NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|496513590|ref|WP_009221873|]
View 

molybdenum cofactor biosynthesis protein B [Peptoniphilus sp. oral taxon 386]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 3-158 3.86e-73

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: 216.91  E-value: 3.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590   3 DKYSAGVLTISNRSYRGEREDLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDLALILTTGGTGFSDRDI 82
Cdd:COG0521    8 VPLRIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTTGGTGLSPRDV 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496513590  83 TPEITIELCDRRVPGISEAMRSYG-AKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEAIIPFLKHGIDILRG 158
Cdd:COG0521   88 TPEATRPLLDKELPGFGELFRALSlEEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHAVDLLNG 164
 
Name Accession Description Interval E-value
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 3-158 3.86e-73

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: 216.91  E-value: 3.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590   3 DKYSAGVLTISNRSYRGEREDLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDLALILTTGGTGFSDRDI 82
Cdd:COG0521    8 VPLRIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTTGGTGLSPRDV 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496513590  83 TPEITIELCDRRVPGISEAMRSYG-AKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEAIIPFLKHGIDILRG 158
Cdd:COG0521   88 TPEATRPLLDKELPGFGELFRALSlEEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHAVDLLNG 164
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 5-156 1.95e-70

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: 209.26  E-value: 1.95e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590   5 YSAGVLTISNRSYRGEREDLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDLALILTTGGTGFSDRDITP 84
Cdd:cd00886    1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRDVTP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496513590  85 EITIELCDRRVPGISEAMRSYGAKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEAIIPFLKHGIDIL 156
Cdd:cd00886   81 EATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 6-160 1.69e-52

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 169.35  E-value: 1.69e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590   6 SAGVLTISNRSYRGEREDLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDdLALILTTGGTGFSDRDITPE 85
Cdd:PRK03604 157 SAAVLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAEG-YALIITTGGTGLGPRDVTPE 235

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496513590  86 ITIELCDRRVPGISEAMRSYGAKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEAIIPFLKHGIDILRGKN 160
Cdd:PRK03604 236 ALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPALFHAFAMVKGEG 310
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 5-146 3.13e-38

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: 127.82  E-value: 3.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590    5 YSAGVLTISNRSYRGERE-------DLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDLalILTTGGTGF 77
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADV--VLTTGGTGV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496513590   78 SDRDITPEITIELCDRRVPGISEAMRSYGAKFtpmsyLSRAES----GIRKNTLIINFPGNPKAIRENFEAII 146
Cdd:TIGR00177  79 GPRDVTPEALEELGEKEIPGFGEFRMLSSLPV-----LSRPGKpataGVRGGTLIFNLPGNPVSALVTFEVLI 146
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 8-151 5.01e-37

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: 124.28  E-value: 5.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590    8 GVLTISNRSYRGEREDLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDLalILTTGGTGFSDRDITPEIT 87
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTPEAL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496513590   88 IELCDRRVPGISEAMRSYGAKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEAII-PFLKH 151
Cdd:pfam00994  79 AELGGRELPGFEELFRGVSLKPGKPVGTAPGAILSRAGKTVFGLPGSPVAAKVMFELLLlPLLRH 143
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 8-145 1.32e-35

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: 120.77  E-value: 1.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590     8 GVLTISNRSYRGER-EDLGGPILIELIEKLGFEVKNFKIV--PDERINIRETIEEWVDEDDLalILTTGGTGFSDRDITP 84
Cdd:smart00852   1 AIISTGDELLSGGQiRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDDLTP 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496513590    85 EITIELCDRRVPGISEAMRsYGAKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEAI 145
Cdd:smart00852  79 EALAELGGRELLGHGVAMR-PGGPPGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
 
Name Accession Description Interval E-value
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 3-158 3.86e-73

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: 216.91  E-value: 3.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590   3 DKYSAGVLTISNRSYRGEREDLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDLALILTTGGTGFSDRDI 82
Cdd:COG0521    8 VPLRIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTTGGTGLSPRDV 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496513590  83 TPEITIELCDRRVPGISEAMRSYG-AKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEAIIPFLKHGIDILRG 158
Cdd:COG0521   88 TPEATRPLLDKELPGFGELFRALSlEEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHAVDLLNG 164
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 5-156 1.95e-70

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: 209.26  E-value: 1.95e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590   5 YSAGVLTISNRSYRGEREDLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDLALILTTGGTGFSDRDITP 84
Cdd:cd00886    1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRDVTP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496513590  85 EITIELCDRRVPGISEAMRSYGAKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEAIIPFLKHGIDIL 156
Cdd:cd00886   81 EATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 6-160 1.69e-52

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 169.35  E-value: 1.69e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590   6 SAGVLTISNRSYRGEREDLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDdLALILTTGGTGFSDRDITPE 85
Cdd:PRK03604 157 SAAVLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAEG-YALIITTGGTGLGPRDVTPE 235

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496513590  86 ITIELCDRRVPGISEAMRSYGAKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEAIIPFLKHGIDILRGKN 160
Cdd:PRK03604 236 ALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPALFHAFAMVKGEG 310
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 8-143 7.03e-46

