|
Name |
Accession |
Description |
Interval |
E-value |
| iodotyrosine_dehalogenase |
cd02144 |
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ... |
92-284 |
5.26e-120 |
|
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: 341.44 E-value: 5.26e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 92 FYREMDTRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKLEVRLIIEEEERMNYEKRMSAQWLHD 171
Cdd:cd02144 1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAAEEEEKEFYEKRMGEEWVWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 172 LEKLRLTWSKPYLTRAPYIIVVFKQLFRVTEEGKKTTNYYQEISASIATGFLLAAVHNAGLVTVTTTPMNaGPRLRTLLE 251
Cdd:cd02144 81 LKPLGTNWEKPYLTEAPYLIVVFKQKYGVLPDGKKKKHYYNEESVGIAVGILLAALHNAGLVTLTHTPSP-MPFLRDLLG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1229173765 252 RPISEKVLVLLPVGHPEDGATVPDLQRKALQEI 284
Cdd:cd02144 160 RPKNEKPLLLLPVGYPAEDATVPDLKRKPLEEI 192
|
|
| NfnB |
COG0778 |
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ... |
92-284 |
4.56e-30 |
|
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 440541 [Multi-domain] Cd Length: 163 Bit Score: 111.10 E-value: 4.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 92 FYREMDTRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKlevrliieeeermnyekrmsaqwlHD 171
Cdd:COG0778 1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELR------------------------ER 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 172 LEKLRLTWSKPYLTRAPYIIVVFKQlfrvTEEGKKTTNYYQEISASIATGFLLAAVHNAGLVTVTTTPMNAgPRLRTLLE 251
Cdd:COG0778 57 LAEALAEANQEWVADAPVLIVVCAD----PDRSEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDP-EKVRELLG 131
|
170 180 190
....*....|....*....|....*....|...
gi 1229173765 252 RPISEKVLVLLPVGHPEDgaTVPDLQRKALQEI 284
Cdd:COG0778 132 LPEGEEPVALLALGYPAE--ELNPRPRKPLEEV 162
|
|
| Nitroreductase |
pfam00881 |
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ... |
99-266 |
2.13e-21 |
|
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: 88.22 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 99 RRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKLEVRLIIEEEerMNYEKRMSAQWLHDLEKLRLT 178
Cdd:pfam00881 4 RRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALEL--LLVEPAAALLLLLRRDANLKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 179 WSKPYLTRAPYIIVVFKQLFRVTEEGKKTTNYYQEISASIATGFLLAAVHNAGLVTVTTTPMNAgPRLRTLLERPISEKV 258
Cdd:pfam00881 82 LLQDFLRGAPVLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDA-AAVRELLGLPDDERL 160
|
....*...
gi 1229173765 259 LVLLPVGH 266
Cdd:pfam00881 161 VGLIAVGY 168
|
|
| BluB |
TIGR02476 |
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ... |
91-283 |
2.05e-12 |
|
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: 64.77 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 91 QFYREMDTRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKLEVRLIIEE---EERMNYEKRMSAQ 167
Cdd:TIGR02476 8 AVYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRanqAAAAIYDGERASQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 168 WlhdlEKLRLTWskpyLTRAPYIIVVFKQLFRVTEE--GKKTTNYYQEISASIATG-FLLAA-VHNAGLVTVTTTPMNAg 243
Cdd:TIGR02476 88 Y----HRLKLEG----IREAPVQLAVFCDDARGEGHglGRHTMPEMLRYSVACAIQnLWLAArAEGLGVGWVSILDPDA- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1229173765 244 prLRTLLERPISEKVLVLLPVGHPEDGATVPDLQRKALQE 283
Cdd:TIGR02476 159 --VRRLLGVPEGWRLVAYLCLGWPDAFYDEPELERAGWQE 196
|
|
| PRK13294 |
PRK13294 |
F420-0--gamma-glutamyl ligase; Provisional |
99-194 |
5.21e-08 |
|
F420-0--gamma-glutamyl ligase; Provisional
Pssm-ID: 183957 [Multi-domain] Cd Length: 448 Bit Score: 53.48 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 99 RRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKleVRLIieeeermnyeKRMSAQWLHDLEKLRLT 178
Cdd:PRK13294 260 RRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVR--TRLL----------DAMRDAWRADLRADGLS 327
|
90 100
....*....|....*....|....
