|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
1-411 |
0e+00 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 878.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 1 MEFTAGLMPLETALTQMLSRITPLTAFETLPLVHCFGRILANDVVSPLDVPGFDNAAMDGYAVRLADLTAGQPLPVAGKA 80
Cdd:PRK10680 1 MEFTAGLMSLETALTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 81 FAGQPFQGEWPAGACIRIMTGAPVPAGCEAVVMQEQTEQTDEGIRFTADVRNGQNIRRRGEDITHDAVVFPAGTRLTTAE 160
Cdd:PRK10680 81 FAGQPFHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 161 LPVLASLGIAEAQVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEA 240
Cdd:PRK10680 161 LPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 241 DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLS 320
Cdd:PRK10680 241 DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 321 GNIASGLPARQRVRTASRLKKTPGRLDFQRGILQRTADGELEVTTTGHQGSHIFSSFSMGNCFIVLERDRGNVDAGEWVE 400
Cdd:PRK10680 321 GNTASGLPPRQRVRTASRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEVGEWVE 400
|
410
....*....|.
gi 501082573 401 VEPFNALFGGL 411
Cdd:PRK10680 401 VEPFNALFGGL 411
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
7-407 |
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: 559.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 7 LMPLETALTQMLSRITPLTAfETLPLVHCFGRILANDVVSPLDVPGFDNAAMDGYAVRLADLTAGQP--LPVAGKAFAGQ 84
Cdd:COG0303 1 MISVEEALALILAAVRPLGT-ETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 85 PFQGEWPAGACIRIMTGAPVPAGCEAVVMQEQTEQTDEGIRFTADVRNGQNIRRRGEDITHDAVVFPAGTRLTTAELPVL 164
Cdd:COG0303 80 PPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 165 ASLGIAEAQVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEADSQA 244
Cdd:COG0303 160 ASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 245 DVVISSGGVSVGEADYTKTILEELG-EIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGnI 323
Cdd:COG0303 240 DLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAG-L 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 324 ASGLPARQRVRTASRLKKTPGRLDFQRGILQRTaDGELEVTTTGHQGSHIFSSFSMGNCFIVLERDRGNVDAGEWVEVEP 403
Cdd:COG0303 319 PPPPPPRVRARLAEDLPKKPGRTEFLRVRLERD-DGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLL 397
|
....
gi 501082573 404 FNAL 407
Cdd:COG0303 398 LDGL 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
13-404 |
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: 520.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 13 ALTQMLSRITPLTAFETLPLVHCFGRILANDVVSPLDVPGFDNAAMDGYAVRLADL-TAGQPLPVAGKAFAGQPFQGEWP 91
Cdd:cd00887 3 AARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTaGASVTLRVVGEIPAGEPPDGPLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 92 AGACIRIMTGAPVPAGCEAVVMQEQTEQTDEGIRFTADVRNGQNIRRRGEDITHDAVVFPAGTRLTTAELPVLASLGIAE 171
Cdd:cd00887 83 PGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 172 AQVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEADSQADVVISSG 251
Cdd:cd00887 163 VPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 252 GVSVGEADYTKTILEEL-GEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNIASGLPaR 330
Cdd:cd00887 243 GVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPP-R 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501082573 331 QRVRTASRLKKTPGRLDFQRGILQRTaDGELEVTTTGHQGSHIFSSFSMGNCFIVLERDRGNVDAGEWVEVEPF 404
Cdd:cd00887 322 VKARLAEDLKSKPGRREFLRVRLERD-EGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
28-168 |
9.67e-53 |
|
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: 172.75 E-value: 9.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 28 ETLPL--VHCFGRILANDVVSPLDVPGFDNAAMDGYAVRLADltaGQPLPVAGKAFAGQPFQGEWPAGACIRIMTGAPVP 105
Cdd:pfam03453 7 ETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAAD---GFGASEVNPIAAGEPPGPLLPGGEAVRIMTGAPLP 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501082573 106 AGCEAVVMQEQTEQTDEG-IRFTADVRNGQNIRRRGEDITHDAVVFPAGTRLTTAELPVLASLG 168
Cdd:pfam03453 84 EGADAVVMVEDTEEGGGRtVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
178-314 |
8.49e-46 |
|
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: 154.78 E-value: 8.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 178 VRVALFSTGDELQLPGQPLGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEADSQADVVISSGGVSVGE 257
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501082573 258 ADYTKTILEELGEIAFWKL-----------AIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQP 314
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGFgefrmlsslpvLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
181-308 |
1.99e-31 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 116.53 E-value: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 181 ALFSTGDELQLPGQplgdgqIYDTNRLTVHLMLEQLGCEVINLGII--RDNPQQLRAAFIEADSQADVVISSGGVSVGEA 258
