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Conserved domains on  [gi|502756402|ref|WP_012991386|]
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molybdopterin adenylyltransferase [Thermocrinis albus]

Protein Classification

molybdopterin adenylyltransferase( domain architecture ID 10013225)

molybdopterin adenylyltransferase catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor

CATH:  3.40.980.10
EC:  2.7.7.75
Gene Ontology:  GO:0005524|GO:0006777|GO:0061598
PubMed:  21206014|12504674
SCOP:  4000598

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 1-175 2.90e-121

molybdenum cofactor biosynthesis protein MogA; Provisional


:

Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 340.01  E-value: 2.90e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402   1 MEKAKFGVLTVSDRASRGEYEDISGKYIIEYLKDVVTSPFEIVYRVVPDERDIIEGALIHMADEEGCCLILTTGGTGPAP 80
Cdd:PRK09417   1 MDTLKIGLVSISDRASSGVYEDKGIPALEEWLASALTSPFEIETRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTGPAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402  81 RDVTPEATMAVCHKILPGFGELMRQVSLQQVPTAILSRQLAGIRNRTLIINLPGKPQSIKLCLD------------AVFP 148
Cdd:PRK09417  81 RDVTPEATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLEglkdadgnvvvpGIFA 160

                        170       180
                 ....*....|....*....|....*..
gi 502756402 149 AVPYCIDLIGGPYITTDENKVKAFRPK 175
Cdd:PRK09417 161 AVPYCIDLIGGPYIETNPEVVKAFRPK 187
 
Name Accession Description Interval E-value
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 1-175 2.90e-121

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 340.01  E-value: 2.90e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402   1 MEKAKFGVLTVSDRASRGEYEDISGKYIIEYLKDVVTSPFEIVYRVVPDERDIIEGALIHMADEEGCCLILTTGGTGPAP 80
Cdd:PRK09417   1 MDTLKIGLVSISDRASSGVYEDKGIPALEEWLASALTSPFEIETRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTGPAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402  81 RDVTPEATMAVCHKILPGFGELMRQVSLQQVPTAILSRQLAGIRNRTLIINLPGKPQSIKLCLD------------AVFP 148
Cdd:PRK09417  81 RDVTPEATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLEglkdadgnvvvpGIFA 160

                        170       180
                 ....*....|....*....|....*..
gi 502756402 149 AVPYCIDLIGGPYITTDENKVKAFRPK 175
Cdd:PRK09417 161 AVPYCIDLIGGPYIETNPEVVKAFRPK 187
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 1-164 2.78e-83

Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440287 [Multi-domain]  Cd Length: 169  Bit Score: 243.10  E-value: 2.78e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402   1 MEKAKFGVLTVSDRASRGEYEDISGKYIIEYLKDvvTSPFEIVYRVVPDERDIIEGALIHMADEEGCCLILTTGGTGPAP 80
Cdd:COG0521    7 FVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE--AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTTGGTGLSP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402  81 RDVTPEATMAVCHKILPGFGELMRQVSLQQ-VPTAILSRQLAGIRNRTLIINLPGKPQSIKLCLDAVFPAVPYCIDLIGG 159
Cdd:COG0521   85 RDVTPEATRPLLDKELPGFGELFRALSLEEiGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHAVDLLNG 164


                 ....*
gi 502756402 160 PYITT 164
Cdd:COG0521  165 VDHEC 169
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 5-157 7.44e-78

MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.


Pssm-ID: 238451 [Multi-domain]  Cd Length: 152  Bit Score: 228.52  E-value: 7.44e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402   5 KFGVLTVSDRASRGEYEDISGKYIIEYLKDvvtSPFEIV-YRVVPDERDIIEGALIHMADEEGCCLILTTGGTGPAPRDV 83
Cdd:cd00886    2 RAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVaYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRDV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502756402  84 TPEATMAVCHKILPGFGELMRQVSLQQVPTAILSRQLAGIRNRTLIINLPGKPQSIKLCLDAVFPAVPYCIDLI 157
Cdd:cd00886   79 TPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 7-146 3.92e-38

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.


