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Conserved domains on  [gi|1386827315|ref|XP_024860792|]
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gephyrin b isoform X5 [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 ...
 414-821 1.39e-161

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: 475.06  E-value: 1.39e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 414 DKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTHTV 490
Cdd:cd00887     2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 491 MPGQVMRVTTGAPIPCGADAVVQVEDTELlresEDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 570
Cdd:cd00887    82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE----EGGR----VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 571 LLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 650
Cdd:cd00887   154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 651 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIPA 730
Cdd:cd00887   234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPG-NPVSALVTFELFVRPA 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 731 LRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQVSSRLMSMRSANGLLMLPPKTEqyvE 809
Cdd:cd00887   308 LRKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---G 382

                         410
                  ....*....|..
gi 1386827315 810 LHKGEVVDVMVI 821
Cdd:cd00887   383 LEAGEEVEVLLL 394
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 77-231 8.89e-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: 215.80  E-value: 8.89e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  77 IRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTTGGTGFAPRD 156
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386827315 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 ...
 414-821 1.39e-161

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: 475.06  E-value: 1.39e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 414 DKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTHTV 490
Cdd:cd00887     2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 491 MPGQVMRVTTGAPIPCGADAVVQVEDTELlresEDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 570
Cdd:cd00887    82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE----EGGR----VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 571 LLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 650
Cdd:cd00887   154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 651 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIPA 730
Cdd:cd00887   234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPG-NPVSALVTFELFVRPA 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 731 LRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQVSSRLMSMRSANGLLMLPPKTEqyvE 809
Cdd:cd00887   308 LRKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---G 382

                         410
                  ....*....|..
gi 1386827315 810 LHKGEVVDVMVI 821
Cdd:cd00887   383 LEAGEEVEVLLL 394
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 410-824 3.38e-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: 435.67  E-value: 3.38e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 410 LTSMDKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF----IIGESQAGEQ 485
Cdd:COG0303     1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtlrVVGEIAAGSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 486 PTHTVMPGQVMRVTTGAPIPCGADAVVQVEDTELlresEDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 565
Cdd:COG0303    81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER----EGDR----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 566 PSEIGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 645
Cdd:COG0303   153 PADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 646 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNL 725
Cdd:COG0303   233 REALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRLG----GKPVFGLPG-NPVSALVTFEL 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 726 FVIPALRKMQGILDPRPTIIKARLSCDV-KLDPRPEYHRCILTWHHQEplPWAQSTGNQVSSRLMSMRSANGLLMLPPKT 804
Cdd:COG0303   307 FVRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLERDDGE--LVVEPLGGQGSGLLSSLAEADGLIVLPEGV 384

                         410       420
                  ....*....|....*....|
gi 1386827315 805 EqyvELHKGEVVDVMVIGRL 824
Cdd:COG0303   385 E---GVEAGEEVEVLLLDGL 401
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 410-801 2.48e-128

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 398.80  E-value: 2.48e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 410 LTSMDKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTH- 488
Cdd:PLN02699    7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGv 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 489 TVMPGQVMRVTTGAPIPCGADAVVQVEDTELLRESEDGTEEleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSE 568
Cdd:PLN02699   87 TLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 569 IGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDD-LHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNE 647
Cdd:PLN02699  165 IGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 648 GISR-ADVIITSGGVSMGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDIDGARK-----LIFALPGrNPVSAVV 721
Cdd:PLN02699  245 AISSgVDILLTSGGVSMGDRDFVKPLL--EKRGTVYFSKVLMKPGKPLTFAEIDAKSAPSnskkmLAFGLPG-NPVSCLV 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 722 TCNLFVIPALRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQE----PLPWAQSTGNQVSSRLMSMRSANG 796
Cdd:PLN02699  322 CFNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPvRPEFHRAIIRWKLNDgsgnPGFVAESTGHQMSSRLLSMKSANA 401