Cdd:smart00852 1 AIISTGDELLSGGQ------IRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501082573 259 DYTKTILEELG--EIAFWKLAIKPGKPFAF---------GKLSNSWFCGLPGNPVSAALTF 308
Cdd:smart00852 75 DLTPEALAELGgrELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMF 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
1-411 |
0e+00 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 878.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 1 MEFTAGLMPLETALTQMLSRITPLTAFETLPLVHCFGRILANDVVSPLDVPGFDNAAMDGYAVRLADLTAGQPLPVAGKA 80
Cdd:PRK10680 1 MEFTAGLMSLETALTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 81 FAGQPFQGEWPAGACIRIMTGAPVPAGCEAVVMQEQTEQTDEGIRFTADVRNGQNIRRRGEDITHDAVVFPAGTRLTTAE 160
Cdd:PRK10680 81 FAGQPFHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 161 LPVLASLGIAEAQVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEA 240
Cdd:PRK10680 161 LPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 241 DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLS 320
Cdd:PRK10680 241 DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 321 GNIASGLPARQRVRTASRLKKTPGRLDFQRGILQRTADGELEVTTTGHQGSHIFSSFSMGNCFIVLERDRGNVDAGEWVE 400
Cdd:PRK10680 321 GNTASGLPPRQRVRTASRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEVGEWVE 400
|
410
....*....|.
gi 501082573 401 VEPFNALFGGL 411
Cdd:PRK10680 401 VEPFNALFGGL 411
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
7-407 |
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: 559.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 7 LMPLETALTQMLSRITPLTAfETLPLVHCFGRILANDVVSPLDVPGFDNAAMDGYAVRLADLTAGQP--LPVAGKAFAGQ 84
Cdd:COG0303 1 MISVEEALALILAAVRPLGT-ETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 85 PFQGEWPAGACIRIMTGAPVPAGCEAVVMQEQTEQTDEGIRFTADVRNGQNIRRRGEDITHDAVVFPAGTRLTTAELPVL 164
Cdd:COG0303 80 PPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 165 ASLGIAEAQVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEADSQA 244
Cdd:COG0303 160 ASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 245 DVVISSGGVSVGEADYTKTILEELG-EIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGnI 323
Cdd:COG0303 240 DLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAG-L 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 324 ASGLPARQRVRTASRLKKTPGRLDFQRGILQRTaDGELEVTTTGHQGSHIFSSFSMGNCFIVLERDRGNVDAGEWVEVEP 403
Cdd:COG0303 319 PPPPPPRVRARLAEDLPKKPGRTEFLRVRLERD-DGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLL 397
|
....
gi 501082573 404 FNAL 407
Cdd:COG0303 398 LDGL 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
13-404 |
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: 520.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 13 ALTQMLSRITPLTAFETLPLVHCFGRILANDVVSPLDVPGFDNAAMDGYAVRLADL-TAGQPLPVAGKAFAGQPFQGEWP 91
Cdd:cd00887 3 AARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTaGASVTLRVVGEIPAGEPPDGPLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 92 AGACIRIMTGAPVPAGCEAVVMQEQTEQTDEGIRFTADVRNGQNIRRRGEDITHDAVVFPAGTRLTTAELPVLASLGIAE 171
Cdd:cd00887 83 PGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 172 AQVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEADSQADVVISSG 251
Cdd:cd00887 163 VPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 252 GVSVGEADYTKTILEEL-GEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNIASGLPaR 330
Cdd:cd00887 243 GVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPP-R 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501082573 331 QRVRTASRLKKTPGRLDFQRGILQRTaDGELEVTTTGHQGSHIFSSFSMGNCFIVLERDRGNVDAGEWVEVEPF 404
Cdd:cd00887 322 VKARLAEDLKSKPGRREFLRVRLERD-EGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
2-407 |
7.14e-162 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 467.94 E-value: 7.14e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 2 EFTAGLMPLETALTQMLSRITPLTAFETLPLVHCFGRILANDVVSPLDVPGFDNAAMDGYAVRLADLTAGqPLPVAGKAF 81
Cdd:PRK14491 193 LLSPAFLSVSQGLDKILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPE-SYTLVGEVL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 82 AGQPFQGEWPAGACIRIMTGAPVPAGCEAVVMQEQTEQTDEGIRFTADVRNGQNIRRRGEDITHDAVVFPAGTRLTTAEL 161
Cdd:PRK14491 272 AGHQYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQ 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 162 PVLASLGIAEAQVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEAD 241
Cdd:PRK14491 352 GLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 242 SQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSG 321
Cdd:PRK14491 432 AQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKLAG 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 322 NI---ASGLPArqrvRTASRLKKTPGRLDFQRGILQRTADGELEVTTTGHQGSHIFSSFSMGNCFIVLERDRGNVDAGEW 398
Cdd:PRK14491 512 EQnwqPLLFPA----IADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGET 587
|
....*....
