|
Name |
Accession |
Description |
Interval |
E-value |
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
9-311 |
4.32e-117 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 339.78 E-value: 4.32e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 9 LGIQYPIVQGGLAYLAYAELAAAVSNAGGLGQITAMTLrTPEKLRAEIKKVRSLTERPFGVNFAVGgQTEGSYKELLDAA 88
Cdd:COG2070 1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNL-TPEALREEIRKIRELTDGPFGVNLIVH-PANPRFEELLEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 89 VEEGVPVISITGANPAPIFERLKGTGIKTLVLVANVRQAQKAEKLGADAVMAVGQEAGGHIGREDLGTMVLIPRVAAAVS 168
Cdd:COG2070 79 LEEGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVREARKAEKAGADAVVAEGAEAGGHRGADEVSTFALVPEVRDAVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 169 IPVLASGGIGNGQGLLAALSLGAEGIEMGTRFIATKECvDAHDAYKQAIIEAKETDTVVIKRSFGAPGRVLKSHYTLDII 248
Cdd:COG2070 159 IPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEES-PAHEAYKQALVDAKEEDTVLTRSFTGRPARALRNSFTREGL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723602993 249 KREEQGErYEELKDVISGGANCRYIYENKIDEGYGWAGQVVGLIDSIPTVQELFDSMIEEVHA 311
Cdd:COG2070 238 DLEAECL-YPILEALTAGKRLRAAAAEGDLEKGLLWAGQGAGLIRDILPAAELVARLVAEAEA 299
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
11-239 |
4.59e-90 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 268.58 E-value: 4.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 11 IQYPIVQGGLAYLAYAELAAAVSNAGGLGQITAMTLrTPEKLRAEIKKVRSLTERPFGVNFAVGgQTEGSYKELLDAAVE 90
Cdd:cd04730 1 IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYL-TPEALRAEIRKIRALTDKPFGVNLLVP-SSNPDFEALLEVALE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 91 EGVPVISITGANPAPIFERLKGTGIKTLVLVANVRQAQKAEKLGADAVMAVGQEAGGHIGREDLGTMVLIPRVAAAVSIP 170
Cdd:cd04730 79 EGVPVVSFSFGPPAEVVERLKAAGIKVIPTVTSVEEARKAEAAGADALVAQGAEAGGHRGTFDIGTFALVPEVRDAVDIP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 723602993 171 VLASGGIGNGQGLLAALSLGAEGIEMGTRFIATKECvDAHDAYKQAIIEAKETDTVVIKRSFGAPGRVL 239
Cdd:cd04730 159 VIAAGGIADGRGIAAALALGADGVQMGTRFLATEES-GASPAYKQALLAATAEDTVLTRAFSGRPARGL 226
|
|
| enACPred_II |
TIGR03151 |
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane ... |
2-316 |
9.26e-85 |
|
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane dioxygenase family (pfam03060) is commonly found in apparent operons with genes involved in fatty acid biosynthesis. Furthermore, this genomic context generally includes the fabG 3-oxoacyl-[ACP] reductase and lacks the fabI enoyl-[ACP] reductase.
