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Conserved domains on  [gi|42794271|ref|NP_981932|]
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iodotyrosine deiodinase 1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
93-285 3.27e-121

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: 344.52  E-value: 3.27e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  93 FYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRWVTD 172
Cdd:cd02144   1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAAEEEEKEFYEKRMGEEWVWD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 173 LKKLRTNWIKEYLDTAPILILIFKQVHGFAANGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLG 252
Cdd:cd02144  81 LKPLGTNWEKPYLTEAPYLIVVFKQKYGVLPDGKKKKHYYNEESVGIAVGILLAALHNAGLVTLTHTPSP-MPFLRDLLG 159
                       170       180       190
                ....*....|....*....|....*....|...
gi 42794271 253 RPAHEKLLMLLPVGYPSKEATVPDLKRKPLDQI 285
Cdd:cd02144 160 RPKNEKPLLLLPVGYPAEDATVPDLKRKPLEEI 192
 
Name Accession Description Interval E-value
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
93-285 3.27e-121

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: 344.52  E-value: 3.27e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  93 FYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRWVTD 172
Cdd:cd02144   1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAAEEEEKEFYEKRMGEEWVWD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 173 LKKLRTNWIKEYLDTAPILILIFKQVHGFAANGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLG 252
Cdd:cd02144  81 LKPLGTNWEKPYLTEAPYLIVVFKQKYGVLPDGKKKKHYYNEESVGIAVGILLAALHNAGLVTLTHTPSP-MPFLRDLLG 159
                       170       180       190
                ....*....|....*....|....*....|...
gi 42794271 253 RPAHEKLLMLLPVGYPSKEATVPDLKRKPLDQI 285
Cdd:cd02144 160 RPKNEKPLLLLPVGYPAEDATVPDLKRKPLEEI 192
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
93-285 2.40e-33

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 119.57  E-value: 2.40e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  93 FYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKiieeeeeinYMKRMGHRWVTD 172
Cdd:COG0778   1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAE---------ALAEANQEWVAD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 173 lkklrtnwikeyldtAPILILIFKQVHgfaaNGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLG 252
Cdd:COG0778  72 ---------------APVLIVVCADPD----RSEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFD-PEKVRELLG 131
                       170       180       190
                ....*....|....*....|....*....|...
gi 42794271 253 RPAHEKLLMLLPVGYPSKEatVPDLKRKPLDQI 285
Cdd:COG0778 132 LPEGEEPVALLALGYPAEE--LNPRPRKPLEEV 162
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
97-267 7.54e-19

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: 81.67  E-value: 7.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271    97 LNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINymKRMGHRWVTDLKKL 176
Cdd:pfam00881   1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVE--PAAALLLLLRRDAN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271   177 RTNWIKEYLDTAPILILIFKQVHGFAANGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLGRPAH 256
Cdd:pfam00881  79 LKLLLQDFLRGAPVLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFD-AAAVRELLGLPDD 157
                         170
                  ....*....|.
gi 42794271   257 EKLLMLLPVGY 267
Cdd:pfam00881 158 ERLVGLIAVGY 168
BluB TIGR02476
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ...
93-280 1.19e-10

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: 59.76  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271    93 FYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEInYMKRMGHRWVTD 172
Cdd:TIGR02476   9 VYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQA-AAAIYDGERASQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271   173 LKKLRTNWIKEyldtAPILILIF-----KQVHGFAANGKKKVHYYneiSVSIACGILLAALQNAGL----VTVTTTplnc 243
Cdd:TIGR02476  88 YHRLKLEGIRE----APVQLAVFcddarGEGHGLGRHTMPEMLRY---SVACAIQNLWLAARAEGLgvgwVSILDP---- 156
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 42794271   244 gPRLRVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRK 280
Cdd:TIGR02476 157 -DAVRRLLGVPEGWRLVAYLCLGWPDAFYDEPELERA 192
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
100-173 1.52e-08

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 55.02  E-value: 1.52e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794271  100 RRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIrkiieeeeeinyMKRMGHRWVTDL 173
Cdd:PRK13294 260 RRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVRTRL------------LDAMRDAWRADL 321
 
Name Accession Description Interval E-value
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
93-285 3.27e-121

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: 344.52  E-value: 3.27e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  93 FYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRWVTD 172
Cdd:cd02144   1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAAEEEEKEFYEKRMGEEWVWD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 173 LKKLRTNWIKEYLDTAPILILIFKQVHGFAANGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLG 252
Cdd:cd02144  81 LKPLGTNWEKPYLTEAPYLIVVFKQKYGVLPDGKKKKHYYNEESVGIAVGILLAALHNAGLVTLTHTPSP-MPFLRDLLG 159
                       170       180       190
                ....*....|....*....|....*....|...
gi 42794271 253 RPAHEKLLMLLPVGYPSKEATVPDLKRKPLDQI 285
Cdd:cd02144 160 RPKNEKPLLLLPVGYPAEDATVPDLKRKPLEEI 192
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
93-285 2.40e-33