gi 1229173765 179 WSK--------PYLTRAPYIIVVF 194
Cdd:PRK13294 328 EESiarrvrrgDILYDAPELVVPF 351
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| iodotyrosine_dehalogenase |
cd02144 |
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ... |
92-284 |
5.26e-120 |
|
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: 341.44 E-value: 5.26e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 92 FYREMDTRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKLEVRLIIEEEERMNYEKRMSAQWLHD 171
Cdd:cd02144 1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREAAEEEEKEFYEKRMGEEWVWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 172 LEKLRLTWSKPYLTRAPYIIVVFKQLFRVTEEGKKTTNYYQEISASIATGFLLAAVHNAGLVTVTTTPMNaGPRLRTLLE 251
Cdd:cd02144 81 LKPLGTNWEKPYLTEAPYLIVVFKQKYGVLPDGKKKKHYYNEESVGIAVGILLAALHNAGLVTLTHTPSP-MPFLRDLLG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1229173765 252 RPISEKVLVLLPVGHPEDGATVPDLQRKALQEI 284
Cdd:cd02144 160 RPKNEKPLLLLPVGYPAEDATVPDLKRKPLEEI 192
|
|
| NfnB |
COG0778 |
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ... |
92-284 |
4.56e-30 |
|
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 440541 [Multi-domain] Cd Length: 163 Bit Score: 111.10 E-value: 4.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 92 FYREMDTRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKlevrliieeeermnyekrmsaqwlHD 171
Cdd:COG0778 1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELR------------------------ER 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 172 LEKLRLTWSKPYLTRAPYIIVVFKQlfrvTEEGKKTTNYYQEISASIATGFLLAAVHNAGLVTVTTTPMNAgPRLRTLLE 251
Cdd:COG0778 57 LAEALAEANQEWVADAPVLIVVCAD----PDRSEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDP-EKVRELLG 131
|
170 180 190
....*....|....*....|....*....|...
gi 1229173765 252 RPISEKVLVLLPVGHPEDgaTVPDLQRKALQEI 284
Cdd:COG0778 132 LPEGEEPVALLALGYPAE--ELNPRPRKPLEEV 162
|
|
| Nitroreductase |
pfam00881 |
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ... |
99-266 |
2.13e-21 |
|
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: 88.22 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 99 RRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKLEVRLIIEEEerMNYEKRMSAQWLHDLEKLRLT 178
Cdd:pfam00881 4 RRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALEL--LLVEPAAALLLLLRRDANLKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 179 WSKPYLTRAPYIIVVFKQLFRVTEEGKKTTNYYQEISASIATGFLLAAVHNAGLVTVTTTPMNAgPRLRTLLERPISEKV 258
Cdd:pfam00881 82 LLQDFLRGAPVLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDA-AAVRELLGLPDDERL 160
|
....*...
gi 1229173765 259 LVLLPVGH 266
Cdd:pfam00881 161 VGLIAVGY 168
|
|
| Nitro_FMN_reductase |
cd02062 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
96-266 |
2.36e-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: 87.35 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 96 MDTRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKLEVRLIIEeeermnyekrmsaqwlhdlekl 175
Cdd:cd02062 1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAKLAA---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 176 rltWSKPYLTRAPYIIVVFkqlfrvteEGKKTTNYYQEISASIATGFLLAAVHNAGLVTVTTTPMNAG-PRLRTLLERPI 254
Cdd:cd02062 59 ---PNQKFIAGAPVVIVVV--------ADPDKSRPWALEDAGAAAQNLLLAAAALGLGSCWIGGFDFReDKVRELLGIPE 127
|
170
....*....|..
