|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
9-404 |
2.09e-120 |
|
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: 355.17 E-value: 2.09e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 9 LRSLSEHLDAVLSLATaPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPGPWTFPVIGDIPAGT 88
Cdd:COG0303 1 MISVEEALALILAAVR-PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 89 DVRTP-RRGAALRIMTGAPVPEepGL-AVVPVEHTNIPRGpqslpsSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRI 166
Cdd:COG0303 80 PPPGPlGPGEAVRIMTGAPLPE--GAdAVVMQEDTEREGD------RVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 167 DAATIAALVSTGNATVPVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA 238
Cdd:COG0303 152 TPADLGLLASLGIAEVPVYRRPRVAILSTGDELvepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 239 -LEAAKGSNLILTTGGISAGAFDIVRELLSP---DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPL 314
Cdd:COG0303 232 lREALAEADLVITSGGVSVGDYDLVKEALEElgaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 315 MRALSGQVPQgldERPQLMASAACEFHADSKRDRFIPVRIKYGTTPQAISSHRSGlGSHFVASLAGVTGLAYLPHGTGTT 394
Cdd:COG0303 312 LRKLAGLPPP---PPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQ-GSGLLSSLAEADGLIVLPEGVEGV 387
|
410
....*....|
gi 2531271090 395 AIGQPVRVLL 404
Cdd:COG0303 388 EAGEEVEVLL 397
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
14-404 |
1.26e-115 |
|
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: 342.55 E-value: 1.26e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 14 EHLDAVLSLATAPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGpGPWTFPVIGDIPAGTD-VRT 92
Cdd:cd00887 2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAG-ASVTLRVVGEIPAGEPpDGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 93 PRRGAALRIMTGAPVPEepGL-AVVPVEHTNIPRGpqslpsSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRIDAATI 171
Cdd:cd00887 81 LGPGEAVRIMTGAPLPE--GAdAVVMVEDTEEEGG------RVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 172 AALVSTGNATVPVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA-LEAA 242
Cdd:cd00887 153 GLLASLGIAEVPVYRRPRVAIISTGDELvepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREAlEEAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 243 KGSNLILTTGGISAGAFDIVRELLS---PDVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPLMRALS 319
Cdd:cd00887 233 EEADVVITSGGVSVGDYDFVKEVLEelgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 320 GQVPqglDERPQLMASAACEFHADSKRDRFIPVRIKYGTTPQAISSHRSGlGSHFVASLAGVTGLAYLPHGTGTTAIGQP 399
Cdd:cd00887 313 GAPE---PEPPRVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQ-GSGLLSSLARADGLIVIPEGVEGLEAGEE 388
|
....*
gi 2531271090 400 VRVLL 404
Cdd:cd00887 389 VEVLL 393
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
1-404 |
2.34e-67 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 225.09 E-value: 2.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 1 MTESELLVLRSLSEHLDAVLS-LATAPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPG---PW 76
Cdd:PRK14498 1 MKRKIFLTLVSLEEAREILESlLSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASeanPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 77 TFPVIGDIPAGTDVRTP-RRGAALRIMTGAPVPEEPGlAVVPVEHTnIPRGPqslpSSVTIFTAPKPSAHIRMRGEDTAI 155
Cdd:PRK14498 81 RLKLGGEVHAGEAPDVEvEPGEAVEIATGAPIPRGAD-AVVMVEDT-EEVDD----DTVEIYRPVAPGENVRPAGEDIVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 156 GELTVAQGTRIDAATIAALVSTGNATVPVHQPIRVSILATGDELDR--------QIPNSNSPMLAALCQSQGAQTHVLPA 227
Cdd:PRK14498 155 GELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEpgeplkpgKIYDVNSYTLAAAVEEAGGEPVRYGI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 228 TGDTPAA-LRAALEAAKGSNLILTTGGISAGAFDIVRELLSP--DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAF 304
