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Conserved domains on  [gi|2359305436|gb|UZW74721|]
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molybdopterin molybdotransferase MoeA [Alkalimarinus sediminis]

Protein Classification

molybdopterin molybdotransferase MoeA( domain architecture ID 11416749)

molybdopterin molybdotransferase MoeA mediates molybdenum ligation to molybdopterin

EC:  2.10.1.1
Gene Ontology:  GO:0046872|GO:0006777|GO:0061599

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
9-407 0e+00

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: 538.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436   9 LRSVDVMLEELLSKAKPAkESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCQGGEPTSLKISQRIPAGS 88
Cdd:COG0303     1 MISVEEALALILAAVRPL-GTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  89 VP-HPLQTGTAARIFTGATIPPNATAVVMQEDCTEQDGTVTLPTNINLNQNIRPQGQDIKSNQVILKRGHRIRAQDMGLM 167
Cdd:COG0303    80 PPpGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 168 ASIGIANINIYRPLKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAA 247
Cdd:COG0303   160 ASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 248 DIIITSGGVSVGEEDHIKAAITKLG-ELDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARPFLLKSQGAE 326
Cdd:COG0303   240 DLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 327 RIEAHSFKLPIGFSLKKPGKRREYLRTRLSYNQGSASIENHPNQSSGVLSSASWADGFAVIPEHTTP-QQGELVEFWPFS 405
Cdd:COG0303   320 PPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGvEAGEEVEVLLLD 399

                  ..
gi 2359305436 406 EL 407
Cdd:COG0303   400 GL 401
 
Name Accession Description Interval E-value
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
9-407 0e+00

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: 538.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436   9 LRSVDVMLEELLSKAKPAkESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCQGGEPTSLKISQRIPAGS 88
Cdd:COG0303     1 MISVEEALALILAAVRPL-GTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  89 VP-HPLQTGTAARIFTGATIPPNATAVVMQEDCTEQDGTVTLPTNINLNQNIRPQGQDIKSNQVILKRGHRIRAQDMGLM 167
Cdd:COG0303    80 PPpGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 168 ASIGIANINIYRPLKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAA 247
Cdd:COG0303   160 ASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 248 DIIITSGGVSVGEEDHIKAAITKLG-ELDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARPFLLKSQGAE 326
Cdd:COG0303   240 DLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 327 RIEAHSFKLPIGFSLKKPGKRREYLRTRLSYNQGSASIENHPNQSSGVLSSASWADGFAVIPEHTTP-QQGELVEFWPFS 405
Cdd:COG0303   320 PPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGvEAGEEVEVLLLD 399

                  ..
gi 2359305436 406 EL 407
Cdd:COG0303   400 GL 401
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
16-404 0e+00

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: 513.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  16 LEELLSKAKPAKESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCQGGePTSLKISQRIPAGSVPH-PLQ 94
Cdd:cd00887     4 ARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGA-SVTLRVVGEIPAGEPPDgPLG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  95 TGTAARIFTGATIPPNATAVVMQEDCTEQDGTVTLPTNINLNQNIRPQGQDIKSNQVILKRGHRIRAQDMGLMASIGIAN 174
Cdd:cd00887    83 PGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 175 INIYRPLKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAADIIITSG 254
Cdd:cd00887   163 VPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 255 GVSVGEEDHIKAAITKL-GELDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARPFLLKSQGAERIEAHSF 333
Cdd:cd00887   243 GVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRV 322
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2359305436 334 KLPIGFSLKKPGKRREYLRTRLSYNQGSASIENHPNQSSGVLSSASWADGFAVIPEHTTP-QQGELVEFWPF 404
Cdd:cd00887   323 KARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGlEAGEEVEVLLL 394
PRK14491 PRK14491
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ...
3-407 6.76e-135

