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Conserved domains on  [gi|446039269|ref|WP_000117124|]
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MULTISPECIES: molybdenum cofactor biosynthesis protein B [Bacillus]

Protein Classification

molybdenum cofactor biosynthesis protein B( domain architecture ID 10001646)

molybdenum cofactor biosynthesis protein B (MoaB) similar to Pyrococcus furiosus MoaB; may be a metal-binding pterin (MPT)-adenylyltransferase which converts MPT to adenylylated MPT (MPT-AMP)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 6-168 5.92e-78

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: 229.23  E-value: 5.92e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269   6 HKKQAPKEVRCKIVTISDTRT--EETDKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGYHKEDVDVVLTNGGTG 83
Cdd:COG0521    2 SSARAFVPLRIAVLTVSDRRSrgEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTTGGTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  84 ITKRDVTIEAVSALLDKEIVGFGELFRMISYlEDIGSSAMLSRAIGGTIGRKVVFSMPGSSGAVRLAMNKlILPELGHIT 163
Cdd:COG0521   82 LSPRDVTPEATRPLLDKELPGFGELFRALSL-EEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEA-ILPELPHAV 159


                 ....*
gi 446039269 164 FELHR 168
Cdd:COG0521  160 DLLNG 164
 
Name Accession Description Interval E-value
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 6-168 5.92e-78

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: 229.23  E-value: 5.92e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269   6 HKKQAPKEVRCKIVTISDTRT--EETDKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGYHKEDVDVVLTNGGTG 83
Cdd:COG0521    2 SSARAFVPLRIAVLTVSDRRSrgEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTTGGTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  84 ITKRDVTIEAVSALLDKEIVGFGELFRMISYlEDIGSSAMLSRAIGGTIGRKVVFSMPGSSGAVRLAMNKlILPELGHIT 163
Cdd:COG0521   82 LSPRDVTPEATRPLLDKELPGFGELFRALSL-EEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEA-ILPELPHAV 159


                 ....*
gi 446039269 164 FELHR 168
Cdd:COG0521  160 DLLNG 164
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 14-166 1.25e-72

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: 215.03  E-value: 1.25e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  14 VRCKIVTISDTRT--EETDKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGYHKEDVDVVLTNGGTGITKRDVTI 91
Cdd:cd00886    1 LRAAVLTVSDTRSagEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRDVTP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446039269  92 EAVSALLDKEIVGFGELFRMISYleDIGSSAMLSRAIGGTIGRKVVFSMPGSSGAVRLAMNKlILPELGHITFEL 166
Cdd:cd00886   81 EATRPLLDKELPGFGEAFRALSL--EETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEV-ILPELPHLLDLL 152
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 18-154 7.97e-41

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: 133.87  E-value: 7.97e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269    18 IVTISDTRTEET---DKSGQLLHELLKEAGHKVTSYEIV--KDDKESIQQAVLAgyHKEDVDVVLTNGGTGITKRDVTIE 92
Cdd:smart00852   2 IISTGDELLSGGqirDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALRE--ALAEADVVITTGGTGPGPDDLTPE 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446039269    93 AVSALLDKEIVGFGELFRMISYledIGSSAMLSRAIGGTIGRKVVFSMPGSSGAVRLAMNKL 154
Cdd:smart00852  80 ALAELGGRELLGHGVAMRPGGP---PGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 18-161 3.50e-40

