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Conserved domains on  [gi|1622950778|ref|XP_028706221|]
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gephyrin isoform X5 [Macaca mulatta]

Protein Classification

bifunctional molybdopterin adenylyltransferase MobB/molybdopterin molybdotransferase MoeA family protein( domain architecture ID 10096827)

bifunctional molybdopterin adenylyltransferase MobB/molybdopterin molybdotransferase MoeA family protein similar to mammalian Gephyrin and Drosophila Cinnamon, which catalyze the adenylation of molybdopterin followed by molybdenum ligation to adenylated molybdopterin during molybdenum cofactor biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 418-824 1.01e-165

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: 485.85  E-value: 1.01e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 418 DKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTQTV 494
Cdd:cd00887     2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 495 MPGQVMRVTTGAPIPCGADAVVQVEDTELiresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 574
Cdd:cd00887    82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE--------EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 575 LLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 654
Cdd:cd00887   154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 655 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 734
Cdd:cd00887   234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELFVRPAL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 735 RKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEqyvEL 813
Cdd:cd00887   309 RKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---GL 383

                         410
                  ....*....|.
gi 1622950778 814 HKGEVVDVMVI 824
Cdd:cd00887   384 EAGEEVEVLLL 394
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 15-182 2.82e-65

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: 214.65  E-value: 2.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRD 94
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPA 174
Cdd:cd00886    78 VTPE-------------ATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPE 144


                  ....*...
gi 1622950778 175 LPHAIDLL 182
Cdd:cd00886   145 LPHLLDLL 152
 
Name Accession Description Interval E-value
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 418-824 1.01e-165

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: 485.85  E-value: 1.01e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 418 DKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTQTV 494
Cdd:cd00887     2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 495 MPGQVMRVTTGAPIPCGADAVVQVEDTELiresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 574
Cdd:cd00887    82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE--------EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 575 LLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 654
Cdd:cd00887   154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 655 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 734
Cdd:cd00887   234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELFVRPAL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 735 RKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEqyvEL 813
Cdd:cd00887   309 RKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---GL 383

                         410
                  ....*....|.
gi 1622950778 814 HKGEVVDVMVI 824
Cdd:cd00887   384 EAGEEVEVLLL 394
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 414-827 1.36e-150

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: 447.23  E-value: 1.36e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 414 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF----IIGESQAGEQ 489
Cdd:COG0303     1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtlrVVGEIAAGSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 490 PTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELiresDDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 569
Cdd:COG0303    81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER----EGDR----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 570 PSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 649
Cdd:COG0303   153 PADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 650 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLF 729
Cdd:COG0303   233 REALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELF 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 730 VVPALRKMQGILDPRPTIIKARLSCDV-KLDPRPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTE 808
Cdd:COG0303   308 VRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLERDDGE--LVVEPLGGQGSGLLSSLAEADGLIVLPEGVE 385

                         410
                  ....*....|....*....
gi 1622950778 809 qyvELHKGEVVDVMVIGRL 827
Cdd:COG0303   386 ---GVEAGEEVEVLLLDGL 401
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 414-804 2.10e-132

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 409.59  E-value: 2.10e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 414 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQ- 492
Cdd:PLN02699    7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGv 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 493 TVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEEleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSE 572
Cdd:PLN02699   87 TLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 573 IGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLP-GKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNE 651
Cdd:PLN02699  165 IGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGrGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 652 GISR-ADVIITSGGVSMGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDI---DGVRKII--FALPGNPVSAVVT 725
Cdd:PLN02699  245 AISSgVDILLTSGGVSMGDRDFVKPLL--EKRGTVYFSKVLMKPGKPLTFAEIDAksaPSNSKKMlaFGLPGNPVSCLVC 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 726 CNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQE----PLPWAQSTGNQMSSRLMSMRSANGL 800
Cdd:PLN02699  323 FNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPvRPEFHRAIIRWKLNDgsgnPGFVAESTGHQMSSRLLSMKSANAL 402


                  ....
gi 1622950778 801 LMLP 804
Cdd:PLN02699  403 LELP 406
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 15-182 2.82e-65