gi 1229173765 255 SEKVLVLLPVGH 266
Cdd:cd02062 128 NLRPVALIAIGY 139
|
|
| nitroreductase |
cd20610 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
99-265 |
1.84e-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: 75.01 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 99 RRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKLEVRLIIEEEERmNYEKRMSAQWLHDLEKLRLT 178
Cdd:cd20610 4 RRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKIGISIKKKNE-EIARLLEKVFAEKPIRFRKF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 179 WSKPY-LTRAPYIIVVfkqLFRVTEEGKKTTNYYQEISASIATgFLLAAvHNAGLVTV-TTTPMNAGPRLRTLLERPISE 256
Cdd:cd20610 83 RRFFTlFGGAPVLVVV---YTEPYKPPEERKPDLQSVSAAIQN-LLLAA-HALGLGTCwMTGPLYAEDEIEEILEIPDDK 157
|
....*....
gi 1229173765 257 KVLVLLPVG 265
Cdd:cd20610 158 ELVAVTPLG 166
|
|
| PnbA_NfnB-like |
cd02136 |
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ... |
98-279 |
1.42e-12 |
|
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: 64.15 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 98 TRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQvklevrliieeeermnyekrmsaqwlhdLEKL-R 176
Cdd:cd02136 4 SRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTGKA----------------------------RERLkK 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 177 LTWSkpyltrAPYIIVVFkqlfrvteeGKKTTNYYQEISASIATGFLLAAVHNAGLVTVtttPMNAGPR----LRTLLER 252
Cdd:cd02136 56 AFFG------APVALFLT---------MDKVLGPWSWFDLGAFLQNLMLAAHALGLGTC---PQGALAGypdvVRKELGI 117
|
170 180
....*....|....*....|....*..
gi 1229173765 253 PISEKVLVLLPVGHPEDGATVPDLQRK 279
Cdd:cd02136 118 PDDEELVCGIALGYPDPDAPVNQFRTP 144
|
|
| BluB |
TIGR02476 |
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ... |
91-283 |
2.05e-12 |
|
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: 64.77 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 91 QFYREMDTRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKLEVRLIIEE---EERMNYEKRMSAQ 167
Cdd:TIGR02476 8 AVYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRanqAAAAIYDGERASQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 168 WlhdlEKLRLTWskpyLTRAPYIIVVFKQLFRVTEE--GKKTTNYYQEISASIATG-FLLAA-VHNAGLVTVTTTPMNAg 243
Cdd:TIGR02476 88 Y----HRLKLEG----IREAPVQLAVFCDDARGEGHglGRHTMPEMLRYSVACAIQnLWLAArAEGLGVGWVSILDPDA- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1229173765 244 prLRTLLERPISEKVLVLLPVGHPEDGATVPDLQRKALQE 283
Cdd:TIGR02476 159 --VRRLLGVPEGWRLVAYLCLGWPDAFYDEPELERAGWQE 196
|
|
| nitroreductase |
cd02150 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
98-268 |
2.19e-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: 63.39 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 98 TRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVklevrliieeeermnyekrmsaqwlhdLEKL-- 175
Cdd:cd02150 3 TRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREK---------------------------LDKIae 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 176 RLTWSKpYLTRAPYIIVVfkqlfRVTEEGKKTTNYYQEiSASIATGFLLAAVHNAGLVTVTTtpmNAGPR------LRTL 249
Cdd:cd02150 56 AHPYGK-MLKEAPLAIVV-----CGDPSKEKAPGYWVQ-DCSAATENILLAAHALGLGAVWL---GVYPFeervkaIREI 125
|
170
....*....|....*....