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


Pssm-ID: 237729 [Multi-domain]  Cd Length: 597  Bit Score: 399.37  E-value: 6.76e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436   3 CCDRGQLR--SVDVMLEELLSKAKPAKESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCqggEPTSLKI 80
Cdd:PRK14491  190 CCDLLSPAflSVSQGLDKILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDL---EPESYTL 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  81 SQRIPAG-SVPHPLQTGTAARIFTGATIPPNATAVVMQEDCTEQDGTVTLPTNINLNQNIRPQGQDIKSNQVILKRGHRI 159
Cdd:PRK14491  267 VGEVLAGhQYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRL 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 160 RAQDMGLMASIGIANINIYRPLKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTA 239
Cdd:PRK14491  347 SAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEAT 426
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 240 LNEAAEAADIIITSGGVSVGEEDHIKAAITKLGELDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARPFL 319
Cdd:PRK14491  427 LEQAAAQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPAL 506
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 320 LKSQGAERIEAHSFKLPIGFSLKKPGKRREYLRTRLSYNQ-GSASIENHPNQSSGVLSSASWADGFAVI-PEHTTPQQGE 397
Cdd:PRK14491  507 RKLAGEQNWQPLLFPAIADETLRSRQGRTEFSRGIYHLGAdGRLHVRTTGKQGSGILSSMSEANCLIEIgPAAETVNAGE 586
                         410
                  ....*....|
gi 2359305436 398 LVEFWPFSEL 407
Cdd:PRK14491  587 TVTIQPLAGL 596
MoeA_N pfam03453
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ...
24-171 1.20e-52

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: 172.37  E-value: 1.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  24 KPAKESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCQGGEPTSlkisqRIPAGSVPHPLQT-GTAARIF 102
Cdd:pfam03453   3 LGTEETVPLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVN-----PIAAGEPPGPLLPgGEAVRIM 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 103 TGATIPPNATAVVMQEDCTEQDG-TVTLPTNINLNQNIRPQGQDIKSNQVILKRGHRIRAQDMGLMASIG 171
Cdd:pfam03453  78 TGAPLPEGADAVVMVEDTEEGGGrTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
181-317 1.08e-39

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: 138.99  E-value: 1.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 181 LKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAADIIITSGGVSVGE 260
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2359305436 261 EDHIKAAITKLGE-----------LDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARP 317
Cdd:TIGR00177  81 RDVTPEALEELGEkeipgfgefrmLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
184-311 6.25e-37

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


Pssm-ID: 214856 [Multi-domain]  Cd Length: 138  Bit Score: 131.17  E-value: 6.25e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  184 AILSTGDELVEPGevakegQIYNSNRYTLKGLLDGFGFEIVDVGIV--EDTLNATLTALNEAAEAADIIITSGGVSVGEE 261
Cdd:smart00852   1 AIISTGDELLSGG------QIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2359305436  262 DHIKAAITKLG--ELDLWKLAIKPGKPFAY---------GQVGNTPILGLPGNPGAVFVTF 311
Cdd:smart00852  75 DLTPEALAELGgrELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMF 135
 
Name Accession Description Interval E-value
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
9-407 0e+00

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: 538.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436   9 LRSVDVMLEELLSKAKPAkESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCQGGEPTSLKISQRIPAGS 88
Cdd:COG0303     1 MISVEEALALILAAVRPL-GTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  89 VP-HPLQTGTAARIFTGATIPPNATAVVMQEDCTEQDGTVTLPTNINLNQNIRPQGQDIKSNQVILKRGHRIRAQDMGLM 167
Cdd:COG0303    80 PPpGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 168 ASIGIANINIYRPLKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAA 247
Cdd:COG0303   160 ASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 248 DIIITSGGVSVGEEDHIKAAITKLG-ELDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARPFLLKSQGAE 326
Cdd:COG0303   240 DLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 327 RIEAHSFKLPIGFSLKKPGKRREYLRTRLSYNQGSASIENHPNQSSGVLSSASWADGFAVIPEHTTP-QQGELVEFWPFS 405
Cdd:COG0303   320 PPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGvEAGEEVEVLLLD 399

                  ..
gi 2359305436 406 EL 407
Cdd:COG0303   400 GL 401
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
16-404 0e+00