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: 132.37  E-value: 3.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269   18 IVTISDTRTEET--DKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGyhKEDVDVVLTNGGTGITKRDVTIEAVS 95
Cdd:pfam00994   2 IITTGDELLPGQirDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAA--AEEADVVITTGGTGPGPDDVTPEALA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269   96 ALLDKEIVGFGELFRMISYLED----IGSSAMLSRAiggtigRKVVFSMPGSSGAVRLAMNKLILPELGH 161
Cdd:pfam00994  80 ELGGRELPGFEELFRGVSLKPGkpvgTAPGAILSRA------GKTVFGLPGSPVAAKVMFELLLLPLLRH 143
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 14-157 4.29e-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: 124.74  E-value: 4.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269   14 VRCKIVTISDTRTE---------ETDKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAgyHKEDVDVVLTNGGTGI 84
Cdd:TIGR00177   1 PRVAVISVGDELVEggqplepgqIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRK--AVDEADVVLTTGGTGV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446039269   85 TKRDVTIEAVSALLDKEIVGFGElFRMISYLEdigssaMLSR----AIGGTIGRKVVFSMPGSSGAVRLAMNKLILP 157
Cdd:TIGR00177  79 GPRDVTPEALEELGEKEIPGFGE-FRMLSSLP------VLSRpgkpATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 6-162 1.43e-33

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 120.43  E-value: 1.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269   6 HKKQAPKEVRCKIVTISDTRTEET--DKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAgYHKEDVDVVLTNGGTG 83
Cdd:PRK03604 148 HKRRFRPRTSAAVLVLSDSIAAGTkeDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAA-WIAEGYALIITTGGTG 226

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446039269  84 ITKRDVTIEAVSALLDKEIVGFGELFRmiSYLEDIGSSAMLSRAIGGTIGRKVVFSMPGSSGAVRLAMNkLILPELGHI 162
Cdd:PRK03604 227 LGPRDVTPEALAPLLERRLPGIAEALR--SWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALA-VLLPALFHA 302
 
Name Accession Description Interval E-value
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 6-168 5.92e-78

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: 229.23  E-value: 5.92e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269   6 HKKQAPKEVRCKIVTISDTRT--EETDKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGYHKEDVDVVLTNGGTG 83
Cdd:COG0521    2 SSARAFVPLRIAVLTVSDRRSrgEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTTGGTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  84 ITKRDVTIEAVSALLDKEIVGFGELFRMISYlEDIGSSAMLSRAIGGTIGRKVVFSMPGSSGAVRLAMNKlILPELGHIT 163
Cdd:COG0521   82 LSPRDVTPEATRPLLDKELPGFGELFRALSL-EEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEA-ILPELPHAV 159


                 ....*
gi 446039269 164 FELHR 168
Cdd:COG0521  160 DLLNG 164
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 14-166 1.25e-72

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: 215.03  E-value: 1.25e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  14 VRCKIVTISDTRT--EETDKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGYHKEDVDVVLTNGGTGITKRDVTI 91
Cdd:cd00886    1 LRAAVLTVSDTRSagEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRDVTP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446039269  92 EAVSALLDKEIVGFGELFRMISYleDIGSSAMLSRAIGGTIGRKVVFSMPGSSGAVRLAMNKlILPELGHITFEL 166
Cdd:cd00886   81 EATRPLLDKELPGFGEAFRALSL--EETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEV-ILPELPHLLDLL 152
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 15-159 4.35e-42

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: 137.09  E-value: 4.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  15 RCKIVTISDTRT--EETDKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGYHKedVDVVLTNGGTGITKRDVTIE 92
Cdd:cd00758    1 RVAIVTVSDELSqgQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASRE--ADLVLTTGGTGVGRRDVTPE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446039269  93 AVSALLDKEIVGfgelfrmisyleDIGSSAMLSRAIGGTIGRKVVFSMPGSSGAVRLAMNKLILPEL 159
Cdd:cd00758   79 ALAELGEREAHG------------KGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 18-154 7.97e-41

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: 133.87  E-value: 7.97e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269    18 IVTISDTRTEET---DKSGQLLHELLKEAGHKVTSYEIV--KDDKESIQQAVLAgyHKEDVDVVLTNGGTGITKRDVTIE 92
Cdd:smart00852   2 IISTGDELLSGGqirDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALRE--ALAEADVVITTGGTGPGPDDLTPE 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446039269    93 AVSALLDKEIVGFGELFRMISYledIGSSAMLSRAIGGTIGRKVVFSMPGSSGAVRLAMNKL 154
Cdd:smart00852  80 ALAELGGRELLGHGVAMRPGGP---PGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 18-161 3.50e-40