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: 214.65  E-value: 2.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRD 94
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPA 174
Cdd:cd00886    78 VTPE-------------ATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPE 144


                  ....*...
gi 1622950778 175 LPHAIDLL 182
Cdd:cd00886   145 LPHLLDLL 152
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 6-183 2.34e-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: 199.19  E-value: 2.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778   6 MILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTT 85
Cdd:COG0521     1 MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE---AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  86 GGTGFAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLN-VTPLGMLSRPVCGIRGKTLIINLPGSKKGS 164
Cdd:COG0521    78 GGTGLSPRDVTPE-------------ATRPLLDKELPGFGELFRALSLEeIGPSAILSRAVAGIRGGTLIFNLPGSPGAV 144

                         170
                  ....*....|....*....
gi 1622950778 165 QECFQFILPALPHAIDLLR 183
Cdd:COG0521   145 REALEAILPELPHAVDLLN 163
MoeA_N pfam03453
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ...
 429-580 4.46e-49

MoeA N-terminal region (domain I and II); This family contains two structural domains. One of these contains the conserved DGXA motif. This region is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this region is uncertain.


Pssm-ID: 460923 [Multi-domain]  Cd Length: 147  Bit Score: 170.05  E-value: 4.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 429 PVLGTEI---INYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGeSQAGEQPTQTVMPGQVMRVTTG 505
Cdd:pfam03453   1 PLLGTEEtvpLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP-IAAGEPPGPLLPGGEAVRIMTG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622950778 506 APIPCGADAVVQVEDTEliresddGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 580
Cdd:pfam03453  80 APLPEGADAVVMVEDTE-------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 12-183 1.60e-47

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 180.01  E-value: 1.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  12 DHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPS--LLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTG 89
Cdd:PLN02699  456 NPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSSSekLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  90 FAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQ 169
Cdd:PLN02699  536 FTPRDVTPE-------------ATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECME 602

                         170
                  ....*....|....
gi 1622950778 170 FILPALPHAIDLLR 183
Cdd:PLN02699  603 ALLPALKHALKQIK 616
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 15-173 2.49e-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: 139.76  E-value: 2.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  15 IRVGVLTVSDSCFRNLAE-------DRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEkeLNLILTTGG 87
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQE---AGFNVVRLGIVPDDPEEIREILRKAVDE--ADVVLTTGG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  88 TGFAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVtplgmLSRP----VCGIRGKTLIINLPGSKKG 163
Cdd:TIGR00177  76 TGVGPRDVTPE-------------ALEELGEKEIPGFGEFRMLSSLPV-----LSRPgkpaTAGVRGGTLIFNLPGNPVS 137

                         170
                  ....*....|.
gi 1622950778 164 SQECFQ-FILP 173
Cdd:TIGR00177 138 ALVTFEvLILP 148
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 590-732 7.50e-35

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: 129.74  E-value: 7.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 590 PVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGE 669
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622950778 670 KDYLKQVLDiDLHAQIHFGR----------VFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVP 732
Cdd:TIGR00177  81 RDVTPEALE-ELGEKEIPGFgefrmlsslpVLSRPGKPATAGVRG----GTLIFNLPGNPVSALVTFEVLILP 148
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 593-729 9.51e-33

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: 123.47  E-value: 9.51e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  593 AVMSTGNELLNPeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVG--DNPDDLLNALNEGISRADVIITSGGVSMGEK 670
Cdd:smart00852   1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622950778  671 DYLKQVLDIDLHAQIHFGRVFMKPGLPTT-----FATLDIDGVRKIIFALPGNPVSAVVTCNLF 729
Cdd:smart00852  75 DLTPEALAELGGRELLGHGVAMRPGGPPGplanlSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 18-171 2.42e-27

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: 107.67  E-value: 2.42e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778   18 GVLTVSDSCFR-NLAEDRSGINLKDLVQDpslLGGTISAYKIV--PDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRD 94
Cdd:smart00852   1 AIISTGDELLSgGQIRDSNGPMLAALLRE---LGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDD 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622950778   95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLnVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFI 171
Cdd:smart00852  76 LTPE-------------ALAELGGRELLGHGVAMRPGGP-PGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 18-177 4.16e-27