Cdd:PRK14498 235 VPDDEEElEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEElgEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 305 VSFHLFVAPLMRALSGQVPqglDERPQLMASAACEFHADSKRDRFIPVRI-----KYGTTPQAISShrsglGShfVASLA 379
Cdd:PRK14498 315 TIFEEFVAPLLRKLAGLPP---PERATVKARLARRVRSELGREEFVPVSLgrvgdGYVAYPLSRGS-----GA--ITSLV 384
|
410 420
....*....|....*....|....*
gi 2531271090 380 GVTGLAYLPHGTGTTAIGQPVRVLL 404
Cdd:PRK14498 385 RADGFIEIPANTEGLEAGEEVEVEL 409
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
35-178 |
3.88e-33 |
|
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: 121.13 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 35 SDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPGPWTFPVIGDIPAgtdvRTPRRGAALRIMTGAPVPEepGL- 113
Cdd:pfam03453 14 LDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIAAGEPPG----PLLPGGEAVRIMTGAPLPE--GAd 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2531271090 114 AVVPVEHTNIPRGPQslpssVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRIDAATIAALVSTG 178
Cdd:pfam03453 88 AVVMVEDTEEGGGRT-----VEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
188-313 |
2.51e-25 |
|
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: 100.47 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 188 IRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA-LEAAKGSNLILTTGGISAGA 258
Cdd:TIGR00177 1 PRVAVISVGDELveggqplePGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREIlRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2531271090 259 FDIVRELLSP--DVWF-----------GQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAP 313
Cdd:TIGR00177 81 RDVTPEALEElgEKEIpgfgefrmlssLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
192-310 |
6.62e-21 |
|
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: 88.03 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 192 ILATGDEL--DRQIPNSNSPMLAALCQSQGAQT--HVLPATGDTPAA-LRAALEAAKGSNLILTTGGISAGAFDIVRELL 266
Cdd:smart00852 2 IISTGDELlsGGQIRDSNGPMLAALLRELGIEVvrVVVVGGPDDPEAiREALREALAEADVVITTGGTGPGPDDLTPEAL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2531271090 267 SP----DVWFGQVALQPGKPQG---------AGTFDGIPILCLPGNPVSAFVSFHLF 310
Cdd:smart00852 82 AElggrELLGHGVAMRPGGPPGplanlsgtaPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
9-404 |
2.09e-120 |
|
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: 355.17 E-value: 2.09e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 9 LRSLSEHLDAVLSLATaPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPGPWTFPVIGDIPAGT 88
Cdd:COG0303 1 MISVEEALALILAAVR-PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 89 DVRTP-RRGAALRIMTGAPVPEepGL-AVVPVEHTNIPRGpqslpsSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRI 166
Cdd:COG0303 80 PPPGPlGPGEAVRIMTGAPLPE--GAdAVVMQEDTEREGD------RVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 167 DAATIAALVSTGNATVPVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA 238
Cdd:COG0303 152 TPADLGLLASLGIAEVPVYRRPRVAILSTGDELvepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 239 -LEAAKGSNLILTTGGISAGAFDIVRELLSP---DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPL 314
Cdd:COG0303 232 lREALAEADLVITSGGVSVGDYDLVKEALEElgaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 315 MRALSGQVPQgldERPQLMASAACEFHADSKRDRFIPVRIKYGTTPQAISSHRSGlGSHFVASLAGVTGLAYLPHGTGTT 394
Cdd:COG0303 312 LRKLAGLPPP---PPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQ-GSGLLSSLAEADGLIVLPEGVEGV 387
|
410
....*....|
gi 2531271090 395 AIGQPVRVLL 404
Cdd:COG0303 388 EAGEEVEVLL 397
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
14-404 |
1.26e-115 |
|
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: 342.55 E-value: 1.26e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 14 EHLDAVLSLATAPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGpGPWTFPVIGDIPAGTD-VRT 92