                  ....*
gi 1386827315 797 LLMLP 801
Cdd:PLN02699  402 LLELP 406
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 77-231 8.89e-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: 215.80  E-value: 8.89e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  77 IRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTTGGTGFAPRD 156
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386827315 157 VTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLL 231
Cdd:cd00886    78 VTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 68-232 4.81e-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: 200.73  E-value: 4.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  68 MILTNHDHQIRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTT 147
Cdd:COG0521     1 MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE---AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 148 GGTGFAPRDVTPEATKEVIEREAPGMSLAMLMGSLN-VTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPH 226
Cdd:COG0521    78 GGTGLSPRDVTPEATRPLLDKELPGFGELFRALSLEeIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPH 157


                  ....*.
gi 1386827315 227 AIDLLR 232
Cdd:COG0521   158 AVDLLN 163
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 74-232 8.61e-49

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 183.47  E-value: 8.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  74 DHQIRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDPS--LLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTTGGTG 151
Cdd:PLN02699  456 NPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSSSekLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 152 FAPRDVTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLL 231
Cdd:PLN02699  536 FTPRDVTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALKQI 615


                  .
gi 1386827315 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 ...
 432-576 1.87e-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: 165.43  E-value: 1.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 432 INYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGeSQAGEQPTHTVMPGQVMRVTTGAPIPCGADAV 511
Cdd:pfam03453  11 LEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP-IAAGEPPGPLLPGGEAVRIMTGAPLPEGADAV 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386827315 512 VQVEDTEllresedGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 576
Cdd:pfam03453  90 VMVEDTE-------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 77-222 8.69e-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: 138.22  E-value: 8.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  77 IRVGVLTVSDSCFRNLAE-------DRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEkeLNLILTTGG 149
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQE---AGFNVVRLGIVPDDPEEIREILRKAVDE--ADVVLTTGG 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386827315 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 ...
 586-729 2.36e-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: 125.51  E-value: 2.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 586 PVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGE 665
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386827315 666 KDYLKQVLDiDLHAQIHFGR----------VFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIP 729
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 ...
 589-726 3.76e-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: 115.76  E-value: 3.76e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  589 AVMSTGNELLNPeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVG--DNPDDLLNALNEGISRADVIITSGGVSMGEK 666
Cdd:smart00852   1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386827315  667 DYLKQVLDIDLHAQIHFGRVFMKPGLPTT-----FATLDIDGARKLIFALPGrNPVSAVVTCNLF 726
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 1.44e-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: 111.53  E-value: 1.44e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315   80 GVLTVSDSCFR-NLAEDRSGVNLKDLVHDpslLGGMIAAYKIV--PDEIDEIKETLVHWCDEKELnlILTTGGTGFAPRD 156
Cdd:smart00852   1 AIISTGDELLSgGQIRDSNGPMLAALLRE---LGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDD 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386827315  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 4.73e-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: 110.03  E-value: 4.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  80 GVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELnlILTTGGTGFAPRDVTP 159
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386827315 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 ...
 414-821 1.39e-161

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: 475.06  E-value: 1.39e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 414 DKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTHTV 490
Cdd:cd00887     2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 491 MPGQVMRVTTGAPIPCGADAVVQVEDTELlresEDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 570
Cdd:cd00887    82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE----EGGR----VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 571 LLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 650
Cdd:cd00887   154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 651 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIPA 730
Cdd:cd00887   234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPG-NPVSALVTFELFVRPA 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 731 LRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQVSSRLMSMRSANGLLMLPPKTEqyvE 809
Cdd:cd00887   308 LRKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---G 382