Pssm-ID: 132195 Cd Length: 307 Bit Score: 257.76 E-value: 9.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 2 KTRVTDLLGIQYPIVQGGLAYLAYAELAAAVSNAGGLGQITAMTlRTPEKLRAEIKKVRSLTERPFGVNFAVggqTEGSY 81
Cdd:TIGR03151 1 KTRLCDLLGIEYPIFQGGMAWVATGSLAAAVSNAGGLGIIGAGN-APPDVVRKEIRKVKELTDKPFGVNIML---LSPFV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 82 KELLDAAVEEGVPVISITGANPAPIFERLKGTGIKTLVLVANVRQAQKAEKLGADAVMAVGQEAGGHIGreDLGTMVLIP 161
Cdd:TIGR03151 77 DELVDLVIEEKVPVVTTGAGNPGKYIPRLKENGVKVIPVVASVALAKRMEKAGADAVIAEGMESGGHIG--ELTTMALVP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 162 RVAAAVSIPVLASGGIGNGQGLLAALSLGAEGIEMGTRFIATKECvDAHDAYKQAIIEAKETDTVVIKRSFGAPGRVLKS 241
Cdd:TIGR03151 155 QVVDAVSIPVIAAGGIADGRGMAAAFALGAEAVQMGTRFLCAKEC-NVHPNYKEKVLKAKDRDTVVTGASTGHPVRVLKN 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 723602993 242 HYTLDIIKREEQGERYEELkDVISGGANCRYIYENKIDEGYGWAGQVVGLIDSIPTVQELFDSMIEEVHAGSKRL 316
Cdd:TIGR03151 234 KLTRKYQELEKEGASPEEF-EKLGAGALRRAVVEGDVENGSVMAGQIAGLIKEIKPAKEIIEDIMSEAKEVIKRL 307
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
2-308 |
6.33e-65 |
|
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.
Pssm-ID: 367316 [Multi-domain] Cd Length: 331 Bit Score: 207.75 E-value: 6.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 2 KTRVTDLLGIQYPIVQGGLAYLAYAELAAAVSNAGGLGQITAMTLrTPEKLRAEIKKVRSLTERPFGVNF-----AVGGQ 76
Cdd:pfam03060 1 KSLLTDIHTIKPPVQQPMMGGISWPRLAAAVSNAGGLGVLASGYL-TPDRLYQEIRKVKALTDKPFGANLflpkpDLADP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 77 TEGSYKELLDAAVE------------------EGVPVISIT-GANPAPIFERLKGTGIKTLVLVANVRQAQKAEKLGADA 137
Cdd:pfam03060 80 AANYAKILGNNALGynieegvpdygkvlvdldEGVNVVSFGfGLPPNDVVFRLHFAGVALIPTISSAKEARIAEARGADA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 138 VMAVGQEAGGHIGR---EDLGTMVLIPRVAAAVSIPVLASGGIGNGQGLLAALSLGAEGIEMGTRFIATKECvDAHDAYK 214
Cdd:pfam03060 160 LIVQGPEAGGHQGTpeyGDKGLFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTRFLLTKES-GAHDAHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 215 QAIIEAKETDTVVIKRSFGAPGRVLKShytlDIIKREEQG--------ERYEELKDVISGGANcryiyENKIDEGYGWAG 286
Cdd:pfam03060 239 QKITEAGEDDTLVTSPFSGRPARALAN----GFLEELEEPkiatlaypEAHEMTKPIRAAAVR-----GGNREEGLLWAG 309
|
330 340
....*....|....*....|..
gi 723602993 287 QVVGLIDSIPTVQELFDSMIEE 308
Cdd:pfam03060 310 QGIYRLDRIISVKELIESLTEE 331
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
53-205 |
3.39e-07 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 51.59 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 53 RAEIKKVRSL---------TERPFGVNFAVGgqTEGSYKELLDAAVEEGVPVISITGANPAPIFER-----LKGTGIKTL 118
Cdd:PLN02274 214 RTDVKRVKGYpklgkpsvgKDGKLLVGAAIG--TRESDKERLEHLVKAGVDVVVLDSSQGDSIYQLemikyIKKTYPELD 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 119 VLVANV---RQAQKAEKLGADAV---MAVG-----QEAGGhIGREDLGTMVLIPRVAAAVSIPVLASGGIGNGQGLLAAL 187
Cdd:PLN02274 292 VIGGNVvtmYQAQNLIQAGVDGLrvgMGSGsicttQEVCA-VGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKAL 370
|
170
....*....|....*...
