|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
14-406 |
1.15e-107 |
|
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: 322.81 E-value: 1.15e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 14 LAHSLAQART-GTITVSPHDAAidCLTLAHDIHAVLPIPPMDNSAMDGFLVRTADLVGSAPWSFPVAGDVPAGAAP-MEV 91
Cdd:COG0303 8 LALILAAVRPlGTETVPLAEAL--GRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGSPPpGPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 92 PPGRAVRIMTGAeVIGENV-TVIPVEKTNIPAGpttcpsHIVVHEADAQPRHIRRRGENVQPGQCIATRGQRVDAGTLAA 170
Cdd:COG0303 86 GPGEAVRIMTGA-PLPEGAdAVVMQEDTEREGD------RVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 171 IVSCGVREIEVLPRLRVTVIATGNELGDSDaDSLKRAHIPDSNSPMIAQLVHDTGLATVN--IVRmcDDIAAFGSAISAA 248
Cdd:COG0303 159 LASLGIAEVPVYRRPRVAILSTGDELVEPG-EPLGPGQIYDSNSYMLAALLREAGAEVVDlgIVP--DDPEALRAALREA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 249 ANSSDLIITTGGISAGAFDVVKESLSSHkDSTMWFGAVAMQPGKPQGHGRVGNTMITCLPGNPVSAFVSFQLFVRPALYT 328
Cdd:COG0303 236 LAEADLVITSGGVSVGDYDLVKEALEEL-GAEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 329 LAGLQPPALGYLEADIQGTLPTPRGRDIFVPATVTYVD-TWQAQPAAF-GSHFIGSLVGVNALIHVPADAHRVAP----R 402
Cdd:COG0303 315 LAGLPPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDgELVVEPLGGqGSGLLSSLAEADGLIVLPEGVEGVEAgeevE 394
|
....
gi 371579846 403 VIPL 406
Cdd:COG0303 395 VLLL 398
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
40-406 |
3.85e-105 |
|
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: 315.97 E-value: 3.85e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 40 LAHDIHAVLPIPPMDNSAMDGFLVRTADLVGsAPWSFPVAGDVPAGAAP-MEVPPGRAVRIMTGAeVIGENV-TVIPVEK 117
Cdd:cd00887 30 LAEDVVAPIDLPPFDNSAMDGYAVRAADTAG-ASVTLRVVGEIPAGEPPdGPLGPGEAVRIMTGA-PLPEGAdAVVMVED 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 118 TNIPAGpttcpsHIVVHEADAQPRHIRRRGENVQPGQCIATRGQRVDAGTLAAIVSCGVREIEVLPRLRVTVIATGNELG 197
Cdd:cd00887 108 TEEEGG------RVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVAIISTGDELV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 198 DSDaDSLKRAHIPDSNSPMIAQLVHDTGLATVN--IVRmcDDIAAFGSAISAAANSSDLIITTGGISAGAFDVVKESLSS 275
Cdd:cd00887 182 EPG-EPLAPGQIYDSNSYMLAALLRELGAEVVDlgIVP--DDPEALREALEEALEEADVVITSGGVSVGDYDFVKEVLEE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 276 HkDSTMWFGAVAMQPGKPQGHGRVGNTMITCLPGNPVSAFVSFQLFVRPALYTLAGLQPPALGYLEADIQGTLPTPRGRD 355
Cdd:cd00887 259 L-GGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRVKARLAEDLKSKPGRR 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 371579846 356 IFVPATVTYVD-TWQAQPAA-FGSHFIGSLVGVNALIHVPADAHRVAP----RVIPL 406
Cdd:cd00887 338 EFLRVRLERDEgGLVVAPPGgQGSGLLSSLARADGLIVIPEGVEGLEAgeevEVLLL 394
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
5-397 |
1.24e-57 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 198.90 E-value: 1.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 5 KIYRETC-IDLAHS-----LAQARTGTITVSPHDAAidCLTLAHDIHAVLPIPPMDNSAMDGFLVRTADLVGS---APWS 75
Cdd:PRK14498 4 KIFLTLVsLEEAREileslLSELPLGTEEVPLEEAL--GRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGAseaNPVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 76 FPVAGDVPAGAAP-MEVPPGRAVRIMTGAeVI--GENvTVIPVEKTnIPAGPTTcpshIVVHEADAQPRHIRRRGENVQP 152
Cdd:PRK14498 82 LKLGGEVHAGEAPdVEVEPGEAVEIATGA-PIprGAD-AVVMVEDT-EEVDDDT----VEIYRPVAPGENVRPAGEDIVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 153 GQCIATRGQRVDAGTLAAIVSCGVREIEVLPRLRVTVIATGNELGDSDADsLKRAHIPDSNSPMIAQLVHDTGLATV--N 230
Cdd:PRK14498 155 GELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEP-LKPGKIYDVNSYTLAAAVEEAGGEPVryG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 231 IVRmcDDIAAFGSAISAAANSSDLIITTGGISAGAFDVVKESLSS------HkdstmwfgAVAMQPGKPQGHGRVGNTMI 304
Cdd:PRK14498 234 IVP--DDEEELEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEElgevlvH--------GVAIKPGKPTILGVIGGKPV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 305 TCLPGNPVSAFVSFQLFVRPALYTLAGLQPPALGYLEADIQGTLPTPRGRDIFVPATVTYV-DTWQAQPAAFGSHFIGSL 383
Cdd:PRK14498 304 VGLPGYPVSALTIFEEFVAPLLRKLAGLPPPERATVKARLARRVRSELGREEFVPVSLGRVgDGYVAYPLSRGSGAITSL 383
|
410
....*....|....