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: 132.37  E-value: 3.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269   18 IVTISDTRTEET--DKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGyhKEDVDVVLTNGGTGITKRDVTIEAVS 95
Cdd:pfam00994   2 IITTGDELLPGQirDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAA--AEEADVVITTGGTGPGPDDVTPEALA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269   96 ALLDKEIVGFGELFRMISYLED----IGSSAMLSRAiggtigRKVVFSMPGSSGAVRLAMNKLILPELGH 161
Cdd:pfam00994  80 ELGGRELPGFEELFRGVSLKPGkpvgTAPGAILSRA------GKTVFGLPGSPVAAKVMFELLLLPLLRH 143
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 14-157 4.29e-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: 124.74  E-value: 4.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269   14 VRCKIVTISDTRTE---------ETDKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAgyHKEDVDVVLTNGGTGI 84
Cdd:TIGR00177   1 PRVAVISVGDELVEggqplepgqIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRK--AVDEADVVLTTGGTGV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446039269   85 TKRDVTIEAVSALLDKEIVGFGElFRMISYLEdigssaMLSR----AIGGTIGRKVVFSMPGSSGAVRLAMNKLILP 157
Cdd:TIGR00177  79 GPRDVTPEALEELGEKEIPGFGE-FRMLSSLP------VLSRpgkpATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 6-162 1.43e-33

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 120.43  E-value: 1.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269   6 HKKQAPKEVRCKIVTISDTRTEET--DKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAgYHKEDVDVVLTNGGTG 83
Cdd:PRK03604 148 HKRRFRPRTSAAVLVLSDSIAAGTkeDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAA-WIAEGYALIITTGGTG 226

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446039269  84 ITKRDVTIEAVSALLDKEIVGFGELFRmiSYLEDIGSSAMLSRAIGGTIGRKVVFSMPGSSGAVRLAMNkLILPELGHI 162
Cdd:PRK03604 227 LGPRDVTPEALAPLLERRLPGIAEALR--SWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALA-VLLPALFHA 302
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 11-154 1.22e-24

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 94.25  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  11 PKEVRCKIVTISD--TRTEETDKSGQLLHELLKEAghkVTS-----YEIVKDDKESIQQAVLAGYHKEDVDVVLTNGGTG 83
Cdd:PRK09417   1 MDTLKIGLVSISDraSSGVYEDKGIPALEEWLASA---LTSpfeieTRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446039269  84 ITKRDVTIEAVSALLDKEIVGFGELFRMISyLEDIgSSAMLSRAIGGTIGRKVVFSMPGSSGAVRLAMNKL 154
Cdd:PRK09417  78 PARRDVTPEATLAVADKEMPGFGEQMRQIS-LKFV-PTAILSRQVAVIRGQSLIINLPGQPKSIKETLEGL 146
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 13-161 1.70e-20

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 87.18  E-value: 1.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  13 EVRCKIVTISDTRTEET--DKSGQLLHELL-----KEAGHKVTSYEIVKDDKESIQQAVLAGYHKEDVDVVLTNGGTGIT 85
Cdd:PLN02699 458 EVKVAILTVSDTVSSGAgpDRSGPRAVSVVnssseKLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTGFT 537

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446039269  86 KRDVTIEAVSALLDKEIVGFgeLFRMISYLEDIGSSAMLSRAIGGTIGRKVVFSMPGSSGAVRLAMNKLiLPELGH 161
Cdd:PLN02699 538 PRDVTPEATKEVIQKETPGL--LYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEAL-LPALKH 610
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 33-142 1.12e-11

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: 61.74  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  33 GQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGyhKEDVDVVLTNGGTGITKRDVTIEAVSALldkeivGFGELFRMI 112
Cdd:cd00887  197 SYMLAALLRELGAEVVDLGIVPDDPEALREALEEA--LEEADVVITSGGVSVGDYDFVKEVLEEL------GGEVLFHGV 268

