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Conserved domains on  [gi|1093259745|emb|SEH73457|]
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Nitroreductase [Stutzerimonas xanthomarina]

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 ...
 184-334 4.31e-39

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


:

Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 136.14  E-value: 4.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 184 LFRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGGTAGFH-DNLPCVIAVVGDLG 262
Cdd:COG0778     4 LLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEANQEWvADAPVLIVVCADPD 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093259745 263 CYPEaRDRHVVYIDGSLAAMQLMLALESLGLSSCSINWPDVEErerqLAKILGLAYQERTVMLLAVGYADPT 334
Cdd:COG0778    84 RSEK-VPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEK----VRELLGLPEGEEPVALLALGYPAEE 150
 
Name Accession Description Interval E-value
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 184-334 4.31e-39

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 136.14  E-value: 4.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 184 LFRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGGTAGFH-DNLPCVIAVVGDLG 262
Cdd:COG0778     4 LLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEANQEWvADAPVLIVVCADPD 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093259745 263 CYPEaRDRHVVYIDGSLAAMQLMLALESLGLSSCSINWPDVEErerqLAKILGLAYQERTVMLLAVGYADPT 334
Cdd:COG0778    84 RSEK-VPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEK----VRELLGLPEGEEPVALLALGYPAEE 150
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 185-330 1.58e-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: 123.56  E-value: 1.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 185 FRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGGTAGFHDNLPCVIAVVGDlgcy 264
Cdd:cd02062     1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAKLAAPNQKFIAGAPVVIVVVAD---- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093259745 265 pEARDRHVVYIDGSLAAMQLMLALESLGLSSCSINWPDveERERQLAKILGLAYQERTVMLLAVGY 330
Cdd:cd02062    77 -PDKSRPWALEDAGAAAQNLLLAAAALGLGSCWIGGFD--FREDKVRELLGIPENLRPVALIAIGY 139
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 186-330 2.29e-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: 119.03  E-value: 2.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 186 RRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYV---SNGKEKAAEVAKCA--------------------G 242
Cdd:pfam00881   2 RQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVvtdGELRYRLAEAALELllvepaaalllllrrdanlkL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 243 GTAGFHDNLPCVIAVVGDLGCY---PEARDRHVVYIDGSLAAMQLMLALESLGLSSCSINWPDVEErerqLAKILGLAYQ 319
Cdd:pfam00881  82 LLQDFLRGAPVLIVITASLSTYlrkAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAA----VRELLGLPDD 157

                         170
                  ....*....|.
gi 1093259745 320 ERTVMLLAVGY 330
Cdd:pfam00881 158 ERLVGLIAVGY 168
PRK05365 PRK05365
malonic semialdehyde reductase; Provisional
 175-293 8.61e-06

malonic semialdehyde reductase; Provisional


Pssm-ID: 180040 [Multi-domain]  Cd Length: 195  Bit Score: 45.96  E-value: 8.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 175 PVSYDELMVLFRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRF-YVSN--GKEKAAE------VAKC--AGG 243
Cdd:PRK05365    3 ALDDAALDQLFTEARTHNGWLDEPVSDEQLRELYDLVKWGPTSANCSPARFvFVRSaeAKERLRPalsegnLAKTlaAPV 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093259745 244 TA------GFHDNLPcviavvgDLGCYPEARD-----RHVVYIDGSL-AAMQ---LMLALESLGL 293
Cdd:PRK05365   83 TAivaydtEFHEHLP-------KLFPHADARSwfagnPALAEETAFRnSSLQgayLILAARALGL 140
 
Name Accession Description Interval E-value
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 184-334 4.31e-39

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 136.14  E-value: 4.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 184 LFRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGGTAGFH-DNLPCVIAVVGDLG 262
Cdd:COG0778     4 LLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEANQEWvADAPVLIVVCADPD 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093259745 263 CYPEaRDRHVVYIDGSLAAMQLMLALESLGLSSCSINWPDVEErerqLAKILGLAYQERTVMLLAVGYADPT 334
Cdd:COG0778    84 RSEK-VPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEK----VRELLGLPEGEEPVALLALGYPAEE 150
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 185-330 1.58e-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: 123.56  E-value: 1.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 185 FRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGGTAGFHDNLPCVIAVVGDlgcy 264
Cdd:cd02062     1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAKLAAPNQKFIAGAPVVIVVVAD---- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093259745 265 pEARDRHVVYIDGSLAAMQLMLALESLGLSSCSINWPDveERERQLAKILGLAYQERTVMLLAVGY 330
Cdd:cd02062    77 -PDKSRPWALEDAGAAAQNLLLAAAALGLGSCWIGGFD--FREDKVRELLGIPENLRPVALIAIGY 139
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 180-330 1.75e-32