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: 107.33  E-value: 4.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  18 GVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRDVTP 97
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  98 EkfptfpfcglqkgATKEVIEREAPGMALAMLMGSL------NVTPLGMLSrpvcgiRGKTLIINLPGSKKGSQECFQ-F 170
Cdd:pfam00994  76 E-------------ALAELGGRELPGFEELFRGVSLkpgkpvGTAPGAILS------RAGKTVFGLPGSPVAAKVMFElL 136


                  ....*..
gi 1622950778 171 ILPALPH 177
Cdd:pfam00994 137 LLPLLRH 143
 
Name Accession Description Interval E-value
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 418-824 1.01e-165

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: 485.85  E-value: 1.01e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 418 DKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTQTV 494
Cdd:cd00887     2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 495 MPGQVMRVTTGAPIPCGADAVVQVEDTELiresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 574
Cdd:cd00887    82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE--------EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 575 LLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 654
Cdd:cd00887   154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 655 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 734
Cdd:cd00887   234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELFVRPAL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 735 RKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEqyvEL 813
Cdd:cd00887   309 RKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---GL 383

                         410
                  ....*....|.
gi 1622950778 814 HKGEVVDVMVI 824
Cdd:cd00887   384 EAGEEVEVLLL 394
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 414-827 1.36e-150

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: 447.23  E-value: 1.36e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 414 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF----IIGESQAGEQ 489
Cdd:COG0303     1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtlrVVGEIAAGSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 490 PTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELiresDDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 569
Cdd:COG0303    81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER----EGDR----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 570 PSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 649
Cdd:COG0303   153 PADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 650 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLF 729
Cdd:COG0303   233 REALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELF 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 730 VVPALRKMQGILDPRPTIIKARLSCDV-KLDPRPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTE 808
Cdd:COG0303   308 VRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLERDDGE--LVVEPLGGQGSGLLSSLAEADGLIVLPEGVE 385

                         410
                  ....*....|....*....
gi 1622950778 809 qyvELHKGEVVDVMVIGRL 827
Cdd:COG0303   386 ---GVEAGEEVEVLLLDGL 401
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 414-804 2.10e-132

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 409.59  E-value: 2.10e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 414 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQ- 492
Cdd:PLN02699    7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGv 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 493 TVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEEleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSE 572
Cdd:PLN02699   87 TLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 573 IGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLP-GKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNE 651
Cdd:PLN02699  165 IGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGrGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 652 GISR-ADVIITSGGVSMGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDI---DGVRKII--FALPGNPVSAVVT 725
Cdd:PLN02699  245 AISSgVDILLTSGGVSMGDRDFVKPLL--EKRGTVYFSKVLMKPGKPLTFAEIDAksaPSNSKKMlaFGLPGNPVSCLVC 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 726 CNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQE----PLPWAQSTGNQMSSRLMSMRSANGL 800
Cdd:PLN02699  323 FNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPvRPEFHRAIIRWKLNDgsgnPGFVAESTGHQMSSRLLSMKSANAL 402


                  ....
gi 1622950778 801 LMLP 804
Cdd:PLN02699  403 LELP 406
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 428-821 2.52e-95

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


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 311.38  E-value: 2.52e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 428 TPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAAD-------GPGDRFIIGESQAGEQPTQTVMPGQVM 500
Cdd:PRK14498   25 ELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADtfgaseaNPVRLKLGGEVHAGEAPDVEVEPGEAV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 501 RVTTGAPIPCGADAVVQVEDTElirESDDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 580
Cdd:PRK14498  105 EIATGAPIPRGADAVVMVEDTE---EVDDDT----VEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 581 VTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVII 660
Cdd:PRK14498  178 VAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVL 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 661 TSGGVSMGEKDYLKQVLDidlhaqiHFGRVF-----MKPGLPTTFATldIDGvrKIIFALPGNPVSAVVTCNLFVVPALR 735
Cdd:PRK14498  258 LSGGTSAGAGDVTYRVIE-------ELGEVLvhgvaIKPGKPTILGV--IGG--KPVVGLPGYPVSALTIFEEFVAPLLR 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 736 KMQGILDPRPTIIKARLScdVKLDP---RPEYHRCILTWHHQEPLPWAQSTGnqmSSRLMSMRSANGLLMLPPKTEQyve 812
Cdd:PRK14498  327 KLAGLPPPERATVKARLA--RRVRSelgREEFVPVSLGRVGDGYVAYPLSRG---SGAITSLVRADGFIEIPANTEG--- 398


