|
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: 818.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 1 MDFTAGLMPLDTALTQMLDRITPLSATETVPLLQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRLNDLRDGAALPVAGKA 80
Cdd:PRK10680 1 MEFTAGLMSLETALTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 81 FAGQPFHETWPAGTCIRIMTGAPVPVDCDAVVMQEETEQSDSGVRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTPLTVAE 160
Cdd:PRK10680 81 FAGQPFHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 161 LPVLASLGIAEVEVVRKVRVAVFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAA 240
Cdd:PRK10680 161 LPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 241 DQQADVVISSGGVSVGEADYTKTILEELGEIGFWKLAIKPGKPFAFGKLSSSWFCGLPGNPVSATVTFCQLVQPLLAKLS 320
Cdd:PRK10680 241 DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 321 GKHGPLQATRLRVRAATRLKKSPGRLDFQRGILQRNPDGELVVTTTGHQGSHIFSSFSLGNCFIVLERERGHVEAGEWVE 400
Cdd:PRK10680 321 GNTASGLPPRQRVRTASRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEVGEWVE 400
|
410
....*....|.
gi 2118711597 401 VETFSHLFGGL 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: 527.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 7 LMPLDTALTQMLDRITPLsATETVPLLQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRLNDLRDG--AALPVAGKAFAGQ 84
Cdd:COG0303 1 MISVEEALALILAAVRPL-GTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAnpVTLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 85 PFHETWPAGTCIRIMTGAPVPVDCDAVVMQEETEQSDSGVRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTPLTVAELPVL 164
Cdd:COG0303 80 PPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 165 ASLGIAEVEVVRKVRVAVFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAADQQA 244
Cdd:COG0303 160 ASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 245 DVVISSGGVSVGEADYTKTILEELG-EIGFWKLAIKPGKPFAFGKLSSSWFCGLPGNPVSATVTFCQLVQPLLAKLSGkH 323
Cdd:COG0303 240 DLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAG-L 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 324 GPLQATRLRVRAATRLKKSPGRLDFQRGILQRNpDGELVVTTTGHQGSHIFSSFSLGNCFIVLERERGHVEAGEWVEVET 403
Cdd:COG0303 319 PPPPPPRVRARLAEDLPKKPGRTEFLRVRLERD-DGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLL 397
|
....
gi 2118711597 404 FSHL 407
Cdd:COG0303 398 LDGL 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
13-404 |
1.50e-174 |
|
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: 492.78 E-value: 1.50e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 13 ALTQMLDRITPLSATETVPLLQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRLNDLRDGAA-LPVAGKAFAGQPFHETWP 91
Cdd:cd00887 3 AARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtLRVVGEIPAGEPPDGPLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 92 AGTCIRIMTGAPVPVDCDAVVMQEETEQSDSGVRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTPLTVAELPVLASLGIAE 171
Cdd:cd00887 83 PGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 172 VEVVRKVRVAVFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAADQQADVVISSG 251
Cdd:cd00887 163 VPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 252 GVSVGEADYTKTILEEL-GEIGFWKLAIKPGKPFAFGKLSSSWFCGLPGNPVSATVTFCQLVQPLLAKLSGkHGPLQATR 330
Cdd:cd00887 243 GVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQG-APEPEPPR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118711597 331 LRVRAATRLKKSPGRLDFQRGILQRNpDGELVVTTTGHQGSHIFSSFSLGNCFIVLERERGHVEAGEWVEVETF 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 |
2.80e-54 |
|
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: 176.60 E-value: 2.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 23 PLSATETVPL--LQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRLndlRDGAALPVAGKAFAGQPFHETWPAGTCIRIMT 100
Cdd:pfam03453 2 LLGTEETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRA---ADGFGASEVNPIAAGEPPGPLLPGGEAVRIMT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2118711597 101 GAPVPVDCDAVVMQEETEQSDSG-VRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTPLTVAELPVLASLG 168
Cdd:pfam03453 79 GAPLPEGADAVVMVEDTEEGGGRtVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
183-314 |
8.11e-43 |
|
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: 147.08 E-value: 8.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 183 FSTGDELQLPGQPLGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAADQQADVVISSGGVSVGEADYTK 262
Cdd:TIGR00177 6 ISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRDVTP 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118711597 263 TILEELGEIGFWKL-----------AIKPGKPFAFGKLSSSWFCGLPGNPVSATVTFCQLVQP 314
Cdd:TIGR00177 86 EALEELGEKEIPGFgefrmlsslpvLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
183-308 |
8.24e-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: 114.99 E-value: 8.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 183 FSTGDELQLPGQplgdgqIYDTNRLAVHLMLQELGCEVINLGII--PDDPAKLRDAFIAADQQADVVISSGGVSVGEADY 260
