NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16128750|ref|NP_415303|]
View 

protein MoaB [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

molybdenum cofactor biosynthesis protein B( domain architecture ID 10798402)

molybdenum cofactor biosynthesis protein B (MoaB) similar to Escherichia coli K-12 MoaB, which may be involved in the biosynthesis of molybdopterin and can bind metal-binding pterin (MPT) but has no MPT adenylyl transferase activity

CATH:  3.40.980.10
Gene Ontology:  GO:0006777
PubMed:  18154309|12504674
SCOP:  4000598

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
moaB_proteo TIGR02667
molybdenum cofactor biosynthesis protein B, proteobacterial; This model represents the MoaB ...
 7-169 8.83e-110

molybdenum cofactor biosynthesis protein B, proteobacterial; This model represents the MoaB protein molybdopterin biosynthesis regions in Proteobacteria. This crystallized but incompletely characterized protein is thought to be involved in, though not required for, early steps in molybdopterin biosynthesis. It may bind a molybdopterin precursor. A distinctive conserved motif PCN near the C-terminus helps distinguish this clade from other homologs, including sets of proteins designated MogA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


:

Pssm-ID: 131715 [Multi-domain]  Cd Length: 163  Bit Score: 309.74  E-value: 8.83e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750     7 EFIPTRIAILTVSNRRGEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIASDDVQVVLITGGTGLTEGDQ 86
Cdd:TIGR02667   1 PFIPLRIAILTVSDTRTEEDDTSGQYLVERLTEAGHRLADRAIVKDDIYQIRAQVSAWIADPDVQVILITGGTGFTGRDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750    87 APEALLPLFDREVEGFGEVFRMLSFEEIGTSTLQSRAVAGVANKTLIFAMPGSTKACRTAWENIIAPQLDARTRPCNFHP 166
Cdd:TIGR02667  81 TPEALEPLFDKTVEGFGELFRQLSYEEIGTSTIQSRALAGLANGTFVFCLPGSTGACRTAWDKIIAAQLDARHRPCNFVE 160


                  ...
gi 16128750   167 HLK 169
Cdd:TIGR02667 161 HLP 163
 
Name Accession Description Interval E-value
moaB_proteo TIGR02667
molybdenum cofactor biosynthesis protein B, proteobacterial; This model represents the MoaB ...
 7-169 8.83e-110

molybdenum cofactor biosynthesis protein B, proteobacterial; This model represents the MoaB protein molybdopterin biosynthesis regions in Proteobacteria. This crystallized but incompletely characterized protein is thought to be involved in, though not required for, early steps in molybdopterin biosynthesis. It may bind a molybdopterin precursor. A distinctive conserved motif PCN near the C-terminus helps distinguish this clade from other homologs, including sets of proteins designated MogA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 131715 [Multi-domain]  Cd Length: 163  Bit Score: 309.74  E-value: 8.83e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750     7 EFIPTRIAILTVSNRRGEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIASDDVQVVLITGGTGLTEGDQ 86
Cdd:TIGR02667   1 PFIPLRIAILTVSDTRTEEDDTSGQYLVERLTEAGHRLADRAIVKDDIYQIRAQVSAWIADPDVQVILITGGTGFTGRDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750    87 APEALLPLFDREVEGFGEVFRMLSFEEIGTSTLQSRAVAGVANKTLIFAMPGSTKACRTAWENIIAPQLDARTRPCNFHP 166
Cdd:TIGR02667  81 TPEALEPLFDKTVEGFGELFRQLSYEEIGTSTIQSRALAGLANGTFVFCLPGSTGACRTAWDKIIAAQLDARHRPCNFVE 160


                  ...
gi 16128750   167 HLK 169
Cdd:TIGR02667 161 HLP 163
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 1-167 2.76e-82

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: 240.02  E-value: 2.76e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750   1 MSQvSTEFIPTRIAILTVSNRR--GEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIASDDVQVVLITGG 78
Cdd:COG0521   1 MSS-ARAFVPLRIAVLTVSDRRsrGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTTGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750  79 TGLTEGDQAPEALLPLFDREVEGFGEVFRMLSFEEIGTSTLQSRAVAGVANKTLIFAMPGSTKACRTAWEnIIAPQLDAR 158
Cdd:COG0521  80 TGLSPRDVTPEATRPLLDKELPGFGELFRALSLEEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALE-AILPELPHA 158


