pfam00881  81 llLQDFLRGAPVLIVITASLSTYLRKAAERayreallDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDERL 160


                  ....*...
gi 1277238141 142 DSIVACGY 149
Cdd:pfam00881 161 VGLIAVGY 168
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
 100-154 5.26e-05

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 42.69  E-value: 5.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238141 100 VGAAIENFILSAWSLGIGTCWIVS--IDREKLRQLLQIPERLVIDSIVACGYPDETP 154
Cdd:PRK13294  377 VGAAVQNLLVALAVEGLGSCWIGStiFAADVVRAVLDLPADWEPLGAVAIGHPAEPP 433
antibiot_sagB TIGR03605
SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation ...
 98-139 9.86e-03

SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation of streptolysin S from a ribosomally produced precursor polypeptide. Chemically similar systems operate on highly diverse sets of bacteriocin precursors in numerous other bacteria. This model describes a domain within SgaB and homologous regions from other proteins, many of which appear to be involved in biosynthesis of secondary metabolites. While some substrates may be intermediates in non-ribosomal peptide syntheses, others are involved in heterocycle-containing bacteriocin biosynthesis, and can be found near SgaC-like (see TIGR03603, cyclodehydratase) and SgaD-like (see TIGR03604, "docking") proteins. Members of this domain family are heterogeneous in length, as many have a partial second copy of the domain represented here. The incomplete second domain scores below the cutoffs to this model in most cases.


Pssm-ID: 188352  Cd Length: 173  Bit Score: 35.36  E-value: 9.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1277238141  98 KDVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPERL 139
Cdd:TIGR03605 121 LDVGIIIQNFYLVATALGLGSCAIGGFDDDYIAELLGLDGIE 162
 
Name Accession Description Interval E-value
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 2-154 7.72e-42

Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 138.06  E-value: 7.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   2 IELIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIFPLLQWAGyiqptgNPKPGKMPTA 81
Cdd:COG0778     2 LELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEAN------QEWVADAPVL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238141  82 YFVIAV---DQNVTDSSAEKDVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPERLVIDSIVACGYPDETP 154
Cdd:COG0778    76 IVVCADpdrSEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEEPVALLALGYPAEEL 151
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 5-149 2.45e-34

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: 118.17  E-value: 2.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   5 IRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIFPLLQWagyiqptgNPKPGKMPTAYFV 84
Cdd:cd02062     1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAKLAAP--------NQKFIAGAPVVIV 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238141  85 IAVDQNVTDSSAEKDVGAAIENFILSAWSLGIGTCWIVSIDR--EKLRQLLQIPERLVIDSIVACGY 149
Cdd:cd02062    73 VVADPDKSRPWALEDAGAAAQNLLLAAAALGLGSCWIGGFDFreDKVRELLGIPENLRPVALIAIGY 139
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 5-149 5.78e-32

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: 113.26  E-value: 5.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   5 IRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIFPLL--------QWAGYIQPT------ 70
Cdd:pfam00881   1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAAlelllvepAAALLLLLRrdanlk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  71 --GNPKPGKMPTAYFVIAVDQNVTDSSAEK-------DVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPERLVI 141
Cdd:pfam00881  81 llLQDFLRGAPVLIVITASLSTYLRKAAERayreallDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDERL 160


                  ....*...
gi 1277238141 142 DSIVACGY 149
Cdd:pfam00881 161 VGLIAVGY 168
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 1-154 2.45e-30

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: 108.71  E-value: 2.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   1 MIELIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRD----RKLVEAIFPllQWAgyiqptgnpkpg 76
Cdd:cd02139     1 VYEAIKKRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDkelkEKLAEAANG--QKF------------ 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  77 kMPTAYFVIAVDQNVTDSSAEK-------DVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPERLVIDSIVACGY 149
Cdd:cd02139    67 -IAEAPVVIVACADPSESGMGCgkpyylvDVAIAMEHLVLAATEEGLGTCWIGAFDEDKVKEILGIPEEYRVVALTPLGY 145


                  ....*
gi 1277238141 150 PDETP 154
Cdd:cd02139   146 PAEEP 150
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 5-154 1.10e-27