gi 501082573 399 VEVEPFNAL 407
Cdd:PRK14491 588 VTIQPLAGL 596
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
7-404 |
5.60e-111 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 338.73 E-value: 5.60e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 7 LMPLETALTQMLSRITPLT-AFETLPLVHCFGRILANDVVSPLDVPGFDNAAMDGYAVRLADlTAG----QP--LPVAGK 79
Cdd:PRK14498 9 LVSLEEAREILESLLSELPlGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAAD-TFGaseaNPvrLKLGGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 80 AFAGQPFQGEWPAGACIRIMTGAPVPAGCEAVVMQEQTEQTDEG-IRFTADVRNGQNIRRRGEDITHDAVVFPAGTRLTT 158
Cdd:PRK14498 88 VHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDtVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 159 AELPVLASLGIAEAQVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFI 238
Cdd:PRK14498 168 RDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 239 EADSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAK 318
Cdd:PRK14498 248 KALKECDLVLLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLRK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 319 LsgniaSGLPARQR----VRTASRLKKTPGRLDFQRGILQRTADGeLEVTTTGhQGSHIFSSFSMGNCFIVLERDRGNVD 394
Cdd:PRK14498 328 L-----AGLPPPERatvkARLARRVRSELGREEFVPVSLGRVGDG-YVAYPLS-RGSGAITSLVRADGFIEIPANTEGLE 400
|
410
....*....|
gi 501082573 395 AGEWVEVEPF 404
Cdd:PRK14498 401 AGEEVEVELF 410
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
9-404 |
4.81e-80 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 252.53 E-value: 4.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 9 PLETALTQMLSRITPLTAFETLPLVHCFGRILANDVVSPLDVPGFDNAAMDGYAVRLADLTAGQPLPV-AGKAFAGQPFQ 87
Cdd:PRK14690 24 PVDTALDLLRARLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQVLPLiEGRAAAGVPFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 88 GEWPAGACIRIMTGAPVPAGCEAVVMQEQTEQTDEGIRFTADVRNGQNIRRRGEDITHDAVVFPAGTRLTTAELPVLASL 167
Cdd:PRK14690 104 GRVPEGMALRILTGAALPEGVDTVVLEEDVAGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 168 GIAEAQVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEADSQADVV 247
Cdd:PRK14690 184 GLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 248 ISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNIASgL 327
Cdd:PRK14690 264 LTSGGASAGDEDHVSALLREAGAMQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEGWS-E 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501082573 328 PARQRVRTASRLKKTPGRLDFQRGilqRTADGELEVTTTghQGSHIFSSFSMGNCFIVLERDRGNVDAGEWVEVEPF 404
Cdd:PRK14690 343 PQGFTVPAAFEKRKKPGRREYLRA---RLRQGHAEVFRS--EGSGRISGLSWAEGLVELGDGARRIAPGDPVRFIPY 414
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
1-399 |
3.27e-68 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 228.16 E-value: 3.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 1 MEFTAGLMPLETALTQMLS---RITPLTafetLPLVHCFGRILANDVVSPLDVPGFDNAAMDGYAVRLADlTAGQpLPVA 77
Cdd:PLN02699 1 GGGKTEMISVEEALSIVLSvaaRLSPVI----VPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASD-GPGE-YPVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 78 GKAFAGQPFQG-EWPAGACIRIMTGAPVPAGCEAVVMQEQTEQTDEG------IRFTADVRNGQNIRRRGEDITHDAVVF 150
Cdd:PLN02699 75 TESRAGNDGLGvTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPldgskrVRILSQASKGQDIRPVGCDIEKDAKVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 151 PAGTRLTTAELPVLASLGIAEAQVVRKVRVALFSTGDELQLPGQP-LGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDN 229
Cdd:PLN02699 155 KAGERLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 230 PQQLRAAFIEA-DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKL---------SNSWFCGLPG 299