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: 118.26  E-value: 1.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 180 ELMVLFRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCaggtAGFHDNLPCVIAVVG 259
Cdd:cd20609     1 DFLELAKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKA----TPRFFGAPLVIVVCY 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093259745 260 DLGC---YPEARDRHVVyIDGSLAAMQLMLALESLGLSSCSINWPDVEErerqLAKILGLAYQERTVMLLAVGY 330
Cdd:cd20609    77 DKDEswkRPYDGKDSGD-IDAAIVATHMMLAATELGLGTCWVGNFDPEK----VREAFNLPENLEPVAILPLGY 145
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 186-330 2.29e-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: 119.03  E-value: 2.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 186 RRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYV---SNGKEKAAEVAKCA--------------------G 242
Cdd:pfam00881   2 RQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVvtdGELRYRLAEAALELllvepaaalllllrrdanlkL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 243 GTAGFHDNLPCVIAVVGDLGCY---PEARDRHVVYIDGSLAAMQLMLALESLGLSSCSINWPDVEErerqLAKILGLAYQ 319
Cdd:pfam00881  82 LLQDFLRGAPVLIVITASLSTYlrkAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAA----VRELLGLPDD 157

                         170
                  ....*....|.
gi 1093259745 320 ERTVMLLAVGY 330
Cdd:pfam00881 158 ERLVGLIAVGY 168
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 184-345 3.52e-29

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: 109.64  E-value: 3.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 184 LFRRRRSVRWYQ-DKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGGTAGFHDNlPCVIAVVGDLg 262
Cdd:cd02137     3 VIKSRRSVRNFDpDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAAYNQPQVTTA-SAVILVLGDL- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 263 cypeardrhvvyiDGSLAAMQLMLALESLGLSSCSINWPDVEererQLAKILGLAYQERTVMLLAVGYADPTGGIPYSDK 342
Cdd:cd02137    81 -------------NAGLAAMNLMLAAKAKGYDTCPMGGFDKE----KVAELLNLPDRYVPVLLIAIGKAADKAPRSGRLP 143


                  ...
gi 1093259745 343 KTE 345
Cdd:cd02137   144 VDE 146
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 184-332 1.43e-28

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: 108.39  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 184 LFRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGGTAGFHDNLPCVIAVVGDlgc 263
Cdd:cd02151     2 LLKKRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKLSECKPHGSAFLKGAPAAIVVLAD--- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093259745 264 yPEARDRHVvyIDGSLAAMQLMLALESLGLSSCsinWPDVEERERQ--------LAKILGLAYQERTVMLLAVGYAD 332
Cdd:cd02151    79 -TEKSDTWI--EDASIAATYIQLAAESLGLGSC---WIQIRNRETQdgktaeeyVRELLGIPENYRVLCIIALGYPD 149
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 186-330 3.05e-27

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: 104.72  E-value: 3.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 186 RRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGGTAGFHDNLPCVIAVVGDlgcyP 265
Cdd:cd20608     5 KTRRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKETLSELAKKESPSNGWLKDAPVIIVVCAD----P 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093259745 266 ---EARDRHVVYI-DGSLAAMQLMLALESLGLSSCSINwpdvEERERQLAKILGLAYQERTVMLLAVGY 330
Cdd:cd20608    81 kdsGWLNGQNYYLvDAAIAMQNLMLAATDLGLGTCWIG----AFDEKKVKEILGIPENIRVVALTPLGY 145
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
 188-334 6.07e-25

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: 98.43  E-value: 6.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 188 RRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKaaevAKCAggTAGFHDnlPCVIAVVGDlgcypeA 267
Cdd:cd02136     5 RRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTGKAR----ERLK--KAFFGA--PVALFLTMD------K 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093259745 268 RDRHVVYIDGSLAAMQLMLALESLGLSSCSIN-WPDVEERERqlaKILGLAYQERTVMLLAVGYADPT 334
Cdd:cd02136    71 VLGPWSWFDLGAFLQNLMLAAHALGLGTCPQGaLAGYPDVVR---KELGIPDDEELVCGIALGYPDPD 135
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 185-332 1.33e-23