Cdd:smart00852 3 ISTGDELLSGGQ------IRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2118711597 261 TKTILEELG--EIGFWKLAIKPGKPFAFGKLSSSWFCG---------LPGNPVSATVTF 308
Cdd:smart00852 77 TPEALAELGgrELLGHGVAMRPGGPPGPLANLSGTAPGvrgkkpvfgLPGNPVAALVMF 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: 818.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 1 MDFTAGLMPLDTALTQMLDRITPLSATETVPLLQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRLNDLRDGAALPVAGKA 80
Cdd:PRK10680 1 MEFTAGLMSLETALTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 81 FAGQPFHETWPAGTCIRIMTGAPVPVDCDAVVMQEETEQSDSGVRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTPLTVAE 160
Cdd:PRK10680 81 FAGQPFHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 161 LPVLASLGIAEVEVVRKVRVAVFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAA 240
Cdd:PRK10680 161 LPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 241 DQQADVVISSGGVSVGEADYTKTILEELGEIGFWKLAIKPGKPFAFGKLSSSWFCGLPGNPVSATVTFCQLVQPLLAKLS 320
Cdd:PRK10680 241 DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 321 GKHGPLQATRLRVRAATRLKKSPGRLDFQRGILQRNPDGELVVTTTGHQGSHIFSSFSLGNCFIVLERERGHVEAGEWVE 400
Cdd:PRK10680 321 GNTASGLPPRQRVRTASRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEVGEWVE 400
|
410
....*....|.
gi 2118711597 401 VETFSHLFGGL 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: 527.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 7 LMPLDTALTQMLDRITPLsATETVPLLQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRLNDLRDG--AALPVAGKAFAGQ 84
Cdd:COG0303 1 MISVEEALALILAAVRPL-GTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAnpVTLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 85 PFHETWPAGTCIRIMTGAPVPVDCDAVVMQEETEQSDSGVRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTPLTVAELPVL 164
Cdd:COG0303 80 PPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 165 ASLGIAEVEVVRKVRVAVFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAADQQA 244
Cdd:COG0303 160 ASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 245 DVVISSGGVSVGEADYTKTILEELG-EIGFWKLAIKPGKPFAFGKLSSSWFCGLPGNPVSATVTFCQLVQPLLAKLSGkH 323
Cdd:COG0303 240 DLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAG-L 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 324 GPLQATRLRVRAATRLKKSPGRLDFQRGILQRNpDGELVVTTTGHQGSHIFSSFSLGNCFIVLERERGHVEAGEWVEVET 403
Cdd:COG0303 319 PPPPPPRVRARLAEDLPKKPGRTEFLRVRLERD-DGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLL 397
|
....
gi 2118711597 404 FSHL 407
Cdd:COG0303 398 LDGL 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
13-404 |
1.50e-174 |
|
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: 492.78 E-value: 1.50e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 13 ALTQMLDRITPLSATETVPLLQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRLNDLRDGAA-LPVAGKAFAGQPFHETWP 91
Cdd:cd00887 3 AARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtLRVVGEIPAGEPPDGPLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 92 AGTCIRIMTGAPVPVDCDAVVMQEETEQSDSGVRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTPLTVAELPVLASLGIAE 171
Cdd:cd00887 83 PGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 172 VEVVRKVRVAVFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAADQQADVVISSG 251
Cdd:cd00887 163 VPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 252 GVSVGEADYTKTILEEL-GEIGFWKLAIKPGKPFAFGKLSSSWFCGLPGNPVSATVTFCQLVQPLLAKLSGkHGPLQATR 330
Cdd:cd00887 243 GVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQG-APEPEPPR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118711597 331 LRVRAATRLKKSPGRLDFQRGILQRNpDGELVVTTTGHQGSHIFSSFSLGNCFIVLERERGHVEAGEWVEVETF 404
Cdd:cd00887 322 VKARLAEDLKSKPGRREFLRVRLERD-EGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
3-407 |
1.60e-155 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 451.76 E-value: 1.60e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 3 FTAGLMPLDTALTQMLDRITPLSATETVPLLQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRLNDL-RDGAALPvaGKAF 81
Cdd:PRK14491 194 LSPAFLSVSQGLDKILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLePESYTLV--GEVL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 82 AGQPFHETWPAGTCIRIMTGAPVPVDCDAVVMQEETEQSDSGVRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTPLTVAEL 161
Cdd:PRK14491 272 AGHQYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQ 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 162 PVLASLGIAEVEVVRKVRVAVFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAAD 241
Cdd:PRK14491 352 GLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 242 QQADVVISSGGVSVGEADYTKTILEELGEIGFWKLAIKPGKPFAFGKLSSSWFCGLPGNPVSATVTFCQLVQPLLAKLSG 321
Cdd:PRK14491 432 AQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKLAG 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 322 KHGpLQATRLRVRAATRLKKSPGRLDFQRGILQRNPDGELVVTTTGHQGSHIFSSFSLGNCFIVLERERGHVEAGEWVEV 401
Cdd:PRK14491 512 EQN-WQPLLFPAIADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGETVTI 590
|
....*.