gi 1229173765 250 LERPISEKVLVLLPVGHPE 268
Cdd:cd02150 126 LNIPENIIPFCVIALGYPA 144
|
|
| nitroreductase |
cd03370 |
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ... |
96-270 |
4.80e-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: 63.49 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 96 MDTRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKlevrliieeeermnyekrmsaqwlhdlEKL 175
Cdd:cd03370 5 IESRRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELK---------------------------EQL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 176 R-LTWSKPYLTRAPYIIVVFKQL------------FRVTEEGKKTT-----NYYQEIS-----------ASIATGFLLAA 226
Cdd:cd03370 58 QaAAYGQAQVTSAPAVIVIYSDMedalanleetihPGLSEERRQREaaglrGAFGKMSveqrgqwglaqANIALGFLLLA 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1229173765 227 VHNAGLVTVtttPM---NAGpRLRTLLERPISEKVLVLLPVGHP-EDG 270
Cdd:cd03370 138 AQSLGYDTS---PMlgfDPE-KVKALLGLPEHVTIAALVALGKPaEEG 181
|
|
| nitroreductase |
cd02151 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
98-269 |
1.42e-11 |
|
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: 61.39 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 98 TRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKLEVRLIieeeermnyeKRMSAQWLHDleklrl 177
Cdd:cd02151 5 KRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKLSEC----------KPHGSAFLKG------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 178 twskpyltrAPYIIVVfkqlfrVTEEGKktTNYYQEiSASIATGFLLAAVHNAGLVT--------VTTTPMNAGPRLRTL 249
Cdd:cd02151 69 ---------APAAIVV------LADTEK--SDTWIE-DASIAATYIQLAAESLGLGScwiqirnrETQDGKTAEEYVREL 130
|
170 180
....*....|....*....|
gi 1229173765 250 LERPISEKVLVLLPVGHPED 269
Cdd:cd02151 131 LGIPENYRVLCIIALGYPDE 150
|
|
| nitroreductase |
cd02139 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
98-284 |
4.08e-11 |
|
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: 60.18 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 98 TRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKlevrliieeeermnyekrmsaqwlhdlEKL-R 176
Cdd:cd02139 7 KRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELK---------------------------EKLaE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 177 LTWSKPYLTRAPYIIV-VFKQLFRVTEEGKKttnYYQeISASIATGFLLAAVHNAGLVTVTTTPMNaGPRLRTLLERPIS 255
Cdd:cd02139 60 AANGQKFIAEAPVVIVaCADPSESGMGCGKP---YYL-VDVAIAMEHLVLAATEEGLGTCWIGAFD-EDKVKEILGIPEE 134
|
170 180
....*....|....*....|....*....
gi 1229173765 256 EKVLVLLPVGHPEDgaTVPDLQRKALQEI 284
Cdd:cd02139 135 YRVVALTPLGYPAE--EPPPRPRKPLEEI 161
|
|
| nitroreductase |
cd20608 |
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ... |
98-266 |
4.38e-11 |
|
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: 59.66 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 98 TRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVklevrliieeeermnyekrmsaqwlhdLEKLRL 177
Cdd:cd20608 6 TRRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKET---------------------------LSELAK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 178 TWSKP--YLTRAPYIIVVfkqlfrVTEEGKKTT----NYYQeISASIATGFLLAAVHNAGLVTVTTTPMNAGpRLRTLLE 251
Cdd:cd20608 59 KESPSngWLKDAPVIIVV------CADPKDSGWlngqNYYL-VDAAIAMQNLMLAATDLGLGTCWIGAFDEK-KVKEILG 130
|
170
....*....|....*
gi 1229173765 252 RPISEKVLVLLPVGH 266
Cdd:cd20608 131 IPENIRVVALTPLGY 145
|
|
| nitroreductase_FeS-like |
cd02143 |
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ... |
98-193 |
1.10e-10 |
|
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: 59.41 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 98 TRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKLEVR-LIIEEEERMNYEKRMSAQWLHdLEKLR 176
Cdd:cd02143 4 SRRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLAeLVIDWMRELIKEDPELAGKLF-LDGIV 82
|
90 100
....*....|....*....|
gi 1229173765 177 LTWSK---PYLTRAPYIIVV 193