Cdd:cd00887 2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAG-ASVTLRVVGEIPAGEPpDGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 93 PRRGAALRIMTGAPVPEepGL-AVVPVEHTNIPRGpqslpsSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRIDAATI 171
Cdd:cd00887 81 LGPGEAVRIMTGAPLPE--GAdAVVMVEDTEEEGG------RVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 172 AALVSTGNATVPVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA-LEAA 242
Cdd:cd00887 153 GLLASLGIAEVPVYRRPRVAIISTGDELvepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREAlEEAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 243 KGSNLILTTGGISAGAFDIVRELLS---PDVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPLMRALS 319
Cdd:cd00887 233 EEADVVITSGGVSVGDYDFVKEVLEelgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 320 GQVPqglDERPQLMASAACEFHADSKRDRFIPVRIKYGTTPQAISSHRSGlGSHFVASLAGVTGLAYLPHGTGTTAIGQP 399
Cdd:cd00887 313 GAPE---PEPPRVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQ-GSGLLSSLARADGLIVIPEGVEGLEAGEE 388
|
....*
gi 2531271090 400 VRVLL 404
Cdd:cd00887 389 VEVLL 393
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
1-404 |
2.34e-67 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 225.09 E-value: 2.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 1 MTESELLVLRSLSEHLDAVLS-LATAPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPG---PW 76
Cdd:PRK14498 1 MKRKIFLTLVSLEEAREILESlLSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASeanPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 77 TFPVIGDIPAGTDVRTP-RRGAALRIMTGAPVPEEPGlAVVPVEHTnIPRGPqslpSSVTIFTAPKPSAHIRMRGEDTAI 155
Cdd:PRK14498 81 RLKLGGEVHAGEAPDVEvEPGEAVEIATGAPIPRGAD-AVVMVEDT-EEVDD----DTVEIYRPVAPGENVRPAGEDIVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 156 GELTVAQGTRIDAATIAALVSTGNATVPVHQPIRVSILATGDELDR--------QIPNSNSPMLAALCQSQGAQTHVLPA 227
Cdd:PRK14498 155 GELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEpgeplkpgKIYDVNSYTLAAAVEEAGGEPVRYGI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 228 TGDTPAA-LRAALEAAKGSNLILTTGGISAGAFDIVRELLSP--DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAF 304
Cdd:PRK14498 235 VPDDEEElEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEElgEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 305 VSFHLFVAPLMRALSGQVPqglDERPQLMASAACEFHADSKRDRFIPVRI-----KYGTTPQAISShrsglGShfVASLA 379
Cdd:PRK14498 315 TIFEEFVAPLLRKLAGLPP---PERATVKARLARRVRSELGREEFVPVSLgrvgdGYVAYPLSRGS-----GA--ITSLV 384
|
410 420
....*....|....*....|....*
gi 2531271090 380 GVTGLAYLPHGTGTTAIGQPVRVLL 404
Cdd:PRK14498 385 RADGFIEIPANTEGLEAGEEVEVEL 409
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
11-403 |
5.22e-48 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 172.49 E-value: 5.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 11 SLSEHLDAVLSLATAPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADfngPGPWTFPVIGDIPAGTDV 90
Cdd:PRK14491 200 SVSQGLDKILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDD---LEPESYTLVGEVLAGHQY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 91 RTP-RRGAALRIMTGAPVPEEpGLAVVPVEHTNIPRGpqslpsSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRIDAA 169
Cdd:PRK14491 277 DGTlQAGEAVRIMTGAPVPAG-ADTVVMRELATQDGD------KVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAP 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 170 TIAALVSTGNATVPVHQPIRVSILATGDEL----DRQIPN----SNSPMLAALCQSQGAQTHVLPATGDTPAALRAA-LE 240
Cdd:PRK14491 350 EQGLLASLGFAEVPVFRRPKVAVFSTGDEVqapgETLKPNciydSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATlEQ 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 241 AAKGSNLILTTGGISAGAFDIVRELLSP--DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPLMRAL 318
Cdd:PRK14491 430 AAAQADVVISSGGVSVGDADYIKTALAKlgQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 319 SGQVPQgldERPQLMASAACEFHADSKRDRFIPVRIKYGTTPQAISSHRSGLGSHFVASLAGVTGLAYLPHGTGTTAIGQ 398
Cdd:PRK14491 510 AGEQNW---QPLLFPAIADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGE 586