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: 513.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  16 LEELLSKAKPAKESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCQGGePTSLKISQRIPAGSVPH-PLQ 94
Cdd:cd00887     4 ARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGA-SVTLRVVGEIPAGEPPDgPLG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  95 TGTAARIFTGATIPPNATAVVMQEDCTEQDGTVTLPTNINLNQNIRPQGQDIKSNQVILKRGHRIRAQDMGLMASIGIAN 174
Cdd:cd00887    83 PGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 175 INIYRPLKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAADIIITSG 254
Cdd:cd00887   163 VPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 255 GVSVGEEDHIKAAITKL-GELDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARPFLLKSQGAERIEAHSF 333
Cdd:cd00887   243 GVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRV 322
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2359305436 334 KLPIGFSLKKPGKRREYLRTRLSYNQGSASIENHPNQSSGVLSSASWADGFAVIPEHTTP-QQGELVEFWPF 404
Cdd:cd00887   323 KARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGlEAGEEVEVLLL 394
PRK14491 PRK14491
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ...
3-407 6.76e-135

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


Pssm-ID: 237729 [Multi-domain]  Cd Length: 597  Bit Score: 399.37  E-value: 6.76e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436   3 CCDRGQLR--SVDVMLEELLSKAKPAKESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCqggEPTSLKI 80
Cdd:PRK14491  190 CCDLLSPAflSVSQGLDKILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDL---EPESYTL 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  81 SQRIPAG-SVPHPLQTGTAARIFTGATIPPNATAVVMQEDCTEQDGTVTLPTNINLNQNIRPQGQDIKSNQVILKRGHRI 159
Cdd:PRK14491  267 VGEVLAGhQYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRL 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 160 RAQDMGLMASIGIANINIYRPLKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTA 239
Cdd:PRK14491  347 SAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEAT 426
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 240 LNEAAEAADIIITSGGVSVGEEDHIKAAITKLGELDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARPFL 319
Cdd:PRK14491  427 LEQAAAQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPAL 506
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 320 LKSQGAERIEAHSFKLPIGFSLKKPGKRREYLRTRLSYNQ-GSASIENHPNQSSGVLSSASWADGFAVI-PEHTTPQQGE 397
Cdd:PRK14491  507 RKLAGEQNWQPLLFPAIADETLRSRQGRTEFSRGIYHLGAdGRLHVRTTGKQGSGILSSMSEANCLIEIgPAAETVNAGE 586
                         410
                  ....*....|
gi 2359305436 398 LVEFWPFSEL 407
Cdd:PRK14491  587 TVTIQPLAGL 596
PRK10680 PRK10680
molybdopterin biosynthesis protein MoeA; Provisional
9-410 3.15e-106

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 182643 [Multi-domain]  Cd Length: 411  Bit Score: 319.73  E-value: 3.15e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436   9 LRSVDVMLEELLSKAKPAKESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCQGGEPtsLKISQRIPAGS 88
Cdd:PRK10680    7 LMSLETALTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQP--LPVAGKAFAGQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  89 vphPLQ----TGTAARIFTGATIPPNATAVVMQEDCTEQDGTVTLPTNINLNQNIRPQGQDIKSNQVILKRGHRIRAQDM 164
Cdd:PRK10680   85 ---PFHgewpAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAEL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 165 GLMASIGIANINIYRPLKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAA 244
Cdd:PRK10680  162 PVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEAD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 245 EAADIIITSGGVSVGEEDHIKAAITKLGELDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARPFLLKSQG 324
Cdd:PRK10680  242 SQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSG 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 325 aerieAHSFKLPI------GFSLKKPGKRREYLRTRLSYN-QGSASIENHPNQSSGVLSSASWADGFAVIP-EHTTPQQG 396
Cdd:PRK10680  322 -----NTASGLPPrqrvrtASRLKKTPGRLDFQRGILQRNaDGELEVTTTGHQGSHIFSSFSLGNCFIVLErERGNVEVG 396
                         410
                  ....*....|....
gi 2359305436 397 ELVEFWPFSELFGN 410
Cdd:PRK10680  397 EWVEVEPFNALFGG 410
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
15-410 3.52e-99

