|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10550 |
PRK10550 |
tRNA dihydrouridine(16) synthase DusC; |
1-312 |
0e+00 |
|
tRNA dihydrouridine(16) synthase DusC;
Pssm-ID: 236713 Cd Length: 312 Bit Score: 693.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 1 MRVLLAPMEGVLDSLVRELLTEVNDYDLCITEFVRVVDQLLPVKVFHRICPELQNASRTPSGTLVRVQLLGQFPQWLAEN 80
Cdd:PRK10550 1 MRVLLAPMEGVLDSLVRELLTEVNDYDLCITEFLRVVDQLLPVKVFHRLCPELHNASRTPSGTLVRIQLLGQYPQWLAEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 81 AARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVPAHLPVSVKVRLGWDSGEKKFEIADAVQQA 160
Cdd:PRK10550 81 AARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVPAHLPVTVKVRLGWDSGERKFEIADAVQQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 161 GATELVVHGRTKEQGYRAEHIDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVKYN 240
Cdd:PRK10550 161 GATELVVHGRTKEDGYRAEHINWQAIGEIRQRLTIPVIANGEIWDWQSAQQCMAITGCDAVMIGRGALNIPNLSRVVKYN 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130078 241 EPRMPWPEVVALLQKYTRLEKQGDTGLYHVARIKQWLSYLRKEYDEATELFQHVRVLNNSPDIARAIQAIDI 312
Cdd:PRK10550 241 EPRMPWPEVVALLQKYTRLEKQGDTGLYHVARIKQWLGYLRKEYDEATELFQEIRALNNSPDIARAIQAIDI 312
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
4-308 |
6.35e-127 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 364.72 E-value: 6.35e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 4 LLAPMEGVLDSLVRELLTEVNDYDLCITEFVRVVDQLLPVKVFHRICPELQNAsrtpsgTLVRVQLLGQFPQWLAENAAR 83
Cdd:pfam01207 1 LLAPMAGVTDLPFRRLVREYGAGDLVYTEMVTAKAQLRPEKVRIRMLSELEEP------TPLAVQLGGSDPALLAEAAKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 84 AVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVPahLPVSVKVRLGWDSG-EKKFEIADAVQQAGA 162
Cdd:pfam01207 75 VEDRGADGIDINMGCPSKKVTRGGGGAALLRNPDLVAQIVKAVVKAVG--IPVTVKIRIGWDDShENAVEIAKIVEDAGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 163 TELVVHGRTKEQGYRAeHIDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVKY--- 239
Cdd:pfam01207 153 QALTVHGRTRAQNYEG-TADWDAIKQVKQAVSIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLFAEQHTvkt 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130078 240 --NEPRMP-WPEVVALLQKYTRLEKQG--DTGLYHVARIKQWLSY-LRKEY---DEATELFQHVRVLNNSPDIARAIQ 308
Cdd:pfam01207 232 geFGPSPPlAEEAEKVLRHLPYLEEFLgeDKGLRHARKHLAWYLKgFPGAAelrRELNDVFDPVEALINLDAALRAAN 309
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
2-307 |
2.73e-117 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 340.15 E-value: 2.73e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 2 RVLLAPMEGVLDSLVRELLTEVNDyDLCITEFVRVVDQLLPVKVFHRIcpelqnASRTPSGTLVRVQLLGQFPQWLAENA 81
Cdd:COG0042 8 PLILAPMAGVTDRPFRRLCRELGA-GLLYTEMVSARALLHGNRKTRRL------LDFDPEEHPVAVQLFGSDPEELAEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 82 ARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVpaHLPVSVKVRLGWDSGEKKF-EIADAVQQA 160
Cdd:COG0042 81 RIAEELGADEIDINMGCPVKKVTKGGAGAALLRDPELVAEIVKAVVEAV--DVPVTVKIRLGWDDDDENAlEFARIAEDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 161 GATELVVHGRTKEQGYRAEhIDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVKYN 240
Cdd:COG0042 159 GAAALTVHGRTREQRYKGP-ADWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDAY 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130078 241 -----EPRMPWPEVVALLQKYTRLEKQGDTGLYHVARIKQWLSYLRKEYDEATELFQHVRVLNNSPDIARAI 307
Cdd:COG0042 238 laggeAPPPSLEEVLELLLEHLELLLEFYGERRGLRRMRKHLLWYFKGLPGARELRRRLSKAKSLAELLELL 309
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
2-241 |