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 119.57  E-value: 2.40e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  93 FYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKiieeeeeinYMKRMGHRWVTD 172
Cdd:COG0778   1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAE---------ALAEANQEWVAD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 173 lkklrtnwikeyldtAPILILIFKQVHgfaaNGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLG 252
Cdd:COG0778  72 ---------------APVLIVVCADPD----RSEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFD-PEKVRELLG 131
                       170       180       190
                ....*....|....*....|....*....|...
gi 42794271 253 RPAHEKLLMLLPVGYPSKEatVPDLKRKPLDQI 285
Cdd:COG0778 132 LPEGEEPVALLALGYPAEE--LNPRPRKPLEEV 162
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
97-267 1.04e-21

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: 88.51  E-value: 1.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  97 LNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKiieeeeeinymkrmghrwvtdlkkl 176
Cdd:cd02062   1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAK------------------------- 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 177 RTNWIKEYLDTAPILILIFkqvhgfaANGKKKVHYYnEISVSIACGILLAALQNAGLVTVTTTPLNCG-PRLRVLLGRPA 255
Cdd:cd02062  56 LAAPNQKFIAGAPVVIVVV-------ADPDKSRPWA-LEDAGAAAQNLLLAAAALGLGSCWIGGFDFReDKVRELLGIPE 127
                       170
                ....*....|..
gi 42794271 256 HEKLLMLLPVGY 267
Cdd:cd02062 128 NLRPVALIAIGY 139
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
97-267 7.54e-19

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: 81.67  E-value: 7.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271    97 LNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINymKRMGHRWVTDLKKL 176
Cdd:pfam00881   1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVE--PAAALLLLLRRDAN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271   177 RTNWIKEYLDTAPILILIFKQVHGFAANGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLGRPAH 256
Cdd:pfam00881  79 LKLLLQDFLRGAPVLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFD-AAAVRELLGLPDD 157
                         170
                  ....*....|.
gi 42794271   257 EKLLMLLPVGY 267
Cdd:pfam00881 158 ERLVGLIAVGY 168
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
93-285 1.82e-17

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: 77.90  E-value: 1.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  93 FYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKiieeeeeinymKRMGHRWVTD 172
Cdd:cd02139   1 VYEAIKKRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLAE-----------AANGQKFIAE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 173 lkklrtnwikeyldtAPILI-LIFKQVHGFAANGKKkvhyYNEISVSIACG-ILLAAlQNAGLVTvtttplnC------G 244
Cdd:cd02139  70 ---------------APVVIvACADPSESGMGCGKP----YYLVDVAIAMEhLVLAA-TEEGLGT-------CwigafdE 122
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 42794271 245 PRLRVLLGRPAHEKLLMLLPVGYPSKEatVPDLKRKPLDQI 285
Cdd:cd02139 123 DKVKEILGIPEEYRVVALTPLGYPAEE--PPPRPRKPLEEI 161
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
95-271 1.90e-16

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: 74.88  E-value: 1.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  95 ELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKiieeeeeinyMKRMGhrwvtdlk 174
Cdd:cd02151   1 ELLKKRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKLSE----------CKPHG-------- 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 175 klrtnwiKEYLDTAPILILIfkqvhgfAANgKKKVHYYNEISvSIACGILLAALQNAGLVT--------VTTTPLNCGPR 246
Cdd:cd02151  63 -------SAFLKGAPAAIVV-------LAD-TEKSDTWIEDA-SIAATYIQLAAESLGLGScwiqirnrETQDGKTAEEY 126
                       170       180
                ....*....|....*....|....*
gi 42794271 247 LRVLLGRPAHEKLLMLLPVGYPSKE 271
Cdd:cd02151 127 VRELLGIPENYRVLCIIALGYPDEE 151
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
95-285 1.13e-15