gi 723602993 188 SLGAEGIEMGTRFIATKE 205
Cdd:PLN02274 371 TLGASTVMMGSFLAGTTE 388
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
9-311 |
4.32e-117 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 339.78 E-value: 4.32e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 9 LGIQYPIVQGGLAYLAYAELAAAVSNAGGLGQITAMTLrTPEKLRAEIKKVRSLTERPFGVNFAVGgQTEGSYKELLDAA 88
Cdd:COG2070 1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNL-TPEALREEIRKIRELTDGPFGVNLIVH-PANPRFEELLEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 89 VEEGVPVISITGANPAPIFERLKGTGIKTLVLVANVRQAQKAEKLGADAVMAVGQEAGGHIGREDLGTMVLIPRVAAAVS 168
Cdd:COG2070 79 LEEGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVREARKAEKAGADAVVAEGAEAGGHRGADEVSTFALVPEVRDAVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 169 IPVLASGGIGNGQGLLAALSLGAEGIEMGTRFIATKECvDAHDAYKQAIIEAKETDTVVIKRSFGAPGRVLKSHYTLDII 248
Cdd:COG2070 159 IPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEES-PAHEAYKQALVDAKEEDTVLTRSFTGRPARALRNSFTREGL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723602993 249 KREEQGErYEELKDVISGGANCRYIYENKIDEGYGWAGQVVGLIDSIPTVQELFDSMIEEVHA 311
Cdd:COG2070 238 DLEAECL-YPILEALTAGKRLRAAAAEGDLEKGLLWAGQGAGLIRDILPAAELVARLVAEAEA 299
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
11-239 |
4.59e-90 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 268.58 E-value: 4.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 11 IQYPIVQGGLAYLAYAELAAAVSNAGGLGQITAMTLrTPEKLRAEIKKVRSLTERPFGVNFAVGgQTEGSYKELLDAAVE 90
Cdd:cd04730 1 IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYL-TPEALRAEIRKIRALTDKPFGVNLLVP-SSNPDFEALLEVALE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 91 EGVPVISITGANPAPIFERLKGTGIKTLVLVANVRQAQKAEKLGADAVMAVGQEAGGHIGREDLGTMVLIPRVAAAVSIP 170
Cdd:cd04730 79 EGVPVVSFSFGPPAEVVERLKAAGIKVIPTVTSVEEARKAEAAGADALVAQGAEAGGHRGTFDIGTFALVPEVRDAVDIP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 723602993 171 VLASGGIGNGQGLLAALSLGAEGIEMGTRFIATKECvDAHDAYKQAIIEAKETDTVVIKRSFGAPGRVL 239
Cdd:cd04730 159 VIAAGGIADGRGIAAALALGADGVQMGTRFLATEES-GASPAYKQALLAATAEDTVLTRAFSGRPARGL 226
|
|
| enACPred_II |
TIGR03151 |
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane ... |
2-316 |
9.26e-85 |
|
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane dioxygenase family (pfam03060) is commonly found in apparent operons with genes involved in fatty acid biosynthesis. Furthermore, this genomic context generally includes the fabG 3-oxoacyl-[ACP] reductase and lacks the fabI enoyl-[ACP] reductase.
Pssm-ID: 132195 Cd Length: 307 Bit Score: 257.76 E-value: 9.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 2 KTRVTDLLGIQYPIVQGGLAYLAYAELAAAVSNAGGLGQITAMTlRTPEKLRAEIKKVRSLTERPFGVNFAVggqTEGSY 81
Cdd:TIGR03151 1 KTRLCDLLGIEYPIFQGGMAWVATGSLAAAVSNAGGLGIIGAGN-APPDVVRKEIRKVKELTDKPFGVNIML---LSPFV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 82 KELLDAAVEEGVPVISITGANPAPIFERLKGTGIKTLVLVANVRQAQKAEKLGADAVMAVGQEAGGHIGreDLGTMVLIP 161
Cdd:TIGR03151 77 DELVDLVIEEKVPVVTTGAGNPGKYIPRLKENGVKVIPVVASVALAKRMEKAGADAVIAEGMESGGHIG--ELTTMALVP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 162 RVAAAVSIPVLASGGIGNGQGLLAALSLGAEGIEMGTRFIATKECvDAHDAYKQAIIEAKETDTVVIKRSFGAPGRVLKS 241
Cdd:TIGR03151 155 QVVDAVSIPVIAAGGIADGRGMAAAFALGAEAVQMGTRFLCAKEC-NVHPNYKEKVLKAKDRDTVVTGASTGHPVRVLKN 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 723602993 242 HYTLDIIKREEQGERYEELkDVISGGANCRYIYENKIDEGYGWAGQVVGLIDSIPTVQELFDSMIEEVHAGSKRL 316
Cdd:TIGR03151 234 KLTRKYQELEKEGASPEEF-EKLGAGALRRAVVEGDVENGSVMAGQIAGLIKEIKPAKEIIEDIMSEAKEVIKRL 307
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
2-308 |
6.33e-65 |
|
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.
