|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
11-408 |
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: 523.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 11 LKPVDEAIAELLARVPaPPAVEEVALRDALGRVLAEPLDASFPVPPWDNSAMDGYALRAADLPAEGGA-LPLAGRIAAGD 89
Cdd:COG0303 1 MISVEEALALILAAVR-PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVtLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 90 AASQQLPAGHAVRIFTGAPLPPGADAVVAQENCRIEGDRIWLP-AVNAGDNVRCLGEETAAGERLIDAGKRLRPQELGLL 168
Cdd:COG0303 80 PPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRkPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 169 ATFGVARVKVYRRLRVALLSSGNELREPGEPLDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADAASRF 248
Cdd:COG0303 160 ASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 249 DLIITSGGVSVGEEDHLKQAIRELG-ELHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVTSLVVARPFLLRAQGCT 327
Cdd:COG0303 240 DLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 328 QVQVTPLRLPAGFAWRKANVRQQFLRARLEAVDGRLEVRLFPRQGSAMLTSATWADGLAIVECQRT-LAEGELVQYLPFS 406
Cdd:COG0303 320 PPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEgVEAGEEVEVLLLD 399
|
..
gi 338800245 407 EL 408
Cdd:COG0303 400 GL 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
15-405 |
6.00e-178 |
|
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: 501.25 E-value: 6.00e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 15 DEAIAELLARVPAPPAVEEVALRDALGRVLAEPLDASFPVPPWDNSAMDGYALRAADLPAEGGALPLAGRIAAGDAASQQ 94
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLRVVGEIPAGEPPDGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 95 LPAGHAVRIFTGAPLPPGADAVVAQENCRIEGDRIWLPA-VNAGDNVRCLGEETAAGERLIDAGKRLRPQELGLLATFGV 173
Cdd:cd00887 81 LGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKpVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 174 ARVKVYRRLRVALLSSGNELREPGEPLDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADAASRFDLIIT 253
Cdd:cd00887 161 AEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 254 SGGVSVGEEDHLKQAIREL-GELHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVTSLVVARPFLLRAQGCTQVQVT 332
Cdd:cd00887 241 SGGVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338800245 333 PLRLPAGFAWRKANVRQQFLRARLEAVDGRLEVRLFPRQGSAMLTSATWADGLAIV-ECQRTLAEGELVQYLPF 405
Cdd:cd00887 321 RVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQGSGLLSSLARADGLIVIpEGVEGLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
3-409 |
1.71e-132 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 393.21 E-value: 1.71e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 3 ACGCDTGGLK--PVDEAIAELLARVPAPPAVEEVALRDALGRVLAEPLDASFPVPPWDNSAMDGYALRAADLPAEGGALP 80
Cdd:PRK14491 188 ACCCDLLSPAflSVSQGLDKILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESYTLV 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 81 laGRIAAGDAASQQLPAGHAVRIFTGAPLPPGADAVVAQENCRIEGDRIWLPA-VNAGDNVRCLGEETAAGERLIDAGKR 159
Cdd:PRK14491 268 --GEVLAGHQYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGgIKAGQNVRLAGEDLAQGQVALAAGTR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 160 LRPQELGLLATFGVARVKVYRRLRVALLSSGNELREPGEPLDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRD 239
Cdd:PRK14491 346 LSAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEA 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 240 ALADAASRFDLIITSGGVSVGEEDHLKQAIRELGELHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVTSLVVARPF 319
Cdd:PRK14491 426 TLEQAAAQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPA 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 320 LLRAQGctQVQVTPLRLPA--GFAWRKANVRQQFLRA--RLEAvDGRLEVRLFPRQGSAMLTSATWADGL-AIVECQRTL 394
Cdd:PRK14491 506 LRKLAG--EQNWQPLLFPAiaDETLRSRQGRTEFSRGiyHLGA-DGRLHVRTTGKQGSGILSSMSEANCLiEIGPAAETV 582
|
410
....*....|....*
gi 338800245 395 AEGELVQYLPFSELL 409
Cdd:PRK14491 583 NAGETVTIQPLAGLL 597
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
26-172 |
1.64e-49 |
|
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: 164.28 E-value: 1.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 26 PAPPAVEEVAL--RDALGRVLAEPLDASFPVPPWDNSAMDGYALRAADLPAEGGALPlagrIAAGDAASQQLPAGHAVRI 103
Cdd:pfam03453 1 PLLGTEETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP----IAAGEPPGPLLPGGEAVRI 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338800245 104 FTGAPLPPGADAVVAQENCRIEGDRI--WLPAVNAGDNVRCLGEETAAGERLIDAGKRLRPQELGLLATFG 172
Cdd:pfam03453 77 MTGAPLPEGADAVVMVEDTEEGGGRTveIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
182-318 |
1.57e-37 |
|
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: 133.21 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 182 LRVALLSSGNELREPGEPLDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADAASRFDLIITSGGVSVGE 261
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338800245 262 EDHLKQAIRELGE-----------LHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVTSLVVARP 318
Cdd:TIGR00177 81 RDVTPEALEELGEkeipgfgefrmLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
185-311 |
1.48e-30 |
|
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: 114.22 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 185 ALLSSGNELREPGepldagQIYNSNRYSLLGVLQSLGCEVHDYPILI--DDLGASRDALADAASRFDLIITSGGVSVGEE 262
Cdd:smart00852 1 AIISTGDELLSGG------QIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 263 DHLKQAIRELG--ELHLWRLAIQPGKP-----LAFGEVNG----TPWIGLPGNPAAALVT 311
Cdd:smart00852 75 DLTPEALAELGgrELLGHGVAMRPGGPpgplaNLSGTAPGvrgkKPVFGLPGNPVAALVM 134
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
11-408 |
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: 523.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 11 LKPVDEAIAELLARVPaPPAVEEVALRDALGRVLAEPLDASFPVPPWDNSAMDGYALRAADLPAEGGA-LPLAGRIAAGD 89
Cdd:COG0303 1 MISVEEALALILAAVR-PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVtLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 90 AASQQLPAGHAVRIFTGAPLPPGADAVVAQENCRIEGDRIWLP-AVNAGDNVRCLGEETAAGERLIDAGKRLRPQELGLL 168
Cdd:COG0303 80 PPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRkPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 169 ATFGVARVKVYRRLRVALLSSGNELREPGEPLDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADAASRF 248
Cdd:COG0303 160 ASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 249 DLIITSGGVSVGEEDHLKQAIRELG-ELHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVTSLVVARPFLLRAQGCT 327
Cdd:COG0303 240 DLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 328 QVQVTPLRLPAGFAWRKANVRQQFLRARLEAVDGRLEVRLFPRQGSAMLTSATWADGLAIVECQRT-LAEGELVQYLPFS 406
Cdd:COG0303 320 PPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEgVEAGEEVEVLLLD 399
|
..