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446039269 113 syledigssAML--SRAIGGTIGRKVVFSMPG 142
Cdd:cd00887  269 ---------AMKpgKPLAFGRLGGKPVFGLPG 291
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 35-142 2.64e-11

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: 60.49  E-value: 2.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  35 LLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGyhKEDVDVVLTNGGTGITKRDVTIEAVSALldkeivGFGELFRMIsy 114
Cdd:COG0303  203 MLAALLREAGAEVVDLGIVPDDPEALRAALREA--LAEADLVITSGGVSVGDYDLVKEALEEL------GAEVLFHKV-- 272

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446039269 115 ledigssAMlsR----AIGGTIGRKVVFSMPG 142
Cdd:COG0303  273 -------AM--KpgkpLAFGRLGGKPVFGLPG 295
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 30-142 6.07e-11

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: 57.88  E-value: 6.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  30 DKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGyhKEDVDVVLTNGGTGITKRDVTIEAVSALLDKEIVGFGELF 109
Cdd:cd00885   18 DTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRA--SERADLVITTGGLGPTHDDLTREAVAKAFGRPLVLDEEAL 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446039269 110 RMIS-YLEDIGSS--------AML-----------SRAIGGTI--GRKVVFSMPG 142
Cdd:cd00885   96 ERIEaRFARRGREmteanlkqAMLpegatllpnpvGTAPGFSVehNGKNVFLLPG 150
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 30-97 3.64e-06

putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 45.97  E-value: 3.64e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446039269  30 DKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGYhkEDVDVVLTNGGTGITKRDVTIEAVSAL 97
Cdd:PRK14498 212 DVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKAL--KECDLVLLSGGTSAGAGDVTYRVIEEL 277
PRK14497 PRK14497
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
 36-156 8.37e-05

putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional


Pssm-ID: 172968 [Multi-domain]  Cd Length: 546  Bit Score: 41.72  E-value: 8.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  36 LHELLKEAGHKVTSYEIVKDDKESIQQAVLAGYHKedVDVVLTNGGTGITKRDVTIEAVSALldKEIVGFGELFRMisyl 115
Cdd:PRK14497 211 LYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISV--ADVLILTGGTSAGEKDFVHQAIREL--GNIIVHGLKIKP---- 282

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446039269 116 ediGSSAMLsraigGTIGRKVVFSMPGSSGAVRLAMNKLIL 156
Cdd:PRK14497 283 ---GKPTIL-----GIVDGKPVIGLPGNIVSTMVVLNMVIL 315
PRK03670 PRK03670
competence damage-inducible protein A; Provisional
 17-103 2.85e-04

competence damage-inducible protein A; Provisional


Pssm-ID: 167581  Cd Length: 252  Bit Score: 39.78  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269  17 KIVTISDTR-TEET-DKSGQLLHELLKEAGHKVTSYEIVKDDKESIQQAVLAGYHKEDvDVVLTNGGTGITKRDVTIEAV 94
Cdd:PRK03670   4 EIITVGDELlTGNTvDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKP-EVLVISGGLGPTHDDVTMLAV 82


                 ....*....
gi 446039269  95 SALLDKEIV 103
Cdd:PRK03670  83 AEALGRELV 91
NAD_binding_10 pfam13460
NAD(P)H-binding;
31-96 8.22e-03

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 35.27  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446039269   31 KSGQLLHELLKEAGHKVTSY----------------EIVK---DDKESIQQAVlagyhkEDVDVVLTNGGTGITKRDVTI 91
Cdd:pfam13460   5 KIGRLLVKQLLARGHEVTALvrnpekladledhpgvEVVDgdvLDPDDLAEAL------AGQDAVISALGGGGTDETGAK 78


                  ....*
gi 446039269   92 EAVSA 96
Cdd:pfam13460  79 NIIDA 83
 
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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