3.31e-93 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 276.30 E-value: 3.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 2 RVLLAPMEGVLDSLVRELLTEVNdYDLCITEFVRVVDQLLPVKVFHRICpelqnaSRTPSGTLVRVQLLGQFPQWLAENA 81
Cdd:cd02801 1 KLILAPMVGVTDLPFRLLCRRYG-ADLVYTEMISAKALLRGNRKRLRLL------TRNPEERPLIVQLGGSDPETLAEAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 82 ARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVPahLPVSVKVRLGWDSGEKKFEIADAVQQAG 161
Cdd:cd02801 74 KIVEELGADGIDLNMGCPSPKVTKGGAGAALLKDPELVAEIVRAVREAVP--IPVTVKIRLGWDDEEETLELAKALEDAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 162 ATELVVHGRTKEQGYRaEHIDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVKYNE 241
Cdd:cd02801 152 ASALTVHGRTREQRYS-GPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELL 230
|
|
| nifR3_yhdG |
TIGR00737 |
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 ... |
2-280 |
1.28e-55 |
|
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 (Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 family). This branch includes NifR3 itself, from Rhodobacter capsulatus. It excludes a broadly distributed but more sparsely populated subfamily that contains sll0926 from Synechocystis PCC6803, HI0634 from Haemophilus influenzae, and BB0225 from Borrelia burgdorferi. It also excludes a shorter and more distant archaeal subfamily.The function of nifR3, a member of this family, is unknown, but it is found in an operon with nitrogen-sensing two component regulators in Rhodobacter capsulatus.Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase. [Unknown function, General]
Pssm-ID: 129820 Cd Length: 319 Bit Score: 182.95 E-value: 1.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 2 RVLLAPMEGVLDSLVRELLTEVNDyDLCITEFVRVVDQL-LPVKVFHRIcpelqnaSRTPSGTLVRVQLLGQFPQWLAEN 80
Cdd:TIGR00737 9 RVVLAPMAGVTDSPFRRLVAEYGA-GLTVCEMVSSEAIVyDSQRTMRLL-------DIAEDETPISVQLFGSDPDTMAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 81 AARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVpaHLPVSVKVRLGWDSGEKKF-EIADAVQQ 159
Cdd:TIGR00737 81 AKINEELGADIIDINMGCPVPKITKKGAGSALLRDPDLIGKIVKAVVDAV--DIPVTVKIRIGWDDAHINAvEAARIAED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 160 AGATELVVHGRTKEQGYRAEHiDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVK- 238
Cdd:TIGR00737 159 AGAQAVTLHGRTRAQGYSGEA-NWDIIARVKQAVRIPVIGNGDIFSPEDAKAMLETTGCDGVMIGRGALGNPWLFRQIEq 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 16130078 239 -----YNEPRMPWPEVVALLQKYTRL--EKQGDTGLYHVARiKQWLSYL 280
Cdd:TIGR00737 238 ylttgKYKPPPTFAEKLDAILRHLQLlaDYYGESKGLRIAR-KHIAWYL 285
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10550 |
PRK10550 |
tRNA dihydrouridine(16) synthase DusC; |
1-312 |
0e+00 |
|
tRNA dihydrouridine(16) synthase DusC;
Pssm-ID: 236713 Cd Length: 312 Bit Score: 693.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 1 MRVLLAPMEGVLDSLVRELLTEVNDYDLCITEFVRVVDQLLPVKVFHRICPELQNASRTPSGTLVRVQLLGQFPQWLAEN 80
Cdd:PRK10550 1 MRVLLAPMEGVLDSLVRELLTEVNDYDLCITEFLRVVDQLLPVKVFHRLCPELHNASRTPSGTLVRIQLLGQYPQWLAEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 81 AARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVPAHLPVSVKVRLGWDSGEKKFEIADAVQQA 160
Cdd:PRK10550 81 AARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVPAHLPVTVKVRLGWDSGERKFEIADAVQQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 161 GATELVVHGRTKEQGYRAEHIDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVKYN 240
Cdd:PRK10550 161 GATELVVHGRTKEDGYRAEHINWQAIGEIRQRLTIPVIANGEIWDWQSAQQCMAITGCDAVMIGRGALNIPNLSRVVKYN 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130078 241 EPRMPWPEVVALLQKYTRLEKQGDTGLYHVARIKQWLSYLRKEYDEATELFQHVRVLNNSPDIARAIQAIDI 312