Pssm-ID: 214856 [Multi-domain]  Cd Length: 138  Bit Score: 127.32  E-value: 3.92e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402     7 GVLTVSDRASRGEY-EDISGKYIIEYLKDVVTSPFEIVYRVVPDERDIIEGALIHMADEegCCLILTTGGTGPAPRDVTP 85
Cdd:smart00852   1 AIISTGDELLSGGQiRDSNGPMLAALLRELGIEVVRVVVVGGPDDPEAIREALREALAE--ADVVITTGGTGPGPDDLTP 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502756402    86 EATMAVCHKILPGFGELMRQVSLqQVPTAILSRQLAGIRNRTLIINLPGKPQSIKLCLDAV 146
Cdd:smart00852  79 EALAELGGRELLGHGVAMRPGGP-PGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 5-147 1.22e-37

molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.


Pssm-ID: 272944 [Multi-domain]  Cd Length: 148  Bit Score: 126.66  E-value: 1.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402    5 KFGVLTVSDRASRG-------EYEDISGKYIIEYLKDVVTSPFEivYRVVPDERDIIEGALIHMADEegCCLILTTGGTG 77
Cdd:TIGR00177   2 RVAVISVGDELVEGgqplepgQIYDSNGPLLAALLQEAGFNVVR--LGIVPDDPEEIREILRKAVDE--ADVVLTTGGTG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502756402   78 PAPRDVTPEATMAVCHKILPGFGELMRQVSLQqvptaILSR----QLAGIRNRTLIINLPGKPQSIKLCLDAVF 147
Cdd:TIGR00177  78 VGPRDVTPEALEELGEKEIPGFGEFRMLSSLP-----VLSRpgkpATAGVRGGTLIFNLPGNPVSALVTFEVLI 146
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 7-146 3.96e-28

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.


Pssm-ID: 425979 [Multi-domain]  Cd Length: 143  Bit Score: 101.94  E-value: 3.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402    7 GVLTVSDRASRGEYEDISGKYIIEYLKDvvtSPFEIV-YRVVPDERDIIEGALIHMADEEGccLILTTGGTGPAPRDVTP 85
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIrYGIVPDDPEAIKEALRAAAEEAD--VVITTGGTGPGPDDVTP 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502756402   86 EATMAVCHKILPGFGELMRQVSLQQ------VPTAILSrqlagiRNRTLIINLPGKPQSIKLCLDAV 146
Cdd:pfam00994  76 EALAELGGRELPGFEELFRGVSLKPgkpvgtAPGAILS------RAGKTVFGLPGSPVAAKVMFELL 136
 
Name Accession Description Interval E-value
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 1-175 2.90e-121

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 340.01  E-value: 2.90e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402   1 MEKAKFGVLTVSDRASRGEYEDISGKYIIEYLKDVVTSPFEIVYRVVPDERDIIEGALIHMADEEGCCLILTTGGTGPAP 80
Cdd:PRK09417   1 MDTLKIGLVSISDRASSGVYEDKGIPALEEWLASALTSPFEIETRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTGPAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402  81 RDVTPEATMAVCHKILPGFGELMRQVSLQQVPTAILSRQLAGIRNRTLIINLPGKPQSIKLCLD------------AVFP 148
Cdd:PRK09417  81 RDVTPEATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLEglkdadgnvvvpGIFA 160

                        170       180
                 ....*....|....*....|....*..
gi 502756402 149 AVPYCIDLIGGPYITTDENKVKAFRPK 175
Cdd:PRK09417 161 AVPYCIDLIGGPYIETNPEVVKAFRPK 187
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 1-164 2.78e-83

Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440287 [Multi-domain]  Cd Length: 169  Bit Score: 243.10  E-value: 2.78e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402   1 MEKAKFGVLTVSDRASRGEYEDISGKYIIEYLKDvvTSPFEIVYRVVPDERDIIEGALIHMADEEGCCLILTTGGTGPAP 80
Cdd:COG0521    7 FVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE--AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTTGGTGLSP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402  81 RDVTPEATMAVCHKILPGFGELMRQVSLQQ-VPTAILSRQLAGIRNRTLIINLPGKPQSIKLCLDAVFPAVPYCIDLIGG 159
Cdd:COG0521   85 RDVTPEATRPLLDKELPGFGELFRALSLEEiGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHAVDLLNG 164


                 ....*
gi 502756402 160 PYITT 164
Cdd:COG0521  165 VDHEC 169
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 5-157 7.44e-78

MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.


