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Conserved domains on  [gi|942706795|ref|WP_055410150|]
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molybdenum cofactor biosynthesis protein B [Pyrodictium delaneyi]

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 ...
 3-155 2.62e-45

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: 146.42  E-value: 2.62e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795   3 RWGLVVTSDRVKEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAAL-HEGAEVVLVTGGTGPNPRDISAD 81
Cdd:COG0521   11 RIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIdDEGVDLVLTTGGTGLSPRDVTPE 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942706795  82 LVSRICDRVLPGVGEEFRRRSLEEGVANAVLSRALACSFRDRLLAVSPGNPGAARLMAELLLEVVDHALHQLRG 155
Cdd:COG0521   91 ATRPLLDKELPGFGELFRALSLEEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHAVDLLNG 164
 
Name Accession Description Interval E-value
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 3-155 2.62e-45

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: 146.42  E-value: 2.62e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795   3 RWGLVVTSDRVKEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAAL-HEGAEVVLVTGGTGPNPRDISAD 81
Cdd:COG0521   11 RIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIdDEGVDLVLTTGGTGLSPRDVTPE 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942706795  82 LVSRICDRVLPGVGEEFRRRSLEEGVANAVLSRALACSFRDRLLAVSPGNPGAARLMAELLLEVVDHALHQLRG 155
Cdd:COG0521   91 ATRPLLDKELPGFGELFRALSLEEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHAVDLLNG 164
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 5-153 7.21e-37

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: 124.51  E-value: 7.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795   5 GLVVTSDRVKEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAALHE-GAEVVLVTGGTGPNPRDISADLV 83
Cdd:cd00886    4 AVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEdGVDLILTTGGTGLAPRDVTPEAT 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795  84 SRICDRVLPGVGEEFRRRSLEEGVAnAVLSRALACSFRDRLLAVSPGNPGAARLMAELLLEVVDHALHQL 153
Cdd:cd00886   84 RPLLDKELPGFGEAFRALSLEETGT-AMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 5-144 2.65e-23

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: 89.62  E-value: 2.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795    5 GLVVTSDRVKEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEIlyhiAAALHEGAE---VVLVTGGTGPNPRDISAD 81
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAI----KEALRAAAEeadVVITTGGTGPGPDDVTPE 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942706795   82 LVSRICDRVLPGVGEEFRRRSLEEGVAN-----AVLSRAlacsfrDRLLAVSPGNPGAARLMAELLLE 144
Cdd:pfam00994  77 ALAELGGRELPGFEELFRGVSLKPGKPVgtapgAILSRA------GKTVFGLPGSPVAAKVMFELLLL 138
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 5-142 3.98e-23

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: 88.80  E-value: 3.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795     5 GLVVTSDRVKEHPEQDETT-PMLRRLLGEHGHELVYTAIAGN--DPVEILYHIAAALhEGAEVVLVTGGTGPNPRDISAD 81
Cdd:smart00852   1 AIISTGDELLSGGQIRDSNgPMLAALLRELGIEVVRVVVVGGpdDPEAIREALREAL-AEADVVITTGGTGPGPDDLTPE 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942706795    82 LVSRICDRVLPGVGEEFRRRSLEEGVANavLSRALACSFRDRLLAVSPGNPGAARLMAELL 142
Cdd:smart00852  80 ALAELGGRELLGHGVAMRPGGPPGPLAN--LSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 3-144 7.02e-23

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: 88.53  E-value: 7.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795    3 RWGLVVTSDRV-------KEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAALhEGAEVVLVTGGTGPNP 75
Cdd:TIGR00177   2 RVAVISVGDELveggqplEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAV-DEADVVLTTGGTGVGP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942706795   76 RDISADLVSRICDRVLPGVGEEFRRRSLEegvanaVLSR----ALACSFRDRLLAVSPGNPGAARLMAELLLE 144
Cdd:TIGR00177  81 RDVTPEALEELGEKEIPGFGEFRMLSSLP------VLSRpgkpATAGVRGGTLIFNLPGNPVSALVTFEVLIL 147
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 2-155 6.11e-22

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 89.62  E-value: 6.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795   2 ARWGLVVTSDRVKEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAALHEGAEVVLVTGGTGPNPRDISAD 81
Cdd:PRK03604 156 TSAAVLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAEGYALIITTGGTGLGPRDVTPE 235

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942706795  82 LVSRICDRVLPGVGEEFRRRSLEEgVANAVLSRALACSFRDRLLAVSPGNPGAARLMAELLLEVVDHALHQLRG 155
Cdd:PRK03604 236 ALAPLLERRLPGIAEALRSWGQGR-TPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPALFHAFAMVKG 308
 
Name Accession Description Interval E-value
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 3-155 2.62e-45

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: 146.42  E-value: 2.62e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795   3 RWGLVVTSDRVKEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAAL-HEGAEVVLVTGGTGPNPRDISAD 81
Cdd:COG0521   11 RIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIdDEGVDLVLTTGGTGLSPRDVTPE 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942706795  82 LVSRICDRVLPGVGEEFRRRSLEEGVANAVLSRALACSFRDRLLAVSPGNPGAARLMAELLLEVVDHALHQLRG 155
Cdd:COG0521   91 ATRPLLDKELPGFGELFRALSLEEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHAVDLLNG 164
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 5-153 7.21e-37

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: 124.51  E-value: 7.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795   5 GLVVTSDRVKEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAALHE-GAEVVLVTGGTGPNPRDISADLV 83
Cdd:cd00886    4 AVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEdGVDLILTTGGTGLAPRDVTPEAT 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795  84 SRICDRVLPGVGEEFRRRSLEEGVAnAVLSRALACSFRDRLLAVSPGNPGAARLMAELLLEVVDHALHQL 153
Cdd:cd00886   84 RPLLDKELPGFGEAFRALSLEETGT-AMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 5-144 2.65e-23

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: 89.62  E-value: 2.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795    5 GLVVTSDRVKEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEIlyhiAAALHEGAE---VVLVTGGTGPNPRDISAD 81
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAI----KEALRAAAEeadVVITTGGTGPGPDDVTPE 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942706795   82 LVSRICDRVLPGVGEEFRRRSLEEGVAN-----AVLSRAlacsfrDRLLAVSPGNPGAARLMAELLLE 144
Cdd:pfam00994  77 ALAELGGRELPGFEELFRGVSLKPGKPVgtapgAILSRA------GKTVFGLPGSPVAAKVMFELLLL 138
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 5-142 3.98e-23

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: 88.80  E-value: 3.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795     5 GLVVTSDRVKEHPEQDETT-PMLRRLLGEHGHELVYTAIAGN--DPVEILYHIAAALhEGAEVVLVTGGTGPNPRDISAD 81
Cdd:smart00852   1 AIISTGDELLSGGQIRDSNgPMLAALLRELGIEVVRVVVVGGpdDPEAIREALREAL-AEADVVITTGGTGPGPDDLTPE 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942706795    82 LVSRICDRVLPGVGEEFRRRSLEEGVANavLSRALACSFRDRLLAVSPGNPGAARLMAELL 142
Cdd:smart00852  80 ALAELGGRELLGHGVAMRPGGPPGPLAN--LSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 3-144 7.02e-23

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: 88.53  E-value: 7.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795    3 RWGLVVTSDRV-------KEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAALhEGAEVVLVTGGTGPNP 75
Cdd:TIGR00177   2 RVAVISVGDELveggqplEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAV-DEADVVLTTGGTGVGP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942706795   76 RDISADLVSRICDRVLPGVGEEFRRRSLEegvanaVLSR----ALACSFRDRLLAVSPGNPGAARLMAELLLE 144
Cdd:TIGR00177  81 RDVTPEALEELGEKEIPGFGEFRMLSSLP------VLSRpgkpATAGVRGGTLIFNLPGNPVSALVTFEVLIL 147
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 2-155 6.11e-22

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 89.62  E-value: 6.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795   2 ARWGLVVTSDRVKEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAALHEGAEVVLVTGGTGPNPRDISAD 81
Cdd:PRK03604 156 TSAAVLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAEGYALIITTGGTGLGPRDVTPE 235

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942706795  82 LVSRICDRVLPGVGEEFRRRSLEEgVANAVLSRALACSFRDRLLAVSPGNPGAARLMAELLLEVVDHALHQLRG 155
Cdd:PRK03604 236 ALAPLLERRLPGIAEALRSWGQGR-TPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPALFHAFAMVKG 308
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 1-152 1.19e-18

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 78.84  E-value: 1.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795   1 MARWGLVVTSDRVKEHPEQDETTPMLRRLLGEH---GHELVYTAIAgnDPVEIlyhIAAAL-----HEGAEVVLVTGGTG 72
Cdd:PRK09417   3 TLKIGLVSISDRASSGVYEDKGIPALEEWLASAltsPFEIETRLIP--DEQDL---IEQTLielvdEMGCDLVLTTGGTG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795  73 PNPRDISADLVSRICDRVLPGVGEEFRRRSLEEgVANAVLSRALACSFRDRLLAVSPGNPGAARLMAELLLEVVDHALHQ 152
Cdd:PRK09417  78 PARRDVTPEATLAVADKEMPGFGEQMRQISLKF-VPTAILSRQVAVIRGQSLIINLPGQPKSIKETLEGLKDADGNVVVP 156
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 3-143 5.28e-17

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: 73.15  E-value: 5.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795   3 RWGLVVTSDRVKEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAALHEgAEVVLVTGGTGPNPRDISADL 82
Cdd:cd00758    1 RVAIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASRE-ADLVLTTGGTGVGRRDVTPEA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942706795  83 VSRICDRVLPGvgeefrrrsleEGVANAVLSRALACSFRDRLLAVSPGNPGAARLMAELLL 143
Cdd:cd00758   80 LAELGEREAHG-----------KGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALV 129
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 60-155 4.25e-08

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 51.74  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795  60 EGAEVVLVTGGTGPNPRDISADLVSRICDRVLPGVGEEFRRRSLEEgVANAVLSRALACSFRDRLLAVSPGNPGAARLMA 139
Cdd:PLN02699 523 DRMDLILTLGGTGFTPRDVTPEATKEVIQKETPGLLYVMMQESLKV-TPFAMLSRSAAGIRGSTLIINMPGNPNAVAECM 601

                         90
                 ....*....|....*.
gi 942706795 140 ELLLEVVDHALHQLRG 155
Cdd:PLN02699 602 EALLPALKHALKQIKG 617
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 19-91 2.67e-06

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: 45.17  E-value: 2.67e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942706795  19 QDETTPMLRRLLGEHGHELVYTAIAGNDPVEIlyhiAAALHEG---AEVVLVTGGTGPNPRDISADLVSRICDRVL 91
Cdd:cd00885   17 VDTNAAFLAKELAELGIEVYRVTVVGDDEDRI----AEALRRAserADLVITTGGLGPTHDDLTREAVAKAFGRPL 88
Transposase_mut pfam00872
Transposase, Mutator family;
77-122 1.49e-04

Transposase, Mutator family;


Pssm-ID: 307151  Cd Length: 380  Bit Score: 41.21  E-value: 1.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 942706795   77 DISADLVSRICDRVLPGVGeEFRRRSLEEGVANAVLSRALACSFRD 122
Cdd:pfam00872 132 SVSKSTVSRITKRLDEAVG-AFRNRPLEENEYPYLFLDATYLKVRE 176
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 23-155 4.04e-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: 39.69  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795  23 TPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAALhEGAEVVLVTGGTGPNPRDISADLVSRIcdrvlpGVGEEFRRRS 102
Cdd:COG0303  201 SYMLAALLREAGAEVVDLGIVPDDPEALRAALREAL-AEADLVITSGGVSVGDYDLVKEALEEL------GAEVLFHKVA 273

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 942706795 103 LEEG--VANAVLSRALACSFrdrllavsPGNPGAARLMAELLlevVDHALHQLRG 155
Cdd:COG0303  274 MKPGkpLAFGRLGGKPVFGL--------PGNPVSALVTFELF---VRPALRKLAG 317
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
 2-78 5.64e-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: 39.07  E-value: 5.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942706795   2 ARWGLVVTSDRVKEHPEQDETTPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAALHEGAEVVLVTGGTGPNPRDI 78
Cdd:cd03522  160 LRVGLIVTGSEVYGGRIEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAAAIAEALEAGAELLILTGGASVDPDDV 236
IS285 COG3328
Transposase (or an inactivated derivative) [Mobilome: prophages, transposons];
77-105 7.29e-04

Transposase (or an inactivated derivative) [Mobilome: prophages, transposons];


Pssm-ID: 442557  Cd Length: 400  Bit Score: 39.02  E-value: 7.29e-04
                         10        20
                 ....*....|....*....|....*....
gi 942706795  77 DISADLVSRICDRVLPGVgEEFRRRSLEE 105
Cdd:COG3328  132 GLSKSTVSRITDKLDEEV-EAWQNRPLEE 159
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 23-155 2.03e-03

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: 37.86  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942706795  23 TPMLRRLLGEHGHELVYTAIAGNDPVEILYHIAAALHEgAEVVLVTGGTGPNPRDISADLVSRICDRVL-------PGvg 95
Cdd:cd00887  197 SYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEE-ADVVITSGGVSVGDYDFVKEVLEELGGEVLfhgvamkPG-- 273

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942706795  96 eefrrrsleegvanavlsRALACSFRDRLLAVS-PGNPGAARLMAELLlevVDHALHQLRG 155
Cdd:cd00887  274 ------------------KPLAFGRLGGKPVFGlPGNPVSALVTFELF---VRPALRKLQG 313
 
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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