NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1845977487|ref|NP_001370857|]
View 

molybdopterin molybdotransferase [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-155 6.04e-64

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: 193.08  E-value: 6.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   1 MRVCVITVSDTCSAGTRTDESGPKLVELVDTSAVVNAtvnegSPFVVPDDVTAIHDALVE--QSKFADVILTTGGTGFAP 78
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVV-----AYEIVPDDKDEIREALIEwaDEDGVDLILTTGGTGLAP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845977487  79 RDVTPEATLKVIDRRCSGLEIALHTASLKITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTLEPLLNHGINLL 155
Cdd:cd00886    76 RDVTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
 
Name Accession Description Interval E-value
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 1-155 6.04e-64

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: 193.08  E-value: 6.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   1 MRVCVITVSDTCSAGTRTDESGPKLVELVDTSAVVNAtvnegSPFVVPDDVTAIHDALVE--QSKFADVILTTGGTGFAP 78
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVV-----AYEIVPDDKDEIREALIEwaDEDGVDLILTTGGTGLAP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845977487  79 RDVTPEATLKVIDRRCSGLEIALHTASLKITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTLEPLLNHGINLL 155
Cdd:cd00886    76 RDVTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 2-156 1.47e-59

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: 182.62  E-value: 1.47e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   2 RVCVITVSDTCSAGTRTDESGPKLVELVDtsavvNATVNEGSPFVVPDDVTAIHDALVE--QSKFADVILTTGGTGFAPR 79
Cdd:COG0521    11 RIAVLTVSDRRSRGEREDTSGPALVELLE-----EAGHEVVARRIVPDDKDAIRAALREliDDEGVDLVLTTGGTGLSPR 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845977487  80 DVTPEATLKVIDRRCSGLEIALHTASL-KITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTLEPLLNHGINLLK 156
Cdd:COG0521    86 DVTPEATRPLLDKELPGFGELFRALSLeEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHAVDLLN 163
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 2-166 2.84e-44

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 154.20  E-value: 2.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   2 RVCVITVSDTCSAGTRTDESGPKLVELVDTS------AVVNATVnegspfVVPDDVTAIHDALVEQSKF--ADVILTTGG 73
Cdd:PLN02699  460 KVAILTVSDTVSSGAGPDRSGPRAVSVVNSSseklggAKVVATA------VVPDDVEKIKDVLQKWSDIdrMDLILTLGG 533

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487  74 TGFAPRDVTPEATLKVIDRRCSGLEIALHTASLKITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTLEPLLNHGIN 153
Cdd:PLN02699  534 TGFTPRDVTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALK 613

                         170
                  ....*....|...
gi 1845977487 154 LLKNtDDGSQHAR 166
Cdd:PLN02699  614 QIKG-DKREKHPR 625
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 4-150 4.95e-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 trimerization.


Pssm-ID: 425979 [Multi-domain]  Cd Length: 143  Bit Score: 119.28  E-value: 4.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   4 CVITVSDTCSAGTRTDESGPKLVELVDtsavvNATVNEGSPFVVPDDVTAIHDALVEQSKFADVILTTGGTGFAPRDVTP 83
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLR-----EAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTP 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845977487  84 EATLKVIDRRCSGLEIALHTASLKITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTL-EPLLNH 150
Cdd:pfam00994  76 EALAELGGRELPGFEELFRGVSLKPGKPVGTAPGAILSRAGKTVFGLPGSPVAAKVMFELLlLPLLRH 143
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 1-144 1.53e-34

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: 118.19  E-value: 1.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   1 MRVCVITVSDTCSAGTRTDESGPklveLVDTSA------VVNATVNEGSPFVVPDDVTAIHDALVEQSKFADVILTTGGT 74
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQ----IYDSNGpllaalLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGT 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487  75 GFAPRDVTPEATLKVIDRRCSGLEIALHTASLKItSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTL 144
Cdd:TIGR00177  77 GVGPRDVTPEALEELGEKEIPGFGEFRMLSSLPV-LSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVL 145
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 4-144 9.33e-31

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: 108.44  E-value: 9.33e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487    4 CVITVSDTCSAGTRTDES-GPKLVELVDTSavvNATVNEGSPFVVPDDVTAIHDALVEQSKFADVILTTGGTGFAPRDVT 82
Cdd:smart00852   1 AIISTGDELLSGGQIRDSnGPMLAALLREL---GIEVVRVVVVGGPDDPEAIREALREALAEADVVITTGGTGPGPDDLT 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845977487   83 PEATLKVIDRRCSGLEIALHTASlKITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTL 144
Cdd:smart00852  78 PEALAELGGRELLGHGVAMRPGG-PPGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
 
Name Accession Description Interval E-value
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 1-155 6.04e-64