Pssm-ID: 238451 [Multi-domain]  Cd Length: 152  Bit Score: 228.52  E-value: 7.44e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402   5 KFGVLTVSDRASRGEYEDISGKYIIEYLKDvvtSPFEIV-YRVVPDERDIIEGALIHMADEEGCCLILTTGGTGPAPRDV 83
Cdd:cd00886    2 RAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVaYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRDV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502756402  84 TPEATMAVCHKILPGFGELMRQVSLQQVPTAILSRQLAGIRNRTLIINLPGKPQSIKLCLDAVFPAVPYCIDLI 157
Cdd:cd00886   79 TPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 3-159 4.44e-41

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 140.08  E-value: 4.44e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402   3 KAKFGVLTVSDRASRGEYEDISGKYIIEYLKDvvtSPFEIV-YRVVPDERDIIEgALIHMADEEGCCLILTTGGTGPAPR 81
Cdd:PRK03604 155 RTSAAVLVLSDSIAAGTKEDRSGKLIVEGLEE---AGFEVShYTIIPDEPAEIA-AAVAAWIAEGYALIITTGGTGLGPR 230

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502756402  82 DVTPEATMAVCHKILPGFGELMRQVSLQQVPTAILSRQLAGIRNRTLIINLPGKPQSIKLCLDAVFPAVPYCIDLIGG 159
Cdd:PRK03604 231 DVTPEALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPALFHAFAMVKG 308
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 7-146 3.92e-38

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.


Pssm-ID: 214856 [Multi-domain]  Cd Length: 138  Bit Score: 127.32  E-value: 3.92e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402     7 GVLTVSDRASRGEY-EDISGKYIIEYLKDVVTSPFEIVYRVVPDERDIIEGALIHMADEegCCLILTTGGTGPAPRDVTP 85
Cdd:smart00852   1 AIISTGDELLSGGQiRDSNGPMLAALLRELGIEVVRVVVVGGPDDPEAIREALREALAE--ADVVITTGGTGPGPDDLTP 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502756402    86 EATMAVCHKILPGFGELMRQVSLqQVPTAILSRQLAGIRNRTLIINLPGKPQSIKLCLDAV 146
Cdd:smart00852  79 EALAELGGRELLGHGVAMRPGGP-PGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 5-147 1.22e-37

molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.


Pssm-ID: 272944 [Multi-domain]  Cd Length: 148  Bit Score: 126.66  E-value: 1.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402    5 KFGVLTVSDRASRG-------EYEDISGKYIIEYLKDVVTSPFEivYRVVPDERDIIEGALIHMADEegCCLILTTGGTG 77
Cdd:TIGR00177   2 RVAVISVGDELVEGgqplepgQIYDSNGPLLAALLQEAGFNVVR--LGIVPDDPEEIREILRKAVDE--ADVVLTTGGTG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502756402   78 PAPRDVTPEATMAVCHKILPGFGELMRQVSLQqvptaILSR----QLAGIRNRTLIINLPGKPQSIKLCLDAVF 147
Cdd:TIGR00177  78 VGPRDVTPEALEELGEKEIPGFGEFRMLSSLP-----VLSRpgkpATAGVRGGTLIFNLPGNPVSALVTFEVLI 146
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 5-150 1.99e-37

MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. The domain is presumed to bind molybdopterin.


Pssm-ID: 238387 [Multi-domain]  Cd Length: 133  Bit Score: 125.53  E-value: 1.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402   5 KFGVLTVSDRASRGEYEDISGKYIIEYLKDVVTSPfeIVYRVVPDERDIIEGALIHMADEegCCLILTTGGTGPAPRDVT 84
Cdd:cd00758    1 RVAIVTVSDELSQGQIEDTNGPALEALLEDLGCEV--IYAGVVPDDADSIRAALIEASRE--ADLVLTTGGTGVGRRDVT 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502756402  85 PEATMAVCHKILPGFGelmrqvslqqVPTAILSRQLAGIRNRTLIINLPGKPQSIKLCLDA-VFPAV 150
Cdd:cd00758   77 PEALAELGEREAHGKG----------VALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEAlVLPAL 133
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 5-159 1.33e-36