                         410
                  ....*....|..
gi 1386827315 810 LHKGEVVDVMVI 821
Cdd:cd00887   383 LEAGEEVEVLLL 394
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 410-824 3.38e-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: 435.67  E-value: 3.38e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 410 LTSMDKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF----IIGESQAGEQ 485
Cdd:COG0303     1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtlrVVGEIAAGSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 486 PTHTVMPGQVMRVTTGAPIPCGADAVVQVEDTELlresEDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 565
Cdd:COG0303    81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER----EGDR----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 566 PSEIGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 645
Cdd:COG0303   153 PADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 646 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNL 725
Cdd:COG0303   233 REALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRLG----GKPVFGLPG-NPVSALVTFEL 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 726 FVIPALRKMQGILDPRPTIIKARLSCDV-KLDPRPEYHRCILTWHHQEplPWAQSTGNQVSSRLMSMRSANGLLMLPPKT 804
Cdd:COG0303   307 FVRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLERDDGE--LVVEPLGGQGSGLLSSLAEADGLIVLPEGV 384

                         410       420
                  ....*....|....*....|
gi 1386827315 805 EqyvELHKGEVVDVMVIGRL 824
Cdd:COG0303   385 E---GVEAGEEVEVLLLDGL 401
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 410-801 2.48e-128

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 398.80  E-value: 2.48e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 410 LTSMDKAFITVLEMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTH- 488
Cdd:PLN02699    7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGv 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 489 TVMPGQVMRVTTGAPIPCGADAVVQVEDTELLRESEDGTEEleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSE 568
Cdd:PLN02699   87 TLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 569 IGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDD-LHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNE 647
Cdd:PLN02699  165 IGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 648 GISR-ADVIITSGGVSMGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDIDGARK-----LIFALPGrNPVSAVV 721
Cdd:PLN02699  245 AISSgVDILLTSGGVSMGDRDFVKPLL--EKRGTVYFSKVLMKPGKPLTFAEIDAKSAPSnskkmLAFGLPG-NPVSCLV 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 722 TCNLFVIPALRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQE----PLPWAQSTGNQVSSRLMSMRSANG 796
Cdd:PLN02699  322 CFNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPvRPEFHRAIIRWKLNDgsgnPGFVAESTGHQMSSRLLSMKSANA 401


                  ....*
gi 1386827315 797 LLMLP 801
Cdd:PLN02699  402 LLELP 406
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 427-818 2.02e-92

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


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 303.29  E-value: 2.02e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 427 LGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAAD-------GPGDRFIIGESQAGEQPTHTVMPGQVMRVT 499
Cdd:PRK14498   28 LGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADtfgaseaNPVRLKLGGEVHAGEAPDVEVEPGEAVEIA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 500 TGAPIPCGADAVVQVEDTEllrESEDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTE 579
Cdd:PRK14498  108 TGAPIPRGADAVVMVEDTE---EVDDDT----VEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGGVAE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 580 VEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSG 659
Cdd:PRK14498  181 VPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVLLSG 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 660 GVSMGEKDYLKQVLDidlhaqiHFGRVF-----MKPGLPTTFATldIDGarKLIFALPGrNPVSAVVTCNLFVIPALRKM 734
Cdd:PRK14498  261 GTSAGAGDVTYRVIE-------ELGEVLvhgvaIKPGKPTILGV--IGG--KPVVGLPG-YPVSALTIFEEFVAPLLRKL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 735 QGILDPRPTIIKARLScdVKLDP---RPEYHRCILTWHHQEPLPWAQSTGnqvSSRLMSMRSANGLLMLPPKTEQyveLH 811
Cdd:PRK14498  329 AGLPPPERATVKARLA--RRVRSelgREEFVPVSLGRVGDGYVAYPLSRG---SGAITSLVRADGFIEIPANTEG---LE 400


                  ....*..
gi 1386827315 812 KGEVVDV 818
Cdd:PRK14498  401 AGEEVEV 407
PRK14491 PRK14491
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ...
 424-806 8.03e-86

