|
Name |
Accession |
Description |
Interval |
E-value |
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
9-192 |
1.68e-64 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 197.33 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 9 PCSILLLAGGRGQRMGGQDKGLLEWHGEPLIAHLHRKTRLLSDDLIISCNRNLEKYAPYADQLVHDDEGDFPGPLAGIRA 88
Cdd:PRK00317 3 PITGVILAGGRSRRMGGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLARYAAFGLPVIPDSLADFPGPLAGILA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 89 GLKAARHTHLLVLPCDVPRIDAALLQNMRETAAQHPDKPLMLRHGEHWEPLLCMIPVVLSGAFETAWNEGERSPGRLMRT 168
Cdd:PRK00317 83 GLKQARTEWVLVVPCDTPFIPPDLVARLAQAAGKDDADVAWAHDGGRLHPTFALYSVALLPDLEAYLAAGERKVMAFYAR 162
|
170 180
....*....|....*....|....
gi 518412306 169 LGAMALQCPDNDPRLANLNTPELL 192
Cdd:PRK00317 163 HGGVAVDFSDPKDAFFNINTPEDL 186
|
|
| molyb_mobA |
TIGR02665 |
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ... |
10-192 |
6.77e-57 |
|
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing enzymes, including nitrate reductase and dimethylsulfoxide reductase, the cofactor is molybdopterin-guanine dinucleotide. The family described here contains MobA, molybdenum cofactor guanylyltransferase, from the Proteobacteria only. MobA can reconstitute molybdopterin-guanine dinucleotide biosynthesis without the product of the neighboring gene MobB. The probable MobA proteins of other lineages differ sufficiently that they are not included in scope of this family. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
Pssm-ID: 274249 Cd Length: 186 Bit Score: 177.86 E-value: 6.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 10 CSILLLAGGRGQRMGGQDKGLLEWHGEPLIAHLHRKTRLLSDDLIISCNRNLEKYAPYADQL--VHDDEGDFPGPLAGIR 87
Cdd:TIGR02665 1 ISGVILAGGRARRMGGRDKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPERYAQAGFGLpvVPDALADFPGPLAGIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 88 AGLKAARHTHLLVLPCDVPRIDAALLQNMRETAAQHPDKPLMLRHGEHWEPLLCMIPVVLSGAFETAWNEGERSPGRLMR 167
Cdd:TIGR02665 81 AGLRWAGTDWVLTVPCDTPFLPEDLVARLAAALEASDADIAVAHDGGRWHPVFALWPVALAPDLEAFLAAGERRVRRFYA 160
|
170 180
....*....|....*....|....*
gi 518412306 168 TLGAMALQCPDNDPRLANLNTPELL 192
Cdd:TIGR02665 161 RHGAVAVDFSDSPDAFANLNTPEDL 185
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
27-190 |
8.38e-46 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440509 [Multi-domain] Cd Length: 188 Bit Score: 149.57 E-value: 8.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 27 DKGLLEWHGEPLIAHLHRKTRLLSDDLIISCNRNlEKYAPYADQLVHDDEGDfPGPLAGIRAGLKAARHTHLLVLPCDVP 106
Cdd:COG0746 21 DKALLPLGGRPLLERVLERLRPQVDEVVIVANRP-ERYAALGVPVVPDDPPG-AGPLAGILAALEAAPAEWVLVLACDMP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 107 RIDAALLQNMRETAAQHPDkPLMLRHGEHWEPLLCMIPVVLSGAFETAWNEGERSPGRLMRTLGAMALQCPDNDPRLANL 186
Cdd:COG0746 99 FLPPDLVRRLLEALEEGAD-AVVPRSGGRLEPLFALYRRSLLPALEAALAEGERSLRALLERLDVVYVPFEDLDDAFFNV 177
|
....
gi 518412306 187 NTPE 190
Cdd:COG0746 178 NTPE 181
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
27-190 |
1.44e-42 |
|
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.
Pssm-ID: 133000 [Multi-domain] Cd Length: 181 Bit Score: 141.17 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 27 DKGLLEWHGEPLIAHLHRKTRLLSDDLIISCNRNLEKYAPYADQLVHDdEGDFPGPLAGIRAGLKAARHTHLLVLPCDVP 106
Cdd:cd02503 17 DKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLGVPVIPD-EPPGKGPLAGILAALRAAPADWVLVLACDMP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 107 RIDAALLQNMRETAAQHPDkPLMLRHGEHWEPLLCMIPVVLSGAFETAWNEGERSPGRLMRTLGAMALQCPDNDPR-LAN 185
Cdd:cd02503 96 FLPPELLERLLAAAEEGAD-AVVPKSGGRLQPLHALYHKSLLPALEELLEAGERRLRRLLEKLGVQYVEFEDERLDaFFN 174
|
....*
gi 518412306 186 LNTPE 190
Cdd:cd02503 175 INTPE 179
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
27-171 |
2.78e-24 |
|
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.
Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 93.41 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 27 DKGLLEWHGEPLIAHLHRKTRLLSDDLIISCNRN--LEKYAPYADQLVHDDEGDfPGPLAGIRAGLKAARHT-HLLVLPC 103
Cdd:pfam12804 15 DKALLPLGGKPLLERVLERLRPAGDEVVVVANDEevLAALAGLGVPVVPDPDPG-QGPLAGLLAALRAAPGAdAVLVLAC 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518412306 104 DVPRIDAALLQNMRETAAQHPDKPLMLRH-GEHWEPLLcmIPVVLSGAFETAwnEGERSPGRLMRTLGA 171
Cdd:pfam12804 94 DMPFLTPELLRRLLAAAEESGADIVVPVYdGGRGHPLL--YRRRLLPALEAL--LGDRGLRRLLRRLDE 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
9-192 |
1.68e-64 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 197.33 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 9 PCSILLLAGGRGQRMGGQDKGLLEWHGEPLIAHLHRKTRLLSDDLIISCNRNLEKYAPYADQLVHDDEGDFPGPLAGIRA 88
Cdd:PRK00317 3 PITGVILAGGRSRRMGGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLARYAAFGLPVIPDSLADFPGPLAGILA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 89 GLKAARHTHLLVLPCDVPRIDAALLQNMRETAAQHPDKPLMLRHGEHWEPLLCMIPVVLSGAFETAWNEGERSPGRLMRT 168
Cdd:PRK00317 83 GLKQARTEWVLVVPCDTPFIPPDLVARLAQAAGKDDADVAWAHDGGRLHPTFALYSVALLPDLEAYLAAGERKVMAFYAR 162
|
170 180
....*....|....*....|....
gi 518412306 169 LGAMALQCPDNDPRLANLNTPELL 192
Cdd:PRK00317 163 HGGVAVDFSDPKDAFFNINTPEDL 186
|
|
| molyb_mobA |
TIGR02665 |
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ... |
10-192 |
6.77e-57 |
|
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing enzymes, including nitrate reductase and dimethylsulfoxide reductase, the cofactor is molybdopterin-guanine dinucleotide. The family described here contains MobA, molybdenum cofactor guanylyltransferase, from the Proteobacteria only. MobA can reconstitute molybdopterin-guanine dinucleotide biosynthesis without the product of the neighboring gene MobB. The probable MobA proteins of other lineages differ sufficiently that they are not included in scope of this family. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
Pssm-ID: 274249 Cd Length: 186 Bit Score: 177.86 E-value: 6.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 10 CSILLLAGGRGQRMGGQDKGLLEWHGEPLIAHLHRKTRLLSDDLIISCNRNLEKYAPYADQL--VHDDEGDFPGPLAGIR 87
Cdd:TIGR02665 1 ISGVILAGGRARRMGGRDKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPERYAQAGFGLpvVPDALADFPGPLAGIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 88 AGLKAARHTHLLVLPCDVPRIDAALLQNMRETAAQHPDKPLMLRHGEHWEPLLCMIPVVLSGAFETAWNEGERSPGRLMR 167
Cdd:TIGR02665 81 AGLRWAGTDWVLTVPCDTPFLPEDLVARLAAALEASDADIAVAHDGGRWHPVFALWPVALAPDLEAFLAAGERRVRRFYA 160
|
170 180
....*....|....*....|....*
gi 518412306 168 TLGAMALQCPDNDPRLANLNTPELL 192
Cdd:TIGR02665 161 RHGAVAVDFSDSPDAFANLNTPEDL 185
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
27-190 |
8.38e-46 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440509 [Multi-domain] Cd Length: 188 Bit Score: 149.57 E-value: 8.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 27 DKGLLEWHGEPLIAHLHRKTRLLSDDLIISCNRNlEKYAPYADQLVHDDEGDfPGPLAGIRAGLKAARHTHLLVLPCDVP 106
Cdd:COG0746 21 DKALLPLGGRPLLERVLERLRPQVDEVVIVANRP-ERYAALGVPVVPDDPPG-AGPLAGILAALEAAPAEWVLVLACDMP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 107 RIDAALLQNMRETAAQHPDkPLMLRHGEHWEPLLCMIPVVLSGAFETAWNEGERSPGRLMRTLGAMALQCPDNDPRLANL 186
Cdd:COG0746 99 FLPPDLVRRLLEALEEGAD-AVVPRSGGRLEPLFALYRRSLLPALEAALAEGERSLRALLERLDVVYVPFEDLDDAFFNV 177
|
....
gi 518412306 187 NTPE 190
Cdd:COG0746 178 NTPE 181
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
27-190 |
1.44e-42 |
|
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.