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: 72.27  E-value: 1.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  95 ELLNKRRSVR-FISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIeeeeeinymkrMGHRWVTdl 173
Cdd:cd02137   2 EVIKSRRSVRnFDPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAA-----------YNQPQVT-- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 174 kklrtnwikeyldTAPILILIFKQvhgfaangkkkvhyyneISVSIACGILLAALQNAGLVTVTTTPLNcGPRLRVLLGR 253
Cdd:cd02137  69 -------------TASAVILVLGD-----------------LNAGLAAMNLMLAAKAKGYDTCPMGGFD-KEKVAELLNL 117
                       170       180       190
                ....*....|....*....|....*....|..
gi 42794271 254 PAHEKLLMLLPVGYPSKEAtvPDLKRKPLDQI 285
Cdd:cd02137 118 PDRYVPVLLIAIGKAADKA--PRSGRLPVDEV 147
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
92-267 1.79e-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: 380330 [Multi-domain]  Cd Length: 145  Bit Score: 68.95  E-value: 1.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  92 EFYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIieeeeeinymkrmghrwvt 171
Cdd:cd20609   1 DFLELAKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKA------------------- 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 172 dlkklrTNWIKEyldtAPILILIFKqVHGFAANGKKKVHYYNEISVSIACG-ILLAAlQNAGLVT--VtttplnCG---P 245
Cdd:cd20609  62 ------TPRFFG----APLVIVVCY-DKDESWKRPYDGKDSGDIDAAIVAThMMLAA-TELGLGTcwV------GNfdpE 123
                       170       180
                ....*....|....*....|..
gi 42794271 246 RLRVLLGRPAHEKLLMLLPVGY 267
Cdd:cd20609 124 KVREAFNLPENLEPVAILPLGY 145
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
96-285 2.82e-13

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: 66.07  E-value: 2.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  96 LLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPdvkhkirkiieeeeEINYMKRMGHrwvtdlkk 175
Cdd:cd02136   1 AIKSRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTGK--------------ARERLKKAFF-------- 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 176 lrtnwikeyldTAPILILIFkqvhgfaanGKKKVHYYNEISVSIACGILLAALQNAGLVTVtttPLNCGPR----LRVLL 251
Cdd:cd02136  59 -----------GAPVALFLT---------MDKVLGPWSWFDLGAFLQNLMLAAHALGLGTC---PQGALAGypdvVRKEL 115
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42794271 252 GRPAHEKLLMLLPVGYPSKEATVPDL--KRKPLDQI 285
Cdd:cd02136 116 GIPDDEELVCGIALGYPDPDAPVNQFrtPREPLEEF 151
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
95-271 1.28e-12

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: 65.03  E-value: 1.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  95 ELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIeeeeeinymkrMGHRWVTdlk 174
Cdd:cd03370   3 EAIESRRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQAAA-----------YGQAQVT--- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 175 klrtnwikeyldTAPILILIFKQ-----------VH-GFAANGKKKV-----HYYNEISVS-----------IACGILLA 226
Cdd:cd03370  69 ------------SAPAVIVIYSDmedalanleetIHpGLSEERRQREaaglrGAFGKMSVEqrgqwglaqanIALGFLLL 136
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42794271 227 ALQNAGLVTVTTTPLNCGpRLRVLLGRPAHEKLLMLLPVGYPSKE 271
Cdd:cd03370 137 AAQSLGYDTSPMLGFDPE-KVKALLGLPEHVTIAALVALGKPAEE 180
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
99-276 3.98e-12

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: 63.00  E-value: 3.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  99 KRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEeeeeinYMKrmghrwvtdlkklrt 178
Cdd:cd02150   3 TRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKIAEAHP------YGK--------------- 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 179 nwikeYLDTAPILILIfkqvhgfAANGKK-KVHYYNEISVSIAC-GILLAAlQNAGLVTVTTtplNCGPR------LRVL 250
Cdd:cd02150  62 -----MLKEAPLAIVV-------CGDPSKeKAPGYWVQDCSAATeNILLAA-HALGLGAVWL---GVYPFeervkaIREI 125
                       170       180
                ....*....|....*....|....*.
gi 42794271 251 LGRPAHEKLLMLLPVGYPSKEATVPD 276
Cdd:cd02150 126 LNIPENIIPFCVIALGYPAEEKEPKD 151
BluB TIGR02476
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ...
93-280 1.19e-10

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: 59.76  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271    93 FYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEInYMKRMGHRWVTD 172
Cdd:TIGR02476   9 VYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQA-AAAIYDGERASQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271   173 LKKLRTNWIKEyldtAPILILIF-----KQVHGFAANGKKKVHYYneiSVSIACGILLAALQNAGL----VTVTTTplnc 243
Cdd:TIGR02476  88 YHRLKLEGIRE----APVQLAVFcddarGEGHGLGRHTMPEMLRY---SVACAIQNLWLAARAEGLgvgwVSILDP---- 156
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 42794271   244 gPRLRVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRK 280
Cdd:TIGR02476 157 -DAVRRLLGVPEGWRLVAYLCLGWPDAFYDEPELERA 192
BluB cd02145
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ...
94-280 2.41e-10

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: 58.91  E-value: 2.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  94 YELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRwVTDL 173
Cdd:cd02145   1 YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEMYTGER-AAQY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 174 KKLRTnwikEYLDTAPILILIF-----KQVHGFAANGKKKVHYYneisvSIACGI----LLAALQNAGLVTVTTtpLNcg 244
Cdd:cd02145  80 RTLKL----EGIEEAPLQLAVFcdrarAGGHGLGRTTMPEMDLY-----SSVCAVqnlwLAARAEGLGVGWVSI--LD-- 146
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 42794271 245 P-RLRVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRK 280
Cdd:cd02145 147 PdEVKRLLGIPEHWEPVAYLCIGYPEFFYDEPELEQA 183
nitroreductase cd20610
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
99-267 2.73e-10

