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Conserved domains on  [gi|1041090164|ref|XP_017267468|]
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gephyrin b isoform X3 [Kryptolebias marmoratus]

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 ...
 433-840 9.96e-162

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: 475.83  E-value: 9.96e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 433 DKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTHTV 509
Cdd:cd00887     2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 510 MPGQVMRVTTGAPIPCGADAVVQVEDTELlresEDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 589
Cdd:cd00887    82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE----EGGR----VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 590 LLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 669
Cdd:cd00887   154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 670 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIPA 749
Cdd:cd00887   234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPG-NPVSALVTFELFVRPA 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 750 LRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQVSSRLMSMRSANGLLMLPPKTEqyvE 828
Cdd:cd00887   308 LRKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---G 382

                         410
                  ....*....|..
gi 1041090164 829 LHKGEVVDVMVI 840
Cdd:cd00887   383 LEAGEEVEVLLL 394
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 77-231 8.50e-66

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: 216.19  E-value: 8.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  77 IRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTTGGTGFAPRD 156
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041090164 157 VTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLL 231
Cdd:cd00886    78 VTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
 
Name Accession Description Interval E-value
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 433-840 9.96e-162

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: 475.83  E-value: 9.96e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 433 DKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTHTV 509
Cdd:cd00887     2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 510 MPGQVMRVTTGAPIPCGADAVVQVEDTELlresEDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 589
Cdd:cd00887    82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE----EGGR----VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 590 LLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 669
Cdd:cd00887   154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 670 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIPA 749
Cdd:cd00887   234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPG-NPVSALVTFELFVRPA 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 750 LRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQVSSRLMSMRSANGLLMLPPKTEqyvE 828
Cdd:cd00887   308 LRKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---G 382

                         410
                  ....*....|..
gi 1041090164 829 LHKGEVVDVMVI 840
Cdd:cd00887   383 LEAGEEVEVLLL 394
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 429-843 2.92e-146

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: 436.44  E-value: 2.92e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 429 LTSMDKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF----IIGESQAGEQ 504
Cdd:COG0303     1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtlrVVGEIAAGSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 505 PTHTVMPGQVMRVTTGAPIPCGADAVVQVEDTELlresEDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 584
Cdd:COG0303    81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER----EGDR----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 585 PSEIGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 664
Cdd:COG0303   153 PADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 665 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNL 744
Cdd:COG0303   233 REALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRLG----GKPVFGLPG-NPVSALVTFEL 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 745 FVIPALRKMQGILDPRPTIIKARLSCDV-KLDPRPEYHRCILTWHHQEplPWAQSTGNQVSSRLMSMRSANGLLMLPPKT 823
Cdd:COG0303   307 FVRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLERDDGE--LVVEPLGGQGSGLLSSLAEADGLIVLPEGV 384

                         410       420
                  ....*....|....*....|
gi 1041090164 824 EqyvELHKGEVVDVMVIGRL 843
Cdd:COG0303   385 E---GVEAGEEVEVLLLDGL 401
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 429-820 1.94e-128

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 399.57  E-value: 1.94e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 429 LTSMDKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTH- 507
Cdd:PLN02699    7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGv 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 508 TVMPGQVMRVTTGAPIPCGADAVVQVEDTELLRESEDGTEEleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSE 587
Cdd:PLN02699   87 TLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 588 IGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDD-LHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNE 666
Cdd:PLN02699  165 IGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 667 GISR-ADVIITSGGVSMGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDIDGARK-----LIFALPGrNPVSAVV 740
Cdd:PLN02699  245 AISSgVDILLTSGGVSMGDRDFVKPLL--EKRGTVYFSKVLMKPGKPLTFAEIDAKSAPSnskkmLAFGLPG-NPVSCLV 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 741 TCNLFVIPALRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQE----PLPWAQSTGNQVSSRLMSMRSANG 815
Cdd:PLN02699  322 CFNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPvRPEFHRAIIRWKLNDgsgnPGFVAESTGHQMSSRLLSMKSANA 401


                  ....*
gi 1041090164 816 LLMLP 820
Cdd:PLN02699  402 LLELP 406
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 77-231 8.50e-66

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: 216.19  E-value: 8.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  77 IRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTTGGTGFAPRD 156
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041090164 157 VTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLL 231
Cdd:cd00886    78 VTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 68-232 4.91e-60