Cdd:PLN02699 235 EEELERILDEAiSSGVDILLTSGGVSMGDRDFVKPLLEKRGTVYFSKVLMKPGKPLTFAEIdaksapsnsKKMLAFGLPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 300 NPVSAALTFYQLVQPLLAKLSGnIASGLPARQRVRTASRLKKTPGRLDFQRGILQ-RTADGELE----VTTTGHQGSHIF 374
Cdd:PLN02699 315 NPVSCLVCFNLFVVPAIRYLAG-WSNPHLLRVQARLREPIKLDPVRPEFHRAIIRwKLNDGSGNpgfvAESTGHQMSSRL 393
|
410 420
....*....|....*....|....*
gi 501082573 375 SSFSMGNCFIVLERDRGNVDAGEWV 399
Cdd:PLN02699 394 LSMKSANALLELPATGNVLSAGTSV 418
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
7-321 |
2.73e-59 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 201.96 E-value: 2.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 7 LMPLETALTQMLSRITPLTAFETLPLVHCFGRILANDVVSPLDVPGFDNAAMDGYAVRlADLTAGQpLPVAGKAFAGQPF 86
Cdd:PRK14497 10 LYSIDEAIKVFLSSLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALK-SSCTPGE-FKVIDKIGIGEFK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 87 QGEWPAGACIRIMTGAPVPAGCEAVVMQEQTEqTDEG--IRFTADVRNGQNIRRRGEDITHDAVVFPAGTRLTTAELPVL 164
Cdd:PRK14497 88 EIHIKECEAVEVDTGSMIPMGADAVIKVENTK-VINGnfIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 165 ASLGIAEAQVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEADSQA 244
Cdd:PRK14497 167 ASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVA 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501082573 245 DVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSG 321
Cdd:PRK14497 247 DVLILTGGTSAGEKDFVHQAIRELGNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYP 323
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
28-168 |
9.67e-53 |
|
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: 172.75 E-value: 9.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 28 ETLPL--VHCFGRILANDVVSPLDVPGFDNAAMDGYAVRLADltaGQPLPVAGKAFAGQPFQGEWPAGACIRIMTGAPVP 105
Cdd:pfam03453 7 ETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAAD---GFGASEVNPIAAGEPPGPLLPGGEAVRIMTGAPLP 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501082573 106 AGCEAVVMQEQTEQTDEG-IRFTADVRNGQNIRRRGEDITHDAVVFPAGTRLTTAELPVLASLG 168
Cdd:pfam03453 84 EGADAVVMVEDTEEGGGRtVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
178-314 |
8.49e-46 |
|
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: 154.78 E-value: 8.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 178 VRVALFSTGDELQLPGQPLGDGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEADSQADVVISSGGVSVGE 257
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501082573 258 ADYTKTILEELGEIAFWKL-----------AIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQP 314
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGFgefrmlsslpvLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
179-316 |
3.92e-42 |
|
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: 144.79 E-value: 3.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 179 RVALFSTGDELQLpgqplgdGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEADSQADVVISSGGVSVGEA 258
Cdd:cd00758 1 RVAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 259 DYTKTILEELGEIAFW--KLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLL 316
Cdd:cd00758 74 DVTPEALAELGEREAHgkGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
181-318 |
3.82e-32 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 118.51 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 181 ALFSTGDELqLPGQplgdgqIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEADSQADVVISSGGVSVGEADY 260
Cdd:pfam00994 1 AIITTGDEL-LPGQ------IRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 261 TKTILEELGE-------IAFWKLAIKPGKPFAFGK---LSNSWFC--GLPGNPVSAALTFYQLVQPLLAK 318
Cdd:pfam00994 74 TPEALAELGGrelpgfeELFRGVSLKPGKPVGTAPgaiLSRAGKTvfGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
