|
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: 877.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 1 MEFSAGLMPLETALTQMLSRITPLTAVETLPLVNCFGRILATDIVSPLDVPGFDNSAMDGYAVRVADLSADKPLPVAGKA 80
Cdd:PRK10680 1 MEFTAGLMSLETALTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 81 FAGQPYQGEWPAGTCIRIMTGAPVPAGCEAVVMQEQTEQTDDGVRFTADVRCGQNIRRRGEDIRQDAVVFPAGTRLTTAE 160
Cdd:PRK10680 81 FAGQPFHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 161 LPVLASLGIADAQVVRKVRVALFSTGDELQLPGQPLEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDA 240
Cdd:PRK10680 161 LPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 241 DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLG 320
Cdd:PRK10680 241 DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 321 GNTASAVPPRQRVRTASRLKKTPGRLDFQRGILQRSANGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEPGEWVE 400
Cdd:PRK10680 321 GNTASGLPPRQRVRTASRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEVGEWVE 400
|
410
....*....|.
gi 1385497867 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: 568.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 7 LMPLETALTQMLSRITPLtAVETLPLVNCFGRILATDIVSPLDVPGFDNSAMDGYAVRVADLSADKP--LPVAGKAFAGQ 84
Cdd:COG0303 1 MISVEEALALILAAVRPL-GTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 85 PYQGEWPAGTCIRIMTGAPVPAGCEAVVMQEQTEQTDDGVRFTADVRCGQNIRRRGEDIRQDAVVFPAGTRLTTAELPVL 164
Cdd:COG0303 80 PPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 165 ASLGIADAQVVRKVRVALFSTGDELQLPGQPLEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQA 244
Cdd:COG0303 160 ASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 245 DVVISSGGVSVGEADYTKTILEELG-EIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLGGNT 323
Cdd:COG0303 240 DLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 324 ASAvPPRQRVRTASRLKKTPGRLDFQRGILQRSaNGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEPGEWVEVEP 403
Cdd:COG0303 320 PPP-PPRVRARLAEDLPKKPGRTEFLRVRLERD-DGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLL 397
|
....
gi 1385497867 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: 532.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 13 ALTQMLSRITPLTAVETLPLVNCFGRILATDIVSPLDVPGFDNSAMDGYAVRVADL-SADKPLPVAGKAFAGQPYQGEWP 91
Cdd:cd00887 3 AARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTaGASVTLRVVGEIPAGEPPDGPLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 92 AGTCIRIMTGAPVPAGCEAVVMQEQTEQTDDGVRFTADVRCGQNIRRRGEDIRQDAVVFPAGTRLTTAELPVLASLGIAD 171
Cdd:cd00887 83 PGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 172 AQVVRKVRVALFSTGDELQLPGQPLEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQADVVISSG 251
Cdd:cd00887 163 VPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 252 GVSVGEADYTKTILEEL-GEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLGGNTASAvPPR 330
Cdd:cd00887 243 GVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPE-PPR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1385497867 331 QRVRTASRLKKTPGRLDFQRGILQRSaNGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEPGEWVEVEPF 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 ... |
23-168 |
2.79e-56 |
|
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: 182.00 E-value: 2.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 23 PLTAVETLPL--VNCFGRILATDIVSPLDVPGFDNSAMDGYAVRVADLSADKPLpvaGKAFAGQPYQGEWPAGTCIRIMT 100
Cdd:pfam03453 2 LLGTEETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEV---NPIAAGEPPGPLLPGGEAVRIMT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1385497867 101 GAPVPAGCEAVVMQEQTEQTDDG-VRFTADVRCGQNIRRRGEDIRQDAVVFPAGTRLTTAELPVLASLG 168
Cdd:pfam03453 79 GAPLPEGADAVVMVEDTEEGGGRtVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
178-314 |
6.50e-48 |
|
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: 160.17 E-value: 6.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 178 VRVALFSTGDELQLPGQPLEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQADVVISSGGVSVGE 257
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1385497867 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 |
1.44e-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 trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 119.62 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 181 ALFSTGDELqlpgqpLEAGQIYDTNRLTIHLMLQQLGCEVINLGII--PDDPGKLRAAFIDADSQADVVISSGGVSVGEA 258