Cdd:PRK10550 241 EPRMPWPEVVALLQKYTRLEKQGDTGLYHVARIKQWLGYLRKEYDEATELFQEIRALNNSPDIARAIQAIDI 312
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
4-308 |
6.35e-127 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 364.72 E-value: 6.35e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 4 LLAPMEGVLDSLVRELLTEVNDYDLCITEFVRVVDQLLPVKVFHRICPELQNAsrtpsgTLVRVQLLGQFPQWLAENAAR 83
Cdd:pfam01207 1 LLAPMAGVTDLPFRRLVREYGAGDLVYTEMVTAKAQLRPEKVRIRMLSELEEP------TPLAVQLGGSDPALLAEAAKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 84 AVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVPahLPVSVKVRLGWDSG-EKKFEIADAVQQAGA 162
Cdd:pfam01207 75 VEDRGADGIDINMGCPSKKVTRGGGGAALLRNPDLVAQIVKAVVKAVG--IPVTVKIRIGWDDShENAVEIAKIVEDAGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 163 TELVVHGRTKEQGYRAeHIDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVKY--- 239
Cdd:pfam01207 153 QALTVHGRTRAQNYEG-TADWDAIKQVKQAVSIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLFAEQHTvkt 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130078 240 --NEPRMP-WPEVVALLQKYTRLEKQG--DTGLYHVARIKQWLSY-LRKEY---DEATELFQHVRVLNNSPDIARAIQ 308
Cdd:pfam01207 232 geFGPSPPlAEEAEKVLRHLPYLEEFLgeDKGLRHARKHLAWYLKgFPGAAelrRELNDVFDPVEALINLDAALRAAN 309
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
2-307 |
2.73e-117 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 340.15 E-value: 2.73e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 2 RVLLAPMEGVLDSLVRELLTEVNDyDLCITEFVRVVDQLLPVKVFHRIcpelqnASRTPSGTLVRVQLLGQFPQWLAENA 81
Cdd:COG0042 8 PLILAPMAGVTDRPFRRLCRELGA-GLLYTEMVSARALLHGNRKTRRL------LDFDPEEHPVAVQLFGSDPEELAEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 82 ARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVpaHLPVSVKVRLGWDSGEKKF-EIADAVQQA 160
Cdd:COG0042 81 RIAEELGADEIDINMGCPVKKVTKGGAGAALLRDPELVAEIVKAVVEAV--DVPVTVKIRLGWDDDDENAlEFARIAEDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 161 GATELVVHGRTKEQGYRAEhIDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVKYN 240
Cdd:COG0042 159 GAAALTVHGRTREQRYKGP-ADWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDAY 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130078 241 -----EPRMPWPEVVALLQKYTRLEKQGDTGLYHVARIKQWLSYLRKEYDEATELFQHVRVLNNSPDIARAI 307
Cdd:COG0042 238 laggeAPPPSLEEVLELLLEHLELLLEFYGERRGLRRMRKHLLWYFKGLPGARELRRRLSKAKSLAELLELL 309
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
2-241 |
3.31e-93 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 276.30 E-value: 3.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 2 RVLLAPMEGVLDSLVRELLTEVNdYDLCITEFVRVVDQLLPVKVFHRICpelqnaSRTPSGTLVRVQLLGQFPQWLAENA 81
Cdd:cd02801 1 KLILAPMVGVTDLPFRLLCRRYG-ADLVYTEMISAKALLRGNRKRLRLL------TRNPEERPLIVQLGGSDPETLAEAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 82 ARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVPahLPVSVKVRLGWDSGEKKFEIADAVQQAG 161
Cdd:cd02801 74 KIVEELGADGIDLNMGCPSPKVTKGGAGAALLKDPELVAEIVRAVREAVP--IPVTVKIRLGWDDEEETLELAKALEDAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 162 ATELVVHGRTKEQGYRaEHIDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVKYNE 241
Cdd:cd02801 152 ASALTVHGRTREQRYS-GPADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELL 230
|
|
| nifR3_yhdG |
TIGR00737 |
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 ... |
2-280 |
1.28e-55 |
|