Pssm-ID: 367316 [Multi-domain] Cd Length: 331 Bit Score: 207.75 E-value: 6.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 2 KTRVTDLLGIQYPIVQGGLAYLAYAELAAAVSNAGGLGQITAMTLrTPEKLRAEIKKVRSLTERPFGVNF-----AVGGQ 76
Cdd:pfam03060 1 KSLLTDIHTIKPPVQQPMMGGISWPRLAAAVSNAGGLGVLASGYL-TPDRLYQEIRKVKALTDKPFGANLflpkpDLADP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 77 TEGSYKELLDAAVE------------------EGVPVISIT-GANPAPIFERLKGTGIKTLVLVANVRQAQKAEKLGADA 137
Cdd:pfam03060 80 AANYAKILGNNALGynieegvpdygkvlvdldEGVNVVSFGfGLPPNDVVFRLHFAGVALIPTISSAKEARIAEARGADA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 138 VMAVGQEAGGHIGR---EDLGTMVLIPRVAAAVSIPVLASGGIGNGQGLLAALSLGAEGIEMGTRFIATKECvDAHDAYK 214
Cdd:pfam03060 160 LIVQGPEAGGHQGTpeyGDKGLFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTRFLLTKES-GAHDAHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 215 QAIIEAKETDTVVIKRSFGAPGRVLKShytlDIIKREEQG--------ERYEELKDVISGGANcryiyENKIDEGYGWAG 286
Cdd:pfam03060 239 QKITEAGEDDTLVTSPFSGRPARALAN----GFLEELEEPkiatlaypEAHEMTKPIRAAAVR-----GGNREEGLLWAG 309
|
330 340
....*....|....*....|..
gi 723602993 287 QVVGLIDSIPTVQELFDSMIEE 308
Cdd:pfam03060 310 QGIYRLDRIISVKELIESLTEE 331
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
56-198 |
1.73e-08 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 53.74 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 56 IKKVRSLTERPFGVNFAVGGqTEGSYKELLDAAVEEGVPVISITGANPAP----------IFERLKGTGIKTLVLVANVR 125
Cdd:cd04722 49 LKEVAAETDLPLGVQLAIND-AAAAVDIAAAAARAAGADGVEIHGAVGYLaredlelireLREAVPDVKVVVKLSPTGEL 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723602993 126 QAQKAEKLGADAVMAVGQEAGGHIGREDLGTMVLIPRVAAAVSIPVLASGGIGNGQGLLAALSLGAEGIEMGT 198
Cdd:cd04722 128 AAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
53-205 |
3.39e-07 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 51.59 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 53 RAEIKKVRSL---------TERPFGVNFAVGgqTEGSYKELLDAAVEEGVPVISITGANPAPIFER-----LKGTGIKTL 118
Cdd:PLN02274 214 RTDVKRVKGYpklgkpsvgKDGKLLVGAAIG--TRESDKERLEHLVKAGVDVVVLDSSQGDSIYQLemikyIKKTYPELD 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 119 VLVANV---RQAQKAEKLGADAV---MAVG-----QEAGGhIGREDLGTMVLIPRVAAAVSIPVLASGGIGNGQGLLAAL 187
Cdd:PLN02274 292 VIGGNVvtmYQAQNLIQAGVDGLrvgMGSGsicttQEVCA-VGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKAL 370
|
170
....*....|....*...