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: 201.11  E-value: 4.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  68 MILTNHDHQIRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTT 147
Cdd:COG0521     1 MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE---AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 148 GGTGFAPRDVTPEATKEVIEREAPGMSLAMLMGSLN-VTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPH 226
Cdd:COG0521    78 GGTGLSPRDVTPEATRPLLDKELPGFGELFRALSLEeIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPH 157


                  ....*.
gi 1041090164 227 AIDLLR 232
Cdd:COG0521   158 AVDLLN 163
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 74-232 7.47e-49

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 183.86  E-value: 7.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  74 DHQIRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDPS--LLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTTGGTG 151
Cdd:PLN02699  456 NPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSSSekLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 152 FAPRDVTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLL 231
Cdd:PLN02699  536 FTPRDVTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALKQI 615


                  .
gi 1041090164 232 R 232
Cdd:PLN02699  616 K 616
MoeA_N pfam03453
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ...
 451-595 1.31e-47

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: 165.82  E-value: 1.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 451 INYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGeSQAGEQPTHTVMPGQVMRVTTGAPIPCGADAV 530
Cdd:pfam03453  11 LEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP-IAAGEPPGPLLPGGEAVRIMTGAPLPEGADAV 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041090164 531 VQVEDTEllresedGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 595
Cdd:pfam03453  90 VMVEDTE-------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 77-222 5.99e-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: 138.60  E-value: 5.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  77 IRVGVLTVSDSCFRNLAE-------DRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEkeLNLILTTGG 149
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQE---AGFNVVRLGIVPDDPEEIREILRKAVDE--ADVVLTTGG 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041090164 150 TGFAPRDVTPEATKEVIEREAPGMSLAMLMGSLNVtplgmLSRP----VCGIRGKTLIINLPGSKKGSQECFQ-FILP 222
Cdd:TIGR00177  76 TGVGPRDVTPEALEELGEKEIPGFGEFRMLSSLPV-----LSRPgkpaTAGVRGGTLIFNLPGNPVSALVTFEvLILP 148
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 605-748 1.60e-33

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: 125.89  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 605 PVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGE 684
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041090164 685 KDYLKQVLDiDLHAQIHFGR----------VFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIP 748
Cdd:TIGR00177  81 RDVTPEALE-ELGEKEIPGFgefrmlsslpVLSRPGKPATAGVRG----GTLIFNLPG-NPVSALVTFEVLILP 148
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 608-745 2.67e-30

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: 116.53  E-value: 2.67e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  608 AVMSTGNELLNPeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVG--DNPDDLLNALNEGISRADVIITSGGVSMGEK 685
Cdd:smart00852   1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041090164  686 DYLKQVLDIDLHAQIHFGRVFMKPGLPTT-----FATLDIDGARKLIFALPGrNPVSAVVTCNLF 745
Cdd:smart00852  75 DLTPEALAELGGRELLGHGVAMRPGGPPGplanlSGTAPGVRGKKPVFGLPG-NPVAALVMFEEL 138
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 80-220 1.03e-28

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: 111.91  E-value: 1.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164   80 GVLTVSDSCFR-NLAEDRSGVNLKDLVHDpslLGGMIAAYKIV--PDEIDEIKETLVHWCDEKELnlILTTGGTGFAPRD 156
Cdd:smart00852   1 AIISTGDELLSgGQIRDSNGPMLAALLRE---LGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDD 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041090164  157 VTPEATKEVIEREAPGMSLAMLMGSLnVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFI 220
Cdd:smart00852  76 LTPEALAELGGRELLGHGVAMRPGGP-PGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 80-226 3.74e-28

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: 110.42  E-value: 3.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  80 GVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELnlILTTGGTGFAPRDVTP 159
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041090164 160 EATKEVIEREAPGMSLAMLMGSL------NVTPLGMLSrpvcgiRGKTLIINLPGSKKGSQECFQ-FILPALPH 226
Cdd:pfam00994  76 EALAELGGRELPGFEELFRGVSLkpgkpvGTAPGAILS------RAGKTVFGLPGSPVAAKVMFElLLLPLLRH 143
 
Name Accession Description Interval E-value
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 433-840 9.96e-162