putative TIM-barrel protein, nifR3 family; This model represents one branch of COG0042 (Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 family). This branch includes NifR3 itself, from Rhodobacter capsulatus. It excludes a broadly distributed but more sparsely populated subfamily that contains sll0926 from Synechocystis PCC6803, HI0634 from Haemophilus influenzae, and BB0225 from Borrelia burgdorferi. It also excludes a shorter and more distant archaeal subfamily.The function of nifR3, a member of this family, is unknown, but it is found in an operon with nitrogen-sensing two component regulators in Rhodobacter capsulatus.Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase. [Unknown function, General]
Pssm-ID: 129820 Cd Length: 319 Bit Score: 182.95 E-value: 1.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 2 RVLLAPMEGVLDSLVRELLTEVNDyDLCITEFVRVVDQL-LPVKVFHRIcpelqnaSRTPSGTLVRVQLLGQFPQWLAEN 80
Cdd:TIGR00737 9 RVVLAPMAGVTDSPFRRLVAEYGA-GLTVCEMVSSEAIVyDSQRTMRLL-------DIAEDETPISVQLFGSDPDTMAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 81 AARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVpaHLPVSVKVRLGWDSGEKKF-EIADAVQQ 159
Cdd:TIGR00737 81 AKINEELGADIIDINMGCPVPKITKKGAGSALLRDPDLIGKIVKAVVDAV--DIPVTVKIRIGWDDAHINAvEAARIAED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 160 AGATELVVHGRTKEQGYRAEHiDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVK- 238
Cdd:TIGR00737 159 AGAQAVTLHGRTRAQGYSGEA-NWDIIARVKQAVRIPVIGNGDIFSPEDAKAMLETTGCDGVMIGRGALGNPWLFRQIEq 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 16130078 239 -----YNEPRMPWPEVVALLQKYTRL--EKQGDTGLYHVARiKQWLSYL 280
Cdd:TIGR00737 238 ylttgKYKPPPTFAEKLDAILRHLQLlaDYYGESKGLRIAR-KHIAWYL 285
|
|
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
2-258 |
1.40e-32 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 122.77 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 2 RVLLAPMEGVLDSLVRELLTEVNDyDLCITEFVRVVDQLLP-----VKVFHRICPELQNasrtpsgtlvrVQLLGQFPQW 76
Cdd:PRK10415 11 RLIAAPMAGITDRPFRTLCYEMGA-GLTVSEMMSSNPQVWEsdksrLRMVHIDEPGIRT-----------VQIAGSDPKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 77 LAENAARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVpaHLPVSVKVRLGWDSGEKK-FEIAD 155
Cdd:PRK10415 79 MADAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDLVKSILTEVVNAV--DVPVTLKIRTGWAPEHRNcVEIAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 156 AVQQAGATELVVHGRTKEQGYRAEhIDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSR 235
Cdd:PRK10415 157 LAEDCGIQALTIHGRTRACLFNGE-AEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFR 235
|
250 260
....*....|....*....|....*....
gi 16130078 236 VVKY----NE--PRMPWPEVVALLQKYTR 258
Cdd:PRK10415 236 EIQHyldtGEllPPLPLAEVKRLLCAHVR 264
|
|
| PRK11815 |
PRK11815 |
tRNA dihydrouridine(20/20a) synthase DusA; |
65-272 |
4.96e-21 |
|
tRNA dihydrouridine(20/20a) synthase DusA;
Pssm-ID: 236991 [Multi-domain] Cd Length: 333 Bit Score: 91.35 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 65 VRVQLLGQFPQWLAEnAARAVElgSWG---VDLNCGCPSKTVNgSGG-GATLLKDPELIYQGAKAMREAVPahLPVSVKV 140
Cdd:PRK11815 67 VALQLGGSDPADLAE-AAKLAE--DWGydeINLNVGCPSDRVQ-NGRfGACLMAEPELVADCVKAMKDAVS--IPVTVKH 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 141 RLGWD---SGEKKFEIADAVQQAGATELVVHGR--------TKEQgyRaehidwqaigDI------------RQRLNIPV 197
Cdd:PRK11815 141 RIGIDdqdSYEFLCDFVDTVAEAGCDTFIVHARkawlkglsPKEN--R----------EIppldydrvyrlkRDFPHLTI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 198 IANGEIwdwQSAQQC-MAISGCDAVMIGRGALNIPNL-----SRVvkYNEPRMP--WPEVVALLQKYTRLEKQGDTGLYH 269
Cdd:PRK11815 209 EINGGI---KTLEEAkEHLQHVDGVMIGRAAYHNPYLlaevdREL--FGEPAPPlsRSEVLEAMLPYIERHLAQGGRLNH 283
|
...