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: 58.06  E-value: 2.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  99 KRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIrKIIEEEEEINYMKRMghRWVTDLKKLR- 177
Cdd:cd20610   3 KRRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKI-GISIKKKNEEIARLL--EKVFAEKPIRf 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 178 TNWIK--EYLDTAPILILIFKQVHgfaangkKKVHYYNEISVSIAcgillAALQNAGLVTVT--------TTPLNCGPRL 247
Cdd:cd20610  80 RKFRRffTLFGGAPVLVVVYTEPY-------KPPEERKPDLQSVS-----AAIQNLLLAAHAlglgtcwmTGPLYAEDEI 147
                       170       180
                ....*....|....*....|
gi 42794271 248 RVLLGRPAHEKLLMLLPVGY 267
Cdd:cd20610 148 EEILEIPDDKELVAVTPLGY 167
YdjA-like cd02135
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ...
95-267 8.04e-09

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: 53.76  E-value: 8.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  95 ELLNKRRSVR-FISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVvkdpdVKHKIRKIIEEEEEINYMKRMGHRWVTDL 173
Cdd:cd02135   2 ELIKTRRSIRkFKLTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIV-----VTGEGRERLAELLAAAAAARAPGADPEKL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 174 KKLRTNWIKeyldtAPILILIFKQVHGfaanGKKKVHYYNEISVSIAC-GILLAALQnAGLVTV-TTTPLNCGPRLRVLL 251
Cdd:cd02135  77 EKAREKALR-----APVVIAVVAKPDE----DPKVPEWEQYAAVGAAVqNLLLAAHA-LGLGAVwRTGPVTYDPAVREAL 146
                       170
                ....*....|....*.
gi 42794271 252 GRPAHEKLLMLLPVGY 267
Cdd:cd02135 147 GLPEDERIVGFLYLGT 162
nitroreductase_FeS-like cd02143
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ...
96-150 9.99e-09

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: 54.02  E-value: 9.99e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42794271  96 LLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIR 150
Cdd:cd02143   1 LLRSRRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLA 55
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
94-267 1.05e-08

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: 53.11  E-value: 1.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  94 YELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIieeeeeinymkrmghrwvtdl 173
Cdd:cd20608   1 FEAIKTRRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKETLSELAKK--------------------- 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 174 kklrTNWIKEYLDTAPILIlifkqvhgfAANGKKKV------HYYNEISVSIACGILLAALQNAGLVTVTTTPLNcGPRL 247
Cdd:cd20608  60 ----ESPSNGWLKDAPVII---------VVCADPKDsgwlngQNYYLVDAAIAMQNLMLAATDLGLGTCWIGAFD-EKKV 125
                       170       180
                ....*....|....*....|
gi 42794271 248 RVLLGRPAHEKLLMLLPVGY 267
Cdd:cd20608 126 KEILGIPENIRVVALTPLGY 145
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
100-173 1.52e-08

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 55.02  E-value: 1.52e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794271  100 RRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIrkiieeeeeinyMKRMGHRWVTDL 173
Cdd:PRK13294 260 RRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVRTRL------------LDAMRDAWRADL 321
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
96-285 2.62e-06

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: 46.77  E-value: 2.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271  96 LLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKirkiieeeeeinymkrmghRWVTDLKK 175
Cdd:cd02138   1 LIAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFVVARRDTEAFE-------------------KLLDLLAE 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794271 176 LRTNWIKEyldtAPILILIFKQVHgFAANGKKKVHYynEISVSIACGILLAALQNAGLVtvtttplnCGP-------RLR 248
Cdd:cd02138  62 GNQSWAKN----APVLIVVLAKTE-FDHNGKPNRYA--LFDTGAAVANLALQATALGLV--------VHQmagfdpeKAK 126
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42794271 249 VLLGRPAHEKLLMLLPVGYPSKEATVPDL---------KRKPLDQI 285
Cdd:cd02138 127 EALGIPDEYEPITMIAIGYPGDPESLPEKllereeaprTRKPLSEI 172
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
95-151 9.08e-06

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: 44.93  E-value: 9.08e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42794271  95 ELLNKRRSVR-FISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRK 151
Cdd:cd02149   4 ELLNFRYATKkFDPNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAP 61
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
95-149 9.16e-06

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: 45.69  E-value: 9.16e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42794271  95 ELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKI 149
Cdd:cd02146   3 ETILNHRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKL 57
 
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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