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


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 308.30  E-value: 3.52e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  15 MLEELLSKAKPAKESIniAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCQG---GEPTSLKISQRIPAGSVPH 91
Cdd:PRK14498   18 ILESLLSELPLGTEEV--PLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGaseANPVRLKLGGEVHAGEAPD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  92 -PLQTGTAARIFTGATIPPNATAVVMQEDCTEQD-GTVTLPTNINLNQNIRPQGQDIKSNQVILKRGHRIRAQDMGLMAS 169
Cdd:PRK14498   96 vEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDdDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 170 IGIANINIYRPLKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAADI 249
Cdd:PRK14498  176 GGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDL 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 250 IITSGGVSVGEEDHIKAAITKLGELDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARPFLLKSQGAERIE 329
Cdd:PRK14498  256 VLLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLRKLAGLPPPE 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 330 AHSFKLPIGFSLKKPGKRREYLrtRLSYNQGSASIENHP-NQSSGVLSSASWADGFAVIPEHT-TPQQGELVEFwpfsEL 407
Cdd:PRK14498  336 RATVKARLARRVRSELGREEFV--PVSLGRVGDGYVAYPlSRGSGAITSLVRADGFIEIPANTeGLEAGEEVEV----EL 409

                  ...
gi 2359305436 408 FGN 410
Cdd:PRK14498  410 FGP 412
PRK14690 PRK14690
molybdopterin biosynthesis protein MoeA; Provisional
12-404 2.49e-95

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 237789 [Multi-domain]  Cd Length: 419  Bit Score: 291.82  E-value: 2.49e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  12 VDVMLEELLSKAKPAKESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCQGGEPTSLkISQRIPAGsVPH 91
Cdd:PRK14690   25 VDTALDLLRARLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQVLPL-IEGRAAAG-VPF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  92 P--LQTGTAARIFTGATIPPNATAVVMQEDCTEQDGTVTLPTNINLNQNIRPQGQDIKSNQVILKRGHRIRAQDMGLMAS 169
Cdd:PRK14690  103 SgrVPEGMALRILTGAALPEGVDTVVLEEDVAGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSA 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 170 IGIANINIYRPLKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAADI 249
Cdd:PRK14690  183 VGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADV 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 250 IITSGGVSVGEEDHIKAAITKLGELDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARPFLLKSQGAERIE 329
Cdd:PRK14690  263 ILTSGGASAGDEDHVSALLREAGAMQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEGWSE 342
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2359305436 330 AHSFKLPIGFSLKKPGKRREYLRTRLSynQGSAsiENHPNQSSGVLSSASWADGFAVIPE---HTTPqqGELVEFWPF 404
Cdd:PRK14690  343 PQGFTVPAAFEKRKKPGRREYLRARLR--QGHA--EVFRSEGSGRISGLSWAEGLVELGDgarRIAP--GDPVRFIPY 414
PRK14497 PRK14497
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
9-400 2.34e-68

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


Pssm-ID: 172968 [Multi-domain]  Cd Length: 546  Bit Score: 225.84  E-value: 2.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436   9 LRSVDVMLEELLSKAKPAKESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCqggePTSLKISQRIPAGS 88
Cdd:PRK14497   10 LYSIDEAIKVFLSSLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCT----PGEFKVIDKIGIGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  89 VPH-PLQTGTAARIFTGATIPPNATAVVMQEDCTEQDGT-VTLPTNINLNQNIRPQGQDIKSNQVILKRGHRIRAQDMGL 166
Cdd:PRK14497   86 FKEiHIKECEAVEVDTGSMIPMGADAVIKVENTKVINGNfIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 167 MASIGIANINIYRPLKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEA 246
Cdd:PRK14497  166 LASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 247 ADIIITSGGVSVGEEDHIKAAITKLGELDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARPFL--LKSQG 324
Cdd:PRK14497  246 ADVLILTGGTSAGEKDFVHQAIRELGNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLksLYPSR 325
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2359305436 325 AERIEAHSFKLPIGFSLKKPGKRREYLRTRLSYNQGSASIENHPNQSS--GVLSSaswADGFAVIPEHTTPQQGELVE 400
Cdd:PRK14497  326 KEILGLGKIKARLALRVKADEHRNTLIPVYLFKSDNSYYALPVPFDSYmvGTFSL---TDGYIMLGPNEEIEEGKEVE 400
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
4-317 7.57e-57