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 148.56  E-value: 7.03e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590   8 GVLTISNRSYRGEREDLGGPILIE-LIEKLG--FEVKnFKIVPDERINIRETIEEWVDEDDLALILTTGGTGFSDRDITP 84
Cdd:PRK09417   7 GLVSISDRASSGVYEDKGIPALEEwLASALTspFEIE-TRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTGPARRDVTP 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 496513590  85 EITIELCDRRVPGISEAMRSYGAKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFE 143
Cdd:PRK09417  86 EATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLE 144
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 7-149 3.74e-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: 134.39  E-value: 3.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590   7 AGVLTISNRSYRGEREDLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDlaLILTTGGTGFSDRDITPEI 86
Cdd:cd00758    2 VAIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREAD--LVLTTGGTGVGRRDVTPEA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496513590  87 TIELCDRRVPGiseamrsygaKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEA-IIPFL 149
Cdd:cd00758   80 LAELGEREAHG----------KGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEAlVLPAL 133
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 5-158 3.05e-40

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 143.03  E-value: 3.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590   5 YSAGVLTISNRSYRGEREDLGGPILIELI----EKL-GFEVKNFKIVPDERINIRETIEEWVDEDDLALILTTGGTGFSD 79
Cdd:PLN02699 459 VKVAILTVSDTVSSGAGPDRSGPRAVSVVnsssEKLgGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTGFTP 538

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496513590  80 RDITPEITIELCDRRVPGISEAMRSYGAKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEAIIPFLKHGIDILRG 158
Cdd:PLN02699 539 RDVTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALKQIKG 617
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 5-146 3.13e-38

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: 127.82  E-value: 3.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590    5 YSAGVLTISNRSYRGERE-------DLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDLalILTTGGTGF 77
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADV--VLTTGGTGV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496513590   78 SDRDITPEITIELCDRRVPGISEAMRSYGAKFtpmsyLSRAES----GIRKNTLIINFPGNPKAIRENFEAII 146
Cdd:TIGR00177  79 GPRDVTPEALEELGEKEIPGFGEFRMLSSLPV-----LSRPGKpataGVRGGTLIFNLPGNPVSALVTFEVLI 146
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 8-151 5.01e-37

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: 124.28  E-value: 5.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590    8 GVLTISNRSYRGEREDLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDLalILTTGGTGFSDRDITPEIT 87
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTPEAL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496513590   88 IELCDRRVPGISEAMRSYGAKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEAII-PFLKH 151
Cdd:pfam00994  79 AELGGRELPGFEELFRGVSLKPGKPVGTAPGAILSRAGKTVFGLPGSPVAAKVMFELLLlPLLRH 143
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 8-145 1.32e-35

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: 120.77  E-value: 1.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590     8 GVLTISNRSYRGER-EDLGGPILIELIEKLGFEVKNFKIV--PDERINIRETIEEWVDEDDLalILTTGGTGFSDRDITP 84
Cdd:smart00852   1 AIISTGDELLSGGQiRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDDLTP 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496513590    85 EITIELCDRRVPGISEAMRsYGAKFTPMSYLSRAESGIRKNTLIINFPGNPKAIRENFEAI 145
Cdd:smart00852  79 EALAELGGRELLGHGVAMR-PGGPPGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 26-135 5.72e-12

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: 62.51  E-value: 5.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590  26 GPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDlaLILTTGGTGFSDRDITPEITIELCDRR-VPGIseAMRS 104
Cdd:cd00887  197 SYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEAD--VVITSGGVSVGDYDFVKEVLEELGGEVlFHGV--AMKP 272

                         90       100       110
                 ....*....|....*....|....*....|.
gi 496513590 105 yGakfTPMSYlsraesGIRKNTLIINFPGNP 135
Cdd:cd00887  273 -G---KPLAF------GRLGGKPVFGLPGNP 293
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 26-135 6.21e-10

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: 56.64  E-value: 6.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590  26 GPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDlaLILTTGGTGFSDRDITPEITIEL-CDRRVPGIseAMRs 104
Cdd:COG0303  201 SYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEAD--LVITSGGVSVGDYDLVKEALEELgAEVLFHKV--AMK- 275

                         90       100       110
                 ....*....|....*....|....*....|.
gi 496513590 105 yGAKftPMSYlsraesGIRKNTLIINFPGNP 135
Cdd:COG0303  276 -PGK--PLAF------GRLGGKPVFGLPGNP 297
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
 6-85 5.56e-08

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: 50.62  E-value: 5.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496513590   6 SAGVLTISNRSYRGEREDLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDLaLILTTGGTGfSDR-DITP 84
Cdd:cd03522  161 RVGLIVTGSEVYGGRIEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAAAIAEALEAGAE-LLILTGGAS-VDPdDVTP 238


                 .
gi 496513590  85 E 85
Cdd:cd03522  239 A 239
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 6-83 1.52e-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: 1.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496513590   6 SAGVLTISNRSYRGEREDLGGPILIELIEKLGFEVKNFKIVPDERINIRETIEEWVDEDDlaLILTTGGTGFSDRDIT 83
Cdd:cd00885    1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERAD--LVITTGGLGPTHDDLT 76
 
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