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: 193.08  E-value: 6.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   1 MRVCVITVSDTCSAGTRTDESGPKLVELVDTSAVVNAtvnegSPFVVPDDVTAIHDALVE--QSKFADVILTTGGTGFAP 78
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVV-----AYEIVPDDKDEIREALIEwaDEDGVDLILTTGGTGLAP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845977487  79 RDVTPEATLKVIDRRCSGLEIALHTASLKITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTLEPLLNHGINLL 155
Cdd:cd00886    76 RDVTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 2-156 1.47e-59

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: 182.62  E-value: 1.47e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   2 RVCVITVSDTCSAGTRTDESGPKLVELVDtsavvNATVNEGSPFVVPDDVTAIHDALVE--QSKFADVILTTGGTGFAPR 79
Cdd:COG0521    11 RIAVLTVSDRRSRGEREDTSGPALVELLE-----EAGHEVVARRIVPDDKDAIRAALREliDDEGVDLVLTTGGTGLSPR 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845977487  80 DVTPEATLKVIDRRCSGLEIALHTASL-KITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTLEPLLNHGINLLK 156
Cdd:COG0521    86 DVTPEATRPLLDKELPGFGELFRALSLeEIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHAVDLLN 163
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 2-166 2.84e-44

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 154.20  E-value: 2.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   2 RVCVITVSDTCSAGTRTDESGPKLVELVDTS------AVVNATVnegspfVVPDDVTAIHDALVEQSKF--ADVILTTGG 73
Cdd:PLN02699  460 KVAILTVSDTVSSGAGPDRSGPRAVSVVNSSseklggAKVVATA------VVPDDVEKIKDVLQKWSDIdrMDLILTLGG 533

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487  74 TGFAPRDVTPEATLKVIDRRCSGLEIALHTASLKITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTLEPLLNHGIN 153
Cdd:PLN02699  534 TGFTPRDVTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALK 613

                         170
                  ....*....|...
gi 1845977487 154 LLKNtDDGSQHAR 166
Cdd:PLN02699  614 QIKG-DKREKHPR 625
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 5-156 1.10e-37

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 131.22  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   5 VITVSDTCSAGTRTDESGPKLVELVDTSAVvnaTVNEgsPFVVPDDVTAIHDALVE-QSKFADVILTTGGTGFAPRDVTP 83
Cdd:PRK03604  160 VLVLSDSIAAGTKEDRSGKLIVEGLEEAGF---EVSH--YTIIPDEPAEIAAAVAAwIAEGYALIITTGGTGLGPRDVTP 234

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845977487  84 EATLKVIDRRCSGLEIALHTASLKITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTLEPLLNHGINLLK 156
Cdd:PRK03604  235 EALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPALFHAFAMVK 307
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 1-144 6.98e-36

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 123.14  E-value: 6.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   1 MRVCVITVSDTCSAGTRTDESGPKLVELVdTSAVVnatvnegSPF-----VVPDDVTAIHDALVE--QSKFADVILTTGG 73
Cdd:PRK09417    4 LKIGLVSISDRASSGVYEDKGIPALEEWL-ASALT-------SPFeietrLIPDEQDLIEQTLIElvDEMGCDLVLTTGG 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845977487  74 TGFAPRDVTPEATLKVIDRRCSGLEIALHTASLKITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTL 144
Cdd:PRK09417   76 TGPARRDVTPEATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLEGL 146
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 2-148 4.26e-35

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: 119.37  E-value: 4.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   2 RVCVITVSDTCSAGTRTDESGPKLVELV-DTSAVVNATVnegspfVVPDDVTAIHDALVEQSKFADVILTTGGTGFAPRD 80
Cdd:cd00758     1 RVAIVTVSDELSQGQIEDTNGPALEALLeDLGCEVIYAG------VVPDDADSIRAALIEASREADLVLTTGGTGVGRRD 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845977487  81 VTPEATLKVIDRRCSGleialhtaslKITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTL-EPLL 148
Cdd:cd00758    75 VTPEALAELGEREAHG----------KGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALvLPAL 133
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 4-150 4.95e-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 trimerization.