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 133.40  E-value: 1.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402   5 KFGVLTVSDRASRGEYEDISGKYIIEylkdVVTSPFE-------IVYRVVPDERDIIEGALIHMADEEGCCLILTTGGTG 77
Cdd:PLN02699 460 KVAILTVSDTVSSGAGPDRSGPRAVS----VVNSSSEklggakvVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402  78 PAPRDVTPEATMAVCHKILPGFGELMRQVSLQQVPTAILSRQLAGIRNRTLIINLPGKPQSIKLCLDAVFPAVPYCIDLI 157
Cdd:PLN02699 536 FTPRDVTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALKQI 615


                 ..
gi 502756402 158 GG 159
Cdd:PLN02699 616 KG 617
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 7-146 3.96e-28

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.


Pssm-ID: 425979 [Multi-domain]  Cd Length: 143  Bit Score: 101.94  E-value: 3.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402    7 GVLTVSDRASRGEYEDISGKYIIEYLKDvvtSPFEIV-YRVVPDERDIIEGALIHMADEEGccLILTTGGTGPAPRDVTP 85
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIrYGIVPDDPEAIKEALRAAAEEAD--VVITTGGTGPGPDDVTP 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502756402   86 EATMAVCHKILPGFGELMRQVSLQQ------VPTAILSrqlagiRNRTLIINLPGKPQSIKLCLDAV 146
Cdd:pfam00994  76 EALAELGGRELPGFEELFRGVSLKPgkpvgtAPGAILS------RAGKTVFGLPGSPVAAKVMFELL 136
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 42-138 9.30e-06

Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440072 [Multi-domain]  Cd Length: 401  Bit Score: 44.69  E-value: 9.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402  42 IVYRVVPDERDIIEGALIHMADEegCCLILTTGGTGPAPRDVTPEAtmavchkilpgFGELMRQVSLQQV------PTAI 115
Cdd:COG0303  216 VDLGIVPDDPEALRAALREALAE--ADLVITSGGVSVGDYDLVKEA-----------LEELGAEVLFHKVamkpgkPLAF 282

                         90       100
                 ....*....|....*....|...
gi 502756402 116 lsrqlaGIRNRTLIINLPGKPQS 138
Cdd:COG0303  283 ------GRLGGKPVFGLPGNPVS 299
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 42-138 6.86e-05

MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF), an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MoeA, together with MoaB, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes.


Pssm-ID: 238452 [Multi-domain]  Cd Length: 394  Bit Score: 42.10  E-value: 6.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402  42 IVYRVVPDERDIIEGALIHMADEegCCLILTTGGTGPAPRDVTPEA------TMAVcHKI--LPGfgelmrqvslqqvpt 113
Cdd:cd00887  212 VDLGIVPDDPEALREALEEALEE--ADVVITSGGVSVGDYDFVKEVleelggEVLF-HGVamKPG--------------- 273

                         90       100
                 ....*....|....*....|....*
gi 502756402 114 ailSRQLAGIRNRTLIINLPGKPQS 138
Cdd:cd00887  274 ---KPLAFGRLGGKPVFGLPGNPVS 295
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
 45-91 2.05e-04

MoeA_like. This domain is similar to a domain found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. There this domain is presumed to bind molybdopterin. The exact function of this subgroup is unknown.


Pssm-ID: 239599  Cd Length: 312  Bit Score: 40.61  E-value: 2.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 502756402  45 RVVPDERDIIEGALIHMAdEEGCCLILTTGGTGPAPRDVTPEATMAV 91
Cdd:cd03522  199 VIVPHDEAAIAAAIAEAL-EAGAELLILTGGASVDPDDVTPAAIRAA 244
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 5-87 2.36e-04

Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.


Pssm-ID: 238450 [Multi-domain]  Cd Length: 170  Bit Score: 39.77  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502756402   5 KFGVLTVSDRASRGEYEDISGKYIIEYLkdvvtspFEI---VYR--VVPDERDIIEGALIHM---ADeegccLILTTGGT 76
Cdd:cd00885    1 TAEIIAIGDELLSGQIVDTNAAFLAKEL-------AELgieVYRvtVVGDDEDRIAEALRRAserAD-----LVITTGGL 68

                         90
                 ....*....|.
gi 502756402  77 GPAPRDVTPEA 87
Cdd:cd00885   69 GPTHDDLTREA 79
 
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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