                  ....*....
gi 1622950778 813 LHKGEVVDV 821
Cdd:PRK14498  399 LEAGEEVEV 407
PRK14491 PRK14491
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ...
 428-809 5.88e-89

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional


Pssm-ID: 237729 [Multi-domain]  Cd Length: 597  Bit Score: 293.44  E-value: 5.88e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 428 TPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF-IIGESQAGEQPTQTVMPGQVMRVTTGA 506
Cdd:PRK14491  213 TPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESYtLVGEVLAGHQYDGTLQAGEAVRIMTGA 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 507 PIPCGADAVVQVEDTELiresDDGTEELEVRILVqarpGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEV 586
Cdd:PRK14491  293 PVPAGADTVVMRELATQ----DGDKVSFDGGIKA----GQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPV 364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 587 NKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVS 666
Cdd:PRK14491  365 FRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVS 444

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 667 MGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPALRKMQGILDPRPT 746
Cdd:PRK14491  445 VGDADYIKTAL--AKLGQIDFWRINMRPGRPLAFGQIG----DSPFFGLPGNPVAVMVSFLQFVEPALRKLAGEQNWQPL 518

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622950778 747 IIKARLSCDVKLDP-RPEYHRCILTWHHQEPLPwAQSTGNQMSSRLMSMRSANGLLMLPPKTEQ 809
Cdd:PRK14491  519 LFPAIADETLRSRQgRTEFSRGIYHLGADGRLH-VRTTGKQGSGILSSMSEANCLIEIGPAAET 581
PRK10680 PRK10680
molybdopterin biosynthesis protein MoeA; Provisional
 414-803 1.84e-75

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 182643 [Multi-domain]  Cd Length: 411  Bit Score: 251.55  E-value: 1.84e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 414 LTSMDKAFITVL-EMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF--IIGESQAGeQP 490
Cdd:PRK10680    7 LMSLETALTEMLsRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPlpVAGKAFAG-QP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 491 TQTVMP-GQVMRVTTGAPIPCGADAVVQVEDTELireSDDGteeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 569
Cdd:PRK10680   86 FHGEWPaGTCIRIMTGAPVPEGCEAVVMQEQTEQ---TDDG-----VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 570 PSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 649
Cdd:PRK10680  158 TAELPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 650 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLhAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLF 729
Cdd:PRK10680  238 IEADSQADVVISSGGVSVGEADYTKTILE-EL-GEIAFWKLAIKPGKPFAFGKLS----NSWFCGLPGNPVSAALTFYQL 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622950778 730 VVPALRKMQGILDPRPTI-IKARLSCDVKLDP-RPEYHRCILTWHHQEPLPwAQSTGNQMSSRLMSMRSANGLLML 803
Cdd:PRK10680  312 VQPLLAKLSGNTASGLPPrQRVRTASRLKKTPgRLDFQRGILQRNADGELE-VTTTGHQGSHIFSSFSLGNCFIVL 386
PRK14497 PRK14497
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
 426-823 1.20e-67