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: 101.91  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   5 IRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIfpllqwagyiqPTGNPKPGKMPTAYFV 84
Cdd:cd02150     1 ILTRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKI-----------AEAHPYGKMLKEAPLA 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238141  85 IAVDQNVTDSSA----EKDVGAAIENFILSAWSLGIGTCWIV---SIDREK-LRQLLQIPERLVIDSIVACGYPDETP 154
Cdd:cd02150    70 IVVCGDPSKEKApgywVQDCSAATENILLAAHALGLGAVWLGvypFEERVKaIREILNIPENIIPFCVIALGYPAEEK 147
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
 4-157 2.24e-27

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: 100.74  E-value: 2.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   4 LIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDR---KLVEAIFpllqwagyiqptgnpkpgKMPT 80
Cdd:cd02136     1 AIKSRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTGKareRLKKAFF------------------GAPV 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238141  81 AYFVIAvDQNVTDSSAEkDVGAAIENFILSAWSLGIGTCWIVSI--DREKLRQLLQIPERLVIDSIVACGYPDETPVVE 157
Cdd:cd02136    63 ALFLTM-DKVLGPWSWF-DLGAFLQNLMLAAHALGLGTCPQGALagYPDVVRKELGIPDDEELVCGIALGYPDPDAPVN 139
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 3-152 1.35e-26

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: 98.85  E-value: 1.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   3 ELIRTRRAIRQFD-QTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIFPLLqwagYIQPtgnpkpgKMPTA 81
Cdd:cd02137     2 EVIKSRRSVRNFDpDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAA----YNQP-------QVTTA 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238141  82 YFVIAVdqnVTDssaeKDVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPERLVIDSIVACGYPDE 152
Cdd:cd02137    71 SAVILV---LGD----LNAGLAAMNLMLAAKAKGYDTCPMGGFDKEKVAELLNLPDRYVPVLLIAIGKAAD 134
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 3-149 2.96e-26

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: 97.79  E-value: 2.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   3 ELIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLveaIFPLLQWAGYIQptgnpkpGKMPTAY 82
Cdd:cd20608     2 EAIKTRRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKET---LSELAKKESPSN-------GWLKDAP 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238141  83 FVIAVDQNVTDSSAEK-------DVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPERLVIDSIVACGY 149
Cdd:cd20608    72 VIIVVCADPKDSGWLNgqnyylvDAAIAMQNLMLAATDLGLGTCWIGAFDEKKVKEILGIPENIRVVALTPLGY 145
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 3-154 1.42e-25

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: 96.45  E-value: 1.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   3 ELIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIfpllqwaGYIQPTGNPKPGKMPTAy 82
Cdd:cd02151     1 ELLKKRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKL-------SECKPHGSAFLKGAPAA- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  83 FVIAVDQNVTDSSAEkDVGAAIENFILSAWSLGIGTCWIVSIDR---------EKLRQLLQIPERLVIDSIVACGYPDET 153
Cdd:cd02151    73 IVVLADTEKSDTWIE-DASIAATYIQLAAESLGLGSCWIQIRNRetqdgktaeEYVRELLGIPENYRVLCIIALGYPDEE 151


                  .
gi 1277238141 154 P 154
Cdd:cd02151   152 K 152
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 2-149 8.51e-25

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: 93.99  E-value: 8.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   2 IELIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIfpllqWAGYIQPTGNPkpgkmptA 81
Cdd:cd20609     3 LELAKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKL-----AKATPRFFGAP-------L 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238141  82 YFVIAVDQNVT-------DSSAEKDVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPERLVIDSIVACGY 149
Cdd:cd20609    71 VIVVCYDKDESwkrpydgKDSGDIDAAIVATHMMLAATELGLGTCWVGNFDPEKVREAFNLPENLEPVAILPLGY 145
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
 4-152 1.27e-21

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: 86.44  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   4 LIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLV-RDRKLVEAIFPLL-----QWAgyiqptgnpkpgk 77
Cdd:cd02138     1 LIAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFVVArRDTEAFEKLLDLLaegnqSWA------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  78 mPTAYFVIAVDQNVTDSSAEK-------DVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPERLVIDSIVACGYP 150
Cdd:cd02138    68 -KNAPVLIVVLAKTEFDHNGKpnryalfDTGAAVANLALQATALGLVVHQMAGFDPEKAKEALGIPDEYEPITMIAIGYP 146


