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Conserved domains on  [gi|639228684|ref|WP_024564270|]
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NTP transferase domain-containing protein [Elizabethkingia anophelis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14490 super family cl36380
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ...
 12-204 6.52e-65

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional


The actual alignment was detected with superfamily member PRK14490:

Pssm-ID: 237728 [Multi-domain]  Cd Length: 369  Bit Score: 204.13  E-value: 6.52e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  12 INGLVLAGGKSTRMGTAKDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQLENF-DTSYNALTDTFLNMGPFGGILSAL 90
Cdd:PRK14490 175 LSGLVLAGGRSSRMGSDKALLSYHESNQLVHTAALLRPHCQEVFISCRAEQAEQYrSFGIPLITDSYLDIGPLGGLLSAQ 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  91 RSQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESPFDGLPEPLITIWEPKS-YPLLLNFLGiGNTCPRKVLIN 169
Cdd:PRK14490 255 RHHPDAAWLVVACDLPFLDEATLQQLVEGRNPFRFATAFRHPDSGRPEPLCAIYEPKSrLRLLLRHAA-GNNSLRSFLAT 333

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 639228684 170 SDTLIIKPQNPDALMNVNTPDDAKKAQQVLNNSKD 204
Cdd:PRK14490 334 SRIEELEPTDPEALQNINDPEEMDRAERALSTTKE 368
 
Name Accession Description Interval E-value
PRK14490 PRK14490
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ...
 12-204 6.52e-65

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional


Pssm-ID: 237728 [Multi-domain]  Cd Length: 369  Bit Score: 204.13  E-value: 6.52e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  12 INGLVLAGGKSTRMGTAKDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQLENF-DTSYNALTDTFLNMGPFGGILSAL 90
Cdd:PRK14490 175 LSGLVLAGGRSSRMGSDKALLSYHESNQLVHTAALLRPHCQEVFISCRAEQAEQYrSFGIPLITDSYLDIGPLGGLLSAQ 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  91 RSQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESPFDGLPEPLITIWEPKS-YPLLLNFLGiGNTCPRKVLIN 169
Cdd:PRK14490 255 RHHPDAAWLVVACDLPFLDEATLQQLVEGRNPFRFATAFRHPDSGRPEPLCAIYEPKSrLRLLLRHAA-GNNSLRSFLAT 333

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 639228684 170 SDTLIIKPQNPDALMNVNTPDDAKKAQQVLNNSKD 204
Cdd:PRK14490 334 SRIEELEPTDPEALQNINDPEEMDRAERALSTTKE 368
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 10-197 2.02e-55

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: 174.22  E-value: 2.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  10 PSINGLVLAGGKSTRMGTAKDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQLENFdTSYNALTDTFLNMGPFGGILSA 89
Cdd:COG0746    3 MPITGVILAGGRSRRMGQDKALLPLGGRPLLERVLERLRPQVDEVVIVANRPERYAA-LGVPVVPDDPPGAGPLAGILAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  90 LRSQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESpfDGLPEPLITIWEPKSYPLLLNFLGIGNTCPRKVLIN 169
Cdd:COG0746   82 LEAAPAEWVLVLACDMPFLPPDLVRRLLEALEEGADAVVPRS--GGRLEPLFALYRRSLLPALEAALAEGERSLRALLER 159

                        170       180
                 ....*....|....*....|....*....
gi 639228684 170 SDTLIIK-PQNPDALMNVNTPDDAKKAQQ 197
Cdd:COG0746  160 LDVVYVPfEDLDDAFFNVNTPEDLARAEE 188
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 12-191 1.25e-49

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: 159.28  E-value: 1.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  12 INGLVLAGGKSTRMGTAKDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQLENFDTSYNALTDTFLNMGPFGGILSALR 91
Cdd:cd02503    1 ITGVILAGGKSRRMGGDKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLGVPVIPDEPPGKGPLAGILAALR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  92 SQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESpfDGLPEPLITIWEPKSYPLLLNFLGIGNTCPRKVLINSD 171
Cdd:cd02503   81 AAPADWVLVLACDMPFLPPELLERLLAAAEEGADAVVPKS--GGRLQPLHALYHKSLLPALEELLEAGERRLRRLLEKLG 158

