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Conserved domains on  [gi|499182430|ref|WP_010879970|]
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molybdopterin adenylyltransferase [Aquifex aeolicus]

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
 5-178 6.09e-121

molybdenum cofactor biosynthesis protein MogA; Provisional


:

Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 339.24  E-value: 6.09e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430   5 KAVIGVVTISDRASKGIYEDISGKAIIDYLKDVIITPFEVEYRVIPDERDLIEKTLIELADEKGCSLILTTGGTGPAPRD 84
Cdd:PRK09417   3 TLKIGLVSISDRASSGVYEDKGIPALEEWLASALTSPFEIETRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTGPARRD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430  85 VTPEATEAVCEKMLPGFGELMRQVSLKQVPTAILSRQTAGIRGSCLIVNLPGKPQSIKVCLD------------AVMPAI 152
Cdd:PRK09417  83 VTPEATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLEglkdadgnvvvpGIFAAV 162

                        170       180
                 ....*....|....*....|....*.
gi 499182430 153 PYCIDLIGGAYIDTDPNKVKAFRPKK 178
Cdd:PRK09417 163 PYCIDLIGGPYIETNPEVVKAFRPKS 188
 
Name Accession Description Interval E-value
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 5-178 6.09e-121

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 339.24  E-value: 6.09e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430   5 KAVIGVVTISDRASKGIYEDISGKAIIDYLKDVIITPFEVEYRVIPDERDLIEKTLIELADEKGCSLILTTGGTGPAPRD 84
Cdd:PRK09417   3 TLKIGLVSISDRASSGVYEDKGIPALEEWLASALTSPFEIETRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTGPARRD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430  85 VTPEATEAVCEKMLPGFGELMRQVSLKQVPTAILSRQTAGIRGSCLIVNLPGKPQSIKVCLD------------AVMPAI 152
Cdd:PRK09417  83 VTPEATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLEglkdadgnvvvpGIFAAV 162

                        170       180
                 ....*....|....*....|....*.
gi 499182430 153 PYCIDLIGGAYIDTDPNKVKAFRPKK 178
Cdd:PRK09417 163 PYCIDLIGGPYIETNPEVVKAFRPKS 188
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 1-166 2.38e-81

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: 238.09  E-value: 2.38e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430   1 MSEKKAV----IGVVTISDRASKGIYEDISGKAIIDYLKDviITPFEVEYRVIPDERDLIEKTLIELADEKGCSLILTTG 76
Cdd:COG0521    1 MSSARAFvplrIAVLTVSDRRSRGEREDTSGPALVELLEE--AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430  77 GTGPAPRDVTPEATEAVCEKMLPGFGELMRQVSLKQ-VPTAILSRQTAGIRGSCLIVNLPGKPQSIKVCLDAVMPAIPYC 155
Cdd:COG0521   79 GTGLSPRDVTPEATRPLLDKELPGFGELFRALSLEEiGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHA 158

                        170
                 ....*....|.
gi 499182430 156 IDLIGGAYIDT 166
Cdd:COG0521  159 VDLLNGVDHEC 169
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 8-159 4.96e-77

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: 226.59  E-value: 4.96e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430   8 IGVVTISDRASKGIYEDISGKAIIDYLKDVIITpfEVEYRVIPDERDLIEKTLIELADEKGCSLILTTGGTGPAPRDVTP 87
Cdd:cd00886    3 AAVLTVSDTRSAGEAEDRSGPALVELLEEAGHE--VVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRDVTP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499182430  88 EATEAVCEKMLPGFGELMRQVSLKQVPTAILSRQTAGIRGSCLIVNLPGKPQSIKVCLDAVMPAIPYCIDLI 159
Cdd:cd00886   81 EATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 8-149 4.36e-40