Pssm-ID: 133000 [Multi-domain] Cd Length: 181 Bit Score: 141.17 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 27 DKGLLEWHGEPLIAHLHRKTRLLSDDLIISCNRNLEKYAPYADQLVHDdEGDFPGPLAGIRAGLKAARHTHLLVLPCDVP 106
Cdd:cd02503 17 DKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLGVPVIPD-EPPGKGPLAGILAALRAAPADWVLVLACDMP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 107 RIDAALLQNMRETAAQHPDkPLMLRHGEHWEPLLCMIPVVLSGAFETAWNEGERSPGRLMRTLGAMALQCPDNDPR-LAN 185
Cdd:cd02503 96 FLPPELLERLLAAAEEGAD-AVVPKSGGRLQPLHALYHKSLLPALEELLEAGERRLRRLLEKLGVQYVEFEDERLDaFFN 174
|
....*
gi 518412306 186 LNTPE 190
Cdd:cd02503 175 INTPE 179
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
27-171 |
2.78e-24 |
|
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.
Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 93.41 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 27 DKGLLEWHGEPLIAHLHRKTRLLSDDLIISCNRN--LEKYAPYADQLVHDDEGDfPGPLAGIRAGLKAARHT-HLLVLPC 103
Cdd:pfam12804 15 DKALLPLGGKPLLERVLERLRPAGDEVVVVANDEevLAALAGLGVPVVPDPDPG-QGPLAGLLAALRAAPGAdAVLVLAC 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518412306 104 DVPRIDAALLQNMRETAAQHPDKPLMLRH-GEHWEPLLcmIPVVLSGAFETAwnEGERSPGRLMRTLGA 171
Cdd:pfam12804 94 DMPFLTPELLRRLLAAAEESGADIVVPVYdGGRGHPLL--YRRRLLPALEAL--LGDRGLRRLLRRLDE 158
|
|
| PRK14489 |
PRK14489 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ... |
13-200 |
5.08e-20 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional
Pssm-ID: 237727 [Multi-domain] Cd Length: 366 Bit Score: 86.34 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 13 LLLAGGRGQRMGGQDKGLLEWHGEPLIAHLHRKTRLLSDDLIISCNRNLEKYAPYADQL--VHDDEGDFPGPLAGIRAGL 90
Cdd:PRK14489 9 VILAGGLSRRMNGRDKALILLGGKPLIERVVDRLRPQFARIHLNINRDPARYQDLFPGLpvYPDILPGFQGPLSGILAGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 91 KAARHTHLLVLPCDVPRIDAALLQNMRETAAQHPDKPLMLRHGEHWEPLLCMIPVVLSGAFETAWNEGERSPGRLMRTLG 170
Cdd:PRK14489 89 EHADSEYLFVVACDTPFLPENLVKRLSKALAIEGADIAVPHDGERAHPLFALYHRSCLPALRRYLAEGERRLFDFFQRQR 168
|
170 180 190
....*....|....*....|....*....|
gi 518412306 171 AMALQCPDNDPRLANLNTPELLSTHHTVSD 200
Cdd:PRK14489 169 VRYVDLSTQKDAFFNVNTPEDLEQLRAIPD 198
|
|
| PRK02726 |
PRK02726 |
molybdenum cofactor guanylyltransferase; |
27-194 |
3.52e-13 |
|
molybdenum cofactor guanylyltransferase;
Pssm-ID: 235063 Cd Length: 200 Bit Score: 65.06 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 27 DKGLLEWHGEPLIAHLHRKTRLLSDDLIIsCNRNLEKYAPYADQLVH--DDEGDFPGPLAGIRAGLKAARHTHLLVLPCD 104
Cdd:PRK02726 24 DKALLPWQGVPLLQRVARIAAACADEVYI-ITPWPERYQSLLPPGCHwlREPPPSQGPLVAFAQGLPQIKTEWVLLLACD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 105 VPRIDAALLQNMRETAAQHPDKPLML--RHGEHWEPLLCMIPVVLSGAFETAWNEGERSPGRLMRTLGAMALQCPDNDpR 182
Cdd:PRK02726 103 LPRLTVDVLQEWLQQLENVPEEAIAAlpKQEKGWEPLCGFYRRRCLPSLEQFIQQGGRSFQGWLAQVPVQELALSDPD-M 181
|
170
....*....|..