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 197.73  E-value: 7.57e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436   4 CDRGQLRSVDVMLEELLSKAKPAkESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCQGGEPtsLKISQR 83
Cdd:PLN02699    2 GGKTEMISVEEALSIVLSVAARL-SPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYP--VITESR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  84 IPAGSVPHPLQTGTAARIFTGATIPPNATAVVMQED-CTEQDG-----TVTLPTNINLNQNIRPQGQDIKSNQVILKRGH 157
Cdd:PLN02699   79 AGNDGLGVTLTPGTVAYVTTGGPIPDGADAVVQVEDtEVVEDPldgskRVRILSQASKGQDIRPVGCDIEKDAKVLKAGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 158 RIRAQDMGLMASIGIANINIYRPLKVAILSTGDELVEPGE-VAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNAT 236
Cdd:PLN02699  159 RLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTgTLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEEL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 237 LTALNEA-AEAADIIITSGGVSVGEEDHIKAAITKLGELDLWKLAIKPGKPFAYGQVGNTP---------ILGLPGNPGA 306
Cdd:PLN02699  239 ERILDEAiSSGVDILLTSGGVSMGDRDFVKPLLEKRGTVYFSKVLMKPGKPLTFAEIDAKSapsnskkmlAFGLPGNPVS 318
                         330
                  ....*....|.
gi 2359305436 307 VFVTFCILARP 317
Cdd:PLN02699  319 CLVCFNLFVVP 329
MoeA_N pfam03453
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ...
24-171 1.20e-52

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: 172.37  E-value: 1.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  24 KPAKESINIAVADALGRVLAEDVVSSINVPPYDNSAVDGYAVIADNCQGGEPTSlkisqRIPAGSVPHPLQT-GTAARIF 102
Cdd:pfam03453   3 LGTEETVPLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVN-----PIAAGEPPGPLLPgGEAVRIM 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 103 TGATIPPNATAVVMQEDCTEQDG-TVTLPTNINLNQNIRPQGQDIKSNQVILKRGHRIRAQDMGLMASIG 171
Cdd:pfam03453  78 TGAPLPEGADAVVMVEDTEEGGGrTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
181-317 1.08e-39

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: 138.99  E-value: 1.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 181 LKVAILSTGDELVEPGEVAKEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAADIIITSGGVSVGE 260
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2359305436 261 EDHIKAAITKLGE-----------LDLWKLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARP 317
Cdd:TIGR00177  81 RDVTPEALEELGEkeipgfgefrmLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
184-311 6.25e-37

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


Pssm-ID: 214856 [Multi-domain]  Cd Length: 138  Bit Score: 131.17  E-value: 6.25e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436  184 AILSTGDELVEPGevakegQIYNSNRYTLKGLLDGFGFEIVDVGIV--EDTLNATLTALNEAAEAADIIITSGGVSVGEE 261
Cdd:smart00852   1 AIISTGDELLSGG------QIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2359305436  262 DHIKAAITKLG--ELDLWKLAIKPGKPFAY---------GQVGNTPILGLPGNPGAVFVTF 311
Cdd:smart00852  75 DLTPEALAELGgrELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMF 135
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
184-321 2.61e-35

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


Pssm-ID: 425979 [Multi-domain]  Cd Length: 143  Bit Score: 126.98  E-value: 2.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 184 AILSTGDELVEpgevakeGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAADIIITSGGVSVGEEDH 263
Cdd:pfam00994   1 AIITTGDELLP-------GQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 264 IKAAITKLGELDL-------WKLAIKPGKP-----FAYGQVGNTPILGLPGNPGAVFVTFCILARPFLLK 321
Cdd:pfam00994  74 TPEALAELGGRELpgfeelfRGVSLKPGKPvgtapGAILSRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
182-319 1.82e-28

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: 108.58  E-value: 1.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 182 KVAILSTGDELVEpgevakeGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAADIIITSGGVSVGEE 261
Cdd:cd00758     1 RVAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 262 DHIKAAITKLGELDLW--KLAIKPGKPFAYGQVGNTPILGLPGNPGAVFVTFCILARPFL 319
Cdd:cd00758    74 DVTPEALAELGEREAHgkGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
MoeA_C pfam03454
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ...
334-404 2.19e-15