Cdd:smart00852 1 AIISTGDEL------LSGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1385497867 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: 877.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 1 MEFSAGLMPLETALTQMLSRITPLTAVETLPLVNCFGRILATDIVSPLDVPGFDNSAMDGYAVRVADLSADKPLPVAGKA 80
Cdd:PRK10680 1 MEFTAGLMSLETALTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 81 FAGQPYQGEWPAGTCIRIMTGAPVPAGCEAVVMQEQTEQTDDGVRFTADVRCGQNIRRRGEDIRQDAVVFPAGTRLTTAE 160
Cdd:PRK10680 81 FAGQPFHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 161 LPVLASLGIADAQVVRKVRVALFSTGDELQLPGQPLEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDA 240
Cdd:PRK10680 161 LPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 241 DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLG 320
Cdd:PRK10680 241 DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 321 GNTASAVPPRQRVRTASRLKKTPGRLDFQRGILQRSANGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEPGEWVE 400
Cdd:PRK10680 321 GNTASGLPPRQRVRTASRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEVGEWVE 400
|
410
....*....|.
gi 1385497867 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: 568.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 7 LMPLETALTQMLSRITPLtAVETLPLVNCFGRILATDIVSPLDVPGFDNSAMDGYAVRVADLSADKP--LPVAGKAFAGQ 84
Cdd:COG0303 1 MISVEEALALILAAVRPL-GTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 85 PYQGEWPAGTCIRIMTGAPVPAGCEAVVMQEQTEQTDDGVRFTADVRCGQNIRRRGEDIRQDAVVFPAGTRLTTAELPVL 164
Cdd:COG0303 80 PPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 165 ASLGIADAQVVRKVRVALFSTGDELQLPGQPLEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQA 244
Cdd:COG0303 160 ASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 245 DVVISSGGVSVGEADYTKTILEELG-EIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLGGNT 323
Cdd:COG0303 240 DLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 324 ASAvPPRQRVRTASRLKKTPGRLDFQRGILQRSaNGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEPGEWVEVEP 403
Cdd:COG0303 320 PPP-PPRVRARLAEDLPKKPGRTEFLRVRLERD-DGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLL 397
|
....
gi 1385497867 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: 532.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 13 ALTQMLSRITPLTAVETLPLVNCFGRILATDIVSPLDVPGFDNSAMDGYAVRVADL-SADKPLPVAGKAFAGQPYQGEWP 91
Cdd:cd00887 3 AARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTaGASVTLRVVGEIPAGEPPDGPLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 92 AGTCIRIMTGAPVPAGCEAVVMQEQTEQTDDGVRFTADVRCGQNIRRRGEDIRQDAVVFPAGTRLTTAELPVLASLGIAD 171
Cdd:cd00887 83 PGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 172 AQVVRKVRVALFSTGDELQLPGQPLEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQADVVISSG 251
Cdd:cd00887 163 VPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 252 GVSVGEADYTKTILEEL-GEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLGGNTASAvPPR 330
Cdd:cd00887 243 GVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPE-PPR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1385497867 331 QRVRTASRLKKTPGRLDFQRGILQRSaNGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEPGEWVEVEPF 404
Cdd:cd00887 322 VKARLAEDLKSKPGRREFLRVRLERD-EGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
2-407 |
9.33e-171 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 490.67 E-value: 9.33e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 2 EFSAGLMPLETALTQMLSRITPLTAVETLPLVNCFGRILATDIVSPLDVPGFDNSAMDGYAVRVADLSADkPLPVAGKAF 81
Cdd:PRK14491 193 LLSPAFLSVSQGLDKILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPE-SYTLVGEVL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 82 AGQPYQGEWPAGTCIRIMTGAPVPAGCEAVVMQEQTEQTDDGVRFTADVRCGQNIRRRGEDIRQDAVVFPAGTRLTTAEL 161
Cdd:PRK14491 272 AGHQYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQ 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 162 PVLASLGIADAQVVRKVRVALFSTGDELQLPGQPLEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDAD 241
Cdd:PRK14491 352 GLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 242 SQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLGG 321
Cdd:PRK14491 432 AQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKLAG 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 322 NTASAvPPRQRVRTASRLKKTPGRLDFQRGILQRSANGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEPGEWVEV 401
Cdd:PRK14491 512 EQNWQ-PLLFPAIADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGETVTI 590
|
....*.