gi 371579846 384 VGVNALIHVPADAH 397
Cdd:PRK14498 384 VRADGFIEIPANTE 397
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
185-324 |
2.96e-28 |
|
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: 108.17 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 185 LRVTVIATGNELGDsDADSLKRAHIPDSNSPMIAQLVHDTGLATV--NIVRmcDDIAAFGSAISAAANSSDLIITTGGIS 262
Cdd:TIGR00177 1 PRVAVISVGDELVE-GGQPLEPGQIYDSNGPLLAALLQEAGFNVVrlGIVP--DDPEEIREILRKAVDEADVVLTTGGTG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 371579846 263 AGAFDVVKESLSSHKD---------STMWFGAVAMQPGKPQGHGRVGNTMITCLPGNPVSAFVSFQLFVRP 324
Cdd:TIGR00177 78 VGPRDVTPEALEELGEkeipgfgefRMLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
22-175 |
2.42e-26 |
|
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: 103.03 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 22 RTGTITVSPHDAAIDCLTLAHDIHAVLPIPPMDNSAMDGFLVRTADLVGSAPWSFPVAGDVPagaaPMEVPPGRAVRIMT 101
Cdd:pfam03453 3 LGTEETVPLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIAAGEPP----GPLLPGGEAVRIMT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371579846 102 GAEV-IGENvTVIPVEKTNIPAGPTtcpshIVVHEADAQPRHIRRRGENVQPGQCIATRGQRVDAGTLAAIVSCG 175
Cdd:pfam03453 79 GAPLpEGAD-AVVMVEDTEEGGGRT-----VEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
189-321 |
3.99e-23 |
|
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: 94.19 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 189 VIATGNELgdsdadsLKRAHIPDSNSPMIAQLVHDTG--LATVNIVRMCDDIAAFGSAISAAANSSDLIITTGGISAGAF 266
Cdd:smart00852 2 IISTGDEL-------LSGGQIRDSNGPMLAALLRELGieVVRVVVVGGPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371579846 267 DVVKESLSSHKDSTMWFGAVAMQPGKPQGH---------GRVGNTMITCLPGNPVSAFVSFQLF 321
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
14-406 |
1.15e-107 |
|
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: 322.81 E-value: 1.15e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 14 LAHSLAQART-GTITVSPHDAAidCLTLAHDIHAVLPIPPMDNSAMDGFLVRTADLVGSAPWSFPVAGDVPAGAAP-MEV 91
Cdd:COG0303 8 LALILAAVRPlGTETVPLAEAL--GRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGSPPpGPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 92 PPGRAVRIMTGAeVIGENV-TVIPVEKTNIPAGpttcpsHIVVHEADAQPRHIRRRGENVQPGQCIATRGQRVDAGTLAA 170
Cdd:COG0303 86 GPGEAVRIMTGA-PLPEGAdAVVMQEDTEREGD------RVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 171 IVSCGVREIEVLPRLRVTVIATGNELGDSDaDSLKRAHIPDSNSPMIAQLVHDTGLATVN--IVRmcDDIAAFGSAISAA 248
Cdd:COG0303 159 LASLGIAEVPVYRRPRVAILSTGDELVEPG-EPLGPGQIYDSNSYMLAALLREAGAEVVDlgIVP--DDPEALRAALREA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 249 ANSSDLIITTGGISAGAFDVVKESLSSHkDSTMWFGAVAMQPGKPQGHGRVGNTMITCLPGNPVSAFVSFQLFVRPALYT 328
Cdd:COG0303 236 LAEADLVITSGGVSVGDYDLVKEALEEL-GAEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 329 LAGLQPPALGYLEADIQGTLPTPRGRDIFVPATVTYVD-TWQAQPAAF-GSHFIGSLVGVNALIHVPADAHRVAP----R 402
Cdd:COG0303 315 LAGLPPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDgELVVEPLGGqGSGLLSSLAEADGLIVLPEGVEGVEAgeevE 394
|
....