                  ..
gi 1277238141 151 DE 152
Cdd:cd02138   147 GD 148
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
 3-153 4.55e-20

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: 83.14  E-value: 4.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   3 ELIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAifplLQWAGYIQPTGNPKPgkmptAY 82
Cdd:cd03370     3 EAIESRRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQ----LQAAAYGQAQVTSAP-----AV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  83 FVIAVD-------------------------QNVTDSSAEKDVGA-----------AIENFILSAWSLGIGTCWIVSIDR 126
Cdd:cd03370    74 IVIYSDmedalanleetihpglseerrqreaAGLRGAFGKMSVEQrgqwglaqaniALGFLLLAAQSLGYDTSPMLGFDP 153

                         170       180
                  ....*....|....*....|....*..
gi 1277238141 127 EKLRQLLQIPERLVIDSIVACGYPDET 153
Cdd:cd03370   154 EKVKALLGLPEHVTIAALVALGKPAEE 180
nitroreductase cd20610
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 5-149 5.33e-20

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: 82.33  E-value: 5.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   5 IRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAI----------FPLLQwagYIQPTGNPK 74
Cdd:cd20610     1 IKKRRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKIgisikkkneeIARLL---EKVFAEKPI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  75 P-----------GKMPTAYFVIAVDQNVT--DSSAEKDVGAAIENFILSAWSLGIGTCWIVS--IDREKLRQLLQIPERL 139
Cdd:cd20610    78 RfrkfrrfftlfGGAPVLVVVYTEPYKPPeeRKPDLQSVSAAIQNLLLAAHALGLGTCWMTGplYAEDEIEEILEIPDDK 157

                         170
                  ....*....|
gi 1277238141 140 VIDSIVACGY 149
Cdd:cd20610   158 ELVAVTPLGY 167
nitroreductase_FeS-like cd02143
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ...
 4-150 2.12e-16

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: 73.28  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   4 LIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIFPL-LQWAGYIQPTGNPKPGKMPTAY 82
Cdd:cd02143     1 LLRSRRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLAELvIDWMRELIKEDPELAGKLFLDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  83 FVIAVDQNVtD-----------SSAEKDVGAAIENFI-------LSAWSLGIGTCW-----IVSIDREKLRQLLQIPErl 139
Cdd:cd02143    81 IVAAWEKGI-DvilrgaphlvvAHAPKDAPTPPVDCAialtyleLAAPSLGLGTCWagfftAAANNYPPLREALGLPE-- 157

                         170
                  ....*....|....*
gi 1277238141 140 viDSIVAC----GYP 150
Cdd:cd02143   158 --GHKVGGammlGYP 170
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 2-149 1.79e-15

nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This domain catalyzes the reduction of flavin, nitrocompound, quinones and azo compounds using NADH or NADPH as an electron donor. The enzyme is a homodimer, and each monomer binds a FMN as co-factor. This family includes FRase I in Vibrio fischeri, wihich reduces FMN into FMNH2 as part of the bioluminescent reaction. The family also includes oxygen-insensitive nitroreductases that use NADH or NADPH as an electron donor in the ping pong bi bi mechanism. This type of nitroreductase can be used in cancer chemotherapy to activate a range of prodrugs.


Pssm-ID: 380324 [Multi-domain]  Cd Length: 156  Bit Score: 69.97  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   2 IELIRTRRAIRQFDQT-EISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIFPLLQWAgyiQPtgnpkpgKMPT 80
Cdd:cd02149     3 LELLNFRYATKKFDPNkKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAAWFN---QP-------QIKD 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238141  81 A-YFVIAVdqNVTDSSAeKDVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPER-LVIDSIVACGY 149
Cdd:cd02149    73 AsHVVVFL--AKKDWSA-KQTYIALGNMLLAAAMLGIDSCPIEGFDPAKLDEILGLDEKgYKISVMVAFGY 140
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
 1-154 2.62e-14