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: 94.98  E-value: 1.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 185 FRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKcAGGTAGFHDNLPCVIAVVGDLGcy 264
Cdd:cd02150     1 ILTRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKIAE-AHPYGKMLKEAPLAIVVCGDPS-- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093259745 265 pEARDRHVVYIDGSLAAMQLMLALESLGLSSCSIN-WPDvEERERQLAKILGLAYQERTVMLLAVGYAD 332
Cdd:cd02150    78 -KEKAPGYWVQDCSAATENILLAAHALGLGAVWLGvYPF-EERVKAIREILNIPENIIPFCVIALGYPA 144
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 186-332 7.35e-23

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: 93.30  E-value: 7.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 186 RRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGGtAGFHDNLPCVIAVVGD----- 260
Cdd:cd02139     6 KKRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLAEAANG-QKFIAEAPVVIVACADpsesg 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093259745 261 LGCYPEARdrhvvYIDGSLAAMQLMLALESLGLSSCSINWPDveerERQLAKILGLAYQERTVMLLAVGYAD 332
Cdd:cd02139    85 MGCGKPYY-----LVDVAIAMEHLVLAATEEGLGTCWIGAFD----EDKVKEILGIPEEYRVVALTPLGYPA 147
nitroreductase cd20610
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 186-330 9.28e-16

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: 73.85  E-value: 9.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 186 RRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGG---------------------- 243
Cdd:cd20610     2 KKRRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKIGISIKKkneeiarllekvfaekpirfrk 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 244 ---TAGFHDNLPCVIAVVGDLgcYPEARDRhvvyiDGSL----AAMQ-LMLALESLGLSSCSINWPDVEERErqLAKILG 315
Cdd:cd20610    82 frrFFTLFGGAPVLVVVYTEP--YKPPEER-----KPDLqsvsAAIQnLLLAAHALGLGTCWMTGPLYAEDE--IEEILE 152

                         170
                  ....*....|....*
gi 1093259745 316 LAYQERTVMLLAVGY 330
Cdd:cd20610   153 IPDDKELVAVTPLGY 167
YdjA-like cd02135
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ...
 184-330 1.29e-15

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: 73.41  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 184 LFRRRRSVRWYQDK-PVSNELIEQAVSAAALAPSACNRQPFRFYVSNG--KEKAAEVAKCAGGTAGFHD----------- 249
Cdd:cd02135     3 LIKTRRSIRKFKLTgAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGegRERLAELLAAAAAARAPGAdpeklekarek 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 250 --NLPCVIAVVGDLGcypeaRDRHVVYID----GSLAAMQLMLALESLGLSSCsINWPDVEERERqLAKILGLAYQERTV 323
Cdd:cd02135    83 alRAPVVIAVVAKPD-----EDPKVPEWEqyaaVGAAVQNLLLAAHALGLGAV-WRTGPVTYDPA-VREALGLPEDERIV 155


                  ....*..
gi 1093259745 324 MLLAVGY 330
Cdd:cd02135   156 GFLYLGT 162
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
 180-348 3.79e-15

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: 72.96  E-value: 3.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 180 ELMvlfRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRF-YVSNGKEK-----AAEV------AKCAG----- 242
Cdd:cd02144     3 ELM---KKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFvVVSDPEIKrkireAAEEeekefyEKRMGeewvw 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 243 -----GTAG---FHDNLPCVIAVVGDL-GCYPEARDRHVVY--IDGSLAAMQLMLALESLGLSSCSINWPDveerERQLA 311
Cdd:cd02144    80 dlkplGTNWekpYLTEAPYLIVVFKQKyGVLPDGKKKKHYYneESVGIAVGILLAALHNAGLVTLTHTPSP----MPFLR 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1093259745 312 KILGLAYQERTVMLLAVGYADPTGGIPysdKKTEKDL 348
Cdd:cd02144   156 DLLGRPKNEKPLLLLPVGYPAEDATVP---DLKRKPL 189
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
 188-335 3.92e-15

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: 72.74  E-value: 3.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 188 RRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGGTAGFhDNLPCVIAVVGDL------ 261
Cdd:cd03370     8 RRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQAAAYGQAQV-TSAPAVIVIYSDMedalan 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 262 -------GCYPEARDRHVVYIDGSLAAMQ------------------LMLALESLGLSSCsinwPDVEERERQLAKILGL 316
Cdd:cd03370    87 leetihpGLSEERRQREAAGLRGAFGKMSveqrgqwglaqanialgfLLLAAQSLGYDTS----PMLGFDPEKVKALLGL 162