gi 16130078 270 VAR 272
Cdd:PRK11815 284 ITR 286
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
124-233 |
1.05e-10 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 61.43 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 124 KAMREAVPAHLPVSVK------VRLGWDSGEKKfEIADAVQQAGA------------TELVVHGRTKEQGYRAEHIDWqa 185
Cdd:cd02803 199 AAVREAVGPDFPVGVRlsaddfVPGGLTLEEAI-EIAKALEEAGVdalhvsggsyesPPPIIPPPYVPEGYFLELAEK-- 275
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 16130078 186 igdIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNL 233
Cdd:cd02803 276 ---IKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVALGRALLADPDL 320
|
|
| arch_FMN |
cd02911 |
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent ... |
93-238 |
2.47e-10 |
|
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent flavin oxidoreductase (oxidored) FMN-binding 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. The specific function of this group is unknown.
Pssm-ID: 239237 [Multi-domain] Cd Length: 233 Bit Score: 59.65 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 93 DLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREavpAHLPVSVKVRLGWDSgeKKFEIADAVQQAGAteLVVHGRTK 172
Cdd:cd02911 102 EINAHCRQPEMVEAGAGEALLKDPERLSEFIKALKE---TGVPVSVKIRAGVDV--DDEELARLIEKAGA--DIIHVDAM 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130078 173 EQGYraeHIDWQAIGDIRQRLNIpvIANGEIWDWQSAQQcMAISGCDAVMIGRGALNiPNLSRVVK 238
Cdd:cd02911 175 DPGN---HADLKKIRDISTELFI--IGNNSVTTIESAKE-MFSYGADMVSVARASLP-ENIEWLVE 233
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
124-233 |
2.31e-09 |
|
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];
Pssm-ID: 441506 [Multi-domain] Cd Length: 365 Bit Score: 57.87 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 124 KAMREAVPAHLPVSVK------VRLGWDSGEKKfEIADAVQQAGATEL-VVHGRT---------KEQGYRAEHIDWqaig 187
Cdd:COG1902 207 EAVRAAVGPDFPVGVRlsptdfVEGGLTLEESV-ELAKALEEAGVDYLhVSSGGYepdamiptiVPEGYQLPFAAR---- 281
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 16130078 188 dIRQRLNIPVIANGEIWDWQSAQQCMAiSG-CDAVMIGRGALNIPNL 233
Cdd:COG1902 282 -IRKAVGIPVIAVGGITTPEQAEAALA-SGdADLVALGRPLLADPDL 326
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
123-233 |
3.30e-09 |
|
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs.
Pssm-ID: 239242 [Multi-domain] Cd Length: 336 Bit Score: 57.12 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 123 AKAMREAVPAHLPVSVkvRLG---WDSGEKKFE----IADAVQQAGAtELV------VHGRTKEQGYRAEHIDWQAigDI 189
Cdd:cd02932 211 VDAVRAVWPEDKPLFV--RISatdWVEGGWDLEdsveLAKALKELGV-DLIdvssggNSPAQKIPVGPGYQVPFAE--RI 285
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 16130078 190 RQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNL 233
Cdd:cd02932 286 RQEAGIPVIAVGLITDPEQAEAILESGRADLVALGRELLRNPYW 329
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
82-263 |
1.89e-07 |
|
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 51.61 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 82 ARAVElgSWGVD---LNCGCPsktvNGSGGGATLLKDPELIYQGAKAMREAvpAHLPVSVKvrLGWDSGEKKfEIADAVQ 158
Cdd:COG0167 111 ARRLA--DAGADyleLNISCP----NTPGGGRALGQDPEALAELLAAVKAA--TDKPVLVK--LAPDLTDIV-EIARAAE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 159 QAGATELVVHGRTKEqgyRAEHIDW----------------------QAIGDIRQRL--NIPVIANGEIWDWQSAQQCMA 214
Cdd:COG0167 180 EAGADGVIAINTTLG---RAIDLETrrpvlaneagglsgpalkpialRMVREVAQAVggDIPIIGVGGISTAEDALEFIL 256
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130078 215 iSGCDAVMIGRGALnipnlsrvvkYNEPRMPwPEVVALLQKYtrLEKQG 263
Cdd:COG0167 257 -AGASAVQVGTALF----------YEGPGLV-RRIIRGLEAY--LEEKG 291
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
78-229 |
8.46e-07 |
|
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) 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. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239204 [Multi-domain] Cd Length: 289 Bit Score: 49.66 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 78 AENAARAVELGSWGVDLNCGCPsktvNGsGGGATLLKDPELIYQGAKAMREAVPahLPVSVKVRlGWDSGEKKFEIADAV 157
Cdd:cd02810 114 VELARKIERAGAKALELNLSCP----NV-GGGRQLGQDPEAVANLLKAVKAAVD--IPLLVKLS-PYFDLEDIVELAKAA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 158 QQAGATELVVHGR---------TKEQGYRAEH-------IDWQAIGDIRQ-----RLNIPVIANGEIWDWQSAQQcMAIS 216
Cdd:cd02810 186 ERAGADGLTAINTisgrvvdlkTVGPGPKRGTgglsgapIRPLALRWVARlaarlQLDIPIIGVGGIDSGEDVLE-MLMA 264
|
170
....*....|...