gi 518412306 183 LANLNTPELLST 194
Cdd:PRK02726 182 LFNCNTPEDLAT 193
|
|
| PRK14490 |
PRK14490 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ... |
27-190 |
1.73e-11 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional
Pssm-ID: 237728 [Multi-domain] Cd Length: 369 Bit Score: 61.99 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 27 DKGLLEWHGEPLIAHLHRKTRLLSDDLIISC-NRNLEKYAPYADQLVHDDEGDFpGPLAGIRAGLKAARHTHLLVLPCDV 105
Cdd:PRK14490 191 DKALLSYHESNQLVHTAALLRPHCQEVFISCrAEQAEQYRSFGIPLITDSYLDI-GPLGGLLSAQRHHPDAAWLVVACDL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 106 PRIDAALLQNMRE--------TAAQHPDKplmlrhgEHWEPLLCM------IPVVLSGAfetawnEGERSPGRLMRTLGA 171
Cdd:PRK14490 270 PFLDEATLQQLVEgrnpfrfaTAFRHPDS-------GRPEPLCAIyepksrLRLLLRHA------AGNNSLRSFLATSRI 336
|
170
....*....|....*....
gi 518412306 172 MALQCPDNDpRLANLNTPE 190
Cdd:PRK14490 337 EELEPTDPE-ALQNINDPE 354
|
|
| PRK14500 |
PRK14500 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; ... |
27-190 |
2.06e-08 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; Provisional
Pssm-ID: 237734 [Multi-domain] Cd Length: 346 Bit Score: 52.97 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 27 DKGLLEWHGEPLIAHLHRKTRLLSDDLIISCNRNLEKYAPYADQLVHDDEGDFPGPLAGIRAGLKAARHTHLLVLPCDVP 106
Cdd:PRK14500 177 DKALLNYQGQPHAQYLYDLLAKYCEQVFLSARPSQWQGTPLENLPTLPDRGESVGPISGILTALQSYPGVNWLVVACDLA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 107 RID----AALLQNMRE----TAAQHPDkplmlrhgEHWEPLLCMIPVVLSGA-FETAWNEGERSPGRLMRtLGAMALQCP 177
Cdd:PRK14500 257 YLNsetvEKLLAHYRQdlvaTCYENPD--------QGFPEALCAIYTPQALQvFEKAYAEGLYCPVKILQ-RAPCQLIKP 327
|
170
....*....|...
gi 518412306 178 DNDPRLANLNTPE 190
Cdd:PRK14500 328 DNLFDIANINTPE 340
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
27-190 |
1.38e-07 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 49.39 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 27 DKGLLEWHGEPLIAH---LHRKTRLlsDDLIISCNRNLEKYAPYADQL----VHDDegDFP-GPLAGIRAGLKAARH--T 96
Cdd:COG2068 20 PKLLLPLGGKPLLERaveAALAAGL--DPVVVVLGADAEEVAAALAGLgvrvVVNP--DWEeGMSSSLRAGLAALPAdaD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 97 HLLVLPCDVPRIDAALLQNMRETAAQHPDKPLMLRHGEHwepllCMIPVVLSGAFetaWNE-----GERSPGRLMRTLGA 171
Cdd:COG2068 96 AVLVLLGDQPLVTAETLRRLLAAFRESPASIVAPTYDGR-----RGHPVLFSRRL---FPEllaltGDQGARALLRRHPD 167
|
170 180
....*....|....*....|
gi 518412306 172 MALQCPDNDPR-LANLNTPE 190
Cdd:COG2068 168 RVRLVPVDDPGvLLDIDTPE 187
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
27-190 |
3.10e-06 |
|
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133025 [Multi-domain] Cd Length: 186 Bit Score: 45.63 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 27 DKGLLEWHGEPLIAH-LHRKTRLLSDDLIISCNRNLEK----YAPYADQLVHDDEGDFpGPLAGIRAGLKAARH--THLL 99
Cdd:cd04182 17 NKLLLPLDGKPLLRHaLDAALAAGLSRVIVVLGAEADAvraaLAGLPVVVVINPDWEE-GMSSSLAAGLEALPAdaDAVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518412306 100 VLPCDVPRIDAALLQNMRETAAQHPDKPLMLRHGEhweplLCMIPVVLSGAFetaWNE-----GERSPGRLMRTLGAMAL 174
Cdd:cd04182 96 ILLADQPLVTAETLRALIDAFREDGAGIVAPVYQG-----RRGHPVLFPRSL---FPEllalsGDKGARSLLRAHPDRVV 167
|
170
....*....|....*.
gi 518412306 175 QCPDNDPRLANLNTPE 190
Cdd:cd04182 168 VEVDDPGVLIDIDTPE 183
|
|
| |
