|
Name |
Accession |
Description |
Interval |
E-value |
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
7-196 |
4.46e-68 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 206.19 E-value: 4.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 7 LPPCSILLLAGGRGQRMGGQDKGLVPWQGEPLIAHLHRQTRAMSDDLIISCNRNAQRYAPYADQLVHDEEGDFPGPLAGI 86
Cdd:PRK00317 1 MPPITGVILAGGRSRRMGGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLARYAAFGLPVIPDSLADFPGPLAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 87 RAGLKAAKHPYLLVLPCDVPQIDANLLDNMRRTASQHPDQPLMVRHGEHWEPLLCVIPLTLAARFEQAWSEGERSPGRIM 166
Cdd:PRK00317 81 LAGLKQARTEWVLVVPCDTPFIPPDLVARLAQAAGKDDADVAWAHDGGRLHPTFALYSVALLPDLEAYLAAGERKVMAFY 160
|
170 180 190
....*....|....*....|....*....|
gi 517432232 167 RALHAVALQCPADDPRLANLNTPELLARHK 196
Cdd:PRK00317 161 ARHGGVAVDFSDPKDAFFNINTPEDLAQLE 190
|
|
| molyb_mobA |
TIGR02665 |
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ... |
10-193 |
7.33e-58 |
|
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: 180.17 E-value: 7.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 10 CSILLLAGGRGQRMGGQDKGLVPWQGEPLIAHLHRQTRAMSDDLIISCNRNAQRYAPYADQL--VHDEEGDFPGPLAGIR 87
Cdd:TIGR02665 1 ISGVILAGGRARRMGGRDKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPERYAQAGFGLpvVPDALADFPGPLAGIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 88 AGLKAAKHPYLLVLPCDVPQIDANLLDNMRRTASQHPDQPLMVRHGEHWEPLLCVIPLTLAARFEQAWSEGERSPGRIMR 167
Cdd:TIGR02665 81 AGLRWAGTDWVLTVPCDTPFLPEDLVARLAAALEASDADIAVAHDGGRWHPVFALWPVALAPDLEAFLAAGERRVRRFYA 160
|
170 180
....*....|....*....|....*.
gi 517432232 168 ALHAVALQCPADDPRLANLNTPELLA 193
Cdd:TIGR02665 161 RHGAVAVDFSDSPDAFANLNTPEDLA 186
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
27-196 |
1.47e-48 |
|
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: 156.51 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEPLIAHLHRQTRAMSDDLIISCNRNaQRYAPYADQLVHDEEGDfPGPLAGIRAGLKAAKHPYLLVLPCDVP 106
Cdd:COG0746 21 DKALLPLGGRPLLERVLERLRPQVDEVVIVANRP-ERYAALGVPVVPDDPPG-AGPLAGILAALEAAPAEWVLVLACDMP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 107 QIDANLLDNMRRTASQHPDqPLMVRHGEHWEPLLCVIPLTLAARFEQAWSEGERSPGRIMRALHAVALQCPADDPRLANL 186
Cdd:COG0746 99 FLPPDLVRRLLEALEEGAD-AVVPRSGGRLEPLFALYRRSLLPALEAALAEGERSLRALLERLDVVYVPFEDLDDAFFNV 177
|
170
....*....|
gi 517432232 187 NTPELLARHK 196
Cdd:COG0746 178 NTPEDLARAE 187
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
27-190 |
1.29e-45 |
|
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: 148.88 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEPLIAHLHRQTRAMSDDLIISCNRNAQRYAPYADQLVHDEEgDFPGPLAGIRAGLKAAKHPYLLVLPCDVP 106
Cdd:cd02503 17 DKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLGVPVIPDEP-PGKGPLAGILAALRAAPADWVLVLACDMP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 107 QIDANLLDNMRRTASQHPDqPLMVRHGEHWEPLLCVIPLTLAARFEQAWSEGERSPGRIMRALHAVALQCPADDPR-LAN 185
Cdd:cd02503 96 FLPPELLERLLAAAEEGAD-AVVPKSGGRLQPLHALYHKSLLPALEELLEAGERRLRRLLEKLGVQYVEFEDERLDaFFN 174
|
....*
gi 517432232 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 ... |
27-172 |
2.42e-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: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEPLIAHLHRQTRAMSDDLIISCNRNAQR--YAPYADQLVHDEEGDfPGPLAGIRAGLKAAK-HPYLLVLPC 103