Pssm-ID: 425979 [Multi-domain]  Cd Length: 143  Bit Score: 119.28  E-value: 4.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   4 CVITVSDTCSAGTRTDESGPKLVELVDtsavvNATVNEGSPFVVPDDVTAIHDALVEQSKFADVILTTGGTGFAPRDVTP 83
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLR-----EAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTP 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845977487  84 EATLKVIDRRCSGLEIALHTASLKITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTL-EPLLNH 150
Cdd:pfam00994  76 EALAELGGRELPGFEELFRGVSLKPGKPVGTAPGAILSRAGKTVFGLPGSPVAAKVMFELLlLPLLRH 143
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 1-144 1.53e-34

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: 118.19  E-value: 1.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487   1 MRVCVITVSDTCSAGTRTDESGPklveLVDTSA------VVNATVNEGSPFVVPDDVTAIHDALVEQSKFADVILTTGGT 74
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQ----IYDSNGpllaalLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGT 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487  75 GFAPRDVTPEATLKVIDRRCSGLEIALHTASLKItSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTL 144
Cdd:TIGR00177  77 GVGPRDVTPEALEELGEKEIPGFGEFRMLSSLPV-LSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVL 145
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 4-144 9.33e-31

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: 108.44  E-value: 9.33e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487    4 CVITVSDTCSAGTRTDES-GPKLVELVDTSavvNATVNEGSPFVVPDDVTAIHDALVEQSKFADVILTTGGTGFAPRDVT 82
Cdd:smart00852   1 AIISTGDELLSGGQIRDSnGPMLAALLREL---GIEVVRVVVVGGPDDPEAIREALREALAEADVVITTGGTGPGPDDLT 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845977487   83 PEATLKVIDRRCSGLEIALHTASlKITSMAALSRAIVGIRGGTLIVNMPGSVKAVKECWDTL 144
Cdd:smart00852  78 PEALAELGGRELLGHGVAMRPGG-PPGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 46-132 7.57e-07

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: 47.78  E-value: 7.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487  46 VVPDDVTAIHDALVEQSKFADVILTTGGTGFAPRDVTPEatlkVIDRRcsGLEIALHtaslKItsmaalsrAI------- 118
Cdd:COG0303   220 IVPDDPEALRAALREALAEADLVITSGGVSVGDYDLVKE----ALEEL--GAEVLFH----KV--------AMkpgkpla 281

                          90
                  ....*....|....
gi 1845977487 119 VGIRGGTLIVNMPG 132
Cdd:COG0303   282 FGRLGGKPVFGLPG 295
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 46-132 1.48e-06

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: 46.72  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487  46 VVPDDVTAIHDALVEQSKFADVILTTGGTGFAPRDVTPEatlkVIDRRcsGLEIALHTASLKITsmaalSRAIVGIRGGT 125
Cdd:cd00887   216 IVPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKE----VLEEL--GGEVLFHGVAMKPG-----KPLAFGRLGGK 284


                  ....*..
gi 1845977487 126 LIVNMPG 132
Cdd:cd00887   285 PVFGLPG 291
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
45-148 2.01e-05

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 43.08  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487  45 FVVPDDVTAIHDALVEQSKFADVILTTGGTGFAPRDVTPEATLKVIDRRCSGLEIAL-------HTASLKIT----SMAA 113
Cdd:PRK01215   43 TVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGFAKALGVELELNEDALrmilekyEKRGIPLTperkKMAM 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1845977487 114 L---SRAI---VGI-------RGGTLIVNMPG---SVKAVKEcwDTLEPLL 148
Cdd:PRK01215  123 MppgAVPLenpVGTapgilieHGGKDIVALPGvprEMEAIFE--NFVEPLL 171
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 46-108 3.73e-05

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: 41.70  E-value: 3.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845977487  46 VVPDDVTAIHDALVEQSKFADVILTTGGTGFAPRDVTPEATLKVIdrrcsGLEIALHTASLKI 108
Cdd:cd00885    40 VVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAVAKAF-----GRPLVLDEEALER 97
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
 46-85 6.90e-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: 38.68  E-value: 6.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1845977487  46 VVPDDVTAIHDALVEQSK-FADVILTTGGTGFAPRDVTPEA 85
Cdd:cd03522   200 IVPHDEAAIAAAIAEALEaGAELLILTGGASVDPDDVTPAA 240
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 46-108 7.25e-04

ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];


Pssm-ID: 440678  Cd Length: 249  Bit Score: 38.56  E-value: 7.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845977487  46 VVPDDVTAIHDALVEQSKFADVILTTGGTGFAPRDVTPEATLKVIdrrcsGLEIALHTASLKI 108
Cdd:COG1058    40 TVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAVAEAL-----GVPLVLDPEALAL 97
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 27-132 3.31e-03

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


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 37.12  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845977487  27 ELVDT-SAVVNATVNE--GSPF---VVPDDVTAIHDALVEQSKFADVILTTGGTGFAPRDVtpeaTLKVIDRRcsGlEIA 100
Cdd:PRK14498  209 KIYDVnSYTLAAAVEEagGEPVrygIVPDDEEELEAALRKALKECDLVLLSGGTSAGAGDV----TYRVIEEL--G-EVL 281

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1845977487 101 LHTASL---KITsmaalsraIVGIRGGTLIVNMPG 132
Cdd:PRK14498  282 VHGVAIkpgKPT--------ILGVIGGKPVVGLPG 308
 
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