gi 371579846 403 VIPL 406
Cdd:COG0303 395 VLLL 398
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
40-406 |
3.85e-105 |
|
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: 315.97 E-value: 3.85e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 40 LAHDIHAVLPIPPMDNSAMDGFLVRTADLVGsAPWSFPVAGDVPAGAAP-MEVPPGRAVRIMTGAeVIGENV-TVIPVEK 117
Cdd:cd00887 30 LAEDVVAPIDLPPFDNSAMDGYAVRAADTAG-ASVTLRVVGEIPAGEPPdGPLGPGEAVRIMTGA-PLPEGAdAVVMVED 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 118 TNIPAGpttcpsHIVVHEADAQPRHIRRRGENVQPGQCIATRGQRVDAGTLAAIVSCGVREIEVLPRLRVTVIATGNELG 197
Cdd:cd00887 108 TEEEGG------RVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVAIISTGDELV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 198 DSDaDSLKRAHIPDSNSPMIAQLVHDTGLATVN--IVRmcDDIAAFGSAISAAANSSDLIITTGGISAGAFDVVKESLSS 275
Cdd:cd00887 182 EPG-EPLAPGQIYDSNSYMLAALLRELGAEVVDlgIVP--DDPEALREALEEALEEADVVITSGGVSVGDYDFVKEVLEE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 276 HkDSTMWFGAVAMQPGKPQGHGRVGNTMITCLPGNPVSAFVSFQLFVRPALYTLAGLQPPALGYLEADIQGTLPTPRGRD 355
Cdd:cd00887 259 L-GGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRVKARLAEDLKSKPGRR 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 371579846 356 IFVPATVTYVD-TWQAQPAA-FGSHFIGSLVGVNALIHVPADAHRVAP----RVIPL 406
Cdd:cd00887 338 EFLRVRLERDEgGLVVAPPGgQGSGLLSSLARADGLIVIPEGVEGLEAgeevEVLLL 394
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
5-397 |
1.24e-57 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 198.90 E-value: 1.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 5 KIYRETC-IDLAHS-----LAQARTGTITVSPHDAAidCLTLAHDIHAVLPIPPMDNSAMDGFLVRTADLVGS---APWS 75
Cdd:PRK14498 4 KIFLTLVsLEEAREileslLSELPLGTEEVPLEEAL--GRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGAseaNPVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 76 FPVAGDVPAGAAP-MEVPPGRAVRIMTGAeVI--GENvTVIPVEKTnIPAGPTTcpshIVVHEADAQPRHIRRRGENVQP 152
Cdd:PRK14498 82 LKLGGEVHAGEAPdVEVEPGEAVEIATGA-PIprGAD-AVVMVEDT-EEVDDDT----VEIYRPVAPGENVRPAGEDIVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 153 GQCIATRGQRVDAGTLAAIVSCGVREIEVLPRLRVTVIATGNELGDSDADsLKRAHIPDSNSPMIAQLVHDTGLATV--N 230
Cdd:PRK14498 155 GELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEP-LKPGKIYDVNSYTLAAAVEEAGGEPVryG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 231 IVRmcDDIAAFGSAISAAANSSDLIITTGGISAGAFDVVKESLSS------HkdstmwfgAVAMQPGKPQGHGRVGNTMI 304
Cdd:PRK14498 234 IVP--DDEEELEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEElgevlvH--------GVAIKPGKPTILGVIGGKPV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 305 TCLPGNPVSAFVSFQLFVRPALYTLAGLQPPALGYLEADIQGTLPTPRGRDIFVPATVTYV-DTWQAQPAAFGSHFIGSL 383
Cdd:PRK14498 304 VGLPGYPVSALTIFEEFVAPLLRKLAGLPPPERATVKARLARRVRSELGREEFVPVSLGRVgDGYVAYPLSRGSGAITSL 383
|
410
....*....|....