gi 16130078 217 GCDAVMIGRGALN 229
Cdd:cd02810 265 GASAVQVATALMW 277
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
153-224 |
4.25e-05 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 43.72 E-value: 4.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130078 153 IADAV--QQAGA----TELvvHGRTKEQGYRAEHiDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAIsGCDAVMIG 224
Cdd:cd04729 133 LEEALnaAKLGFdiigTTL--SGYTEETAKTEDP-DFELLKELRKALGIPVIAEGRINSPEQAAKALEL-GADAVVVG 206
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
124-247 |
1.31e-04 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 43.39 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 124 KAMREAVPAHLPVSVKVRL-----GWDSGEKKFEIADAVQQAGA------------TELVVHGRTkeqgYRAEHIDwqai 186
Cdd:PRK08255 609 RAVRAVWPAEKPMSVRISAhdwveGGNTPDDAVEIARAFKAAGAdlidvssgqvskDEKPVYGRM----YQTPFAD---- 680
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130078 187 gDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPN--LSRVVKYNEPRMPWP 247
Cdd:PRK08255 681 -RIRNEAGIATIAVGAISEADHVNSIIAAGRADLCALARPHLADPAwtLHEAAEIGYRDVAWP 742
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
151-228 |
1.92e-04 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 42.06 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 151 FEIADAVQQAGA----TELvvHGRTKEQGYRAEHiDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAIsGCDAVMIGrG 226
Cdd:PRK01130 129 LEEGLAAQKLGFdfigTTL--SGYTEETKKPEEP-DFALLKELLKAVGCPVIAEGRINTPEQAKKALEL-GAHAVVVG-G 203
|
..
gi 16130078 227 AL 228
Cdd:PRK01130 204 AI 205
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
76-224 |
2.14e-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: 42.15 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 76 WLAENAARAVELgswgvdlNCGCPsktvNGSGGGATLLKDPELIYQGAKAMREAVPahLPVSVKvrLG-WDSGEKkfEIA 154
Cdd:cd04740 110 KLADAGADAIEL-------NISCP----NVKGGGMAFGTDPEAVAEIVKAVKKATD--VPVIVK--LTpNVTDIV--EIA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 155 DAVQQAGATELV----VhgrtkeqgyRAEHIDWQ------------------------AIGDIRQRLNIPVIANGEIWDW 206
Cdd:cd04740 173 RAAEEAGADGLTlintL---------KGMAIDIEtrkpilgnvtgglsgpaikpialrMVYQVYKAVEIPIIGVGGIASG 243
|
170
....*....|....*...
gi 16130078 207 QSAQQCMaISGCDAVMIG 224
Cdd:cd04740 244 EDALEFL-MAGASAVQVG 260
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
78-224 |
4.30e-04 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 41.29 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 78 AENAARAVELGswGVD---LNCGCPsktvNGSGGGATLLKDPELIYQGAKAMREAVpaHLPVSVKvrLGWDSGEKKfEIA 154
Cdd:PRK07259 107 AEVAEKLSKAP--NVDaieLNISCP----NVKHGGMAFGTDPELAYEVVKAVKEVV--KVPVIVK--LTPNVTDIV-EIA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130078 155 DAVQQAGATELV-----------VHGR-----TKEQGY--RAEH-IDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMaI 215
Cdd:PRK07259 176 KAAEEAGADGLSlintlkgmaidIKTRkpilaNVTGGLsgPAIKpIALRMVYQVYQAVDIPIIGMGGISSAEDAIEFI-M 254
|
....*....
gi 16130078 216 SGCDAVMIG 224
Cdd:PRK07259 255 AGASAVQVG 263
|
|
| |