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: 132.83  E-value: 4.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430    8 IGVVTISDRASKG-------IYEDISGKAIIDYLKDVIITPFEveYRVIPDERDLIEKTLIELADEkgCSLILTTGGTGP 80
Cdd:TIGR00177   3 VAVISVGDELVEGgqplepgQIYDSNGPLLAALLQEAGFNVVR--LGIVPDDPEEIREILRKAVDE--ADVVLTTGGTGV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499182430   81 APRDVTPEATEAVCEKMLPGFGELMRQVSLkqvptAILSR----QTAGIRGSCLIVNLPGKPQSIKVCLDAVM 149
Cdd:TIGR00177  79 GPRDVTPEALEELGEKEIPGFGEFRMLSSL-----PVLSRpgkpATAGVRGGTLIFNLPGNPVSALVTFEVLI 146
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 9-148 2.60e-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: 128.09  E-value: 2.60e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430     9 GVVTISDRASKG-IYEDISGKAIIDYLKDVIITPFEVEYRVIPDERDLIEKTLIELADEkgCSLILTTGGTGPAPRDVTP 87
Cdd:smart00852   1 AIISTGDELLSGgQIRDSNGPMLAALLRELGIEVVRVVVVGGPDDPEAIREALREALAE--ADVVITTGGTGPGPDDLTP 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499182430    88 EATEAVCEKMLPGFGELMRQVSlKQVPTAILSRQTAGIRGSCLIVNLPGKPQSIKVCLDAV 148
Cdd:smart00852  79 EALAELGGRELLGHGVAMRPGG-PPGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 9-153 4.80e-30

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: 106.95  E-value: 4.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430    9 GVVTISDRASKGIYEDISGKAIIDYLKDviiTPFEV-EYRVIPDERDLIEKTLIELADEkgCSLILTTGGTGPAPRDVTP 87
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEViRYGIVPDDPEAIKEALRAAAEE--ADVVITTGGTGPGPDDVTP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499182430   88 EATEAVCEKMLPGFGELMRQVSLKQ------VPTAILSrqtagiRGSCLIVNLPGKPQSIKVCLDA-VMPAIP 153
Cdd:pfam00994  76 EALAELGGRELPGFEELFRGVSLKPgkpvgtAPGAILS------RAGKTVFGLPGSPVAAKVMFELlLLPLLR 142
 
Name Accession Description Interval E-value
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 5-178 6.09e-121

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 339.24  E-value: 6.09e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430   5 KAVIGVVTISDRASKGIYEDISGKAIIDYLKDVIITPFEVEYRVIPDERDLIEKTLIELADEKGCSLILTTGGTGPAPRD 84
Cdd:PRK09417   3 TLKIGLVSISDRASSGVYEDKGIPALEEWLASALTSPFEIETRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTGPARRD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430  85 VTPEATEAVCEKMLPGFGELMRQVSLKQVPTAILSRQTAGIRGSCLIVNLPGKPQSIKVCLD------------AVMPAI 152
Cdd:PRK09417  83 VTPEATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLEglkdadgnvvvpGIFAAV 162

                        170       180
                 ....*....|....*....|....*.
gi 499182430 153 PYCIDLIGGAYIDTDPNKVKAFRPKK 178
Cdd:PRK09417 163 PYCIDLIGGPYIETNPEVVKAFRPKS 188
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 1-166 2.38e-81

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: 238.09  E-value: 2.38e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430   1 MSEKKAV----IGVVTISDRASKGIYEDISGKAIIDYLKDviITPFEVEYRVIPDERDLIEKTLIELADEKGCSLILTTG 76
Cdd:COG0521    1 MSSARAFvplrIAVLTVSDRRSRGEREDTSGPALVELLEE--AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430  77 GTGPAPRDVTPEATEAVCEKMLPGFGELMRQVSLKQ-VPTAILSRQTAGIRGSCLIVNLPGKPQSIKVCLDAVMPAIPYC 155
Cdd:COG0521   79 GTGLSPRDVTPEATRPLLDKELPGFGELFRALSLEEiGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHA 158