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


Pssm-ID: 237729 [Multi-domain]  Cd Length: 597  Bit Score: 284.97  E-value: 8.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 424 TVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF-IIGESQAGEQPTHTVMPGQVMRVTTGA 502
Cdd:PRK14491  213 TPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESYtLVGEVLAGHQYDGTLQAGEAVRIMTGA 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 503 PIPCGADAVVQVEDTELlresEDGTEELEVRILVqarpGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEV 582
Cdd:PRK14491  293 PVPAGADTVVMRELATQ----DGDKVSFDGGIKA----GQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPV 364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 583 QKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVS 662
Cdd:PRK14491  365 FRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVS 444

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 663 MGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIPALRKMQGILDPRP 742
Cdd:PRK14491  445 VGDADYIKTAL--AKLGQIDFWRINMRPGRPLAFGQIG----DSPFFGLPG-NPVAVMVSFLQFVEPALRKLAGEQNWQP 517

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386827315 743 TIIKARLSCDVKLDP-RPEYHRCILTWHHQEPLPwAQSTGNQVSSRLMSMRSANGLLMLPPKTEQ 806
Cdd:PRK14491  518 LLFPAIADETLRSRQgRTEFSRGIYHLGADGRLH-VRTTGKQGSGILSSMSEANCLIEIGPAAET 581
PRK10680 PRK10680
molybdopterin biosynthesis protein MoeA; Provisional
 410-800 4.86e-72

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 182643 [Multi-domain]  Cd Length: 411  Bit Score: 242.30  E-value: 4.86e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 410 LTSMDKAFITVLEMTVVL-GTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF--IIGESQAGeQP 486
Cdd:PRK10680    7 LMSLETALTEMLSRVTPLtATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPlpVAGKAFAG-QP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 487 THTVMP-GQVMRVTTGAPIPCGADAVVQVEDTELlreSEDGteeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 565
Cdd:PRK10680   86 FHGEWPaGTCIRIMTGAPVPEGCEAVVMQEQTEQ---TDDG-----VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 566 PSEIGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 645
Cdd:PRK10680  158 TAELPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 646 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLhAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNL 725
Cdd:PRK10680  238 IEADSQADVVISSGGVSVGEADYTKTILE-EL-GEIAFWKLAIKPGKPFAFGKLS----NSWFCGLPG-NPVSAALTFYQ 310

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386827315 726 FVIPALRKMQGILDPRPTI-IKARLSCDVKLDP-RPEYHRCILTWHHQEPLPwAQSTGNQVSSRLMSMRSANGLLML 800
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 8.89e-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: 215.80  E-value: 8.89e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  77 IRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTTGGTGFAPRD 156
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386827315 157 VTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLL 231
Cdd:cd00886    78 VTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
PRK14497 PRK14497
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
 422-820 1.43e-65

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


Pssm-ID: 172968 [Multi-domain]  Cd Length: 546  Bit Score: 228.54  E-value: 1.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 422 EMTVVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTHTVMPGQVMRVTTG 501
Cdd:PRK14497   23 SLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGEFKVIDKIGIGEFKEIHIKECEAVEVDTG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 502 APIPCGADAVVQVEDTELLresedgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVE 581
Cdd:PRK14497  103 SMIPMGADAVIKVENTKVI-------NGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVK 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 582 VQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGV 661
Cdd:PRK14497  176 VYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGT 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 662 SMGEKDYLKQVL----DIDLHAqihfgrVFMKPGLPTTFATldIDGarKLIFALPGrNPVSAVVTCNLFVIPALRKMQG- 736
Cdd:PRK14497  256 SAGEKDFVHQAIrelgNIIVHG------LKIKPGKPTILGI--VDG--KPVIGLPG-NIVSTMVVLNMVILEYLKSLYPs 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 737 ---ILDPRPtiIKARLSCDVKLDprpeYHRCIL---------TWHHQEPLPWAqstgnqvSSRLMSMRSANGLLMLPPKT 804
Cdd:PRK14497  325 rkeILGLGK--IKARLALRVKAD----EHRNTLipvylfksdNSYYALPVPFD-------SYMVGTFSLTDGYIMLGPNE 391