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: 70.33  E-value: 2.19e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2359305436 334 KLPIGFSLKKPGKRREYLRTRLSYNQGSASIENHPNQSSGVLSSASWADGFAVIPEHTTP-QQGELVEFWPF 404
Cdd:pfam03454   1 KARLARDLKSDPGRREFVRVRLHEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGlEAGEEVEVILL 72
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
178-302 2.36e-11

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: 64.10  E-value: 2.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 178 YRPLKVAILSTGDELVEPGEVAKEGQIynsnrytLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEA-ADIIITSGGV 256
Cdd:cd03522   157 FRPLRVGLIVTGSEVYGGRIEDKFGPV-------LRARLAALGVELVEQVIVPHDEAAIAAAIAEALEAgAELLILTGGA 229
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2359305436 257 SVGEEDHIKAAITKLG-ELDLWKLAIKPGKPFAYGQVGNTPILGLPG 302
Cdd:cd03522   230 SVDPDDVTPAAIRAAGgEVIRYGMPVDPGNLLLLGYLGGVPVIGLPG 276
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
182-255 8.90e-08

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: 51.72  E-value: 8.90e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2359305436 182 KVAILSTGDELVEpgevakeGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAADIIITSGG 255
Cdd:cd00885     1 TAEIIAIGDELLS-------GQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
179-307 2.48e-07

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: 50.12  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 179 RPLKVAILSTGDELVEPGEVAKEGQIynsnrytLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAA--EAADIIITSGGV 256
Cdd:COG0521     8 VPLRIAVLTVSDRRSRGEREDTSGPA-------LVELLEEAGHEVVARRIVPDDKDAIRAALRELIddEGVDLVLTTGGT 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2359305436 257 SVGEEDH----IKAAITK----LGELdLWKLAIKPGKPFAY------GQVGNTPILGLPGNPGAV 307
Cdd:COG0521    81 GLSPRDVtpeaTRPLLDKelpgFGEL-FRALSLEEIGPSAIlsravaGIRGGTLIFNLPGSPGAV 144
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
212-307 2.17e-05

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: 44.39  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 212 LKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEA--ADIIITSGGVSVGEEDH----IKAAITK----LGELdLWKLAI 281
Cdd:cd00886    25 LVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEdgVDLILTTGGTGLAPRDVtpeaTRPLLDKelpgFGEA-FRALSL 103
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2359305436 282 KPGkPFAY------GQVGNTPILGLPGNPGAV 307
Cdd:cd00886   104 EET-GTAMlsravaGIRGGTLIFNLPGSPKAV 134
PRK03673 PRK03673
nicotinamide mononucleotide deamidase-related protein YfaY;
181-273 6.84e-05

nicotinamide mononucleotide deamidase-related protein YfaY;


Pssm-ID: 179629 [Multi-domain]  Cd Length: 396  Bit Score: 44.69  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 181 LKVAILSTGDELVepgevakEGQIYNSNRYTLKGLLDGFGFEIVDVGIVEDTLNATLTALNEAAEAADIIITSGGVSVGE 260
Cdd:PRK03673    2 LRVEMLSTGDEVL-------HGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGGLGPTS 74
                          90
                  ....*....|....
gi 2359305436 261 ED-HIKAAITKLGE 273
Cdd:PRK03673   75 DDlSALAAATAAGE 88
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
211-307 1.79e-04

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 43.01  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2359305436 211 TLKGLLDGFGFEIVDVGIVED---TLNATLTALneAAEAADIIITSGGVSVGEEDHIKAAITKLGELDLwklaikPG--- 284
Cdd:PRK03604  179 LIVEGLEEAGFEVSHYTIIPDepaEIAAAVAAW--IAEGYALIITTGGTGLGPRDVTPEALAPLLERRL------PGiae 250
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2359305436 285 KPFAYGQ---------------VGNTPILGLPGNPGAV 307
Cdd:PRK03604  251 ALRSWGQgrtptamlsrlvagmIGNSLVVALPGSPGGA 288
 
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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