                         170
                  ....*....|....*....
gi 1093259745 317 AYQERTVMLLAVGYADPTG 335
Cdd:cd03370   163 PEHVTIAALVALGKPAEEG 181
nitroreductase_FeS-like cd02143
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ...
 184-316 2.24e-14

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: 70.58  E-value: 2.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 184 LFRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKC-------------AGGTAGFHDN 250
Cdd:cd02143     1 LLRSRRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLAELvidwmrelikedpELAGKLFLDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 251 L---------------PCVIAVVGDlgcypeaRDRHVVYIDGSLAAMQLMLALESLGLSSC--------SINWPDveere 307
Cdd:cd02143    81 IvaawekgidvilrgaPHLVVAHAP-------KDAPTPPVDCAIALTYLELAAPSLGLGTCwagfftaaANNYPP----- 148


                  ....*....
gi 1093259745 308 rqLAKILGL 316
Cdd:cd02143   149 --LREALGL 155
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
 188-352 5.11e-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: 70.34  E-value: 5.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 188 RRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGGTAgFHDNLPCVIAVVGDLGCYPEA 267
Cdd:cd02146     8 HRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAELAGNQP-YVAQAPVFLVFCADLYRHQKI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 268 RDRHVVY--------------IDGSLAAMQLMLALESLGLSSCSI----NWPDveererQLAKILGLAyqERTVML--LA 327
Cdd:cd02146    87 AEEAGGKdvgldylesflvgvVDAALAAQNALVAAESLGLGIVYIggirNNPE------EVIELLGLP--EYVFPLfgLT 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1093259745 328 VGYADPTGGI-P------------YSDKKTEKDLIIYN 352
Cdd:cd02146   159 VGHPDPTPEVkPrlpleavvheetYQDLTDLEDLAAYD 196
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
 184-333 1.92e-11

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: 61.79  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 184 LFRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKA-AEVAKC-AGGTAGFHDNLPCVIAVVGD- 260
Cdd:cd02138     1 LIAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFVVARRDTEAfEKLLDLlAEGNQSWAKNAPVLIVVLAKt 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093259745 261 -LGCYPEARdRHVVYiDGSLAAMQLMLALESLGLSSCSINWPDVEErerqLAKILGLAYQERTVMLLAVGYADP 333
Cdd:cd02138    81 eFDHNGKPN-RYALF-DTGAAVANLALQATALGLVVHQMAGFDPEK----AKEALGIPDEYEPITMIAIGYPGD 148
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 184-330 9.43e-08

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: 51.10  E-value: 9.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 184 LFRRRRSVRWYQD-KPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGgtaGFHDNLPCVIAVVgdLG 262
Cdd:cd02149     5 LLNFRYATKKFDPnKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAAW---FNQPQIKDASHVV--VF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093259745 263 CYPEARDRHVVYIdgslAAMQLMLALESLGLSSCSINWPDVEererQLAKILGLAYQE-RTVMLLAVGY 330
Cdd:cd02149    80 LAKKDWSAKQTYI----ALGNMLLAAAMLGIDSCPIEGFDPA----KLDEILGLDEKGyKISVMVAFGY 140
RutE-like cd02148
nitroreductase similar to Escherichia coli RutE; A subfamily of the nitroreductase family ...
 181-293 1.27e-07

nitroreductase similar to Escherichia coli RutE; A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to nitroreductase. 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. RutE is involved in the utilization of uracil as the sole nitrogen source; it appears to have the same function as YdfG, which reduces malonic semialdehyde to 3-hydroxypropionic acid.


Pssm-ID: 380323 [Multi-domain]  Cd Length: 186  Bit Score: 51.10  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 181 LMVLFRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKCAGG-------TAG------- 246
Cdd:cd02148     2 LDQLFTEARTHNAWEDKPVSDEELRAIYDLAKWGPTAANCSPARIVFVRSAEAKERLVPHLSEgnrektmAAPvtailay 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1093259745 247 ---FHDNLPcVIAVVGD-----LGCYPEARDRhVVYIDGSLAAMQLMLALESLGL 293
Cdd:cd02148    82 dteFYEHLP-RLFPHGDarswfFGSGPARAEE-TAFRNASLQAAYFILAARALGL 134
PRK05365 PRK05365
malonic semialdehyde reductase; Provisional
 175-293 8.61e-06