Cdd:pfam12804 15 DKALLPLGGKPLLERVLERLRPAGDEVVVVANDEEVLaaLAGLGVPVVPDPDPG-QGPLAGLLAALRAAPgADAVLVLAC 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 104 DVPQIDANLLDNMRRTASQHPDQPLMVRH-GEHWEPLLcvIPLTLAARFEQAwsEGERSPGRIMRALHAV 172
Cdd:pfam12804 94 DMPFLTPELLRRLLAAAEESGADIVVPVYdGGRGHPLL--YRRRLLPALEAL--LGDRGLRRLLRRLDEV 159
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
7-196 |
4.46e-68 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 206.19 E-value: 4.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 7 LPPCSILLLAGGRGQRMGGQDKGLVPWQGEPLIAHLHRQTRAMSDDLIISCNRNAQRYAPYADQLVHDEEGDFPGPLAGI 86
Cdd:PRK00317 1 MPPITGVILAGGRSRRMGGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLARYAAFGLPVIPDSLADFPGPLAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 87 RAGLKAAKHPYLLVLPCDVPQIDANLLDNMRRTASQHPDQPLMVRHGEHWEPLLCVIPLTLAARFEQAWSEGERSPGRIM 166
Cdd:PRK00317 81 LAGLKQARTEWVLVVPCDTPFIPPDLVARLAQAAGKDDADVAWAHDGGRLHPTFALYSVALLPDLEAYLAAGERKVMAFY 160
|
170 180 190
....*....|....*....|....*....|
gi 517432232 167 RALHAVALQCPADDPRLANLNTPELLARHK 196
Cdd:PRK00317 161 ARHGGVAVDFSDPKDAFFNINTPEDLAQLE 190
|
|
| molyb_mobA |
TIGR02665 |
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ... |
10-193 |
7.33e-58 |
|
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: 180.17 E-value: 7.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 10 CSILLLAGGRGQRMGGQDKGLVPWQGEPLIAHLHRQTRAMSDDLIISCNRNAQRYAPYADQL--VHDEEGDFPGPLAGIR 87
Cdd:TIGR02665 1 ISGVILAGGRARRMGGRDKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPERYAQAGFGLpvVPDALADFPGPLAGIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 88 AGLKAAKHPYLLVLPCDVPQIDANLLDNMRRTASQHPDQPLMVRHGEHWEPLLCVIPLTLAARFEQAWSEGERSPGRIMR 167
Cdd:TIGR02665 81 AGLRWAGTDWVLTVPCDTPFLPEDLVARLAAALEASDADIAVAHDGGRWHPVFALWPVALAPDLEAFLAAGERRVRRFYA 160
|
170 180
....*....|....*....|....*.
gi 517432232 168 ALHAVALQCPADDPRLANLNTPELLA 193
Cdd:TIGR02665 161 RHGAVAVDFSDSPDAFANLNTPEDLA 186
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
27-196 |
1.47e-48 |
|
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: 156.51 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEPLIAHLHRQTRAMSDDLIISCNRNaQRYAPYADQLVHDEEGDfPGPLAGIRAGLKAAKHPYLLVLPCDVP 106
Cdd:COG0746 21 DKALLPLGGRPLLERVLERLRPQVDEVVIVANRP-ERYAALGVPVVPDDPPG-AGPLAGILAALEAAPAEWVLVLACDMP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 107 QIDANLLDNMRRTASQHPDqPLMVRHGEHWEPLLCVIPLTLAARFEQAWSEGERSPGRIMRALHAVALQCPADDPRLANL 186
Cdd:COG0746 99 FLPPDLVRRLLEALEEGAD-AVVPRSGGRLEPLFALYRRSLLPALEAALAEGERSLRALLERLDVVYVPFEDLDDAFFNV 177
|
170
....*....|
gi 517432232 187 NTPELLARHK 196
Cdd:COG0746 178 NTPEDLARAE 187
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
27-190 |
1.29e-45 |
|
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: 148.88 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEPLIAHLHRQTRAMSDDLIISCNRNAQRYAPYADQLVHDEEgDFPGPLAGIRAGLKAAKHPYLLVLPCDVP 106
Cdd:cd02503 17 DKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLGVPVIPDEP-PGKGPLAGILAALRAAPADWVLVLACDMP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 107 QIDANLLDNMRRTASQHPDqPLMVRHGEHWEPLLCVIPLTLAARFEQAWSEGERSPGRIMRALHAVALQCPADDPR-LAN 185
Cdd:cd02503 96 FLPPELLERLLAAAEEGAD-AVVPKSGGRLQPLHALYHKSLLPALEELLEAGERRLRRLLEKLGVQYVEFEDERLDaFFN 174
|
....*
gi 517432232 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 ... |
27-172 |
2.42e-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: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEPLIAHLHRQTRAMSDDLIISCNRNAQR--YAPYADQLVHDEEGDfPGPLAGIRAGLKAAK-HPYLLVLPC 103