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: 475.83  E-value: 9.96e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 433 DKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTHTV 509
Cdd:cd00887     2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 510 MPGQVMRVTTGAPIPCGADAVVQVEDTELlresEDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 589
Cdd:cd00887    82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE----EGGR----VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 590 LLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 669
Cdd:cd00887   154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 670 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIPA 749
Cdd:cd00887   234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPG-NPVSALVTFELFVRPA 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 750 LRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQVSSRLMSMRSANGLLMLPPKTEqyvE 828
Cdd:cd00887   308 LRKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---G 382

                         410
                  ....*....|..
gi 1041090164 829 LHKGEVVDVMVI 840
Cdd:cd00887   383 LEAGEEVEVLLL 394
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 429-843 2.92e-146

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: 436.44  E-value: 2.92e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 429 LTSMDKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF----IIGESQAGEQ 504
Cdd:COG0303     1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtlrVVGEIAAGSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 505 PTHTVMPGQVMRVTTGAPIPCGADAVVQVEDTELlresEDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 584
Cdd:COG0303    81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER----EGDR----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 585 PSEIGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 664
Cdd:COG0303   153 PADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 665 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNL 744
Cdd:COG0303   233 REALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRLG----GKPVFGLPG-NPVSALVTFEL 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 745 FVIPALRKMQGILDPRPTIIKARLSCDV-KLDPRPEYHRCILTWHHQEplPWAQSTGNQVSSRLMSMRSANGLLMLPPKT 823
Cdd:COG0303   307 FVRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLERDDGE--LVVEPLGGQGSGLLSSLAEADGLIVLPEGV 384

                         410       420
                  ....*....|....*....|
gi 1041090164 824 EqyvELHKGEVVDVMVIGRL 843
Cdd:COG0303   385 E---GVEAGEEVEVLLLDGL 401
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 429-820 1.94e-128

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 399.57  E-value: 1.94e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 429 LTSMDKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTH- 507
Cdd:PLN02699    7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGv 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 508 TVMPGQVMRVTTGAPIPCGADAVVQVEDTELLRESEDGTEEleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSE 587
Cdd:PLN02699   87 TLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 588 IGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDD-LHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNE 666
Cdd:PLN02699  165 IGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 667 GISR-ADVIITSGGVSMGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDIDGARK-----LIFALPGrNPVSAVV 740
Cdd:PLN02699  245 AISSgVDILLTSGGVSMGDRDFVKPLL--EKRGTVYFSKVLMKPGKPLTFAEIDAKSAPSnskkmLAFGLPG-NPVSCLV 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 741 TCNLFVIPALRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQE----PLPWAQSTGNQVSSRLMSMRSANG 815
Cdd:PLN02699  322 CFNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPvRPEFHRAIIRWKLNDgsgnPGFVAESTGHQMSSRLLSMKSANA 401


                  ....*
gi 1041090164 816 LLMLP 820
Cdd:PLN02699  402 LLELP 406
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 446-837 1.93e-92

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


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 304.06  E-value: 1.93e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 446 LGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAAD-------GPGDRFIIGESQAGEQPTHTVMPGQVMRVT 518
Cdd:PRK14498   28 LGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADtfgaseaNPVRLKLGGEVHAGEAPDVEVEPGEAVEIA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 519 TGAPIPCGADAVVQVEDTEllrESEDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTE 598
Cdd:PRK14498  108 TGAPIPRGADAVVMVEDTE---EVDDDT----VEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGGVAE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 599 VEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSG 678
Cdd:PRK14498  181 VPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVLLSG 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 679 GVSMGEKDYLKQVLDidlhaqiHFGRVF-----MKPGLPTTFATldIDGarKLIFALPGrNPVSAVVTCNLFVIPALRKM 753
Cdd:PRK14498  261 GTSAGAGDVTYRVIE-------ELGEVLvhgvaIKPGKPTILGV--IGG--KPVVGLPG-YPVSALTIFEEFVAPLLRKL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 754 QGILDPRPTIIKARLScdVKLDP---RPEYHRCILTWHHQEPLPWAQSTGnqvSSRLMSMRSANGLLMLPPKTEQyveLH 830
Cdd:PRK14498  329 AGLPPPERATVKARLA--RRVRSelgREEFVPVSLGRVGDGYVAYPLSRG---SGAITSLVRADGFIEIPANTEG---LE 400


                  ....*..
gi 1041090164 831 KGEVVDV 837
Cdd:PRK14498  401 AGEEVEV 407
PRK14491 PRK14491
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ...
 443-825 1.10e-85