gi 1385497867 402 EPFNAL 407
Cdd:PRK14491 591 QPLAGL 596
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
7-404 |
5.49e-116 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 351.82 E-value: 5.49e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 7 LMPLETALTQMLSRITPLT-AVETLPLVNCFGRILATDIVSPLDVPGFDNSAMDGYAVRVADL---SADKP--LPVAGKA 80
Cdd:PRK14498 9 LVSLEEAREILESLLSELPlGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTfgaSEANPvrLKLGGEV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 81 FAGQPYQGEWPAGTCIRIMTGAPVPAGCEAVVMQEQTEQTDDG-VRFTADVRCGQNIRRRGEDIRQDAVVFPAGTRLTTA 159
Cdd:PRK14498 89 HAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDtVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 160 ELPVLASLGIADAQVVRKVRVALFSTGDELQLPGQPLEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFID 239
Cdd:PRK14498 169 DIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 240 ADSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKL 319
Cdd:PRK14498 249 ALKECDLVLLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLRKL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 320 GGntasaVPPRQR----VRTASRLKKTPGRLDFQRGILQRSANGeLEVTTTGhQGSHIFSSFSLGNCFIVLERERGNVEP 395
Cdd:PRK14498 329 AG-----LPPPERatvkARLARRVRSELGREEFVPVSLGRVGDG-YVAYPLS-RGSGAITSLVRADGFIEIPANTEGLEA 401
|
....*....
gi 1385497867 396 GEWVEVEPF 404
Cdd:PRK14498 402 GEEVEVELF 410
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
9-404 |
5.38e-81 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 255.23 E-value: 5.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 9 PLETALTQMLSRITPLTAVETLPLVNCFGRILATDIVSPLDVPGFDNSAMDGYAVRVADLSADKPLPV-AGKAFAGQPYQ 87
Cdd:PRK14690 24 PVDTALDLLRARLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQVLPLiEGRAAAGVPFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 88 GEWPAGTCIRIMTGAPVPAGCEAVVMQEQTEQTDDGVRFTADVRCGQNIRRRGEDIRQDAVVFPAGTRLTTAELPVLASL 167
Cdd:PRK14690 104 GRVPEGMALRILTGAALPEGVDTVVLEEDVAGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 168 GIADAQVVRKVRVALFSTGDELQLPGQPLEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQADVV 247
Cdd:PRK14690 184 GLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 248 ISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLGGNTASaV 327
Cdd:PRK14690 264 LTSGGASAGDEDHVSALLREAGAMQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEGWS-E 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1385497867 328 PPRQRVRTASRLKKTPGRLDFQRGilqRSANGELEVTTTghQGSHIFSSFSLGNCFIVLERERGNVEPGEWVEVEPF 404
Cdd:PRK14690 343 PQGFTVPAAFEKRKKPGRREYLRA---RLRQGHAEVFRS--EGSGRISGLSWAEGLVELGDGARRIAPGDPVRFIPY 414
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
1-371 |
7.53e-68 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 227.00 E-value: 7.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 1 MEFSAGLMPLETALTQMLSRITPLTAVeTLPLVNCFGRILATDIVSPLDVPGFDNSAMDGYAVrvadLSADKP--LPVAG 78
Cdd:PLN02699 1 GGGKTEMISVEEALSIVLSVAARLSPV-IVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAV----VASDGPgeYPVIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 79 KAFAGQPYQG-EWPAGTCIRIMTGAPVPAGCEAVVMQEQTEQTDDG------VRFTADVRCGQNIRRRGEDIRQDAVVFP 151
Cdd:PLN02699 76 ESRAGNDGLGvTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPldgskrVRILSQASKGQDIRPVGCDIEKDAKVLK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 152 AGTRLTTAELPVLASLGIADAQVVRKVRVALFSTGDELQLPGQP-LEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDP 230
Cdd:PLN02699 156 AGERLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 231 GKLRAAFIDA-DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKL---------SNSWFCGLPGN 300