                        170       180
                 ....*....|....*....|..
gi 639228684 172 TLIIK--PQNPDALMNVNTPDD 191
Cdd:cd02503  159 VQYVEfeDERLDAFFNINTPED 180
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 14-157 8.96e-30

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: 107.67  E-value: 8.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684   14 GLVLAGGKSTRMGTAKDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQLENFDTSYNA--LTDTFLNMGPFGGILSALR 91
Cdd:pfam12804   1 AVILAGGRSSRMGGDKALLPLGGKPLLERVLERLRPAGDEVVVVANDEEVLAALAGLGVpvVPDPDPGQGPLAGLLAALR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639228684   92 -SQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESPFDGLPEPLitIWEPKSYPLLLNFLG 157
Cdd:pfam12804  81 aAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDGGRGHPL--LYRRRLLPALEALLG 145
molyb_mobA TIGR02665
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ...
 12-191 2.67e-23

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: 91.57  E-value: 2.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684   12 INGLVLAGGKSTRMGTA-KDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQ--LENFDTSYNALTDTFLNM-GPFGGIL 87
Cdd:TIGR02665   1 ISGVILAGGRARRMGGRdKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPerYAQAGFGLPVVPDALADFpGPLAGIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684   88 SALRSQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESPFdGLPEPLITIWEPKSYPLLLNFLGIGNTCPRKVL 167
Cdd:TIGR02665  81 AGLRWAGTDWVLTVPCDTPFLPEDLVARLAAALEASDADIAVAHDG-GRWHPVFALWPVALAPDLEAFLAAGERRVRRFY 159

                         170       180
                  ....*....|....*....|....*
gi 639228684  168 INSDTLIIK-PQNPDALMNVNTPDD 191
Cdd:TIGR02665 160 ARHGAVAVDfSDSPDAFANLNTPED 184
 
Name Accession Description Interval E-value
PRK14490 PRK14490
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ...
 12-204 6.52e-65

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional


Pssm-ID: 237728 [Multi-domain]  Cd Length: 369  Bit Score: 204.13  E-value: 6.52e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  12 INGLVLAGGKSTRMGTAKDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQLENF-DTSYNALTDTFLNMGPFGGILSAL 90
Cdd:PRK14490 175 LSGLVLAGGRSSRMGSDKALLSYHESNQLVHTAALLRPHCQEVFISCRAEQAEQYrSFGIPLITDSYLDIGPLGGLLSAQ 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  91 RSQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESPFDGLPEPLITIWEPKS-YPLLLNFLGiGNTCPRKVLIN 169
Cdd:PRK14490 255 RHHPDAAWLVVACDLPFLDEATLQQLVEGRNPFRFATAFRHPDSGRPEPLCAIYEPKSrLRLLLRHAA-GNNSLRSFLAT 333

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 639228684 170 SDTLIIKPQNPDALMNVNTPDDAKKAQQVLNNSKD 204
Cdd:PRK14490 334 SRIEELEPTDPEALQNINDPEEMDRAERALSTTKE 368
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 10-197 2.02e-55

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: 174.22  E-value: 2.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  10 PSINGLVLAGGKSTRMGTAKDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQLENFdTSYNALTDTFLNMGPFGGILSA 89
Cdd:COG0746    3 MPITGVILAGGRSRRMGQDKALLPLGGRPLLERVLERLRPQVDEVVIVANRPERYAA-LGVPVVPDDPPGAGPLAGILAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  90 LRSQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESpfDGLPEPLITIWEPKSYPLLLNFLGIGNTCPRKVLIN 169
Cdd:COG0746   82 LEAAPAEWVLVLACDMPFLPPDLVRRLLEALEEGADAVVPRS--GGRLEPLFALYRRSLLPALEAALAEGERSLRALLER 159