Cdd:pfam12804 15 DKALLPLGGKPLLERVLERLRPAGDEVVVVANDEEVLaaLAGLGVPVVPDPDPG-QGPLAGLLAALRAAPgADAVLVLAC 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 104 DVPQIDANLLDNMRRTASQHPDQPLMVRH-GEHWEPLLcvIPLTLAARFEQAwsEGERSPGRIMRALHAV 172
Cdd:pfam12804 94 DMPFLTPELLRRLLAAAEESGADIVVPVYdGGRGHPLL--YRRRLLPALEAL--LGDRGLRRLLRRLDEV 159
|
|
| PRK14489 |
PRK14489 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ... |
27-194 |
7.74e-24 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional
Pssm-ID: 237727 [Multi-domain] Cd Length: 366 Bit Score: 96.74 E-value: 7.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEPLIAHLHRQTRAMSDDLIISCNRNAQRYAPYADQL--VHDEEGDFPGPLAGIRAGLKAAKHPYLLVLPCD 104
Cdd:PRK14489 23 DKALILLGGKPLIERVVDRLRPQFARIHLNINRDPARYQDLFPGLpvYPDILPGFQGPLSGILAGLEHADSEYLFVVACD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 105 VPQIDANLLDNMRRTASQHPDQPLMVRHGEHWEPLLCVIPLTLAARFEQAWSEGERSPGRIMRALHAVALQCPADDPRLA 184
Cdd:PRK14489 103 TPFLPENLVKRLSKALAIEGADIAVPHDGERAHPLFALYHRSCLPALRRYLAEGERRLFDFFQRQRVRYVDLSTQKDAFF 182
|
170
....*....|
gi 517432232 185 NLNTPELLAR 194
Cdd:PRK14489 183 NVNTPEDLEQ 192
|
|
| PRK02726 |
PRK02726 |
molybdenum cofactor guanylyltransferase; |
27-200 |
5.41e-15 |
|
molybdenum cofactor guanylyltransferase;
Pssm-ID: 235063 Cd Length: 200 Bit Score: 70.06 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEPLIAHLHRQTRAMSDDLIIsCNRNAQRYAPYADQLVH--DEEGDFPGPLAGIRAGLKAAKHPYLLVLPCD 104
Cdd:PRK02726 24 DKALLPWQGVPLLQRVARIAAACADEVYI-ITPWPERYQSLLPPGCHwlREPPPSQGPLVAFAQGLPQIKTEWVLLLACD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 105 VPQIDANLLDNMRRTASQHPDQPL--MVRHGEHWEPLLCVIPLTLAARFEQAWSEGERSPGRIMRALHAVALqcPADDPR 182
Cdd:PRK02726 103 LPRLTVDVLQEWLQQLENVPEEAIaaLPKQEKGWEPLCGFYRRRCLPSLEQFIQQGGRSFQGWLAQVPVQEL--ALSDPD 180
|
170
....*....|....*....
gi 517432232 183 -LANLNTPELLARHKGVSD 200
Cdd:PRK02726 181 mLFNCNTPEDLATIQGIGR 199
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
27-194 |
1.56e-08 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 52.09 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEPLIAH-LHRQTRAMSDDLIISCNRNAQRYAPYADQL----VHDEegDFP-GPLAGIRAGLKAAKHPY--L 98
Cdd:COG2068 20 PKLLLPLGGKPLLERaVEAALAAGLDPVVVVLGADAEEVAAALAGLgvrvVVNP--DWEeGMSSSLRAGLAALPADAdaV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 99 LVLPCDVPQIDANLLDNMRRTASQHPDQPLMVRHGE---HwePLLcvIPLTLAARFEQAwsEGERSPGRIMRALHAVALQ 175
Cdd:COG2068 98 LVLLGDQPLVTAETLRRLLAAFRESPASIVAPTYDGrrgH--PVL--FSRRLFPELLAL--TGDQGARALLRRHPDRVRL 171
|
170 180
....*....|....*....|
gi 517432232 176 CPADDPR-LANLNTPELLAR 194
Cdd:COG2068 172 VPVDDPGvLLDIDTPEDLAR 191
|
|
| PRK14500 |
PRK14500 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; ... |
27-190 |
1.35e-07 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; Provisional
Pssm-ID: 237734 [Multi-domain] Cd Length: 346 Bit Score: 50.66 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEPLIAHLHRQTRAMSDDLIISCNRNAQRYAPYADQLVHDEEGDFPGPLAGIRAGLKAAKHPYLLVLPCDVP 106
Cdd:PRK14500 177 DKALLNYQGQPHAQYLYDLLAKYCEQVFLSARPSQWQGTPLENLPTLPDRGESVGPISGILTALQSYPGVNWLVVACDLA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 107 QID----ANLLDNMRR----TASQHPDQPLMvrhgehwEPlLCVIPLTLAAR-FEQAWSEGERSPGRIMRaLHAVALQCP 177
Cdd:PRK14500 257 YLNsetvEKLLAHYRQdlvaTCYENPDQGFP-------EA-LCAIYTPQALQvFEKAYAEGLYCPVKILQ-RAPCQLIKP 327
|
170
....*....|...