                         410
                  ....*....|....*.
gi 1386827315 805 eqyvELHKGEVVDVMV 820
Cdd:PRK14497  392 ----EIEEGKEVEVDL 403
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 68-232 4.81e-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: 200.73  E-value: 4.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  68 MILTNHDHQIRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTT 147
Cdd:COG0521     1 MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE---AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 148 GGTGFAPRDVTPEATKEVIEREAPGMSLAMLMGSLN-VTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPH 226
Cdd:COG0521    78 GGTGLSPRDVTPEATRPLLDKELPGFGELFRALSLEeIGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPH 157


                  ....*.
gi 1386827315 227 AIDLLR 232
Cdd:COG0521   158 AVDLLN 163
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
 74-232 8.61e-49

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 183.47  E-value: 8.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  74 DHQIRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDPS--LLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTTGGTG 151
Cdd:PLN02699  456 NPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSSSekLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 152 FAPRDVTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLL 231
Cdd:PLN02699  536 FTPRDVTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALKQI 615


                  .
gi 1386827315 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 ...
 432-576 1.87e-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: 165.43  E-value: 1.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 432 INYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGeSQAGEQPTHTVMPGQVMRVTTGAPIPCGADAV 511
Cdd:pfam03453  11 LEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP-IAAGEPPGPLLPGGEAVRIMTGAPLPEGADAV 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386827315 512 VQVEDTEllresedGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 576
Cdd:pfam03453  90 VMVEDTE-------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
PRK14690 PRK14690
molybdopterin biosynthesis protein MoeA; Provisional
 426-801 2.16e-45

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 237789 [Multi-domain]  Cd Length: 419  Bit Score: 168.56  E-value: 2.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 426 VLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDR---FIIGESQAGEQPTHTVMPGQVMRVTTGA 502
Cdd:PRK14690   39 VTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQvlpLIEGRAAAGVPFSGRVPEGMALRILTGA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 503 PIPCGADAVVQVEDTELlresedGTEELEVRILVQArpGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEV 582
Cdd:PRK14690  119 ALPEGVDTVVLEEDVAG------DGHRIAFHGPLKM--GANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSV 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 583 QKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVS 662
Cdd:PRK14690  191 RRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGAS 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 663 MGEKDYLKQVLDIDlhAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIPALRKM--QGILDP 740
Cdd:PRK14690  271 AGDEDHVSALLREA--GAMQSWRIALKPGRPLALGLWQ----GVPVFGLPG-NPVAALVCTLVFARPAMSLLagEGWSEP 343

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386827315 741 RPTIIKARLSCDvKLDPRPEYHRCILTWHHQEPLpwaQSTGnqvSSRLMSMRSANGLLMLP 801
Cdd:PRK14690  344 QGFTVPAAFEKR-KKPGRREYLRARLRQGHAEVF---RSEG---SGRISGLSWAEGLVELG 397
mogA PRK09417
molybdenum cofactor biosynthesis protein MogA; Provisional
 77-238 8.69e-43

molybdenum cofactor biosynthesis protein MogA; Provisional


Pssm-ID: 181837 [Multi-domain]  Cd Length: 193  Bit Score: 153.96  E-value: 8.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  77 IRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpSLLGGMIAAYKIVPDEIDEIKETLVHWCDEKELNLILTTGGTGFAPRD 156
Cdd:PRK09417    4 LKIGLVSISDRASSGVYEDKGIPALEEWLAS-ALTSPFEIETRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTGPARRD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 157 VTPEATKEVIEREAPGMSLAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQF------------ILPAL 224
Cdd:PRK09417   83 VTPEATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLEGlkdadgnvvvpgIFAAV 162