Cdd:cd02143 83 AAWEKgidVILRGAPHLVVA 102
|
|
| BluB |
cd02145 |
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ... |
93-283 |
3.17e-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: 58.52 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 93 YREMDTRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKLEVRLIIEE---EERMNYEKRMSAQWl 169
Cdd:cd02145 1 YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRanaEAAEMYTGERAAQY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 170 hdlEKLRLTWskpyLTRAPYIIVVFKQLFRVTEE--GKKTTNYYQEISASIATG--FLLAAVHNAGLVTVTTTPMNagpR 245
Cdd:cd02145 80 ---RTLKLEG----IEEAPLQLAVFCDRARAGGHglGRTTMPEMDLYSSVCAVQnlWLAARAEGLGVGWVSILDPD---E 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 1229173765 246 LRTLLERPISEKVLVLLPVGHPEDGATVPDLQRKALQE 283
Cdd:cd02145 150 VKRLLGIPEHWEPVAYLCIGYPEFFYDEPELEQAGWEQ 187
|
|
| MhqN-like |
cd02137 |
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ... |
96-284 |
5.88e-10 |
|
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: 56.48 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 96 MDTRRSVRDI-SDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKlevrliieeeermnyekrmsaqwlhdlEK 174
Cdd:cd02137 4 IKSRRSVRNFdPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELK---------------------------AK 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 175 LR-LTWSKPYLTRAPYIIVVFKQLfrvteegkkttnyyqeiSASIATGFLLAAVHNAGLVtvtTTPMNA--GPRLRTLLE 251
Cdd:cd02137 57 LAeAAYNQPQVTTASAVILVLGDL-----------------NAGLAAMNLMLAAKAKGYD---TCPMGGfdKEKVAELLN 116
|
170 180 190
....*....|....*....|....*....|...
gi 1229173765 252 RPISEKVLVLLPVGHPEDGAtvPDLQRKALQEI 284
Cdd:cd02137 117 LPDRYVPVLLIAIGKAADKA--PRSGRLPVDEV 147
|
|
| YdjA-like |
cd02135 |
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ... |
98-266 |
3.05e-08 |
|
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: 52.22 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 98 TRRSVRD-ISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKLEVRLIIEEEERMnyEKRMSAqwlHDLEKLR 176
Cdd:cd02135 6 TRRSIRKfKLTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGEGRERLAELLAAAAAAR--APGADP---EKLEKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 177 ltwSKPylTRAPYIIVVFKQLfrvtEEGKKTTNYYQEISASIAT-GFLLAAvHNAGLVTV-TTTPMNAGPRLRTLLERPI 254
Cdd:cd02135 81 ---EKA--LRAPVVIAVVAKP----DEDPKVPEWEQYAAVGAAVqNLLLAA-HALGLGAVwRTGPVTYDPAVREALGLPE 150
|
170
....*....|..
gi 1229173765 255 SEKVLVLLPVGH 266
Cdd:cd02135 151 DERIVGFLYLGT 162
|
|
| PRK13294 |
PRK13294 |
F420-0--gamma-glutamyl ligase; Provisional |
99-194 |
5.21e-08 |
|
F420-0--gamma-glutamyl ligase; Provisional
Pssm-ID: 183957 [Multi-domain] Cd Length: 448 Bit Score: 53.48 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 99 RRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPQVKleVRLIieeeermnyeKRMSAQWLHDLEKLRLT 178
Cdd:PRK13294 260 RRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVR--TRLL----------DAMRDAWRADLRADGLS 327
|
90 100
....*....|....*....|....
gi 1229173765 179 WSK--------PYLTRAPYIIVVF 194
Cdd:PRK13294 328 EESiarrvrrgDILYDAPELVVPF 351
|
|
| nitroreductase |
cd20609 |
nitroreductase family protein; A subfamily of the nitroreductase family containing ... |
99-266 |
1.42e-07 |
|
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: 49.69 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 99 RRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFavlsnpqvklevrLIIEEEErmnyekrmsaqwlhDLEKLRLT 178
Cdd:cd20609 9 RYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRI-------------LVVRSEE--------------ALEKLAKA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 179 WskPYLTRAPYIIVV-------FKQLFrvteEGKKTTnyyqEISASIA-TGFLLAAvHNAGLVTVTTTPMNAgPRLRTLL 250
Cdd:cd20609 62 T--PRFFGAPLVIVVcydkdesWKRPY----DGKDSG----DIDAAIVaTHMMLAA-TELGLGTCWVGNFDP-EKVREAF 129
|
170
....*....|....*.