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: 68.42  E-value: 2.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   1 MIELIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIFPLlqwagyiqpTGNPKPGKMPT 80
Cdd:cd02146     1 TIETILNHRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAEL---------AGNQPYVAQAP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  81 AYFVIAVDQNVTDSSAEK-------------------DVGAAIENFILSAWSLGIGTCWIVSI--DREKLRQLLQIPE-- 137
Cdd:cd02146    72 VFLVFCADLYRHQKIAEEaggkdvgldylesflvgvvDAALAAQNALVAAESLGLGIVYIGGIrnNPEEVIELLGLPEyv 151

                         170       180
                  ....*....|....*....|.
gi 1277238141 138 ----RLVIdsivacGYPDETP 154
Cdd:cd02146   152 fplfGLTV------GHPDPTP 166
YdjA-like cd02135
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ...
 2-149 3.89e-14

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: 66.47  E-value: 3.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   2 IELIRTRRAIRQF-DQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRD---RKLVEAIFPLLQWAGyiqPTGNP---- 73
Cdd:cd02135     1 LELIKTRRSIRKFkLTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGegrERLAELLAAAAAARA---PGADPekle 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  74 ----KPGKMPtAYFVIAVDQNVTDSSAEKD----VGAAIENFILSAWSLGIGTCWIV--SIDREKLRQLLQIPERLVIDS 143
Cdd:cd02135    78 kareKALRAP-VVIAVVAKPDEDPKVPEWEqyaaVGAAVQNLLLAAHALGLGAVWRTgpVTYDPAVREALGLPEDERIVG 156


                  ....*.
gi 1277238141 144 IVACGY 149
Cdd:cd02135   157 FLYLGT 162
BluB cd02145
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ...
 3-154 5.39e-14

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: 67.00  E-value: 5.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   3 ELIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRDRKLVEAIFPLLQWAGyiQPTGNPKPGKMPTAY 82
Cdd:cd02145     2 RVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRAN--AEAAEMYTGERAAQY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  83 ------------FVIAVdqnVTDSSAEKDVG---------------AAIENFILSAWSLGIGTCWIVSIDREKLRQLLQI 135
Cdd:cd02145    80 rtlklegieeapLQLAV---FCDRARAGGHGlgrttmpemdlyssvCAVQNLWLAARAEGLGVGWVSILDPDEVKRLLGI 156

                         170
                  ....*....|....*....
gi 1277238141 136 PERLVIDSIVACGYPDETP 154
Cdd:cd02145   157 PEHWEPVAYLCIGYPEFFY 175
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
 1-156 3.47e-10

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: 56.39  E-value: 3.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   1 MIELIRTRRAIRQFDQTEISLDDLLKCAECAGLAPSGENLQPLKFLLVRD-------RKLVEA---------IFPLLQWA 64
Cdd:cd02144     1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDpeikrkiREAAEEeekefyekrMGEEWVWD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  65 gyIQPTG-NPKPGKMPTAYFVIAV---DQNVTDSSAEKD-------VGAAIENFILSAWSLGIGTCWIVSIDREKLRQLL 133
Cdd:cd02144    81 --LKPLGtNWEKPYLTEAPYLIVVfkqKYGVLPDGKKKKhyyneesVGIAVGILLAALHNAGLVTLTHTPSPMPFLRDLL 158

                         170       180
                  ....*....|....*....|....*
gi 1277238141 134 QIP--ERLVIdsIVACGYPDETPVV 156
Cdd:cd02144   159 GRPknEKPLL--LLPVGYPAEDATV 181
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
 100-154 5.26e-05

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 42.69  E-value: 5.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238141 100 VGAAIENFILSAWSLGIGTCWIVS--IDREKLRQLLQIPERLVIDSIVACGYPDETP 154
Cdd:PRK13294  377 VGAAVQNLLVALAVEGLGSCWIGStiFAADVVRAVLDLPADWEPLGAVAIGHPAEPP 433
FbiB_C-like cd20607
nitroreductase family domain similar to the C-terminal domain of F420:gamma-glutamyl ligase ...
 94-154 9.96e-05

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: 40.92  E-value: 9.96e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238141  94 SSAEKD-----VGAAIENFILSAWSLGIGTCWIVS--IDREKLRQLLQIPERLVIDSIVACGYPDETP 154
Cdd:cd20607    78 TDAEHTmftvaVGAAVQALLVALAVRGLGSCWIGStiFAPDVVRDELDLPDDWEPLGAIAIGYPLEPP 145
TM1586_NiRdase pfam14512
Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase ...
 2-155 5.38e-04

Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase family, this family is a duplication, consisting of two similar domains arranged as the subunits of the dimeric NADH oxidase/flavin reductase with one conserved active site.