|
....*
gi 2531271090 399 PVRVL 403
Cdd:PRK14491 587 TVTIQ 591
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
9-329 |
5.79e-45 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 160.26 E-value: 5.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 9 LRSLSEHLDAVLSLATAPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPGPwtFPVIGDIPAGT 88
Cdd:PRK10680 7 LMSLETALTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQP--LPVAGKAFAGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 89 --DVRTPrRGAALRIMTGAPVPEEPGlAVVPVEHTniprgpqSLPSSVTIFTAP-KPSAHIRMRGEDTAIGELTVAQGTR 165
Cdd:PRK10680 85 pfHGEWP-AGTCIRIMTGAPVPEGCE-AVVMQEQT-------EQTDDGVRFTAEvRSGQNIRRRGEDISQGAVVFPAGTR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 166 IDAATIAALVSTGNATVPVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRA 237
Cdd:PRK10680 156 LTTAELPVLASLGIAEVPVVRKVRVALFSTGDELqlpgqplgDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 238 A-LEAAKGSNLILTTGGISAGAFDIVRELLSP--DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPL 314
Cdd:PRK10680 236 AfIEADSQADVVISSGGVSVGEADYTKTILEElgEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPL 315
|
330
....*....|....*
gi 2531271090 315 MRALSGQVPQGLDER 329
Cdd:PRK10680 316 LAKLSGNTASGLPPR 330
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
27-403 |
1.64e-41 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 151.22 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 27 TPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHAdfNGPGPWTFPVI-GDIPAGT--DVRTPRrGAALRIMT 103
Cdd:PRK14690 40 TDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGA--APEGAQVLPLIeGRAAAGVpfSGRVPE-GMALRILT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 104 GAPVPEepGLAVVPVEHtNIPRGPQSLPssvtiFTAP-KPSAHIRMRGEDTAIGELTVAQGTRIDAATIAALVSTGNATV 182
Cdd:PRK14690 117 GAALPE--GVDTVVLEE-DVAGDGHRIA-----FHGPlKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 183 PVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAALEAAKG-SNLILTTGG 253
Cdd:PRK14690 189 SVRRPLRVAVLSTGDELvepgalaeVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAeADVILTSGG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 254 ISAGAFDIVRELLSP----DVWfgQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPLMRALSGQ---VPQGL 326
Cdd:PRK14690 269 ASAGDEDHVSALLREagamQSW--RIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEgwsEPQGF 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2531271090 327 DerpqlmASAACEFHADSKRDRFIPVRIKYGTTPQAISShrsglGSHFVASLAGVTGLAYLPHGTGTTAIGQPVRVL 403
Cdd:PRK14690 347 T------VPAAFEKRKKPGRREYLRARLRQGHAEVFRSE-----GSGRISGLSWAEGLVELGDGARRIAPGDPVRFI 412
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
11-322 |
9.60e-40 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 150.35 E-value: 9.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 11 SLSEHLDAVLSLATAPTPVTtMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADfngpGPWTFPVIGDIPAGTD- 89
Cdd:PLN02699 9 SVEEALSIVLSVAARLSPVI-VPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASD----GPGEYPVITESRAGNDg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 90 ---VRTPrrGAALRIMTGAPVPEEPGlAVVPVEHTNIPRGPQSLPSSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRI 166
Cdd:PLN02699 84 lgvTLTP--GTVAYVTTGGPIPDGAD-AVVQVEDTEVVEDPLDGSKRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 167 DAATIAALVSTGNATVPVHQPIRVSILATGDELDR---------QIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRA 237
Cdd:PLN02699 161 GASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEpttgtlgrgQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 238 A--LEAAKGSNLILTTGGISAGAFDIVRELLSP--DVWFGQVALQPGKPQGAGTFDGIP---------ILCLPGNPVSAF 304
Cdd:PLN02699 241 IldEAISSGVDILLTSGGVSMGDRDFVKPLLEKrgTVYFSKVLMKPGKPLTFAEIDAKSapsnskkmlAFGLPGNPVSCL 320
|
330
....*....|....*...