gi 371579846 384 VGVNALIHVPADAH 397
Cdd:PRK14498 384 VRADGFIEIPANTE 397
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
40-337 |
4.18e-47 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 166.04 E-value: 4.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 40 LAHDIHAVLPIPPMDNSAMDGFLVRTADLVGSAPwsFPVAGDVPAGAaPM--EVPPGRAVRIMTGAEVIGENVTVIPVEK 117
Cdd:PRK10680 40 TASDIVSPLDVPGFDNSAMDGYAVRLADLASGQP--LPVAGKAFAGQ-PFhgEWPAGTCIRIMTGAPVPEGCEAVVMQEQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 118 TNIPAGPttcpshiVVHEADAQP-RHIRRRGENVQPGQCIATRGQRVDAGTLAAIVSCGVREIEVLPRLRVTVIATGNEL 196
Cdd:PRK10680 117 TEQTDDG-------VRFTAEVRSgQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVRVALFSTGDEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 197 gDSDADSLKRAHIPDSNSPMIAQLVHDTGLATVNIVRMCDDIAAFGSAISAAANSSDLIITTGGISAGAFDVVKESLSSH 276
Cdd:PRK10680 190 -QLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEADYTKTILEEL 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 371579846 277 KDSTMWfgAVAMQPGKPQGHGRVGNTMITCLPGNPVSAFVSFQLFVRPALYTLAGLQPPAL 337
Cdd:PRK10680 269 GEIAFW--KLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNTASGL 327
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
12-406 |
2.98e-46 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 167.48 E-value: 2.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 12 IDLAHSLAQARTGTITVsphdAAIDCL--TLAHDIHAVLPIPPMDNSAMDGFLVRTADLvgsAPWSFPVAGDVPAGAA-P 88
Cdd:PRK14491 205 LDKILSLVTPVTETEDV----ALDELDgrVLAQDVISPVNVPQHTNSAMDGYAFRSDDL---EPESYTLVGEVLAGHQyD 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 89 MEVPPGRAVRIMTGAEVIGENVTVIPVEKTNIPAGPTTCPSHIVVHEadaqprHIRRRGENVQPGQCIATRGQRVDAGTL 168
Cdd:PRK14491 278 GTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQ------NVRLAGEDLAQGQVALAAGTRLSAPEQ 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 169 AAIVSCGVREIEVLPRLRVTVIATGNELgDSDADSLKRAHIPDSNSPMIAQLVHDTGLATVNIVRMCDDIAAFGSAISAA 248
Cdd:PRK14491 352 GLLASLGFAEVPVFRRPKVAVFSTGDEV-QAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 249 ANSSDLIITTGGISAGAFDVVKESLSshKDSTMWFGAVAMQPGKPQGHGRVGNTMITCLPGNPVSAFVSFQLFVRPALYT 328
Cdd:PRK14491 431 AAQADVVISSGGVSVGDADYIKTALA--KLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRK 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 329 LAGLQPPALGYLEADIQGTLPTPRGRDIFV-------PATVTYVDTWQAQpaafGSHFIGSLVGVNALIHVPADAHRVAP 401
Cdd:PRK14491 509 LAGEQNWQPLLFPAIADETLRSRQGRTEFSrgiyhlgADGRLHVRTTGKQ----GSGILSSMSEANCLIEIGPAAETVNA 584
|
....*....