                         170       180
                  ....*....|....*....|.
gi 1386827315 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 ...
 588-731 6.01e-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: 6.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 588 VAVMSTGNELLNpeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKD 667
Cdd:cd00758     2 VAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRD 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386827315 668 YLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIPAL 731
Cdd:cd00758    75 VTPEALAELGEREAHGKGVALAPGSRTAFGIIG----KVLIINLPG-SPKSALTTFEALVLPAL 133
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 77-233 7.54e-39

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 146.63  E-value: 7.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  77 IRVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCdEKELNLILTTGGTGFAPRD 156
Cdd:PRK03604  156 TSAAVLVLSDSIAAGTKEDRSGKLIVEGLEE---AGFEVSHYTIIPDEPAEIAAAVAAWI-AEGYALIITTGGTGLGPRD 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386827315 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 1.07e-38

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: 140.17  E-value: 1.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  78 RVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEkeLNLILTTGGTGFAPRDV 157
Cdd:cd00758     1 RVAIVTVSDELSQGQIEDTNGPALEALLED---LGCEVIYAGVVPDDADSIRAALIEASRE--ADLVLTTGGTGVGRRDV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386827315 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 8.69e-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: 138.22  E-value: 8.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  77 IRVGVLTVSDSCFRNLAE-------DRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEkeLNLILTTGG 149
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQE---AGFNVVRLGIVPDDPEEIREILRKAVDE--ADVVLTTGG 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386827315 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 ...
 586-729 2.36e-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: 125.51  E-value: 2.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 586 PVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGE 665
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386827315 666 KDYLKQVLDiDLHAQIHFGR----------VFMKPGLPTTFATLDidgaRKLIFALPGrNPVSAVVTCNLFVIP 729
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 ...
 589-733 1.28e-31

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.


Pssm-ID: 425979 [Multi-domain]  Cd Length: 143  Bit Score: 120.43  E-value: 1.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 589 AVMSTGNELLnpeddlhPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDY 668
Cdd:pfam00994   1 AIITTGDELL-------PGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386827315 669 LKQVL------DIDLHAQIhFGRVFMKPGLPTTFATL-DIDGARKLIFALPGrNPVSAVVTCNLFVIPALRK 733
Cdd:pfam00994  74 TPEALaelggrELPGFEEL-FRGVSLKPGKPVGTAPGaILSRAGKTVFGLPG-SPVAAKVMFELLLLPLLRH 143
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 589-726 3.76e-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: 115.76  E-value: 3.76e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  589 AVMSTGNELLNPeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVG--DNPDDLLNALNEGISRADVIITSGGVSMGEK 666
Cdd:smart00852   1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386827315  667 DYLKQVLDIDLHAQIHFGRVFMKPGLPTT-----FATLDIDGARKLIFALPGrNPVSAVVTCNLF 726
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 1.44e-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: 111.53  E-value: 1.44e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315   80 GVLTVSDSCFR-NLAEDRSGVNLKDLVHDpslLGGMIAAYKIV--PDEIDEIKETLVHWCDEKELnlILTTGGTGFAPRD 156
Cdd:smart00852   1 AIISTGDELLSgGQIRDSNGPMLAALLRE---LGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDD 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386827315  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 4.73e-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: 110.03  E-value: 4.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  80 GVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELnlILTTGGTGFAPRDVTP 159
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386827315 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 ...
 746-821 2.73e-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: 2.73e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386827315 746 KARLSCDVKLDP-RPEYHRCILtwHHQEPLPWAQSTGNQVSSRLMSMRSANGLLMLPPKTEQYVElhkGEVVDVMVI 821
Cdd:pfam03454   1 KARLARDLKSDPgRREFVRVRL--HEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEA---GEEVEVILL 72
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 588-660 5.88e-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: 5.88e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386827315 588 VAVMSTGNELLNpeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 660
Cdd:COG1058     2 AEIITIGDELLS-------GRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGG 67
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 588-660 8.76e-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: 8.76e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386827315 588 VAVMSTGNELLNpeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 660
Cdd:cd00885     2 AEIIAIGDELLS-------GQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
cinA_nterm TIGR00200
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ...
 588-661 2.24e-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: 50.68  E-value: 2.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386827315 588 VAVMSTGNELLNpeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGV 661
Cdd:TIGR00200   3 AEIISVGDELLL-------GQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGL 69
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
 590-673 3.27e-06