gi 2118711597 402 ETFSHL 407
Cdd:PRK14491 591 QPLAGL 596
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
7-405 |
7.77e-107 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 328.33 E-value: 7.77e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 7 LMPLDTALTQMLDRITPLS-ATETVPLLQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRLNDLRdGA------ALPVAGK 79
Cdd:PRK14498 9 LVSLEEAREILESLLSELPlGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTF-GAseanpvRLKLGGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 80 AFAGQPFHETWPAGTCIRIMTGAPVPVDCDAVVMQEETEQSDSG-VRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTPLTV 158
Cdd:PRK14498 88 VHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDtVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 159 AELPVLASLGIAEVEVVRKVRVAVFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFI 238
Cdd:PRK14498 168 RDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 239 AADQQADVVISSGGVSVGEADYTKTILEELGEIGFWKLAIKPGKPFAFGKLSSSWFCGLPGNPVSATVTFCQLVQPLLAK 318
Cdd:PRK14498 248 KALKECDLVLLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLRK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 319 LSGKHGPLQATrLRVRAATRLKKSPGRLDFQRGILQRNPDGeLVVTTTGhQGSHIFSSFSLGNCFIVLERERGHVEAGEW 398
Cdd:PRK14498 328 LAGLPPPERAT-VKARLARRVRSELGREEFVPVSLGRVGDG-YVAYPLS-RGSGAITSLVRADGFIEIPANTEGLEAGEE 404
|
....*..
gi 2118711597 399 VEVETFS 405
Cdd:PRK14498 405 VEVELFG 411
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
9-350 |
5.90e-74 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 236.74 E-value: 5.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 9 PLDTALTQMLDRITPLSATETVPLLQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRLNDLRDGAALPV-AGKAFAGQPFH 87
Cdd:PRK14690 24 PVDTALDLLRARLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQVLPLiEGRAAAGVPFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 88 ETWPAGTCIRIMTGAPVPVDCDAVVMQEETEQSDSGVRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTPLTVAELPVLASL 167
Cdd:PRK14690 104 GRVPEGMALRILTGAALPEGVDTVVLEEDVAGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 168 GIAEVEVVRKVRVAVFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAADQQADVV 247
Cdd:PRK14690 184 GLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 248 ISSGGVSVGEADYTKTILEELGEIGFWKLAIKPGKPFAFGKLSSSWFCGLPGNPVSATVtfCQLV--QPLLAKLSGKhGP 325
Cdd:PRK14690 264 LTSGGASAGDEDHVSALLREAGAMQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALV--CTLVfaRPAMSLLAGE-GW 340
|
330 340
....*....|....*....|....*
gi 2118711597 326 LQATRLRVRAATRLKKSPGRLDFQR 350
Cdd:PRK14690 341 SEPQGFTVPAAFEKRKKPGRREYLR 365
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
6-399 |
3.15e-61 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 209.28 E-value: 3.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 6 GLMPLDTALTQMLD---RITPLsateTVPLLQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRLNDlrDGAALPVAGKAFA 82
Cdd:PLN02699 6 EMISVEEALSIVLSvaaRLSPV----IVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASD--GPGEYPVITESRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 83 GQ-PFHETWPAGTCIRIMTGAPVPVDCDAVVMQEETEQSDSG------VRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTP 155
Cdd:PLN02699 80 GNdGLGVTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPldgskrVRILSQASKGQDIRPVGCDIEKDAKVLKAGER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 156 LTVAELPVLASLGIAEVEVVRKVRVAVFSTGDELQLPGQP-LGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLR 234
Cdd:PLN02699 160 LGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 235 DAFIAA-DQQADVVISSGGVSVGEADYTKTILEELGEIGFWKLAIKPGKPFAFGKLSSS---------WFCGLPGNPVSA 304
Cdd:PLN02699 240 RILDEAiSSGVDILLTSGGVSMGDRDFVKPLLEKRGTVYFSKVLMKPGKPLTFAEIDAKsapsnskkmLAFGLPGNPVSC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 305 TVTFCQLVQPLLAKLSGKHGPlQATRLRVRAATRLKKSPGRLDFQRGILQ-RNPDGE----LVVTTTGHQGSHIFSSFSL 379