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


Pssm-ID: 237729 [Multi-domain]  Cd Length: 597  Bit Score: 284.97  E-value: 1.10e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 443 TVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF-IIGESQAGEQPTHTVMPGQVMRVTTGA 521
Cdd:PRK14491  213 TPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESYtLVGEVLAGHQYDGTLQAGEAVRIMTGA 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 522 PIPCGADAVVQVEDTELlresEDGTEELEVRILVqarpGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEV 601
Cdd:PRK14491  293 PVPAGADTVVMRELATQ----DGDKVSFDGGIKA----GQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPV 364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 602 QKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVS 681
Cdd:PRK14491  365 FRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVS 444

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 682 MGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIPALRKMQGILDPRP 761
Cdd:PRK14491  445 VGDADYIKTAL--AKLGQIDFWRINMRPGRPLAFGQIG----DSPFFGLPG-NPVAVMVSFLQFVEPALRKLAGEQNWQP 517

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041090164 762 TIIKARLSCDVKLDP-RPEYHRCILTWHHQEPLPwAQSTGNQVSSRLMSMRSANGLLMLPPKTEQ 825
Cdd:PRK14491  518 LLFPAIADETLRSRQgRTEFSRGIYHLGADGRLH-VRTTGKQGSGILSSMSEANCLIEIGPAAET 581
PRK10680 PRK10680
molybdopterin biosynthesis protein MoeA; Provisional
 429-819 5.09e-72

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 182643 [Multi-domain]  Cd Length: 411  Bit Score: 242.30  E-value: 5.09e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 429 LTSMDKAFITVLEMTVVL-GTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF--IIGESQAGeQP 505
Cdd:PRK10680    7 LMSLETALTEMLSRVTPLtATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPlpVAGKAFAG-QP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 506 THTVMP-GQVMRVTTGAPIPCGADAVVQVEDTELlreSEDGteeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 584
Cdd:PRK10680   86 FHGEWPaGTCIRIMTGAPVPEGCEAVVMQEQTEQ---TDDG-----VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 585 PSEIGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 664
Cdd:PRK10680  158 TAELPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 665 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLhAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNL 744
Cdd:PRK10680  238 IEADSQADVVISSGGVSVGEADYTKTILE-EL-GEIAFWKLAIKPGKPFAFGKLS----NSWFCGLPG-NPVSAALTFYQ 310

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041090164 745 FVIPALRKMQGILDPRPTI-IKARLSCDVKLDP-RPEYHRCILTWHHQEPLPwAQSTGNQVSSRLMSMRSANGLLML 819
Cdd:PRK10680  311 LVQPLLAKLSGNTASGLPPrQRVRTASRLKKTPgRLDFQRGILQRNADGELE-VTTTGHQGSHIFSSFSLGNCFIVL 386
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 77-231 8.50e-66

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: 216.19  E-value: 8.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  77 IRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTTGGTGFAPRD 156
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041090164 157 VTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLL 231
Cdd:cd00886    78 VTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
PRK14497 PRK14497
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
 441-839 9.38e-66

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


Pssm-ID: 172968 [Multi-domain]  Cd Length: 546  Bit Score: 229.31  E-value: 9.38e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 441 EMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTHTVMPGQVMRVTTG 520
Cdd:PRK14497   23 SLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGEFKVIDKIGIGEFKEIHIKECEAVEVDTG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 521 APIPCGADAVVQVEDTELLresedgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVE 600
Cdd:PRK14497  103 SMIPMGADAVIKVENTKVI-------NGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVK 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 601 VQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGV 680
Cdd:PRK14497  176 VYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGT 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 681 SMGEKDYLKQVL----DIDLHAqihfgrVFMKPGLPTTFATldIDGarKLIFALPGrNPVSAVVTCNLFVIPALRKMQG- 755
Cdd:PRK14497  256 SAGEKDFVHQAIrelgNIIVHG------LKIKPGKPTILGI--VDG--KPVIGLPG-NIVSTMVVLNMVILEYLKSLYPs 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 756 ---ILDPRPtiIKARLSCDVKLDprpeYHRCIL---------TWHHQEPLPWAqstgnqvSSRLMSMRSANGLLMLPPKT 823
Cdd:PRK14497  325 rkeILGLGK--IKARLALRVKAD----EHRNTLipvylfksdNSYYALPVPFD-------SYMVGTFSLTDGYIMLGPNE 391