                        170
                 ....*....|.
gi 499182430 156 IDLIGGAYIDT 166
Cdd:COG0521  159 VDLLNGVDHEC 169
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 8-159 4.96e-77

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: 226.59  E-value: 4.96e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430   8 IGVVTISDRASKGIYEDISGKAIIDYLKDVIITpfEVEYRVIPDERDLIEKTLIELADEKGCSLILTTGGTGPAPRDVTP 87
Cdd:cd00886    3 AAVLTVSDTRSAGEAEDRSGPALVELLEEAGHE--VVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRDVTP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499182430  88 EATEAVCEKMLPGFGELMRQVSLKQVPTAILSRQTAGIRGSCLIVNLPGKPQSIKVCLDAVMPAIPYCIDLI 159
Cdd:cd00886   81 EATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 10-161 7.63e-42

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 142.39  E-value: 7.63e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430  10 VVTISDRASKGIYEDISGKAIIDYLKDVIITPfeVEYRVIPDERDLIEKTLIELAdEKGCSLILTTGGTGPAPRDVTPEA 89
Cdd:PRK03604 160 VLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEV--SHYTIIPDEPAEIAAAVAAWI-AEGYALIITTGGTGLGPRDVTPEA 236

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499182430  90 TEAVCEKMLPGFGELMRQVSLKQVPTAILSRQTAGIRGSCLIVNLPGKPQSIKVCLDAVMPAIPYCIDLIGG 161
Cdd:PRK03604 237 LAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPALFHAFAMVKG 308
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 8-149 4.36e-40

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: 132.83  E-value: 4.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430    8 IGVVTISDRASKG-------IYEDISGKAIIDYLKDVIITPFEveYRVIPDERDLIEKTLIELADEkgCSLILTTGGTGP 80
Cdd:TIGR00177   3 VAVISVGDELVEGgqplepgQIYDSNGPLLAALLQEAGFNVVR--LGIVPDDPEEIREILRKAVDE--ADVVLTTGGTGV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499182430   81 APRDVTPEATEAVCEKMLPGFGELMRQVSLkqvptAILSR----QTAGIRGSCLIVNLPGKPQSIKVCLDAVM 149
Cdd:TIGR00177  79 GPRDVTPEALEELGEKEIPGFGEFRMLSSL-----PVLSRpgkpATAGVRGGTLIFNLPGNPVSALVTFEVLI 146
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 9-148 2.60e-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: 128.09  E-value: 2.60e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430     9 GVVTISDRASKG-IYEDISGKAIIDYLKDVIITPFEVEYRVIPDERDLIEKTLIELADEkgCSLILTTGGTGPAPRDVTP 87
Cdd:smart00852   1 AIISTGDELLSGgQIRDSNGPMLAALLRELGIEVVRVVVVGGPDDPEAIREALREALAE--ADVVITTGGTGPGPDDLTP 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499182430    88 EATEAVCEKMLPGFGELMRQVSlKQVPTAILSRQTAGIRGSCLIVNLPGKPQSIKVCLDAV 148
Cdd:smart00852  79 EALAELGGRELLGHGVAMRPGG-PPGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 8-161 5.56e-37

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 134.55  E-value: 5.56e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430   8 IGVVTISDRASKGIYEDISGK---AIIDYLKDVIITPFEVEYRVIPDERDLIEKTLIELADEKGCSLILTTGGTGPAPRD 84
Cdd:PLN02699 461 VAILTVSDTVSSGAGPDRSGPravSVVNSSSEKLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTGFTPRD 540

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499182430  85 VTPEATEAVCEKMLPGFGELMRQVSLKQVPTAILSRQTAGIRGSCLIVNLPGKPQSIKVCLDAVMPAIPYCIDLIGG 161
Cdd:PLN02699 541 VTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALKQIKG 617
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 8-152 1.43e-35