Cdd:PLN02699 236 EELERILDEAiSSGVDILLTSGGVSMGDRDFVKPLLEKRGTVYFSKVLMKPGKPLTFAEIdaksapsnsKKMLAFGLPGN 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1385497867 301 PVSAALTFYQLVQPLLAKLGGnTASAVPPRQRVRTASRLKKTPGRLDFQRGILQRSAN-GELE----VTTTGHQGS 371
Cdd:PLN02699 316 PVSCLVCFNLFVVPAIRYLAG-WSNPHLLRVQARLREPIKLDPVRPEFHRAIIRWKLNdGSGNpgfvAESTGHQMS 390
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
7-401 |
6.61e-61 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 206.20 E-value: 6.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 7 LMPLETALTQMLSRITPLTAVETLPLVNCFGRILATDIVSPLDVPGFDNSAMDGYAVRvadlSADKP--LPVAGKAFAGQ 84
Cdd:PRK14497 10 LYSIDEAIKVFLSSLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALK----SSCTPgeFKVIDKIGIGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 85 PYQGEWPAGTCIRIMTGAPVPAGCEAVVMQEQTEQTD-DGVRFTADVRCGQNIRRRGEDIRQDAVVFPAGTRLTTAELPV 163
Cdd:PRK14497 86 FKEIHIKECEAVEVDTGSMIPMGADAVIKVENTKVINgNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 164 LASLGIADAQVVRKVRVALFSTGDELQLPGQPLEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQ 243
Cdd:PRK14497 166 LASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 244 ADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLGGN- 322
Cdd:PRK14497 246 ADVLILTGGTSAGEKDFVHQAIRELGNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPSr 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1385497867 323 TASAVPPRQRVRTASRLKKTPGRLDFQRGILQRSANGELEVTTTGHqgSHIFSSFSLGNCFIVLERERgNVEPGEWVEV 401
Cdd:PRK14497 326 KEILGLGKIKARLALRVKADEHRNTLIPVYLFKSDNSYYALPVPFD--SYMVGTFSLTDGYIMLGPNE-EIEEGKEVEV 401
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
23-168 |
2.79e-56 |
|
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: 182.00 E-value: 2.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 23 PLTAVETLPL--VNCFGRILATDIVSPLDVPGFDNSAMDGYAVRVADLSADKPLpvaGKAFAGQPYQGEWPAGTCIRIMT 100
Cdd:pfam03453 2 LLGTEETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEV---NPIAAGEPPGPLLPGGEAVRIMT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1385497867 101 GAPVPAGCEAVVMQEQTEQTDDG-VRFTADVRCGQNIRRRGEDIRQDAVVFPAGTRLTTAELPVLASLG 168
Cdd:pfam03453 79 GAPLPEGADAVVMVEDTEEGGGRtVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
178-314 |
6.50e-48 |
|
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: 160.17 E-value: 6.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 178 VRVALFSTGDELQLPGQPLEAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQADVVISSGGVSVGE 257
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1385497867 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 |
1.42e-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: 145.95 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 179 RVALFSTGDELQLpgqpleaGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQADVVISSGGVSVGEA 258
Cdd:cd00758 1 RVAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 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 |
5.25e-33 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 120.82 E-value: 5.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 181 ALFSTGDELqLPGQpleagqIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQADVVISSGGVSVGEADY 260
Cdd:pfam00994 1 AIITTGDEL-LPGQ------IRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 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 |
1.44e-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 trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 119.62 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 181 ALFSTGDELqlpgqpLEAGQIYDTNRLTIHLMLQQLGCEVINLGII--PDDPGKLRAAFIDADSQADVVISSGGVSVGEA 258
Cdd:smart00852 1 AIISTGDEL------LSGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1385497867 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 |