                         410
                  ....*....|....*.
gi 1041090164 824 eqyvELHKGEVVDVMV 839
Cdd:PRK14497  392 ----EIEEGKEVEVDL 403
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 68-232 4.91e-60

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: 201.11  E-value: 4.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  68 MILTNHDHQIRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTT 147
Cdd:COG0521     1 MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE---AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 148 GGTGFAPRDVTPEATKEVIEREAPGMSLAMLMGSLN-VTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPH 226
Cdd:COG0521    78 GGTGLSPRDVTPEATRPLLDKELPGFGELFRALSLEeIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPH 157


                  ....*.
gi 1041090164 227 AIDLLR 232
Cdd:COG0521   158 AVDLLN 163
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 74-232 7.47e-49

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 183.86  E-value: 7.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  74 DHQIRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDPS--LLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTTGGTG 151
Cdd:PLN02699  456 NPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSSSekLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 152 FAPRDVTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLL 231
Cdd:PLN02699  536 FTPRDVTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALKQI 615


                  .
gi 1041090164 232 R 232
Cdd:PLN02699  616 K 616
MoeA_N pfam03453
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ...
 451-595 1.31e-47

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: 165.82  E-value: 1.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 451 INYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGeSQAGEQPTHTVMPGQVMRVTTGAPIPCGADAV 530
Cdd:pfam03453  11 LEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP-IAAGEPPGPLLPGGEAVRIMTGAPLPEGADAV 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041090164 531 VQVEDTEllresedGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 595
Cdd:pfam03453  90 VMVEDTE-------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
PRK14690 PRK14690
molybdopterin biosynthesis protein MoeA; Provisional
 445-820 2.19e-45

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 237789 [Multi-domain]  Cd Length: 419  Bit Score: 168.56  E-value: 2.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 445 VLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDR---FIIGESQAGEQPTHTVMPGQVMRVTTGA 521
Cdd:PRK14690   39 VTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQvlpLIEGRAAAGVPFSGRVPEGMALRILTGA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 522 PIPCGADAVVQVEDTELlresedGTEELEVRILVQArpGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEV 601
Cdd:PRK14690  119 ALPEGVDTVVLEEDVAG------DGHRIAFHGPLKM--GANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSV 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 602 QKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVS 681
Cdd:PRK14690  191 RRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGAS 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 682 MGEKDYLKQVLDIDlhAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIPALRKM--QGILDP 759
Cdd:PRK14690  271 AGDEDHVSALLREA--GAMQSWRIALKPGRPLALGLWQ----GVPVFGLPG-NPVAALVCTLVFARPAMSLLagEGWSEP 343

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1041090164 760 RPTIIKARLSCDvKLDPRPEYHRCILTWHHQEPLpwaQSTGnqvSSRLMSMRSANGLLMLP 820
Cdd:PRK14690  344 QGFTVPAAFEKR-KKPGRREYLRARLRQGHAEVF---RSEG---SGRISGLSWAEGLVELG 397
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 77-238 7.39e-43

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 154.34  E-value: 7.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  77 IRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpSLLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTTGGTGFAPRD 156
Cdd:PRK09417    4 LKIGLVSISDRASSGVYEDKGIPALEEWLAS-ALTSPFEIETRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTGPARRD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 157 VTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQF------------ILPAL 224
Cdd:PRK09417   83 VTPEATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLEGlkdadgnvvvpgIFAAV 162

                         170       180
                  ....*....|....*....|.
gi 1041090164 225 PHAIDLL-------RDAVVKV 238
Cdd:PRK09417  163 PYCIDLIggpyietNPEVVKA 183
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 607-750 3.84e-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: 141.33  E-value: 3.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 607 VAVMSTGNELLNpeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKD 686
Cdd:cd00758     2 VAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRD 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041090164 687 YLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIPAL 750
Cdd:cd00758    75 VTPEALAELGEREAHGKGVALAPGSRTAFGIIG----KVLIINLPG-SPKSALTTFEALVLPAL 133
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 77-233 5.73e-39