gi 723602993 188 SLGAEGIEMGTRFIATKE 205
Cdd:PLN02274 371 TLGASTVMMGSFLAGTTE 388
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
121-197 |
6.96e-07 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 50.13 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 121 VANVRQAQKAEKLGADAVMaVGqeagGHIGRE-D--LGTMVLIPRVAAAV--SIPVLASGGIGNGQGLLAALSLGAEGIE 195
Cdd:COG1304 233 VLSPEDARRAVDAGVDGID-VS----NHGGRQlDggPPTIDALPEIRAAVggRIPVIADGGIRRGLDVAKALALGADAVG 307
|
..
gi 723602993 196 MG 197
Cdd:COG1304 308 LG 309
|
|
| NPD_PKS |
cd04743 |
2-Nitropropane dioxygenase (NPD)-like domain, associated with polyketide synthases (PKS). NPD ... |
12-224 |
2.19e-06 |
|
2-Nitropropane dioxygenase (NPD)-like domain, associated with polyketide synthases (PKS). NPD is part of the nitroalkaneoxidizing enzyme family, that catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDPs are members of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240094 Cd Length: 320 Bit Score: 48.66 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 12 QYPIVQGGLAYLAYAEL-AAAVSNAGGLGQItAMTLRTPEKLRAEIKKVRS-LTERPFGVNFaVGGQTEGSYKELLDAAV 89
Cdd:cd04743 2 RYPIVQGPMTRVSDVAEfAVAVAEGGGLPFI-ALALMRGEQVKALLEETAElLGDKPWGVGI-LGFVDTELRAAQLAVVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 90 EEGVPVISITGANPAPIFErLKGTGIKTLVLVANVRQAQKAEKLGADAVMAVGQEAGGHIGreDLGTMVL---------- 159
Cdd:cd04743 80 AIKPTFALIAGGRPDQARA-LEAIGISTYLHVPSPGLLKQFLENGARKFIFEGRECGGHVG--PRSSFVLwesaidalla 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 723602993 160 --IPRvaAAVSIPVLASGGIGNG------QGLLAALS-LGAE-GIEMGTRFIATKECVDA---HDAYKQAIIEAKETD 224
Cdd:cd04743 157 anGPD--KAGKIHLLFAGGIHDErsaamvSALAAPLAeRGAKvGVLMGTAYLFTEEAVSAgaiLPTFQDQAIAATRTA 232
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
69-205 |
2.48e-06 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 48.81 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 69 VNFAVGgqTEGSYKELLDAAVEEGVPVISITGANPAPIF-----ERLKGTGIKTLVLVANVRQAQKAEKL---GADAV-- 138
Cdd:PTZ00314 232 VGAAIS--TRPEDIERAAALIEAGVDVLVVDSSQGNSIYqidmiKKLKSNYPHVDIIAGNVVTADQAKNLidaGADGLri 309
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723602993 139 -MAVG-----QEAGGhIGREDLGTMVLIPRVAAAVSIPVLASGGIGNGQGLLAALSLGAEGIEMGTRFIATKE 205
Cdd:PTZ00314 310 gMGSGsicitQEVCA-VGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEE 381
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
110-197 |
1.30e-04 |
|
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.