1.00e-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: 88.05 E-value: 1.00e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1385497867 332 RVRTASRLKKTPGRLDFQRGILqRSANGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEPGEWVEVEPF 404
Cdd:pfam03454 1 KARLARDLKSDPGRREFVRVRL-HEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
152-319 |
3.43e-08 |
|
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: 54.47 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 152 AGTR---LTTAELPVLASLGIADAQVV------RKVRVALFSTGDElqlPGQpleaGQIYDTNRLTIHLMLQQLGCEVIN 222
Cdd:cd03522 125 ATVKiipLAVPEALVERAEALARDGPLlrvapfRPLRVGLIVTGSE---VYG----GRIEDKFGPVLRARLAALGVELVE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 223 LGIIPDDPGKLRAAFIDADSQ-ADVVISSGGVSVGEADYTKTILEELG-EIAFWKLAIKPGKPFAFGKLSNSWFCGLPGN 300
Cdd:cd03522 198 QVIVPHDEAAIAAAIAEALEAgAELLILTGGASVDPDDVTPAAIRAAGgEVIRYGMPVDPGNLLLLGYLGGVPVIGLPGC 277
|
170 180
....*....|....*....|
gi 1385497867 301 PVSAALTFYQLVQP-LLAKL 319
Cdd:cd03522 278 ARSPKLNGFDLVLPrLLAGE 297
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
179-252 |
1.98e-07 |
|
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: 50.56 E-value: 1.98e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1385497867 179 RVALFSTGDELQLpgqpleaGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQADVVISSGG 252
Cdd:cd00885 1 TAEIIAIGDELLS-------GQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
179-252 |
4.66e-07 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 50.50 E-value: 4.66e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1385497867 179 RVALFSTGDELqlpgqpLeAGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQADVVISSGG 252
Cdd:COG1058 1 KAEIITIGDEL------L-SGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGG 67
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
212-261 |
7.83e-05 |
|
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: 42.80 E-value: 7.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1385497867 212 MLQQLGCEVINLGIIPDDPGKLRAAFID--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 |
3.92e-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: 40.54 E-value: 3.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1385497867 212 MLQQLGCEVINLGIIPDDPGKLRAAFIDA--DSQADVVISSGG 252
Cdd:cd00886 28 LLEEAGHEVVAYEIVPDDKDEIREALIEWadEDGVDLILTTGG 70
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
179-270 |
1.35e-03 |
|
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: 40.66 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 179 RVALFSTGDELQLpgqpleaGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQADVVISSGGVSVGEA 258
Cdd:TIGR00200 2 KAEIISVGDELLL-------GQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSD 74
|
90
....*....|...
gi 1385497867 259 DYTK-TILEELGE 270
Cdd:TIGR00200 75 DLTAeTIATAKGE 87
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
198-270 |
3.04e-03 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 39.15 E-value: 3.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1385497867 198 AGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQ-ADVVISSGGVSVGEADYTKTILEELGE 270
Cdd:PRK03604 169 AGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAEgYALIITTGGTGLGPRDVTPEALAPLLE 242
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
184-269 |
8.26e-03 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 38.23 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385497867 184 STGDELQLpgqpleaGQIYDTNRLTIHLMLQQLGCEVINLGIIPDDPGKLRAAFIDADSQADVVISSGGVSVGEADYTK- 262
Cdd:PRK00549 7 AVGTELLL-------GQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLGPTKDDLTKe 79
|
....*..
gi 1385497867 263 TILEELG 269
Cdd:PRK00549 80 TVAKFLG 86
|
|
| |