Cdd:PLN02699 320 LVCFNLFVVPAIRYLAGWSNP-HLLRVQARLREPIKLDPVRPEFHRAIIRwKLNDGSgnpgFVAESTGHQMSSRLLSMKS 398
|
410 420
....*....|....*....|
gi 2118711597 380 GNCFIVLERERGHVEAGEWV 399
Cdd:PLN02699 399 ANALLELPATGNVLSAGTSV 418
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
23-168 |
2.80e-54 |
|
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: 176.60 E-value: 2.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 23 PLSATETVPL--LQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRLndlRDGAALPVAGKAFAGQPFHETWPAGTCIRIMT 100
Cdd:pfam03453 2 LLGTEETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRA---ADGFGASEVNPIAAGEPPGPLLPGGEAVRIMT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2118711597 101 GAPVPVDCDAVVMQEETEQSDSG-VRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTPLTVAELPVLASLG 168
Cdd:pfam03453 79 GAPLPEGADAVVMVEDTEEGGGRtVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
7-321 |
4.88e-52 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 182.32 E-value: 4.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 7 LMPLDTALTQMLDRITPLSATETVPLLQAFSRVTAHDIVSPLDVPGFDNAAMDGYAVRlNDLRDGAaLPVAGKAFAGQpF 86
Cdd:PRK14497 10 LYSIDEAIKVFLSSLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALK-SSCTPGE-FKVIDKIGIGE-F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 87 HE-TWPAGTCIRIMTGAPVPVDCDAVVMQEETE-QSDSGVRFTAPVKAGQHIRRRGEDIAHGAVVFPAGTPLTVAELPVL 164
Cdd:PRK14497 87 KEiHIKECEAVEVDTGSMIPMGADAVIKVENTKvINGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 165 ASLGIAEVEVVRKVRVAVFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAADQQA 244
Cdd:PRK14497 167 ASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVA 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118711597 245 DVVISSGGVSVGEADYTKTILEELGEIGFWKLAIKPGKPFAFGKLSSSWFCGLPGNPVSATVTFCQLVQPLLAKLSG 321
Cdd:PRK14497 247 DVLILTGGTSAGEKDFVHQAIRELGNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYP 323
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
183-314 |
8.11e-43 |
|
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: 147.08 E-value: 8.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 183 FSTGDELQLPGQPLGDGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAADQQADVVISSGGVSVGEADYTK 262
Cdd:TIGR00177 6 ISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRDVTP 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118711597 263 TILEELGEIGFWKL-----------AIKPGKPFAFGKLSSSWFCGLPGNPVSATVTFCQLVQP 314
Cdd:TIGR00177 86 EALEELGEKEIPGFgefrmlsslpvLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
183-316 |
3.05e-40 |
|
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: 139.79 E-value: 3.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 183 FSTGDELQLpgqplgdGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAADQQADVVISSGGVSVGEADYTK 262
Cdd:cd00758 5 VTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2118711597 263 TILEELGEIGFW--KLAIKPGKPFAFGKLSSSWFCGLPGNPVSATVTFCQLVQPLL 316
Cdd:cd00758 78 EALAELGEREAHgkGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
184-318 |
3.01e-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 trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 116.19 E-value: 3.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 184 STGDELqLPGQplgdgqIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAADQQADVVISSGGVSVGEADYTKT 263
Cdd:pfam00994 4 TTGDEL-LPGQ------IRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPE 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118711597 264 ILEELGEIG-------FWKLAIKPGKPFAFGKL------SSSWFCgLPGNPVSATVTFCQLVQPLLAK 318
Cdd:pfam00994 77 ALAELGGRElpgfeelFRGVSLKPGKPVGTAPGailsraGKTVFG-LPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
183-308 |
8.24e-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: 114.99 E-value: 8.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 183 FSTGDELQLPGQplgdgqIYDTNRLAVHLMLQELGCEVINLGII--PDDPAKLRDAFIAADQQADVVISSGGVSVGEADY 260
Cdd:smart00852 3 ISTGDELLSGGQ------IRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2118711597 261 TKTILEELG--EIGFWKLAIKPGKPFAFGKLSSSWFCG---------LPGNPVSATVTF 308
Cdd:smart00852 77 TPEALAELGgrELLGHGVAMRPGGPPGPLANLSGTAPGvrgkkpvfgLPGNPVAALVMF 135
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
332-404 |
7.95e-22 |
|
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: 88.44 E-value: 7.95e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118711597 332 RVRAATRLKKSPGRLDFQRGILqRNPDGELVVTTTGHQGSHIFSSFSLGNCFIVLERERGHVEAGEWVEVETF 404
Cdd:pfam03454 1 KARLARDLKSDPGRREFVRVRL-HEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
184-252 |
5.17e-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: 49.40 E-value: 5.17e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118711597 184 STGDELQLpgqplgdGQIYDTNrlAVHL--MLQELGCEVINLGIIPDDPAKLRDAFIAADQQADVVISSGG 252
Cdd:cd00885 6 AIGDELLS-------GQIVDTN--AAFLakELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
184-252 |
5.35e-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: 5.35e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118711597 184 STGDELQLpgqplgdGQIYDTNrlAVHL--MLQELGCEVINLGIIPDDPAKLRDAFIAADQQADVVISSGG 252
Cdd:COG1058 6 TIGDELLS-------GRIVDTN--AAWLarELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGG 67
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
212-261 |
2.74e-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: 44.34 E-value: 2.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2118711597 212 MLQELGCEVINLGIIPDDPAKLRDAFI--AADQQADVVISSGGVSVGEADYT 261
Cdd:COG0521 37 LLEEAGHEVVARRIVPDDKDAIRAALRelIDDEGVDLVLTTGGTGLSPRDVT 88
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
213-299 |
5.96e-05 |
|
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: 44.46 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 213 LQELGCEVINLGIIPDDPAKLRDAFI-AADQQADVVISSGGVSVGEADYTKTILEELG-EIGFWKLAIKPGKPFAFGKLS 290
Cdd:cd03522 188 LAALGVELVEQVIVPHDEAAIAAAIAeALEAGAELLILTGGASVDPDDVTPAAIRAAGgEVIRYGMPVDPGNLLLLGYLG 267
|
....*....
gi 2118711597 291 SSWFCGLPG 299
Cdd:cd03522 268 GVPVIGLPG 276
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
212-252 |
8.90e-05 |
|
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.
Pssm-ID: 238451 [Multi-domain] Cd Length: 152 Bit Score: 42.46 E-value: 8.90e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2118711597 212 MLQELGCEVINLGIIPDDPAKLRDAFI--AADQQADVVISSGG 252
Cdd:cd00886 28 LLEEAGHEVVAYEIVPDDKDEIREALIewADEDGVDLILTTGG 70
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
184-270 |
7.90e-04 |
|
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: 41.43 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 184 STGDELQLpgqplgdGQIYDTNRLAVHLMLQELGCEVINLGIIPDDPAKLRDAFIAADQQADVVISSGGVSVGEADYTK- 262
Cdd:TIGR00200 7 SVGDELLL-------GQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSDDLTAe 79
|
....*...
gi 2118711597 263 TILEELGE 270
Cdd:TIGR00200 80 TIATAKGE 87
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
184-269 |
1.04e-03 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 40.93 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118711597 184 STGDELQLpgqplgdGQIYDTN------RLAvhlmlqELGCEVINLGIIPDDPAKLRDAFIAADQQADVVISSGGVSVGE 257
Cdd:PRK00549 7 AVGTELLL-------GQIVNTNaqflseKLA------ELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLGPTK 73
|
90
....*....|...
gi 2118711597 258 ADYTK-TILEELG 269
Cdd:PRK00549 74 DDLTKeTVAKFLG 86
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
213-270 |
1.68e-03 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 40.31 E-value: 1.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2118711597 213 LQELGCEVINLGIIPDDPAKLRDAFIAA-DQQADVVISSGGVSVGEADYTKTILEELGE 270
Cdd:PRK03604 184 LEEAGFEVSHYTIIPDEPAEIAAAVAAWiAEGYALIITTGGTGLGPRDVTPEALAPLLE 242
|
|
| |