Pssm-ID: 239203 [Multi-domain] Cd Length: 299 Bit Score: 42.82 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 110 LKGtgiktlvlVANVRQAQKAEKLGADAVMAvgqeaGGHIGRE-D--LGTMVLIPRVAAAV--SIPVLASGGIGNGQGLL 184
Cdd:cd02809 177 LKG--------ILTPEDALRAVDAGADGIVV-----SNHGGRQlDgaPATIDALPEIVAAVggRIEVLLDGGIRRGTDVL 243
|
90
....*....|...
gi 723602993 185 AALSLGAEGIEMG 197
Cdd:cd02809 244 KALALGADAVLIG 256
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
36-206 |
1.42e-04 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 42.89 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 36 GGLGQITAMTlrTPEKLRAEIKKVRsltERPFgVNFAVGgqTEGSYKELLDAAVEEGVPVISITGANPAPIF-----ERL 110
Cdd:cd00381 58 GGIGVIHRNM--SIEEQAEEVRKVK---GRLL-VGAAVG--TREDDKERAEALVEAGVDVIVIDSAHGHSVYviemiKFI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 111 KGTGIKTLVLVANVRQAQKAEKL---GADAVMaVGQEAG-GHIGREDLGTMV----LIPRVAAAVS---IPVLASGGIGN 179
Cdd:cd00381 130 KKKYPNVDVIAGNVVTAEAARDLidaGADGVK-VGIGPGsICTTRIVTGVGVpqatAVADVAAAARdygVPVIADGGIRT 208
|
170 180
....*....|....*....|....*..
gi 723602993 180 GQGLLAALSLGAEGIEMGTRFIATKEC 206
Cdd:cd00381 209 SGDIVKALAAGADAVMLGSLLAGTDES 235
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
123-194 |
3.62e-04 |
|
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 40.94 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 123 NVRQAQKAEKLGADAVmAVG--------QEAGGHIGREDLGtmvlipRVAAAVSIPVLASGGIG--NGQGLLAAlslGAE 192
Cdd:COG0352 109 SLEEALRAEEAGADYV-GFGpvfptptkPGAPPPLGLEGLA------WWAELVEIPVVAIGGITpeNAAEVLAA---GAD 178
|
..
gi 723602993 193 GI 194
Cdd:COG0352 179 GV 180
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
127-201 |
5.78e-04 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 41.16 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 127 AQKAEKLGADAVMAvgqeaGGHIGRE-D--LGTMVLIPRVAAAVS--IPVLASGGIGNGQGLLAALSLGAEGIEMGTRFI 201
Cdd:PRK11197 259 ARDAVRFGADGIVV-----SNHGGRQlDgvLSSARALPAIADAVKgdITILADSGIRNGLDVVRMIALGADTVLLGRAFV 333
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
110-197 |
6.65e-04 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 40.98 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 110 LKGtgiktlvlVANVRQAQKAEKLGADAVMaVGqeagGHIGRE-D--LGTMVLIPRVAAAV--SIPVLASGGIGNGQGLL 184
Cdd:pfam01070 223 VKG--------ILSPEDAKRAVEAGVDGIV-VS----NHGGRQlDgaPATIDALPEIVAAVggRIPVLVDGGIRRGTDVL 289
|
90
....*....|...
gi 723602993 185 AALSLGAEGIEMG 197
Cdd:pfam01070 290 KALALGADAVLLG 302
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
121-194 |
8.57e-04 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 40.00 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 121 VANVRQAQKAEKLGADAVMAvgqeagGHI-------GREDLGtMVLIPRVAAAVSIPVLASGGI--GNGQGLLAAlslGA 191
Cdd:PRK07695 102 VHSLEEAIQAEKNGADYVVY------GHVfptdckkGVPARG-LEELSDIARALSIPVIAIGGItpENTRDVLAA---GV 171
|
...