gi 1229173765 251 ERPISEKVLVLLPVGH 266
Cdd:cd20609 130 NLPENLEPVAILPLGY 145
|
|
| TdsD-like |
cd02138 |
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ... |
99-284 |
1.82e-07 |
|
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: 49.85 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 99 RRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSnpqvklevrliiEEEErmNYEKrmsaqwLHD-LEKLRL 177
Cdd:cd02138 5 RWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFVVAR------------RDTE--AFEK------LLDlLAEGNQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 178 TWSKpyltRAPYIIVVF-KQLFrvTEEGKKttNYYQEISASIATGFL-LAAVHnAGLVtvtTTPMnAG---PRLRTLLER 252
Cdd:cd02138 65 SWAK----NAPVLIVVLaKTEF--DHNGKP--NRYALFDTGAAVANLaLQATA-LGLV---VHQM-AGfdpEKAKEALGI 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1229173765 253 PISEKVLVLLPVGHPEDGATVPDLQ---------RKALQEI 284
Cdd:cd02138 132 PDEYEPITMIAIGYPGDPESLPEKLlereeaprtRKPLSEI 172
|
|
| NfsA-like |
cd02146 |
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ... |
96-280 |
6.18e-05 |
|
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: 43.38 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 96 MDTRRSVRDISDKPVPLEVIENCIRMAGTAPSGAHMQPWTFAVLSNPqvklevrliieeeermnyEKRmsaqwlhdlEKL 175
Cdd:cd02146 5 ILNHRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDP------------------ELR---------EKL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 176 -RLTWSKPYLTRAP--YIIVV-FKQLFRVTEEGKKTTNYYQE--------ISASIATGFLLAAVHNAGLVTVTTTPMNAG 243
Cdd:cd02146 58 aELAGNQPYVAQAPvfLVFCAdLYRHQKIAEEAGGKDVGLDYlesflvgvVDAALAAQNALVAAESLGLGIVYIGGIRNN 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1229173765 244 P-RLRTLLERPisEKVLVL--LPVGHPEDGATV-PDLQRKA 280
Cdd:cd02146 138 PeEVIELLGLP--EYVFPLfgLTVGHPDPTPEVkPRLPLEA 176
|
|
| NfsB-like |
cd02149 |
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ... |
96-266 |
2.48e-04 |
|
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: 40.70 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 96 MDTRRSVRDI-SDKPVP---LEVIENCIRMAgtaPSGAHMQPWTFAVLSNPQVKLEVRliieeeermnyekrmSAQWlhd 171
Cdd:cd02149 6 LNFRYATKKFdPNKKISdedLETILEALRLS---PSSFGLEPWKFLVVENPELKAKLA---------------PAAW--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 172 leklrltWSKPYLTRAPYIIVVFKQlfrvTEEGKKTTnYyqeisasIATGFLLAAvhnAGLVTVTTTPM---NAGPRLRT 248
Cdd:cd02149 65 -------FNQPQIKDASHVVVFLAK----KDWSAKQT-Y-------IALGNMLLA---AAMLGIDSCPIegfDPAKLDEI 122
|
170
....*....|....*...
gi 1229173765 249 LLERPISEKVLVLLPVGH 266
Cdd:cd02149 123 LGLDEKGYKISVMVAFGY 140
|
|
| PRK10828 |
PRK10828 |
putative oxidoreductase; Provisional |
99-219 |
1.38e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182761 Cd Length: 183 Bit Score: 38.90 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229173765 99 RRSVRDISDkPVPL-EVIENCIRMAGTAPSGAHMQPWTFavlsnpqvklevrLIIEEEERmnyeKRMSaQWLHD------ 171
Cdd:PRK10828 10 RRSASRLAE-PAPTgEQLQNILRAGMRAPDHGSLQPWRF-------------FVIEGEGR----ERFS-ALLEQgaiaag 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1229173765 172 -----LEKLRltwSKPYltRAPYIIVVFKQLfrvtEEGKKTTNYYQEISASIA 219
Cdd:PRK10828 71 sdekaIEKAR---NAPF--RAPLIITVVAKC----EENHKVPRWEQEVSAGCA 114
|
|
| |