                ....*....
gi 16128750 159 TRPCNFHPH 167
Cdd:COG0521 159 VDLLNGVDH 167
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 12-156 8.21e-67

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: 200.40  E-value: 8.21e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750  12 RIAILTVSNRR--GEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIASDDVQVVLITGGTGLTEGDQAPE 89
Cdd:cd00886   2 RAAVLTVSDTRsaGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRDVTPE 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128750  90 ALLPLFDREVEGFGEVFRMLSFEEIGTsTLQSRAVAGVANKTLIFAMPGSTKACRTAWEnIIAPQLD 156
Cdd:cd00886  82 ATRPLLDKELPGFGEAFRALSLEETGT-AMLSRAVAGIRGGTLIFNLPGSPKAVREALE-VILPELP 146
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 14-150 1.50e-36

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: 123.08  E-value: 1.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750     14 AILTVSNRR---GEEDDTSGHYLRDSAQEAGHHVVDKAIV--KENRYAIRAQVSAWIASDDVqvVLITGGTGLTEGDQAP 88
Cdd:smart00852   1 AIISTGDELlsgGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDDLTP 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128750     89 EALLPLFDREVEGFGEVFRMLSFeeIGTSTLQSRAVAGVANKTLIFAMPGSTKACRTAWENI 150
Cdd:smart00852  79 EALAELGGRELLGHGVAMRPGGP--PGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 14-157 6.43e-36

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: 121.59  E-value: 6.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750    14 AILTVSNRR--GEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIASDDVqvVLITGGTGLTEGDQAPEAL 91
Cdd:pfam00994   1 AIITTGDELlpGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTPEAL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128750    92 LPLFDREVEGFGEVFRMLSFEEIGTSTLQSRAVAGVANKTlIFAMPGSTKACRTAWENIIAPQLDA 157
Cdd:pfam00994  79 AELGGRELPGFEELFRGVSLKPGKPVGTAPGAILSRAGKT-VFGLPGSPVAAKVMFELLLLPLLRH 143
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 2-156 2.70e-28

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 106.56  E-value: 2.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750    2 SQVSTEFIP-TRIAILTVSNR--RGEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIASDdVQVVLITGG 78
Cdd:PRK03604 146 SGHKRRFRPrTSAAVLVLSDSiaAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAEG-YALIITTGG 224

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128750   79 TGLTEGDQAPEALLPLFDREVEGFGEVFRMLSFEEIGTSTLqSRAVAGVANKTLIFAMPGSTKACRTAWEnIIAPQLD 156
Cdd:PRK03604 225 TGLGPRDVTPEALAPLLERRLPGIAEALRSWGQGRTPTAML-SRLVAGMIGNSLVVALPGSPGGASDALA-VLLPALF 300
 
Name Accession Description Interval E-value
moaB_proteo TIGR02667
molybdenum cofactor biosynthesis protein B, proteobacterial; This model represents the MoaB ...
 7-169 8.83e-110

molybdenum cofactor biosynthesis protein B, proteobacterial; This model represents the MoaB protein molybdopterin biosynthesis regions in Proteobacteria. This crystallized but incompletely characterized protein is thought to be involved in, though not required for, early steps in molybdopterin biosynthesis. It may bind a molybdopterin precursor. A distinctive conserved motif PCN near the C-terminus helps distinguish this clade from other homologs, including sets of proteins designated MogA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 131715 [Multi-domain]  Cd Length: 163  Bit Score: 309.74  E-value: 8.83e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750     7 EFIPTRIAILTVSNRRGEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIASDDVQVVLITGGTGLTEGDQ 86
Cdd:TIGR02667   1 PFIPLRIAILTVSDTRTEEDDTSGQYLVERLTEAGHRLADRAIVKDDIYQIRAQVSAWIADPDVQVILITGGTGFTGRDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750    87 APEALLPLFDREVEGFGEVFRMLSFEEIGTSTLQSRAVAGVANKTLIFAMPGSTKACRTAWENIIAPQLDARTRPCNFHP 166
Cdd:TIGR02667  81 TPEALEPLFDKTVEGFGELFRQLSYEEIGTSTIQSRALAGLANGTFVFCLPGSTGACRTAWDKIIAAQLDARHRPCNFVE 160