gi 723602993 192 EGI 194
Cdd:PRK07695 172 SGI 174
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
39-198 |
8.99e-04 |
|
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 40.23 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 39 GQITAMTLRTP--EKLRAEIKKVRSLTERPFGVNfaVGGQTEGSYKELLDAAVEEGVPVISIT-------------GANP 103
Cdd:cd04740 62 GMLNAIGLQNPgvEAFLEELLPWLREFGTPVIAS--IAGSTVEEFVEVAEKLADAGADAIELNiscpnvkgggmafGTDP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 104 ---APIFERLKG-TGIKTLV-LVANV----RQAQKAEKLGADAVMAVGQEAGGHI----GREDLGTMV------------ 158
Cdd:cd04740 140 eavAEIVKAVKKaTDVPVIVkLTPNVtdivEIARAAEEAGADGLTLINTLKGMAIdietRKPILGNVTgglsgpaikpia 219
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 723602993 159 --LIPRVAAAVSIPVLASGGIGNGQGLLAALSLGAEGIEMGT 198
Cdd:cd04740 220 lrMVYQVYKAVEIPIIGVGGIASGEDALEFLMAGASAVQVGT 261
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
126-217 |
9.40e-04 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 40.50 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 126 QAQKAEKLGADAVMAVGQEAGGHIGREDLGTMVLIprvAAAVSIPVLASGGIGNGQGLLAALSLGAEGIEMGTRFIATKE 205
Cdd:PRK11840 210 AAKRLEDAGAVAVMPLGAPIGSGLGIQNPYTIRLI---VEGATVPVLVDAGVGTASDAAVAMELGCDGVLMNTAIAEAKN 286
|
90
....*....|..
gi 723602993 206 CVDAHDAYKQAI 217
Cdd:PRK11840 287 PVLMARAMKLAV 298
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
121-178 |
1.71e-03 |
|
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.
Pssm-ID: 240078 Cd Length: 283 Bit Score: 39.54 E-value: 1.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723602993 121 VANVRQAQKAEKLGADAVMAVGQ-----EAGGHIGRedLGTMVLIPRVAAAVSIPVLASGGIG 178
Cdd:cd04727 15 VTNAEQARIAEEAGAVAVMALERvpadiRAAGGVAR--MADPKMIKEIMDAVSIPVMAKVRIG 75
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
119-197 |
1.88e-03 |
|
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).
Pssm-ID: 240087 Cd Length: 361 Bit Score: 39.43 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 119 VLVANVRQAQKAEK---LGADAVMAvgqeaGGHIGREDLGT---MVLIPRVAAAVSIPVLASGGIGNGQGLLAALSLGAE 192
Cdd:cd04736 239 LLVKGIVTAEDAKRcieLGADGVIL-----SNHGGRQLDDAiapIEALAEIVAATYKPVLIDSGIRRGSDIVKALALGAN 313
|
....*
gi 723602993 193 GIEMG 197
Cdd:cd04736 314 AVLLG 318
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
121-178 |
5.11e-03 |
|
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine/pyridoxal 5-phosphate biosynthesis. This family was formerly known as UPF0019.
Pssm-ID: 460291 Cd Length: 206 Bit Score: 37.46 E-value: 5.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723602993 121 VANVRQAQKAEKLGADAVMAVGQ-----EAGGHIGRedLGTMVLIPRVAAAVSIPVLASGGIG 178
Cdd:pfam01680 20 VTNAEQAKIAEEAGAVAVMALERvpadiRKAGGVAR--MSDPKMIKEIMDAVSIPVMAKARIG 80
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
163-194 |
5.45e-03 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 37.46 E-value: 5.45e-03
10 20 30
....*....|....*....|....*....|..
gi 723602993 163 VAAAVSIPVLASGGIGNGQGLLAALSLGAEGI 194
Cdd:pfam00977 185 LAEAVNIPVIASGGVGSLEDLKELFTEGVDGV 216
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
121-194 |
8.76e-03 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 36.73 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723602993 121 VANVRQAQKAEKLGADAVmAVG--------QEAGGHIGREDLGtmvlipRVAAAVSIPVLASGGIG--NGQGLLAAlslG 190
Cdd:cd00564 102 THSLEEALRAEELGADYV-GFGpvfptptkPGAGPPLGLELLR------EIAELVEIPVVAIGGITpeNAAEVLAA---G 171
|
....
gi 723602993 191 AEGI 194
Cdd:cd00564 172 ADGV 175
|
|
| |