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


Pssm-ID: 172968 [Multi-domain]  Cd Length: 546  Bit Score: 234.32  E-value: 1.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 426 EMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQTVMPGQVMRVTTG 505
Cdd:PRK14497   23 SLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGEFKVIDKIGIGEFKEIHIKECEAVEVDTG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 506 APIPCGADAVVQVEDTELIresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVE 585
Cdd:PRK14497  103 SMIPMGADAVIKVENTKVI-------NGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVK 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 586 VNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGV 665
Cdd:PRK14497  176 VYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGT 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 666 SMGEKDYLKQVL----DIDLHAqihfgrVFMKPGLPTTFATldIDGvrKIIFALPGNPVSAVVTCNLFVVPALRKMQG-- 739
Cdd:PRK14497  256 SAGEKDFVHQAIrelgNIIVHG------LKIKPGKPTILGI--VDG--KPVIGLPGNIVSTMVVLNMVILEYLKSLYPsr 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 740 --ILDPRPtiIKARLSCDVKLDprpeYHRCIL---------TWHHQEPLPWAqstgnqmSSRLMSMRSANGLLMLPPKTe 808
Cdd:PRK14497  326 keILGLGK--IKARLALRVKAD----EHRNTLipvylfksdNSYYALPVPFD-------SYMVGTFSLTDGYIMLGPNE- 391

                         410
                  ....*....|....*
gi 1622950778 809 qyvELHKGEVVDVMV 823
Cdd:PRK14497  392 ---EIEEGKEVEVDL 403
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 15-182 2.82e-65

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: 214.65  E-value: 2.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRD 94
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPA 174
Cdd:cd00886    78 VTPE-------------ATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPE 144


                  ....*...
gi 1622950778 175 LPHAIDLL 182
Cdd:cd00886   145 LPHLLDLL 152
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 6-183 2.34e-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: 199.19  E-value: 2.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778   6 MILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTT 85
Cdd:COG0521     1 MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE---AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  86 GGTGFAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLN-VTPLGMLSRPVCGIRGKTLIINLPGSKKGS 164
Cdd:COG0521    78 GGTGLSPRDVTPE-------------ATRPLLDKELPGFGELFRALSLEeIGPSAILSRAVAGIRGGTLIFNLPGSPGAV 144

                         170
                  ....*....|....*....
gi 1622950778 165 QECFQFILPALPHAIDLLR 183
Cdd:COG0521   145 REALEAILPELPHAVDLLN 163
MoeA_N pfam03453
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ...
 429-580 4.46e-49

MoeA N-terminal region (domain I and II); This family contains two structural domains. One of these contains the conserved DGXA motif. This region is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this region is uncertain.


Pssm-ID: 460923 [Multi-domain]  Cd Length: 147  Bit Score: 170.05  E-value: 4.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 429 PVLGTEI---INYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGeSQAGEQPTQTVMPGQVMRVTTG 505
Cdd:pfam03453   1 PLLGTEEtvpLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP-IAAGEPPGPLLPGGEAVRIMTG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622950778 506 APIPCGADAVVQVEDTEliresddGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 580
Cdd:pfam03453  80 APLPEGADAVVMVEDTE-------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
PRK14690 PRK14690
molybdopterin biosynthesis protein MoeA; Provisional
 415-804 1.01e-48

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 237789 [Multi-domain]  Cd Length: 419  Bit Score: 178.19  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 415 TSMDKAFITVLE-MTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDR---FIIGESQAGEQP 490
Cdd:PRK14690   23 TPVDTALDLLRArLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQvlpLIEGRAAAGVPF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 491 TQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELiresddGTEELEVRILVQArpGQDIRPIGHDIKRGECVLAKGTHMGP 570
Cdd:PRK14690  103 SGRVPEGMALRILTGAALPEGVDTVVLEEDVAG------DGHRIAFHGPLKM--GANTRKAGEDVIAGDVALPAGRRLTP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 571 SEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALN 650
Cdd:PRK14690  175 ADLALLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLD 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 651 EGISRADVIITSGGVSMGEKDYLKQVLDIDlhAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFV 730
Cdd:PRK14690  255 RAAAEADVILTSGGASAGDEDHVSALLREA--GAMQSWRIALKPGRPLALGLWQ----GVPVFGLPGNPVAALVCTLVFA 328

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622950778 731 VPALRKM--QGILDPRPTIIKARLScDVKLDPRPEYHRCILTWHHQEPLpwaQSTGnqmSSRLMSMRSANGLLMLP 804
Cdd:PRK14690  329 RPAMSLLagEGWSEPQGFTVPAAFE-KRKKPGRREYLRARLRQGHAEVF---RSEG---SGRISGLSWAEGLVELG 397
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 12-183 1.60e-47