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 50.17  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 590 VMSTGNELLNpeddlhpGKIRDSNRSTL---LATIQ-EHGYPTInlgiVGDNPDDLLNALNEGISRADVIITSGGVSMGE 665
Cdd:PRK00549    5 IIAVGTELLL-------GQIVNTNAQFLsekLAELGiDVYHQTV----VGDNPERLLSALEIAEERSDLIITTGGLGPTK 73


                  ....*...
gi 1386827315 666 KDYLKQVL 673
Cdd:PRK00549   74 DDLTKETV 81
PRK03673 PRK03673
nicotinamide mononucleotide deamidase-related protein YfaY;
588-660 7.86e-06

nicotinamide mononucleotide deamidase-related protein YfaY;


Pssm-ID: 179629 [Multi-domain]  Cd Length: 396  Bit Score: 48.93  E-value: 7.86e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386827315 588 VAVMSTGNELLNpeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 660
Cdd:PRK03673    4 VEMLSTGDEVLH-------GQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGG 69
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 111-224 1.09e-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: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 111 LGGMIAAYKIVPDEIDEIKETL---VHWCDekelnLILTTGGTGFAPRDVtpeaTKEVIEREAPGmslaMLMGSLNVTPl 187
Cdd:cd00887   207 LGAEVVDLGIVPDDPEALREALeeaLEEAD-----VVITSGGVSVGDYDF----VKEVLEELGGE----VLFHGVAMKP- 272

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1386827315 188 GmlsRPV-CGIRGKTLIINLPGSKKGSQECF-QFILPAL 224
Cdd:cd00887   273 G---KPLaFGRLGGKPVFGLPGNPVSALVTFeLFVRPAL 308
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
586-660 8.48e-05

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 45.00  E-value: 8.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386827315 586 PVVAVMSTGNELLNpeddlhpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 660
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 1.10e-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: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315  78 RVGVLTVSDSCFRNLAEDRSGVNLKDLVHDpslLGGMIAAYKIVPDEIDEIKETLVHWCDEKELnLILTTGGTGFAPRDV 157
Cdd:cd03522   161 RVGLIVTGSEVYGGRIEDKFGPVLRARLAA---LGVELVEQVIVPHDEAAIAAAIAEALEAGAE-LLILTGGASVDPDDV 236

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1386827315 158 TPEATK----EVIEREAPGMSLAMLMgslnvtpLGML-SRPVCGIRG 199
Cdd:cd03522   237 TPAAIRaaggEVIRYGMPVDPGNLLL-------LGYLgGVPVIGLPG 276
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 111-224 1.40e-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: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386827315 111 LGGMIAAYKIVPDEIDEIKETL---VHWCDekelnLILTTGGTGFAPRDVtpeaTKEVIEREapGMSLamLMGSLNVTPl 187
Cdd:COG0303   211 AGAEVVDLGIVPDDPEALRAALreaLAEAD-----LVITSGGVSVGDYDL----VKEALEEL--GAEV--LFHKVAMKP- 276

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1386827315 188 GmlsRPV-CGIRGKTLIINLPG---SkkgSQECF-QFILPAL 224
Cdd:COG0303   277 G---KPLaFGRLGGKPVFGLPGnpvS---ALVTFeLFVRPAL 312
PRK03670 PRK03670
competence damage-inducible protein A; Provisional
 596-661 6.00e-03

competence damage-inducible protein A; Provisional


Pssm-ID: 167581  Cd Length: 252  Bit Score: 39.40  E-value: 6.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386827315 596 ELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRA-DVIITSGGV 661
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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