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 147.01  E-value: 5.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  77 IRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCdEKELNLILTTGGTGFAPRD 156
Cdd:PRK03604  156 TSAAVLVLSDSIAAGTKEDRSGKLIVEGLEE---AGFEVSHYTIIPDEPAEIAAAVAAWI-AEGYALIITTGGTGLGPRD 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041090164 157 VTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLLRD 233
Cdd:PRK03604  232 VTPEALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPALFHAFAMVKG 308
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 78-224 6.50e-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: 140.94  E-value: 6.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  78 RVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEkeLNLILTTGGTGFAPRDV 157
Cdd:cd00758     1 RVAIVTVSDELSQGQIEDTNGPALEALLED---LGCEVIYAGVVPDDADSIRAALIEASRE--ADLVLTTGGTGVGRRDV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041090164 158 TPEATKEVIEREAPGmslamlmgslNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECF-QFILPAL 224
Cdd:cd00758    76 TPEALAELGEREAHG----------KGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFeALVLPAL 133
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 77-222 5.99e-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: 138.60  E-value: 5.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  77 IRVGVLTVSDSCFRNLAE-------DRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEkeLNLILTTGG 149
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQE---AGFNVVRLGIVPDDPEEIREILRKAVDE--ADVVLTTGG 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041090164 150 TGFAPRDVTPEATKEVIEREAPGMSLAMLMGSLNVtplgmLSRP----VCGIRGKTLIINLPGSKKGSQECFQ-FILP 222
Cdd:TIGR00177  76 TGVGPRDVTPEALEELGEKEIPGFGEFRMLSSLPV-----LSRPgkpaTAGVRGGTLIFNLPGNPVSALVTFEvLILP 148
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 605-748 1.60e-33

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: 125.89  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 605 PVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGE 684
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041090164 685 KDYLKQVLDiDLHAQIHFGR----------VFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIP 748
Cdd:TIGR00177  81 RDVTPEALE-ELGEKEIPGFgefrmlsslpVLSRPGKPATAGVRG----GTLIFNLPG-NPVSALVTFEVLILP 148
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 608-752 9.43e-32

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: 120.82  E-value: 9.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 608 AVMSTGNELLnpeddlhPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDY 687
Cdd:pfam00994   1 AIITTGDELL-------PGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1041090164 688 LKQVL------DIDLHAQIhFGRVFMKPGLPTTFATL-DIDGARKLIFALPGrNPVSAVVTCNLFVIPALRK 752
Cdd:pfam00994  74 TPEALaelggrELPGFEEL-FRGVSLKPGKPVGTAPGaILSRAGKTVFGLPG-SPVAAKVMFELLLLPLLRH 143
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 608-745 2.67e-30

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: 116.53  E-value: 2.67e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  608 AVMSTGNELLNPeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVG--DNPDDLLNALNEGISRADVIITSGGVSMGEK 685
Cdd:smart00852   1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041090164  686 DYLKQVLDIDLHAQIHFGRVFMKPGLPTT-----FATLDIDGARKLIFALPGrNPVSAVVTCNLF 745
Cdd:smart00852  75 DLTPEALAELGGRELLGHGVAMRPGGPPGplanlSGTAPGVRGKKPVFGLPG-NPVAALVMFEEL 138
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 80-220 1.03e-28

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: 111.91  E-value: 1.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164   80 GVLTVSDSCFR-NLAEDRSGVNLKDLVHDpslLGGMIAAYKIV--PDEIDEIKETLVHWCDEKELnlILTTGGTGFAPRD 156
Cdd:smart00852   1 AIISTGDELLSgGQIRDSNGPMLAALLRE---LGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDD 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041090164  157 VTPEATKEVIEREAPGMSLAMLMGSLnVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFI 220
Cdd:smart00852  76 LTPEALAELGGRELLGHGVAMRPGGP-PGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 80-226 3.74e-28

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: 110.42  E-value: 3.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  80 GVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELnlILTTGGTGFAPRDVTP 159
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041090164 160 EATKEVIEREAPGMSLAMLMGSL------NVTPLGMLSrpvcgiRGKTLIINLPGSKKGSQECFQ-FILPALPH 226
Cdd:pfam00994  76 EALAELGGRELPGFEELFRGVSLkpgkpvGTAPGAILS------RAGKTVFGLPGSPVAAKVMFElLLLPLLRH 143
MoeA_C pfam03454
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ...
 765-840 2.77e-18