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: 120.91  E-value: 1.43e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430   8 IGVVTISDRASKGIYEDISGKAIIDYLKDVIITPfeVEYRVIPDERDLIEKTLIELADEkgCSLILTTGGTGPAPRDVTP 87
Cdd:cd00758    2 VAIVTVSDELSQGQIEDTNGPALEALLEDLGCEV--IYAGVVPDDADSIRAALIEASRE--ADLVLTTGGTGVGRRDVTP 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499182430  88 EATEAVCEKMLPGFGelmrqvslkqVPTAILSRQTAGIRGSCLIVNLPGKPQSIKVCLDA-VMPAI 152
Cdd:cd00758   78 EALAELGEREAHGKG----------VALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEAlVLPAL 133
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 9-153 4.80e-30

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: 106.95  E-value: 4.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430    9 GVVTISDRASKGIYEDISGKAIIDYLKDviiTPFEV-EYRVIPDERDLIEKTLIELADEkgCSLILTTGGTGPAPRDVTP 87
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEViRYGIVPDDPEAIKEALRAAAEE--ADVVITTGGTGPGPDDVTP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499182430   88 EATEAVCEKMLPGFGELMRQVSLKQ------VPTAILSrqtagiRGSCLIVNLPGKPQSIKVCLDA-VMPAIP 153
Cdd:pfam00994  76 EALAELGGRELPGFEELFRGVSLKPgkpvgtAPGAILS------RAGKTVFGLPGSPVAAKVMFELlLLPLLR 142
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 44-152 6.27e-09

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: 53.94  E-value: 6.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430  44 VEYRVIPDERDLIEKTLIELADEkgCSLILTTGGTGPAPRDVTPEATEAVcekmlpGFGELMRQVSLKqvPTailSRQTA 123
Cdd:COG0303  216 VDLGIVPDDPEALRAALREALAE--ADLVITSGGVSVGDYDLVKEALEEL------GAEVLFHKVAMK--PG---KPLAF 282

                         90       100       110
                 ....*....|....*....|....*....|
gi 499182430 124 GIRGSCLIVNLPGKPQSIKVCLDA-VMPAI 152
Cdd:COG0303  283 GRLGGKPVFGLPGNPVSALVTFELfVRPAL 312
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 44-152 8.48e-08

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: 50.57  E-value: 8.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499182430  44 VEYRVIPDERDLIEKTLIELADEkgCSLILTTGGTGPAPRDVTPEATEAVcekmlpGFGELMRQVSLKqvPTailSRQTA 123
Cdd:cd00887  212 VDLGIVPDDPEALREALEEALEE--ADVVITSGGVSVGDYDFVKEVLEEL------GGEVLFHGVAMK--PG---KPLAF 278

                         90       100       110
                 ....*....|....*....|....*....|
gi 499182430 124 GIRGSCLIVNLPGKPQSIKVCLDA-VMPAI 152
Cdd:cd00887  279 GRLGGKPVFGLPGNPVSALVTFELfVRPAL 308
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 42-95 7.09e-05

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: 41.32  E-value: 7.09e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499182430  42 FEVEY-RVIPDERDLIEKTLIELADEkgCSLILTTGGTGPAPRDVTpeaTEAVCE 95
Cdd:cd00885   33 IEVYRvTVVGDDEDRIAEALRRASER--ADLVITTGGLGPTHDDLT---REAVAK 82
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 42-95 7.24e-05

ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];


Pssm-ID: 440678  Cd Length: 249  Bit Score: 41.64  E-value: 7.24e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499182430  42 FEVEY-RVIPDERDLIEKTLIELADEkgCSLILTTGGTGPAPRDVTpeaTEAVCE 95
Cdd:COG1058   33 IDVYRiTTVGDDPERIVEALREALAR--ADLVITTGGLGPTPDDLT---REAVAE 82
 
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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