gi 371579846 402 ----RVIPL 406
Cdd:PRK14491 585 getvTIQPL 593
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
21-405 |
4.39e-38 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 145.34 E-value: 4.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 21 ARTGTITVSPHDAAidCLTLAHDIHAVLPIPPMDNSAMDGFLVRTADlvgsAPWSFPVAGDVPAG--AAPMEVPPGRAVR 98
Cdd:PLN02699 22 ARLSPVIVPLHEAL--GKVLAEDIRAPDPLPPYPASVKDGYAVVASD----GPGEYPVITESRAGndGLGVTLTPGTVAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 99 IMTGAEVIGENVTVIPVEKTNIPAGPTTCPSHIVVHEADAQPRHIRRRGENVQPGQCIATRGQRVDAGTLAAIVSCGVRE 178
Cdd:PLN02699 96 VTTGGPIPDGADAVVQVEDTEVVEDPLDGSKRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASEIGLLATVGVTM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 179 IEVLPRLRVTVIATGNELGDSDADSLKRAHIPDSNSPMI--AQLVHDTGLATVNIVRmcDDIAAFGSA-ISAAANSSDLI 255
Cdd:PLN02699 176 VKVYPRPTVAILSTGDELVEPTTGTLGRGQIRDSNRAMLlaAAIQQQCKVVDLGIAR--DDEEELERIlDEAISSGVDIL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 256 ITTGGISAGAFDVVKESLSshKDSTMWFGAVAMQPGKP--------QGHGRVGNTMITC-LPGNPVSAFVSFQLFVRPAL 326
Cdd:PLN02699 254 LTSGGVSMGDRDFVKPLLE--KRGTVYFSKVLMKPGKPltfaeidaKSAPSNSKKMLAFgLPGNPVSCLVCFNLFVVPAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 327 YTLAGLQPPALGYLEADIQGTLPTPRGRDIFVPATVTYVDTWQAQPAAFGSHFIG--------SLVGVNALIHVPAdahr 398
Cdd:PLN02699 332 RYLAGWSNPHLLRVQARLREPIKLDPVRPEFHRAIIRWKLNDGSGNPGFVAESTGhqmssrllSMKSANALLELPA---- 407
|
....*..
gi 371579846 399 vAPRVIP 405
Cdd:PLN02699 408 -TGNVLS 413
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
10-405 |
5.67e-38 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 141.98 E-value: 5.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 10 TCIDLAHSLAQARTGTITVSPHDAAIDCL--TLAHDIHAVLPIPPMDNSAMDGFlvrtaDLVGSAP---WSFPVAGDVPA 84
Cdd:PRK14690 23 TPVDTALDLLRARLGPVTDIKELDLSDALghVLAHDAVALRSNPPQANSAVDGY-----GFAGAAPegaQVLPLIEGRAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 85 GAAPME--VPPGRAVRIMTGAEVIGENVTVIPVEKTNIPAGpttcpsHIVVHEADAQPRHIRRRGENVQPGQCIATRGQR 162
Cdd:PRK14690 98 AGVPFSgrVPEGMALRILTGAALPEGVDTVVLEEDVAGDGH------RIAFHGPLKMGANTRKAGEDVIAGDVALPAGRR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 163 VDAGTLAAIVSCGVREIEVLPRLRVTVIATGNELGDsDADSLKRAHIPDSNSPMIAQLVHDTGLATVNIVRMCDDIAAFG 242
Cdd:PRK14690 172 LTPADLALLSAVGLTRVSVRRPLRVAVLSTGDELVE-PGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 243 SAISAAANSSDLIITTGGISAGAFDVVKESLSSHKDSTMWfgAVAMQPGKPQGHGRVGNTMITCLPGNPVSAFVSFQLFV 322
Cdd:PRK14690 251 ARLDRAAAEADVILTSGGASAGDEDHVSALLREAGAMQSW--RIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 323 RPALYTLAGlqppaLGYLEAdiQG-TLPTP------RGRDIFVPATVT--YVDTWQAQpaafGSHFIGSLVGVNALIHVP 393
Cdd:PRK14690 329 RPAMSLLAG-----EGWSEP--QGfTVPAAfekrkkPGRREYLRARLRqgHAEVFRSE----GSGRISGLSWAEGLVELG 397
|
410
....*....|....*.