                        170       180
                 ....*....|....*....|....*....
gi 639228684 170 SDTLIIK-PQNPDALMNVNTPDDAKKAQQ 197
Cdd:COG0746  160 LDVVYVPfEDLDDAFFNVNTPEDLARAEE 188
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 12-191 1.25e-49

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: 159.28  E-value: 1.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  12 INGLVLAGGKSTRMGTAKDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQLENFDTSYNALTDTFLNMGPFGGILSALR 91
Cdd:cd02503    1 ITGVILAGGKSRRMGGDKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLGVPVIPDEPPGKGPLAGILAALR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  92 SQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESpfDGLPEPLITIWEPKSYPLLLNFLGIGNTCPRKVLINSD 171
Cdd:cd02503   81 AAPADWVLVLACDMPFLPPELLERLLAAAEEGADAVVPKS--GGRLQPLHALYHKSLLPALEELLEAGERRLRRLLEKLG 158

                        170       180
                 ....*....|....*....|..
gi 639228684 172 TLIIK--PQNPDALMNVNTPDD 191
Cdd:cd02503  159 VQYVEfeDERLDAFFNINTPED 180
PRK14500 PRK14500
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; ...
 14-196 7.57e-48

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; Provisional


Pssm-ID: 237734 [Multi-domain]  Cd Length: 346  Bit Score: 159.67  E-value: 7.57e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  14 GLVLAGGKSTRMGTAKDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQ-----LENFDTsynaLTDTFLNMGPFGGILS 88
Cdd:PRK14500 163 GLVLTGGKSRRMGKDKALLNYQGQPHAQYLYDLLAKYCEQVFLSARPSQwqgtpLENLPT----LPDRGESVGPISGILT 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  89 ALRSQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESPFDGLPEPLITIWEPKSYPLLLNFLGIGNTCPRKVLI 168
Cdd:PRK14500 239 ALQSYPGVNWLVVACDLAYLNSETVEKLLAHYRQDLVATCYENPDQGFPEALCAIYTPQALQVFEKAYAEGLYCPVKILQ 318

                        170       180
                 ....*....|....*....|....*...
gi 639228684 169 NSDTLIIKPQNPDALMNVNTPDDAKKAQ 196
Cdd:PRK14500 319 RAPCQLIKPDNLFDIANINTPEEYGQIN 346
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 14-157 8.96e-30

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: 107.67  E-value: 8.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684   14 GLVLAGGKSTRMGTAKDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQLENFDTSYNA--LTDTFLNMGPFGGILSALR 91
Cdd:pfam12804   1 AVILAGGRSSRMGGDKALLPLGGKPLLERVLERLRPAGDEVVVVANDEEVLAALAGLGVpvVPDPDPGQGPLAGLLAALR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639228684   92 -SQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESPFDGLPEPLitIWEPKSYPLLLNFLG 157
Cdd:pfam12804  81 aAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDGGRGHPL--LYRRRLLPALEALLG 145
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 10-199 2.06e-29

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 107.58  E-value: 2.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  10 PSINGLVLAGGKSTRM-GTAKDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQLENFDTSYNALTDTFLNM-GPFGGIL 87
Cdd:PRK00317   2 PPITGVILAGGRSRRMgGVDKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLARYAAFGLPVIPDSLADFpGPLAGIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  88 SALRSQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESPfDGLPEPLITIWEPKSYPLLLNFLGIGNTCPRKVL 167
Cdd:PRK00317  82 AGLKQARTEWVLVVPCDTPFIPPDLVARLAQAAGKDDADVAWAHD-GGRLHPTFALYSVALLPDLEAYLAAGERKVMAFY 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 639228684 168 INSDTLIIK-PQNPDALMNVNTPDDAKKAQQVL 199
Cdd:PRK00317 161 ARHGGVAVDfSDPKDAFFNINTPEDLAQLEELL 193
molyb_mobA TIGR02665
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ...
 12-191 2.67e-23