181-308 |
1.99e-31 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 116.53 E-value: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 181 ALFSTGDELQLPGQplgdgqIYDTNRLTVHLMLEQLGCEVINLGII--RDNPQQLRAAFIEADSQADVVISSGGVSVGEA 258
Cdd:smart00852 1 AIISTGDELLSGGQ------IRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501082573 259 DYTKTILEELG--EIAFWKLAIKPGKPFAF---------GKLSNSWFCGLPGNPVSAALTF 308
Cdd:smart00852 75 DLTPEALAELGgrELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMF 135
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
332-404 |
1.64e-21 |
|
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: 87.67 E-value: 1.64e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501082573 332 RVRTASRLKKTPGRLDFQRGILqRTADGELEVTTTGHQGSHIFSSFSMGNCFIVLERDRGNVDAGEWVEVEPF 404
Cdd:pfam03454 1 KARLARDLKSDPGRREFVRVRL-HEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
179-252 |
3.64e-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: 52.49 E-value: 3.64e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501082573 179 RVALFSTGDELQLpgqplgdGQIYDTNrlTVHL--MLEQLGCEVINLGIIRDNPQQLRAAFIEADSQADVVISSGG 252
Cdd:cd00885 1 TAEIIAIGDELLS-------GQIVDTN--AAFLakELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
152-319 |
1.68e-06 |
|
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: 49.47 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 152 AGTR---LTTAELPVLASLGIAEAQVV------RKVRVALFSTGDElqlPGQplgdGQIYDTNRLTVHLMLEQLGCEVIN 222
Cdd:cd03522 125 ATVKiipLAVPEALVERAEALARDGPLlrvapfRPLRVGLIVTGSE---VYG----GRIEDKFGPVLRARLAALGVELVE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 223 LGIIRDNPQQLRAAFIEADSQ-ADVVISSGGVSVGEADYTKTILEELG-EIAFWKLAIKPGKPFAFGKLSNSWFCGLPGN 300
Cdd:cd03522 198 QVIVPHDEAAIAAAIAEALEAgAELLILTGGASVDPDDVTPAAIRAAGgEVIRYGMPVDPGNLLLLGYLGGVPVIGLPGC 277
|
170 180
....*....|....*....|
gi 501082573 301 PVSAALTFYQLVQP-LLAKL 319
Cdd:cd03522 278 ARSPKLNGFDLVLPrLLAGE 297
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
179-270 |
9.20e-05 |
|
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 161761 [Multi-domain] Cd Length: 413 Bit Score: 44.51 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 179 RVALFSTGDELQLpgqplgdGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEADSQADVVISSGGVSVGEA 258
Cdd:TIGR00200 2 KAEIISVGDELLL-------GQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSD 74
|
90
....*....|...
gi 501082573 259 DYTK-TILEELGE 270
Cdd:TIGR00200 75 DLTAeTIATAKGE 87
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
212-261 |
1.92e-04 |
|
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: 41.64 E-value: 1.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 501082573 212 MLEQLGCEVINLGIIRDNPQQLRAAFIE--ADSQADVVISSGGVSVGEADYT 261
Cdd:COG0521 37 LLEEAGHEVVARRIVPDDKDAIRAALREliDDEGVDLVLTTGGTGLSPRDVT 88
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
212-252 |
7.00e-04 |
|
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: 39.77 E-value: 7.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 501082573 212 MLEQLGCEVINLGIIRDNPQQLRAAFIEA--DSQADVVISSGG 252
Cdd:cd00886 28 LLEEAGHEVVAYEIVPDDKDEIREALIEWadEDGVDLILTTGG 70
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
184-269 |
1.08e-03 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 40.93 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501082573 184 STGDELQLpgqplgdGQIYDTNRLTVHLMLEQLGCEVINLGIIRDNPQQLRAAFIEADSQADVVISSGGVSVGEADYTK- 262
Cdd:PRK00549 7 AVGTELLL-------GQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLGPTKDDLTKe 79
|
....*..
gi 501082573 263 TILEELG 269
Cdd:PRK00549 80 TVAKFLG 86
|
|
| |