                  ...
gi 16128750   167 HLK 169
Cdd:TIGR02667 161 HLP 163
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 1-167 2.76e-82

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: 240.02  E-value: 2.76e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750   1 MSQvSTEFIPTRIAILTVSNRR--GEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIASDDVQVVLITGG 78
Cdd:COG0521   1 MSS-ARAFVPLRIAVLTVSDRRsrGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTTGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750  79 TGLTEGDQAPEALLPLFDREVEGFGEVFRMLSFEEIGTSTLQSRAVAGVANKTLIFAMPGSTKACRTAWEnIIAPQLDAR 158
Cdd:COG0521  80 TGLSPRDVTPEATRPLLDKELPGFGELFRALSLEEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALE-AILPELPHA 158


                ....*....
gi 16128750 159 TRPCNFHPH 167
Cdd:COG0521 159 VDLLNGVDH 167
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 12-156 8.21e-67

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: 200.40  E-value: 8.21e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750  12 RIAILTVSNRR--GEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIASDDVQVVLITGGTGLTEGDQAPE 89
Cdd:cd00886   2 RAAVLTVSDTRsaGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRDVTPE 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128750  90 ALLPLFDREVEGFGEVFRMLSFEEIGTsTLQSRAVAGVANKTLIFAMPGSTKACRTAWEnIIAPQLD 156
Cdd:cd00886  82 ATRPLLDKELPGFGEAFRALSLEETGT-AMLSRAVAGIRGGTLIFNLPGSPKAVREALE-VILPELP 146
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 12-153 2.04e-42

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: 138.60  E-value: 2.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750    12 RIAILTVSNRR---------GEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIasDDVQVVLITGGTGLT 82
Cdd:TIGR00177   2 RVAVISVGDELveggqplepGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAV--DEADVVLTTGGTGVG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128750    83 EGDQAPEALLPLFDREVEGFGEvFRMLSFEEIgtstlQSR----AVAGVANKTLIFAMPGSTKACRTAWENIIAP 153
Cdd:TIGR00177  80 PRDVTPEALEELGEKEIPGFGE-FRMLSSLPV-----LSRpgkpATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 12-155 6.23e-41

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: 134.01  E-value: 6.23e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750  12 RIAILTVSNRR--GEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWiaSDDVQVVLITGGTGLTEGDQAPE 89
Cdd:cd00758   1 RVAIVTVSDELsqGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEA--SREADLVLTTGGTGVGRRDVTPE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128750  90 ALLPLFDREVEGfgevfrmlsfeEIGTSTLQSRAVAGVANKTLIFAMPGSTKACRTAWENIIAPQL 155
Cdd:cd00758  79 ALAELGEREAHG-----------KGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 14-150 1.50e-36

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: 123.08  E-value: 1.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750     14 AILTVSNRR---GEEDDTSGHYLRDSAQEAGHHVVDKAIV--KENRYAIRAQVSAWIASDDVqvVLITGGTGLTEGDQAP 88
Cdd:smart00852   1 AIISTGDELlsgGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDDLTP 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128750     89 EALLPLFDREVEGFGEVFRMLSFeeIGTSTLQSRAVAGVANKTLIFAMPGSTKACRTAWENI 150
Cdd:smart00852  79 EALAELGGRELLGHGVAMRPGGP--PGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 14-157 6.43e-36

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: 121.59  E-value: 6.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750    14 AILTVSNRR--GEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIASDDVqvVLITGGTGLTEGDQAPEAL 91
Cdd:pfam00994   1 AIITTGDELlpGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTPEAL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128750    92 LPLFDREVEGFGEVFRMLSFEEIGTSTLQSRAVAGVANKTlIFAMPGSTKACRTAWENIIAPQLDA 157
Cdd:pfam00994  79 AELGGRELPGFEELFRGVSLKPGKPVGTAPGAILSRAGKT-VFGLPGSPVAAKVMFELLLLPLLRH 143
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 2-156 2.70e-28