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: 91.57  E-value: 2.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684   12 INGLVLAGGKSTRMGTA-KDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQ--LENFDTSYNALTDTFLNM-GPFGGIL 87
Cdd:TIGR02665   1 ISGVILAGGRARRMGGRdKGLVELGGKPLIEHVLARLRPQVSDLAISANRNPerYAQAGFGLPVVPDALADFpGPLAGIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684   88 SALRSQRDKAWLVVACDLPLLDKNSLSFLTASRNSEKVATTYESPFdGLPEPLITIWEPKSYPLLLNFLGIGNTCPRKVL 167
Cdd:TIGR02665  81 AGLRWAGTDWVLTVPCDTPFLPEDLVARLAAALEASDADIAVAHDG-GRWHPVFALWPVALAPDLEAFLAAGERRVRRFY 159

                         170       180
                  ....*....|....*....|....*
gi 639228684  168 INSDTLIIK-PQNPDALMNVNTPDD 191
Cdd:TIGR02665 160 ARHGAVAVDfSDSPDAFANLNTPED 184
PRK02726 PRK02726
molybdenum cofactor guanylyltransferase;
10-191 2.84e-17

molybdenum cofactor guanylyltransferase;


Pssm-ID: 235063  Cd Length: 200  Bit Score: 76.23  E-value: 2.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  10 PSINGLVLAGGKSTRMGTAKDLLNWHGKEQRYFAADLLAPFCDEVFISC----RQDQLenFDTSYNALTDTFLNMGPFGG 85
Cdd:PRK02726   6 NNLVALILAGGKSSRMGQDKALLPWQGVPLLQRVARIAAACADEVYIITpwpeRYQSL--LPPGCHWLREPPPSQGPLVA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  86 ILSALRsQRDKAW-LVVACDLPLLDKNSLsfltaSRNSEKVATTYESPFDGLP------EPLITIWEPKSYPLLLNFLGI 158
Cdd:PRK02726  84 FAQGLP-QIKTEWvLLLACDLPRLTVDVL-----QEWLQQLENVPEEAIAALPkqekgwEPLCGFYRRRCLPSLEQFIQQ 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 639228684 159 GNTCPRKVLINSDTLIIKPQNPDALMNVNTPDD 191
Cdd:PRK02726 158 GGRSFQGWLAQVPVQELALSDPDMLFNCNTPED 190
PRK00560 PRK00560
molybdenum cofactor guanylyltransferase MobA;
9-201 9.31e-14

molybdenum cofactor guanylyltransferase MobA;


Pssm-ID: 167003  Cd Length: 196  Bit Score: 66.71  E-value: 9.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684   9 IPSINGLVLAGGKSTRMGTAKDLLNWHGKEQ-RYFAADLLAPFCDEVFISCRQDQLEnFDTSY--NALTDTFlnmGPFGG 85
Cdd:PRK00560   6 IDNIPCVILAGGKSSRMGENKALLPFGSYSSlLEYQYTRLLKLFKKVYISTKDKKFE-FNAPFllEKESDLF---SPLFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  86 ILSALRSQRDKAWLVVACDLPLLDKNSLSFLTASRNSEkvATTYESPfdGLPEPLITIWEPKSYPLLLNFLGIGNTCPRK 165
Cdd:PRK00560  82 IINAFLTLQTPEIFFISVDTPFVSFESIKKLCGKENFS--VTYAKSP--TKEHYLISLWHQSLLNALIYALKTQNYRLSD 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 639228684 166 VLINSDTLIIKPQNPDALMNVNTPDDAKKAQQVLNN 201
Cdd:PRK00560 158 LVKNTSSQAVHFEDEEEFLNLNTLKDYELALQILKS 193
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 12-191 3.18e-13