gi 517432232 178 ADDPRLANLNTPE 190
Cdd:PRK14500 328 DNLFDIANINTPE 340
|
|
| PRK14490 |
PRK14490 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ... |
27-190 |
1.14e-05 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional
Pssm-ID: 237728 [Multi-domain] Cd Length: 369 Bit Score: 45.04 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEPLIAHLHRQTRAMSDDLIISC-NRNAQRYAPYADQLVHDEEGDFpGPLAGIRAGLKAAKHPYLLVLPCDV 105
Cdd:PRK14490 191 DKALLSYHESNQLVHTAALLRPHCQEVFISCrAEQAEQYRSFGIPLITDSYLDI-GPLGGLLSAQRHHPDAAWLVVACDL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 106 PQIDANLLDNMRR--------TASQHPDQplmvrhgEHWEPLL-CVIPLTLAARFEQAwSEGERSPGRIMRALHAVALQc 176
Cdd:PRK14490 270 PFLDEATLQQLVEgrnpfrfaTAFRHPDS-------GRPEPLCaIYEPKSRLRLLLRH-AAGNNSLRSFLATSRIEELE- 340
|
170
....*....|....
gi 517432232 177 PADDPRLANLNTPE 190
Cdd:PRK14490 341 PTDPEALQNINDPE 354
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
27-190 |
1.81e-05 |
|
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: 43.32 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEPLIAH-LHRQTRAMSDDLIISCNRNAQR----YAPYADQLVHDEEGDFpGPLAGIRAGLKAAKHPY--LL 99
Cdd:cd04182 17 NKLLLPLDGKPLLRHaLDAALAAGLSRVIVVLGAEADAvraaLAGLPVVVVINPDWEE-GMSSSLAAGLEALPADAdaVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 100 VLPCDVPQIDANLLDNMRRTASQHPDQPLMVRHGE---HwePllCVIPLTLAARFEQAwsEGERSPGRIMRAlHAVALQC 176
Cdd:cd04182 96 ILLADQPLVTAETLRALIDAFREDGAGIVAPVYQGrrgH--P--VLFPRSLFPELLAL--SGDKGARSLLRA-HPDRVVV 168
|
170
....*....|....*
gi 517432232 177 PADDPR-LANLNTPE 190
Cdd:cd04182 169 EVDDPGvLIDIDTPE 183
|
|
| PRK00560 |
PRK00560 |
molybdenum cofactor guanylyltransferase MobA; |
27-190 |
6.48e-03 |
|
molybdenum cofactor guanylyltransferase MobA;
Pssm-ID: 167003 Cd Length: 196 Bit Score: 36.28 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 27 DKGLVPWQGEP-LIAHLHRQTRAMSDDLIISCNRNAQRY-APYadqlVHDEEGDFPGPLAGIRAGLKAAKHPYLLVLPCD 104
Cdd:PRK00560 25 NKALLPFGSYSsLLEYQYTRLLKLFKKVYISTKDKKFEFnAPF----LLEKESDLFSPLFGIINAFLTLQTPEIFFISVD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517432232 105 VPQIDANLL------DNMRRTASQHPDqplmvrhGEHwePLLCVIPLTLAARFEQAWSEGERSPGRIMRALHAVALQCpA 178
Cdd:PRK00560 101 TPFVSFESIkklcgkENFSVTYAKSPT-------KEH--YLISLWHQSLLNALIYALKTQNYRLSDLVKNTSSQAVHF-E 170
|
170
....*....|..
gi 517432232 179 DDPRLANLNTPE 190
Cdd:PRK00560 171 DEEEFLNLNTLK 182
|
|
| |