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 180.01  E-value: 1.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  12 DHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPS--LLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTG 89
Cdd:PLN02699  456 NPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSSSekLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  90 FAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQ 169
Cdd:PLN02699  536 FTPRDVTPE-------------ATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECME 602

                         170
                  ....*....|....
gi 1622950778 170 FILPALPHAIDLLR 183
Cdd:PLN02699  603 ALLPALKHALKQIK 616
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 592-734 1.95e-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: 147.88  E-value: 1.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 592 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKD 671
Cdd:cd00758     2 VAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRD 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622950778 672 YLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 734
Cdd:cd00758    75 VTPEALAELGEREAHGKGVALAPGSRTAFGIIG----KVLIINLPGSPKSALTTFEALVLPAL 133
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 15-182 4.69e-40

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 146.25  E-value: 4.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  15 IRVGVLTVSDSCFRNLAEDRSGINLKDLvqdpslLGGTISA-----YKIVPDEIEEIKETLIDWCDEKELNLILTTGGTG 89
Cdd:PRK09417    4 LKIGLVSISDRASSGVYEDKGIPALEEW------LASALTSpfeieTRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  90 FAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQ 169
Cdd:PRK09417   78 PARRDVTPE-------------ATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLE 144

                         170       180
                  ....*....|....*....|....*
gi 1622950778 170 F------------ILPALPHAIDLL 182
Cdd:PRK09417  145 GlkdadgnvvvpgIFAAVPYCIDLI 169
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 15-184 1.09e-39

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 149.32  E-value: 1.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCdEKELNLILTTGGTGFAPRD 94
Cdd:PRK03604  156 TSAAVLVLSDSIAAGTKEDRSGKLIVEGLEE---AGFEVSHYTIIPDEPAEIAAAVAAWI-AEGYALIITTGGTGLGPRD 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPA 174
Cdd:PRK03604  232 VTPE-------------ALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPA 298

                         170
                  ....*....|
gi 1622950778 175 LPHAIDLLRD 184
Cdd:PRK03604  299 LFHAFAMVKG 308
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 16-175 1.68e-39

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: 142.48  E-value: 1.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  16 RVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEkeLNLILTTGGTGFAPRDV 95
Cdd:cd00758     1 RVAIVTVSDELSQGQIEDTNGPALEALLED---LGCEVIYAGVVPDDADSIRAALIEASRE--ADLVLTTGGTGVGRRDV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  96 TPEkfptfpfcglqkgATKEVIEREAPGmalamlmgslNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECF-QFILPA 174
Cdd:cd00758    76 TPE-------------ALAELGEREAHG----------KGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFeALVLPA 132


                  .
gi 1622950778 175 L 175
Cdd:cd00758   133 L 133
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 15-173 2.49e-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: 139.76  E-value: 2.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  15 IRVGVLTVSDSCFRNLAE-------DRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEkeLNLILTTGG 87
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQE---AGFNVVRLGIVPDDPEEIREILRKAVDE--ADVVLTTGG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  88 TGFAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVtplgmLSRP----VCGIRGKTLIINLPGSKKG 163
Cdd:TIGR00177  76 TGVGPRDVTPE-------------ALEELGEKEIPGFGEFRMLSSLPV-----LSRPgkpaTAGVRGGTLIFNLPGNPVS 137

                         170
                  ....*....|.
gi 1622950778 164 SQECFQ-FILP 173
Cdd:TIGR00177 138 ALVTFEvLILP 148
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 590-732 7.50e-35

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: 129.74  E-value: 7.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 590 PVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGE 669
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622950778 670 KDYLKQVLDiDLHAQIHFGR----------VFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVP 732
Cdd:TIGR00177  81 RDVTPEALE-ELGEKEIPGFgefrmlsslpVLSRPGKPATAGVRG----GTLIFNLPGNPVSALVTFEVLILP 148
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 593-736 2.84e-33

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: 125.05  E-value: 2.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 593 AVMSTGNELLnpeddllPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDY 672
Cdd:pfam00994   1 AIITTGDELL-------PGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622950778 673 LKQVL------DIDLHAQIhFGRVFMKPGLPTTFATL-DIDGVRKIIFALPGNPVSAVVTCNLFVVPALRK 736
Cdd:pfam00994  74 TPEALaelggrELPGFEEL-FRGVSLKPGKPVGTAPGaILSRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 593-729 9.51e-33