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 67.08  E-value: 3.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  12 INGLVLAGGKSTRM-GTAKDLLNWHGKEQRYFAADLLAPFCDEVFISCRQDQlENFDTSYNALT---DTFLNM-GPFGGI 86
Cdd:PRK14489   6 IAGVILAGGLSRRMnGRDKALILLGGKPLIERVVDRLRPQFARIHLNINRDP-ARYQDLFPGLPvypDILPGFqGPLSGI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  87 LSALrSQRDKAWL-VVACDLPLLDKNSLSFLTASRNSEKVATTYesPFDG-LPEPLITIWEPKSYPLLLNFLGIGNtcpR 164
Cdd:PRK14489  85 LAGL-EHADSEYLfVVACDTPFLPENLVKRLSKALAIEGADIAV--PHDGeRAHPLFALYHRSCLPALRRYLAEGE---R 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 639228684 165 KVL-----INSDTLIIKPQNpDALMNVNTPDD 191
Cdd:PRK14489 159 RLFdffqrQRVRYVDLSTQK-DAFFNVNTPED 189
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 17-199 2.02e-09

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 54.51  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  17 LAGGKSTRMGTA-KDLLNWHGKE--QRYFAAdLLAPFCDEVFIScrqdqlenfdTSYNA-LTDTFLN-------MGPFGG 85
Cdd:COG2266    1 MAGGKGTRLGGGeKPLLEICGKPmiDRVIDA-LEESCIDKIYVA----------VSPNTpKTREYLKergveviETPGEG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  86 ----ILSALRSQRDKAwLVVACDLPLLDKNSL-SFLTASRNSEKVATTYESPFD-----GLPEPLITIWEPKSYPLLLNF 155
Cdd:COG2266   70 yvedLNEALESISGPV-LVVPADLPLLTPEIIdDIIDAYLESGKPSLTVVVPAAlkrelGVSPDTTFEIDGELVPTGINI 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 639228684 156 LGigntcPRKVLINSDTLIIKpqNPDALMNVNTPDDAKKAQQVL 199
Cdd:COG2266  149 VD-----GSDGEQEETNLVLD--DPRLALNVNTPEDLKLAEKLL 185
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 12-191 2.04e-09

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: 54.49  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  12 INGLVLAGGKSTRMGTAKDLLNWHGKEQ-RYFAADLLAPFCDEVFISCRQDQLENFDTSYNALTDTFLNMGPFGGILSAL 90
Cdd:cd04182    1 IAAIILAAGRSSRMGGNKLLLPLDGKPLlRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEEGMSSSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  91 R------SQRDKAWLVVACDLPLLDKNSLSFLTASRNSEK---VATTYE-SPfdGLPepliTIWEPKSYPLLLNFLgiGN 160
Cdd:cd04182   81 AaglealPADADAVLILLADQPLVTAETLRALIDAFREDGagiVAPVYQgRR--GHP----VLFPRSLFPELLALS--GD 152

                        170       180       190
                 ....*....|....*....|....*....|..
gi 639228684 161 TCPRKVL-INSDTLIIKPQNPDALMNVNTPDD 191
Cdd:cd04182  153 KGARSLLrAHPDRVVVEVDDPGVLIDIDTPED 184
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
10-197 2.27e-07

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 49.00  E-value: 2.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  10 PSINGLVLAGGKSTRMGTAKDLLNWHGK---EQryfAAD-LLAPFCDEVFI------SCRQDQLENFDTS--YNALTDTf 77
Cdd:COG2068    2 SKVAAIILAAGASSRMGRPKLLLPLGGKpllER---AVEaALAAGLDPVVVvlgadaEEVAAALAGLGVRvvVNPDWEE- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639228684  78 lnmGPFGGI---LSALRSQRDkAWLVVACDLPLLDKNSL-SFLTASRNSEK--VATTYE----SPfdglpePLItiwePK 147
Cdd:COG2068   78 ---GMSSSLragLAALPADAD-AVLVLLGDQPLVTAETLrRLLAAFRESPAsiVAPTYDgrrgHP------VLF----SR 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 639228684 148 SY-PLLLNfLGiGNTCPRKVLIN--SDTLIIKPQNPDALMNVNTPDDAKKAQQ 197
Cdd:COG2068  144 RLfPELLA-LT-GDQGARALLRRhpDRVRLVPVDDPGVLLDIDTPEDLARLLA 194
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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