Pssm-ID: 405236 [Multi-domain]  Cd Length: 214  Bit Score: 39.20  E-value: 5.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   2 IELIRTRRAIRQFDQTEIS---LDDLLK-CAECAGLapSGENLQplkflLVRDrklVEAIFPLLqwAGYIQPTGNPkpgk 77
Cdd:pfam14512   3 YEAIFKRHSVRKYTDEPIPeelLEELKNaIDEINKL--SGLNIQ-----LVID---DPDAFKGK--AKYGKFKGVP---- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238141  78 mptAYFVIAVDQnvtDSSAEKDVGAAIENFILSAWSLGIGTCWI-VSIDREKLRQLLQIPERLVIdsIVACGYPDETPV 155
Cdd:pfam14512  67 ---NYIAAYGEK---DDDLLENAGYYGEQIVLYATALGLGTCWVgGTYSKSKVKAKIKKGEKLVI--VIAFGYGATKGV 137
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 2-138 8.48e-04

oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain of NRPS (non-ribosomal peptide synthetase) and other systems that modify polypeptides by cyclizing a thioester to form a ring. These include EpoB, part of the epothilone biosynthesis pathway; TubD, part of the tubulysin biosynthesis pathway, MtsD, part of the myxothiozol biosynthesis pathway; IndC, part of the indigoidine biosynthesis pathway and TfxB, part of the trifitoxin processing pathway. All are FMN-dependent and oxidize the product of the cyclization of thioesters in short polypeptides.


Pssm-ID: 380318  Cd Length: 200  Bit Score: 38.55  E-value: 8.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141   2 IELIRTRRAIRQFDQTEISLDDLLKCAECAGL--------APSGENLQPLK-FLLVRDRKLVEA-----------IFPLl 61
Cdd:cd02142    21 SEALLNRRSRRTFSSEPLTLRELSRLAARGIPgsgyglrpYPSAGALYPIEvYVIVKNVEGLPAgiyhydpkrhrLVLI- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238141  62 qWAGYIQPTGNPKPGKMP---TAYFVIAVdqnVTDSSAE-------------KDVGAAIENFILSAWSLGIGTCWIVSID 125
Cdd:cd02142   100 -REGDFRLDLAHAAGNQAafgSAAFSLII---VARFERIawkygerayryilLEAGHLAQNLYLAATALGLGLCAIGAFD 175

                         170
                  ....*....|...
gi 1277238141 126 REKLRQLLQIPER 138
Cdd:cd02142   176 DDALRELLGLDEV 188
antibiot_sagB TIGR03605
SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation ...
 98-139 9.86e-03

SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation of streptolysin S from a ribosomally produced precursor polypeptide. Chemically similar systems operate on highly diverse sets of bacteriocin precursors in numerous other bacteria. This model describes a domain within SgaB and homologous regions from other proteins, many of which appear to be involved in biosynthesis of secondary metabolites. While some substrates may be intermediates in non-ribosomal peptide syntheses, others are involved in heterocycle-containing bacteriocin biosynthesis, and can be found near SgaC-like (see TIGR03603, cyclodehydratase) and SgaD-like (see TIGR03604, "docking") proteins. Members of this domain family are heterogeneous in length, as many have a partial second copy of the domain represented here. The incomplete second domain scores below the cutoffs to this model in most cases.


Pssm-ID: 188352  Cd Length: 173  Bit Score: 35.36  E-value: 9.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1277238141  98 KDVGAAIENFILSAWSLGIGTCWIVSIDREKLRQLLQIPERL 139
Cdd:TIGR03605 121 LDVGIIIQNFYLVATALGLGSCAIGGFDDDYIAELLGLDGIE 162
 
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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