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: 123.47  E-value: 9.51e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  593 AVMSTGNELLNPeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVG--DNPDDLLNALNEGISRADVIITSGGVSMGEK 670
Cdd:smart00852   1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622950778  671 DYLKQVLDIDLHAQIHFGRVFMKPGLPTT-----FATLDIDGVRKIIFALPGNPVSAVVTCNLF 729
Cdd:smart00852  75 DLTPEALAELGGRELLGHGVAMRPGGPPGplanlSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 18-171 2.42e-27

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: 107.67  E-value: 2.42e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778   18 GVLTVSDSCFR-NLAEDRSGINLKDLVQDpslLGGTISAYKIV--PDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRD 94
Cdd:smart00852   1 AIISTGDELLSgGQIRDSNGPMLAALLRE---LGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDD 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622950778   95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLnVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFI 171
Cdd:smart00852  76 LTPE-------------ALAELGGRELLGHGVAMRPGGP-PGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 18-177 4.16e-27

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: 107.33  E-value: 4.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  18 GVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRDVTP 97
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  98 EkfptfpfcglqkgATKEVIEREAPGMALAMLMGSL------NVTPLGMLSrpvcgiRGKTLIINLPGSKKGSQECFQ-F 170
Cdd:pfam00994  76 E-------------ALAELGGRELPGFEELFRGVSLkpgkpvGTAPGAILS------RAGKTVFGLPGSPVAAKVMFElL 136


                  ....*..
gi 1622950778 171 ILPALPH 177
Cdd:pfam00994 137 LLPLLRH 143
MoeA_C pfam03454
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ...
 749-824 1.64e-19

MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this domain is uncertain. The structure of this domain is known and forms an incomplete beta barrel.


Pssm-ID: 460924 [Multi-domain]  Cd Length: 72  Bit Score: 83.04  E-value: 1.64e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622950778 749 KARLSCDVKLDP-RPEYHRCILtwHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVElhkGEVVDVMVI 824
Cdd:pfam03454   1 KARLARDLKSDPgRREFVRVRL--HEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEA---GEEVEVILL 72
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 592-664 3.54e-11

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


Pssm-ID: 440678  Cd Length: 249  Bit Score: 64.36  E-value: 3.54e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622950778 592 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 664
Cdd:COG1058     2 AEIITIGDELLS-------GRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGG 67
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 592-664 6.00e-11

Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.


Pssm-ID: 238450 [Multi-domain]  Cd Length: 170  Bit Score: 61.73  E-value: 6.00e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622950778 592 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 664
Cdd:cd00885     2 AEIIAIGDELLS-------GQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
cinA_nterm TIGR00200
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ...
 600-665 1.08e-06

competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 161761 [Multi-domain]  Cd Length: 413  Bit Score: 51.83  E-value: 1.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622950778 600 ELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGV 665
Cdd:TIGR00200   4 EIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGL 69
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
 594-677 2.62e-06

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 50.56  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 594 VMSTGNELLNpeddllpGKIRDSNRSTL---LATIQ-EHGYPTInlgiVGDNPDDLLNALNEGISRADVIITSGGVSMGE 669
Cdd:PRK00549    5 IIAVGTELLL-------GQIVNTNAQFLsekLAELGiDVYHQTV----VGDNPERLLSALEIAEERSDLIITTGGLGPTK 73


                  ....*...
gi 1622950778 670 KDYLKQVL 677
Cdd:PRK00549   74 DDLTKETV 81
PRK03673 PRK03673
nicotinamide mononucleotide deamidase-related protein YfaY;
592-664 5.34e-06

nicotinamide mononucleotide deamidase-related protein YfaY;


Pssm-ID: 179629 [Multi-domain]  Cd Length: 396  Bit Score: 49.70  E-value: 5.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622950778 592 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 664
Cdd:PRK03673    4 VEMLSTGDEVLH-------GQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGG 69
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 39-190 1.11e-05