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 106.56  E-value: 2.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750    2 SQVSTEFIP-TRIAILTVSNR--RGEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIASDdVQVVLITGG 78
Cdd:PRK03604 146 SGHKRRFRPrTSAAVLVLSDSiaAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAEG-YALIITTGG 224

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128750   79 TGLTEGDQAPEALLPLFDREVEGFGEVFRMLSFEEIGTSTLqSRAVAGVANKTLIFAMPGSTKACRTAWEnIIAPQLD 156
Cdd:PRK03604 225 TGLGPRDVTPEALAPLLERRLPGIAEALRSWGQGRTPTAML-SRLVAGMIGNSLVVALPGSPGGASDALA-VLLPALF 300
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 12-144 4.63e-17

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 74.60  E-value: 4.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750   12 RIAILTVSNR--RGEEDDTSGHYLRDSAQEA--GHHVVDKAIVKENRYAIRAQVSAWIASDDVQVVLITGGTGLTEGDQA 87
Cdd:PRK09417   5 KIGLVSISDRasSGVYEDKGIPALEEWLASAltSPFEIETRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTGPARRDVT 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128750   88 PEALLPLFDREVEGFGEVFRMLSFEEIGTSTLqSRAVAGVANKTLIFAMPGSTKACR 144
Cdd:PRK09417  85 PEATLAVADKEMPGFGEQMRQISLKFVPTAIL-SRQVAVIRGQSLIINLPGQPKSIK 140
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 12-142 2.41e-15

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 72.54  E-value: 2.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750   12 RIAILTVSN--RRGEEDDTSGHY---LRDSAQE--AGHHVVDKAIVKENRYAIRAQVSAWIASDDVQVVLITGGTGLTEG 84
Cdd:PLN02699 460 KVAILTVSDtvSSGAGPDRSGPRavsVVNSSSEklGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTGFTPR 539

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16128750   85 DQAPEALLPLFDREVEGFGEVFRMLSFEEIGTSTLqSRAVAGVANKTLIFAMPGSTKA 142
Cdd:PLN02699 540 DVTPEATKEVIQKETPGLLYVMMQESLKVTPFAML-SRSAAGIRGSTLIINMPGNPNA 596
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 27-167 1.80e-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: 43.64  E-value: 1.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750  27 DTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAWIASDDvqVVLITGGTGLTEGDQAPEALLPLfdrevegFGEVF 106
Cdd:cd00887 194 DSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEAD--VVITSGGVSVGDYDFVKEVLEEL-------GGEVL 264

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128750 107 rmlsFEEI----GTSTLqsravAGVANKTLIFAMPGSTKACRTAWENIIAPQLDARTRPCNFHPH 167
Cdd:cd00887 265 ----FHGVamkpGKPLA-----FGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPP 320
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 27-138 2.82e-04

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: 40.07  E-value: 2.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750  27 DTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAwiASDDVQVVLITGGTGLTEGDQAPEALlplfdrevegfgevf 106
Cdd:COG0303 198 DSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALRE--ALAEADLVITSGGVSVGDYDLVKEAL--------------- 260

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 16128750 107 rmlsfEEIGTSTLQSRaVA---------GVANKTLIFAMPG 138
Cdd:COG0303 261 -----EELGAEVLFHK-VAmkpgkplafGRLGGKPVFGLPG 295
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 12-158 3.05e-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: 39.39  E-value: 3.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750  12 RIAILTVSNR--RGEEDDTSGHYLRDSAQEAGHHVVDKAIVKENRYAIRAQVSAwiASDDVQVVLITGGTGLTEGDQAPE 89
Cdd:cd00885   1 TAEIIAIGDEllSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRR--ASERADLVITTGGLGPTHDDLTRE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128750  90 ALLPLFDREVEGFGEVFRMLS--FEEIGTSTLQSR------------------AVAGVA---NKTLIFAMPGSTKACRTA 146
Cdd:cd00885  79 AVAKAFGRPLVLDEEALERIEarFARRGREMTEANlkqamlpegatllpnpvgTAPGFSvehNGKNVFLLPGVPSEMKPM 158

                       170
                ....*....|..
gi 16128750 147 WENIIAPQLDAR 158
Cdd:cd00885 159 LEEEVLPRLRER 170
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH