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Conserved domains on  [gi|1949187520|ref|WP_198499511|]
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MULTISPECIES: MogA/MoaB family molybdenum cofactor biosynthesis protein [Brevibacterium]

Protein Classification

MogA/MoaB family molybdenum cofactor biosynthesis protein( domain architecture ID 10096825)

MogA/MoaB family molybdenum cofactor biosynthesis protein similar to Bacillus anthracis MoaB, which may be involved in the biosynthesis of molybdopterin; may be a metal-binding pterin (MPT)-adenylyltransferase which converts MPT to adenylylated MPT (MPT-AMP)

Gene Ontology:  GO:0030151|GO:0046872
PubMed:  16261263

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 15-165 1.73e-54

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: 169.58  E-value: 1.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520  15 RSAAVIIASTSAARGEAPDTTGPLLVEWLRGRGYDCPDAIVVRDGEpvgQTLRGLLIDTPEDKRPRIIVTSGGTGLAPDD 94
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDK---DEIREALIEWADEDGVDLILTTGGTGLAPRD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187520  95 RTPEFTAELLERQSPGLIYAMWRKGLESTSSAVMSRGVAGVRGRSFVINLPGSKGGVRDGITVIDDLLEHI 165
Cdd:cd00886    78 VTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHL 148
 
Name Accession Description Interval E-value
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 15-165 1.73e-54

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: 169.58  E-value: 1.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520  15 RSAAVIIASTSAARGEAPDTTGPLLVEWLRGRGYDCPDAIVVRDGEpvgQTLRGLLIDTPEDKRPRIIVTSGGTGLAPDD 94
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDK---DEIREALIEWADEDGVDLILTTGGTGLAPRD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187520  95 RTPEFTAELLERQSPGLIYAMWRKGLESTSSAVMSRGVAGVRGRSFVINLPGSKGGVRDGITVIDDLLEHI 165
Cdd:cd00886    78 VTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHL 148
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 7-165 6.64e-52

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: 163.75  E-value: 6.64e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520   7 TTDRLGAGRSAAVIIASTSAARGEAPDTTGPLLVEWLRGRGYDCPDAIVVRDG-EPVGQTLRGLLidtpEDKRPRIIVTS 85
Cdd:COG0521     2 SSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDkDAIRAALRELI----DDEGVDLVLTT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520  86 GGTGLAPDDRTPEFTAELLERQSPGLIYAMWRKGL-ESTSSAVMSRGVAGVRGRSFVINLPGSKGGVRDGITVIDDLLEH 164
Cdd:COG0521    78 GGTGLSPRDVTPEATRPLLDKELPGFGELFRALSLeEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPH 157


                  .
gi 1949187520 165 I 165
Cdd:COG0521   158 A 158
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 16-165 4.02e-40

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 137.77  E-value: 4.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520  16 SAAVIIASTSAARGEAPDTTGPLLVEWLRGRGYDCPDAIVVRDG-EPVGQTLRGLLidtpeDKRPRIIVTSGGTGLAPDD 94
Cdd:PRK03604  157 SAAVLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEpAEIAAAVAAWI-----AEGYALIITTGGTGLGPRD 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187520  95 RTPEFTAELLERQSPGLIYAMWRKGLESTSSAVMSRGVAGVRGRSFVINLPGSKGGVRDGITVIDDLLEHI 165
Cdd:PRK03604  232 VTPEALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPALFHA 302
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 18-164 1.06e-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: 90.77  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520  18 AVIIASTSAARGEAPDTTGPLLVEWLRGRGYDCPDAIVVRD-GEPVGQTLRGLLidtpedKRPRIIVTSGGTGLAPDDRT 96
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDdPEAIKEALRAAA------EEADVVITTGGTGPGPDDVT 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187520  97 PEFTAELLERQSPGLIYAMWRKGLESTSSAVMSRGVAGVRGRSFVINLPGSKGGVRDGI-TVIDDLLEH 164
Cdd:pfam00994  75 PEALAELGGRELPGFEELFRGVSLKPGKPVGTAPGAILSRAGKTVFGLPGSPVAAKVMFeLLLLPLLRH 143
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 18-158 1.33e-21

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: 85.33  E-value: 1.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520   18 AVIIASTSAARGEA-PDTTGPLLVEWLRGRGYDCPDAIVVR---DGEPVGQTLRGLLidtpedKRPRIIVTSGGTGLAPD 93
Cdd:smart00852   1 AIISTGDELLSGGQiRDSNGPMLAALLRELGIEVVRVVVVGgpdDPEAIREALREAL------AEADVVITTGGTGPGPD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949187520   94 DRTPEFTAELLERQSPGLIYAMWRKGLEsTSSAVMSRGVAGVRGRSFVINLPGSKGGVRDGITVI 158
Cdd:smart00852  75 DLTPEALAELGGRELLGHGVAMRPGGPP-GPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 6-158 3.80e-18

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: 76.59  E-value: 3.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520   6 TTTDRLGAGrsaaviiaSTSAARGEAPDTTGPLLVEWLRGRGYDCPDAIVVRDG-EPVGQTLRGLLIDTpedkrpRIIVT 84
Cdd:TIGR00177   7 SVGDELVEG--------GQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDpEEIREILRKAVDEA------DVVLT 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949187520  85 SGGTGLAPDDRTPEFTAELLERQSPGLIYAMWRkglesTSSAVMSRG----VAGVRGRSFVINLPGSKGGVRDGITVI 158
Cdd:TIGR00177  73 TGGTGVGPRDVTPEALEELGEKEIPGFGEFRML-----SSLPVLSRPgkpaTAGVRGGTLIFNLPGNPVSALVTFEVL 145
 
Name Accession Description Interval E-value
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 15-165 1.73e-54

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: 169.58  E-value: 1.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520  15 RSAAVIIASTSAARGEAPDTTGPLLVEWLRGRGYDCPDAIVVRDGEpvgQTLRGLLIDTPEDKRPRIIVTSGGTGLAPDD 94
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDK---DEIREALIEWADEDGVDLILTTGGTGLAPRD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187520  95 RTPEFTAELLERQSPGLIYAMWRKGLESTSSAVMSRGVAGVRGRSFVINLPGSKGGVRDGITVIDDLLEHI 165
Cdd:cd00886    78 VTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHL 148
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 7-165 6.64e-52

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: 163.75  E-value: 6.64e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520   7 TTDRLGAGRSAAVIIASTSAARGEAPDTTGPLLVEWLRGRGYDCPDAIVVRDG-EPVGQTLRGLLidtpEDKRPRIIVTS 85
Cdd:COG0521     2 SSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDkDAIRAALRELI----DDEGVDLVLTT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520  86 GGTGLAPDDRTPEFTAELLERQSPGLIYAMWRKGL-ESTSSAVMSRGVAGVRGRSFVINLPGSKGGVRDGITVIDDLLEH 164
Cdd:COG0521    78 GGTGLSPRDVTPEATRPLLDKELPGFGELFRALSLeEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPH 157


                  .
gi 1949187520 165 I 165
Cdd:COG0521   158 A 158
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 16-165 4.02e-40

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 137.77  E-value: 4.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520  16 SAAVIIASTSAARGEAPDTTGPLLVEWLRGRGYDCPDAIVVRDG-EPVGQTLRGLLidtpeDKRPRIIVTSGGTGLAPDD 94
Cdd:PRK03604  157 SAAVLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEpAEIAAAVAAWI-----AEGYALIITTGGTGLGPRD 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187520  95 RTPEFTAELLERQSPGLIYAMWRKGLESTSSAVMSRGVAGVRGRSFVINLPGSKGGVRDGITVIDDLLEHI 165
Cdd:PRK03604  232 VTPEALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPALFHA 302
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 18-164 1.06e-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: 90.77  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520  18 AVIIASTSAARGEAPDTTGPLLVEWLRGRGYDCPDAIVVRD-GEPVGQTLRGLLidtpedKRPRIIVTSGGTGLAPDDRT 96
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDdPEAIKEALRAAA------EEADVVITTGGTGPGPDDVT 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187520  97 PEFTAELLERQSPGLIYAMWRKGLESTSSAVMSRGVAGVRGRSFVINLPGSKGGVRDGI-TVIDDLLEH 164
Cdd:pfam00994  75 PEALAELGGRELPGFEELFRGVSLKPGKPVGTAPGAILSRAGKTVFGLPGSPVAAKVMFeLLLLPLLRH 143
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 18-158 1.33e-21

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: 85.33  E-value: 1.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520   18 AVIIASTSAARGEA-PDTTGPLLVEWLRGRGYDCPDAIVVR---DGEPVGQTLRGLLidtpedKRPRIIVTSGGTGLAPD 93
Cdd:smart00852   1 AIISTGDELLSGGQiRDSNGPMLAALLRELGIEVVRVVVVGgpdDPEAIREALREAL------AEADVVITTGGTGPGPD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949187520   94 DRTPEFTAELLERQSPGLIYAMWRKGLEsTSSAVMSRGVAGVRGRSFVINLPGSKGGVRDGITVI 158
Cdd:smart00852  75 DLTPEALAELGGRELLGHGVAMRPGGPP-GPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 9-164 2.90e-20

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 87.18  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520   9 DRLGAGRSAAVIIASTSAARGEAPDTTGPLLVEWL-----RGRGYDCPDAIVVRDGEPvgqTLRGLLIDTPEDKRPRIIV 83
Cdd:PLN02699  453 EAQNPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVnssseKLGGAKVVATAVVPDDVE---KIKDVLQKWSDIDRMDLIL 529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520  84 TSGGTGLAPDDRTPEFTAELLERQSPGLIYAMWRKGLESTSSAVMSRGVAGVRGRSFVINLPGSKGGVRDGITVIDDLLE 163
Cdd:PLN02699  530 TLGGTGFTPRDVTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALK 609


                  .
gi 1949187520 164 H 164
Cdd:PLN02699  610 H 610
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 17-153 5.52e-19

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: 78.15  E-value: 5.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520  17 AAVIIASTSAARGEAPDTTGPLLVEWLRGRGYDCPDAIVVRDGEpvgQTLRGLLIdtPEDKRPRIIVTSGGTGLAPDDRT 96
Cdd:cd00758     2 VAIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDA---DSIRAALI--EASREADLVLTTGGTGVGRRDVT 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1949187520  97 PEFTAELLERQSPGLIYAMwrkglestssAVMSRGVAGVRGRSFVINLPGSKGGVRD 153
Cdd:cd00758    77 PEALAELGEREAHGKGVAL----------APGSRTAFGIIGKVLIINLPGSPKSALT 123
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 18-146 6.87e-19

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 79.61  E-value: 6.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520  18 AVIIASTSAARGEAPDTTGPLLVEWLrGRGYDCPDAIVVR---DGEPvgqTLRGLLIDTPEDKRPRIIVTSGGTGLAPDD 94
Cdd:PRK09417    7 GLVSISDRASSGVYEDKGIPALEEWL-ASALTSPFEIETRlipDEQD---LIEQTLIELVDEMGCDLVLTTGGTGPARRD 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1949187520  95 RTPEFTAELLERQSPGLIYAMWRKGLESTSSAVMSRGVAGVRGRSFVINLPG 146
Cdd:PRK09417   83 VTPEATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPG 134
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 6-158 3.80e-18

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: 76.59  E-value: 3.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187520   6 TTTDRLGAGrsaaviiaSTSAARGEAPDTTGPLLVEWLRGRGYDCPDAIVVRDG-EPVGQTLRGLLIDTpedkrpRIIVT 84
Cdd:TIGR00177   7 SVGDELVEG--------GQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDpEEIREILRKAVDEA------DVVLT 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949187520  85 SGGTGLAPDDRTPEFTAELLERQSPGLIYAMWRkglesTSSAVMSRG----VAGVRGRSFVINLPGSKGGVRDGITVI 158
Cdd:TIGR00177  73 TGGTGVGPRDVTPEALEELGEKEIPGFGEFRML-----SSLPVLSRPgkpaTAGVRGGTLIFNLPGNPVSALVTFEVL 145
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 33-106 1.97e-03

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: 37.08  E-value: 1.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949187520  33 DTTGPLLVEWLRGRGYDCPDAIVVRD-GEPVGQTLRGLLidtpedKRPRIIVTSGGTGLAPDDRTPEFTAELLER 106
Cdd:cd00885    18 DTNAAFLAKELAELGIEVYRVTVVGDdEDRIAEALRRAS------ERADLVITTGGLGPTHDDLTREAVAKAFGR 86
 
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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