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: 48.64  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  39 LKDLVQDpslLGGTISAYKIVPDEIEEIKETL---IDWCDekelnLILTTGGTGFAPRDVtpekfptfpfcglqkgaTKE 115
Cdd:cd00887   200 LAALLRE---LGAEVVDLGIVPDDPEALREALeeaLEEAD-----VVITSGGVSVGDYDF-----------------VKE 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 116 VIEREAPGmalaMLMGSLNVTPlGmlsRPV-CGIRGKTLIINLPG---SkkgSQECF-QFILPALPHAIDLLRDAIVKVK 190
Cdd:cd00887   255 VLEELGGE----VLFHGVAMKP-G---KPLaFGRLGGKPVFGLPGnpvS---ALVTFeLFVRPALRKLQGAPEPEPPRVK 323
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
590-664 7.25e-05

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 45.39  E-value: 7.25e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622950778 590 PVVAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 664
Cdd:PRK01215    4 WFAWIITIGNELLI-------GRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGG 71
PRK03670 PRK03670
competence damage-inducible protein A; Provisional
 600-665 5.12e-04

competence damage-inducible protein A; Provisional


Pssm-ID: 167581  Cd Length: 252  Bit Score: 42.48  E-value: 5.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622950778 600 ELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRA-DVIITSGGV 665
Cdd:PRK03670    4 EIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKpEVLVISGGL 70
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 625-734 7.63e-04

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: 40.87  E-value: 7.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 625 IQEHGYPTINLGIVGDNPDDLLNALNEGISR--ADVIITSGGVSMGEKDY----LKQVLDIDLHAqihFGRVF----MKP 694
Cdd:COG0521    38 LEEAGHEVVARRIVPDDKDAIRAALRELIDDegVDLVLTTGGTGLSPRDVtpeaTRPLLDKELPG---FGELFralsLEE 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622950778 695 GLPTTFATLDIDGVRK--IIFALPGNPvSAVVTCNLFVVPAL 734
Cdd:COG0521   115 IGPSAILSRAVAGIRGgtLIFNLPGSP-GAVREALEAILPEL 155
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 49-175 9.94e-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: 42.38  E-value: 9.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  49 LGGTISAYKIVPDEIEEIKETL---IDWCDekelnLILTTGGTGFAPRDVtpekfptfpfcglqkgaTKEVIEREapGMA 125
Cdd:COG0303   211 AGAEVVDLGIVPDDPEALRAALreaLAEAD-----LVITSGGVSVGDYDL-----------------VKEALEEL--GAE 266

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622950778 126 LamLMGSLNVTPlGmlsRPV-CGIRGKTLIINLPG---SkkgSQECF-QFILPAL 175
Cdd:COG0303   267 V--LFHKVAMKP-G---KPLaFGRLGGKPVFGLPGnpvS---ALVTFeLFVRPAL 312
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
 16-150 2.18e-03

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: 40.99  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778  16 RVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELnLILTTGGTGFAPRDV 95
Cdd:cd03522   161 RVGLIVTGSEVYGGRIEDKFGPVLRARLAA---LGVELVEQVIVPHDEAAIAAAIAEALEAGAE-LLILTGGASVDPDDV 236

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622950778  96 TPekfptfpfCGLqKGATKEVIEREAPGMALAMLMgslnvtpLGML-SRPVCGIRG 150
Cdd:cd03522   237 TP--------AAI-RAAGGEVIRYGMPVDPGNLLL-------LGYLgGVPVIGLPG 276
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 611-734 9.13e-03

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 39.15  E-value: 9.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622950778 611 GKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISR-ADVIITSGGVSMGEKDY----LKQVLDIDLHAQI 685
Cdd:PRK03604  170 GTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAEgYALIITTGGTGLGPRDVtpeaLAPLLERRLPGIA 249

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622950778 686 HFGRVFMKPGLPTTFATLDIDGV--RKIIFALPGNPvSAVVTCNLFVVPAL 734
Cdd:PRK03604  250 EALRSWGQGRTPTAMLSRLVAGMigNSLVVALPGSP-GGASDALAVLLPAL 299
 
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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