gi 2531271090 305 VSFHLFVAPLMRALSGQV 322
Cdd:PLN02699 321 VCFNLFVVPAIRYLAGWS 338
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
35-178 |
3.88e-33 |
|
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: 121.13 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 35 SDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPGPWTFPVIGDIPAgtdvRTPRRGAALRIMTGAPVPEepGL- 113
Cdd:pfam03453 14 LDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIAAGEPPG----PLLPGGEAVRIMTGAPLPE--GAd 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2531271090 114 AVVPVEHTNIPRGPQslpssVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRIDAATIAALVSTG 178
Cdd:pfam03453 88 AVVMVEDTEEGGGRT-----VEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
36-354 |
2.20e-31 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 125.31 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 36 DALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADfngpGPWTFPVIGDIPAG--TDVRTpRRGAALRIMTGAPVPEEpGL 113
Cdd:PRK14497 37 DSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSC----TPGEFKVIDKIGIGefKEIHI-KECEAVEVDTGSMIPMG-AD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 114 AVVPVEHTNIPRGPQSLPSSVTIFtapkpSAHIRMRGEDTAIGELTVAQGTRIDAATIAALVSTGNATVPVHQPIRVSIL 193
Cdd:PRK14497 111 AVIKVENTKVINGNFIKIDKKINF-----GQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPKIYLI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 194 ATGDELDR--------QIPNSNSPMLAALCQSQGAQ----THVlpaTGDTPAALRAALEAAKGSNLILTTGGISAGAFDI 261
Cdd:PRK14497 186 ATGDELVEpgnslspgKIYESNLHYLYSKLKSEGYKivglSLL---SDDKESIKNEIKRAISVADVLILTGGTSAGEKDF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 262 VRELLSPdvwFGQVALQ-----PGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPLMRALSGQVPQGLDErPQLMASA 336
Cdd:PRK14497 263 VHQAIRE---LGNIIVHglkikPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPSRKEILGL-GKIKARL 338
|
330
....*....|....*...
gi 2531271090 337 ACEFHADSKRDRFIPVRI 354
Cdd:PRK14497 339 ALRVKADEHRNTLIPVYL 356
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
188-313 |
2.51e-25 |
|
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: 100.47 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 188 IRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA-LEAAKGSNLILTTGGISAGA 258
Cdd:TIGR00177 1 PRVAVISVGDELveggqplePGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREIlRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2531271090 259 FDIVRELLSP--DVWF-----------GQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAP 313
Cdd:TIGR00177 81 RDVTPEALEElgEKEIpgfgefrmlssLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
192-317 |
9.68e-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: 95.78 E-value: 9.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 192 ILATGDELDR-QIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA-LEAAKGSNLILTTGGISAGAFDIVRELLSP- 268
Cdd:pfam00994 2 IITTGDELLPgQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEAlRAAAEEADVVITTGGTGPGPDDVTPEALAEl 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2531271090 269 --------DVWFGQVALQPGKPQGAGTF-----DGIPILCLPGNPVSAFVSFHLFVAPLMRA 317
Cdd:pfam00994 82 ggrelpgfEELFRGVSLKPGKPVGTAPGailsrAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
192-310 |
6.62e-21 |
|
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: 88.03 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 192 ILATGDEL--DRQIPNSNSPMLAALCQSQGAQT--HVLPATGDTPAA-LRAALEAAKGSNLILTTGGISAGAFDIVRELL 266
Cdd:smart00852 2 IISTGDELlsGGQIRDSNGPMLAALLRELGIEVvrVVVVGGPDDPEAiREALREALAEADVVITTGGTGPGPDDLTPEAL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2531271090 267 SP----DVWFGQVALQPGKPQG---------AGTFDGIPILCLPGNPVSAFVSFHLF 310
Cdd:smart00852 82 AElggrELLGHGVAMRPGGPPGplanlsgtaPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
189-314 |
6.33e-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: 82.39 E-value: 6.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 189 RVSILATGDELDR-QIPNSNSPMLAALCQSQGAQTHVLPATGDTPAA-LRAALEAAKGSNLILTTGGISAGAFDIVRELL 266
Cdd:cd00758 1 RVAIVTVSDELSQgQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSiRAALIEASREADLVLTTGGTGVGRRDVTPEAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2531271090 267 SP----DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPL 314
Cdd:cd00758 81 AElgerEAHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPA 132
|
|
|