malonic semialdehyde reductase; Provisional


Pssm-ID: 180040 [Multi-domain]  Cd Length: 195  Bit Score: 45.96  E-value: 8.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 175 PVSYDELMVLFRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRF-YVSN--GKEKAAE------VAKC--AGG 243
Cdd:PRK05365    3 ALDDAALDQLFTEARTHNGWLDEPVSDEQLRELYDLVKWGPTSANCSPARFvFVRSaeAKERLRPalsegnLAKTlaAPV 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093259745 244 TA------GFHDNLPcviavvgDLGCYPEARD-----RHVVYIDGSL-AAMQ---LMLALESLGL 293
Cdd:PRK05365   83 TAivaydtEFHEHLP-------KLFPHADARSwfagnPALAEETAFRnSSLQgayLILAARALGL 140
BluB cd02145
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ...
 184-338 2.90e-05

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: 44.27  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 184 LFRRRRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRFYVSNGKEKAAEVAKC------------AGGTAGFHDNL 251
Cdd:cd02145     3 VIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELfqranaeaaemyTGERAAQYRTL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 252 --------PCVIAVvgdlgCYPEARDRHVVYIDGSLAAMQ------------LMLALESLGLSSCSINWPDveererQLA 311
Cdd:cd02145    83 klegieeaPLQLAV-----FCDRARAGGHGLGRTTMPEMDlyssvcavqnlwLAARAEGLGVGWVSILDPD------EVK 151

                         170       180
                  ....*....|....*....|....*..
gi 1093259745 312 KILGLAYQERTVMLLAVGYADPTGGIP 338
Cdd:cd02145   152 RLLGIPEHWEPVAYLCIGYPEFFYDEP 178
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
 179-225 5.86e-05

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 44.62  E-value: 5.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1093259745 179 DELMVLFRR-----RRSVRWYQDKPVSNELIEQAVSAAALAPSACNRQPFRF 225
Cdd:PRK13294  246 AEALELGRReavllRRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRF 297
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 164-329 3.18e-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: 41.25  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 164 VPYPHSQLPDCPVSYDELMVLFRRRRSVRWYQDKPVS-NELIEQAVSAAAL-------APSACNRQPFRFYVSngkekaa 235
Cdd:cd02142     3 VPLPDPNLKPALLATLDLSEALLNRRSRRTFSSEPLTlRELSRLAARGIPGsgyglrpYPSAGALYPIEVYVI------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 236 eVAKCAGGTAG-------------------------------FHDNLPCVIAVVGDLGCY-PEARDR--HVVYIDGSLAA 281
Cdd:cd02142    76 -VKNVEGLPAGiyhydpkrhrlvliregdfrldlahaagnqaAFGSAAFSLIIVARFERIaWKYGERayRYILLEAGHLA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1093259745 282 MQLMLALESLGLSSCSINWPDVEererQLAKILGL-AYQERTVMLLAVG 329
Cdd:cd02142   155 QNLYLAATALGLGLCAIGAFDDD----ALRELLGLdEVEEVVLYAFVVG 199
TM1586_NiRdase pfam14512
Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase ...
 200-232 8.33e-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: 40.35  E-value: 8.33e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1093259745 200 SNELIEQAVSAAALAPSACNRQPFRFYVSNGKE 232
Cdd:pfam14512 155 LPEWFKEGMEAARLAPSAMNQQPWRFVLVDDNR 187
TM1586_NiRdase pfam14512
Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase ...
 188-352 1.15e-03

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: 39.58  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 188 RRSVRWYQDKPVSNELIEQAVSAAalapSACNRQP---FRFYVSNGKEKAAEVAkcaggtAGFHDNLPCVIAVVGDLGcy 264
Cdd:pfam14512   9 RHSVRKYTDEPIPEELLEELKNAI----DEINKLSglnIQLVIDDPDAFKGKAK------YGKFKGVPNYIAAYGEKD-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093259745 265 pEARDRHVVYIdgslaAMQLMLALESLGLSSC----SINWPDVEERERQlakilglayQERTVMLLAVGYADpTGGIPYs 340
Cdd:pfam14512  77 -DDLLENAGYY-----GEQIVLYATALGLGTCwvggTYSKSKVKAKIKK---------GEKLVIVIAFGYGA-TKGVRA- 139

                         170
                  ....*....|..
gi 1093259745 341 DKKTEKDLIIYN 352
Cdd:pfam14512 140 KRKPLDELCVVK 151
 
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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