gi 371579846 394 ADAHRVAP----RVIP 405
Cdd:PRK14690 398 DGARRIAPgdpvRFIP 413
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
185-324 |
2.96e-28 |
|
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: 108.17 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 185 LRVTVIATGNELGDsDADSLKRAHIPDSNSPMIAQLVHDTGLATV--NIVRmcDDIAAFGSAISAAANSSDLIITTGGIS 262
Cdd:TIGR00177 1 PRVAVISVGDELVE-GGQPLEPGQIYDSNGPLLAALLQEAGFNVVrlGIVP--DDPEEIREILRKAVDEADVVLTTGGTG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 371579846 263 AGAFDVVKESLSSHKD---------STMWFGAVAMQPGKPQGHGRVGNTMITCLPGNPVSAFVSFQLFVRP 324
Cdd:TIGR00177 78 VGPRDVTPEALEELGEkeipgfgefRMLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
22-175 |
2.42e-26 |
|
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: 103.03 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 22 RTGTITVSPHDAAIDCLTLAHDIHAVLPIPPMDNSAMDGFLVRTADLVGSAPWSFPVAGDVPagaaPMEVPPGRAVRIMT 101
Cdd:pfam03453 3 LGTEETVPLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIAAGEPP----GPLLPGGEAVRIMT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371579846 102 GAEV-IGENvTVIPVEKTNIPAGPTtcpshIVVHEADAQPRHIRRRGENVQPGQCIATRGQRVDAGTLAAIVSCG 175
Cdd:pfam03453 79 GAPLpEGAD-AVVMVEDTEEGGGRT-----VEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
41-403 |
4.67e-25 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 107.20 E-value: 4.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 41 AHDIHAVLPIPPMDNSAMDGFLVRTAdlvgSAPWSFPVAGDVPAGA-APMEVPPGRAVRIMTGAeVIGENVT-VIPVEKT 118
Cdd:PRK14497 44 AEDLMSPIDYPPFSRSTVDGYALKSS----CTPGEFKVIDKIGIGEfKEIHIKECEAVEVDTGS-MIPMGADaVIKVENT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 119 NIPAGPTtcpshIVVHEADAQPRHIRRRGENVQPGQCIATRGQRVDAGTLAAIVSCGVREIEVLPRLRVTVIATGNELGD 198
Cdd:PRK14497 119 KVINGNF-----IKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPKIYLIATGDELVE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 199 SdADSLKRAHIPDSNSPMIAQLVHDTGLATVNIVRMCDDIAAFGSAISAAANSSDLIITTGGISAGAFDVVKESLssHKD 278
Cdd:PRK14497 194 P-GNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKDFVHQAI--REL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 279 STMWFGAVAMQPGKPQGHGRVGNTMITCLPGNPVSAFVSFQLFVRPALYTLAGLQPPALGYLEADIQGTLPTP--RGRDI 356
Cdd:PRK14497 271 GNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPSRKEILGLGKIKARLALRVKadEHRNT 350
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 371579846 357 FVPATVTYVD-TWQAQPAAFGSHFIGSLVGVNALIHV-PADAHRVAPRV 403
Cdd:PRK14497 351 LIPVYLFKSDnSYYALPVPFDSYMVGTFSLTDGYIMLgPNEEIEEGKEV 399
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
189-326 |
1.87e-24 |
|
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: 97.70 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 189 VIATGNELgdsdadslKRAHIPDSNSPMIAQLVHDTGLATVNIVRMCDDIAAFGSAISAAANSSDLIITTGGISAGAFDV 268
Cdd:pfam00994 2 IITTGDEL--------LPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 371579846 269 VKESLSSHKDSTM-----WFGAVAMQPGKPQGHGRV-----GNTMITCLPGNPVSAFVSFQLFVRPAL 326
Cdd:pfam00994 74 TPEALAELGGRELpgfeeLFRGVSLKPGKPVGTAPGailsrAGKTVFGLPGSPVAAKVMFELLLLPLL 141
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
189-321 |
3.99e-23 |
|
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: 94.19 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 189 VIATGNELgdsdadsLKRAHIPDSNSPMIAQLVHDTG--LATVNIVRMCDDIAAFGSAISAAANSSDLIITTGGISAGAF 266
Cdd:smart00852 2 IISTGDEL-------LSGGQIRDSNGPMLAALLRELGieVVRVVVVGGPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371579846 267 DVVKESLSSHKDSTMWFGAVAMQPGKPQGH---------GRVGNTMITCLPGNPVSAFVSFQLF 321
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
186-326 |
1.48e-19 |
|
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: 83.93 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371579846 186 RVTVIATGNELGdsdadslkRAHIPDSNSPMIAQLVHDTGLATVNIVRMCDDIAAFGSAISAAANSSDLIITTGGISAGA 265
Cdd:cd00758 1 RVAIVTVSDELS--------QGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGR 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 371579846 266 FDVVKESLSSHKDSTMWFGAVAMQPGKPQGHGRVGNTMITCLPGNPVSAFVSFQLFVRPAL 326
Cdd:cd00758 73 RDVTPEALAELGEREAHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
|