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: 79.58  E-value: 2.77e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041090164 765 KARLSCDVKLDP-RPEYHRCILtwHHQEPLPWAQSTGNQVSSRLMSMRSANGLLMLPPKTEQYVElhkGEVVDVMVI 840
Cdd:pfam03454   1 KARLARDLKSDPgRREFVRVRL--HEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEA---GEEVEVILL 72
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 607-679 5.66e-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: 63.59  E-value: 5.66e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1041090164 607 VAVMSTGNELLNpeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 679
Cdd:COG1058     2 AEIITIGDELLS-------GRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGG 67
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 607-679 7.94e-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: 61.35  E-value: 7.94e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1041090164 607 VAVMSTGNELLNpeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 679
Cdd:cd00885     2 AEIIAIGDELLS-------GQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
cinA_nterm TIGR00200
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ...
 607-680 2.29e-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: 51.06  E-value: 2.29e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041090164 607 VAVMSTGNELLNpeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGV 680
Cdd:TIGR00200   3 AEIISVGDELLL-------GQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGL 69
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
 609-692 3.36e-06

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 50.17  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 609 VMSTGNELLNpeddlhpGKIRDSNRSTL---LATIQ-EHGYPTInlgiVGDNPDDLLNALNEGISRADVIITSGGVSMGE 684
Cdd:PRK00549    5 IIAVGTELLL-------GQIVNTNAQFLsekLAELGiDVYHQTV----VGDNPERLLSALEIAEERSDLIITTGGLGPTK 73


                  ....*...
gi 1041090164 685 KDYLKQVL 692
Cdd:PRK00549   74 DDLTKETV 81
PRK03673 PRK03673
nicotinamide mononucleotide deamidase-related protein YfaY;
607-679 8.23e-06

nicotinamide mononucleotide deamidase-related protein YfaY;


Pssm-ID: 179629 [Multi-domain]  Cd Length: 396  Bit Score: 48.93  E-value: 8.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1041090164 607 VAVMSTGNELLNpeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 679
Cdd:PRK03673    4 VEMLSTGDEVLH-------GQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGG 69
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 111-224 1.05e-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: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 111 LGGMIAAYKIVPDEIDEIKETL---VHWCDekelnLILTTGGTGFAPRDVtpeaTKEVIEREAPGmslaMLMGSLNVTPl 187
Cdd:cd00887   207 LGAEVVDLGIVPDDPEALREALeeaLEEAD-----VVITSGGVSVGDYDF----VKEVLEELGGE----VLFHGVAMKP- 272

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1041090164 188 GmlsRPV-CGIRGKTLIINLPGSKKGSQECF-QFILPAL 224
Cdd:cd00887   273 G---KPLaFGRLGGKPVFGLPGNPVSALVTFeLFVRPAL 308
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
605-679 7.62e-05

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 45.39  E-value: 7.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1041090164 605 PVVAVMSTGNELLNpeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 679
Cdd:PRK01215    4 WFAWIITIGNELLI-------GRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGG 71
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
 78-199 1.04e-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: 45.23  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164  78 RVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELnLILTTGGTGFAPRDV 157
Cdd:cd03522   161 RVGLIVTGSEVYGGRIEDKFGPVLRARLAA---LGVELVEQVIVPHDEAAIAAAIAEALEAGAE-LLILTGGASVDPDDV 236

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1041090164 158 TPEATK----EVIEREAPGMSLAMLMgslnvtpLGML-SRPVCGIRG 199
Cdd:cd03522   237 TPAAIRaaggEVIRYGMPVDPGNLLL-------LGYLgGVPVIGLPG 276
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 111-224 1.29e-03

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: 42.00  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041090164 111 LGGMIAAYKIVPDEIDEIKETL---VHWCDekelnLILTTGGTGFAPRDVtpeaTKEVIEREapGMSLamLMGSLNVTPl 187
Cdd:COG0303   211 AGAEVVDLGIVPDDPEALRAALreaLAEAD-----LVITSGGVSVGDYDL----VKEALEEL--GAEV--LFHKVAMKP- 276

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1041090164 188 GmlsRPV-CGIRGKTLIINLPG---SkkgSQECF-QFILPAL 224
Cdd:COG0303   277 G---KPLaFGRLGGKPVFGLPGnpvS---ALVTFeLFVRPAL 312
PRK03670 PRK03670
competence damage-inducible protein A; Provisional
 615-680 6.16e-03

competence damage-inducible protein A; Provisional


Pssm-ID: 167581  Cd Length: 252  Bit Score: 39.40  E-value: 6.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1041090164 615 ELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRA-DVIITSGGV 680
Cdd:PRK03670    4 EIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKpEVLVISGGL 70
 
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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