gi 338800245 407 EL 408
Cdd:COG0303 400 GL 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
15-405 |
6.00e-178 |
|
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: 501.25 E-value: 6.00e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 15 DEAIAELLARVPAPPAVEEVALRDALGRVLAEPLDASFPVPPWDNSAMDGYALRAADLPAEGGALPLAGRIAAGDAASQQ 94
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLRVVGEIPAGEPPDGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 95 LPAGHAVRIFTGAPLPPGADAVVAQENCRIEGDRIWLPA-VNAGDNVRCLGEETAAGERLIDAGKRLRPQELGLLATFGV 173
Cdd:cd00887 81 LGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKpVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 174 ARVKVYRRLRVALLSSGNELREPGEPLDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADAASRFDLIIT 253
Cdd:cd00887 161 AEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 254 SGGVSVGEEDHLKQAIREL-GELHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVTSLVVARPFLLRAQGCTQVQVT 332
Cdd:cd00887 241 SGGVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338800245 333 PLRLPAGFAWRKANVRQQFLRARLEAVDGRLEVRLFPRQGSAMLTSATWADGLAIV-ECQRTLAEGELVQYLPF 405
Cdd:cd00887 321 RVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQGSGLLSSLARADGLIVIpEGVEGLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
3-409 |
1.71e-132 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 393.21 E-value: 1.71e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 3 ACGCDTGGLK--PVDEAIAELLARVPAPPAVEEVALRDALGRVLAEPLDASFPVPPWDNSAMDGYALRAADLPAEGGALP 80
Cdd:PRK14491 188 ACCCDLLSPAflSVSQGLDKILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESYTLV 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 81 laGRIAAGDAASQQLPAGHAVRIFTGAPLPPGADAVVAQENCRIEGDRIWLPA-VNAGDNVRCLGEETAAGERLIDAGKR 159
Cdd:PRK14491 268 --GEVLAGHQYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGgIKAGQNVRLAGEDLAQGQVALAAGTR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 160 LRPQELGLLATFGVARVKVYRRLRVALLSSGNELREPGEPLDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRD 239
Cdd:PRK14491 346 LSAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEA 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 240 ALADAASRFDLIITSGGVSVGEEDHLKQAIRELGELHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVTSLVVARPF 319
Cdd:PRK14491 426 TLEQAAAQADVVISSGGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPA 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 320 LLRAQGctQVQVTPLRLPA--GFAWRKANVRQQFLRA--RLEAvDGRLEVRLFPRQGSAMLTSATWADGL-AIVECQRTL 394
Cdd:PRK14491 506 LRKLAG--EQNWQPLLFPAiaDETLRSRQGRTEFSRGiyHLGA-DGRLHVRTTGKQGSGILSSMSEANCLiEIGPAAETV 582
|
410
....*....|....*
gi 338800245 395 AEGELVQYLPFSELL 409
Cdd:PRK14491 583 NAGETVTIQPLAGLL 597
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
6-410 |
2.31e-118 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 350.55 E-value: 2.31e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 6 CDTGGLKPVDEAIAELLARVPAPPAVEEVALRDALGRVLAEPLDASFPVPPWDNSAMDGYALRAADLpAEGGALPLAGRI 85
Cdd:PRK10680 2 EFTAGLMSLETALTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADL-ASGQPLPVAGKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 86 AAGDAASQQLPAGHAVRIFTGAPLPPGADAVVAQENCRIEGDRIWLPA-VNAGDNVRCLGEETAAGERLIDAGKRLRPQE 164
Cdd:PRK10680 81 FAGQPFHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAeVRSGQNIRRRGEDISQGAVVFPAGTRLTTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 165 LGLLATFGVARVKVYRRLRVALLSSGNELREPGEPLDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADA 244
Cdd:PRK10680 161 LPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 245 ASRFDLIITSGGVSVGEEDHLKQAIRELGELHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVTSLVVARPFLLRAQ 324
Cdd:PRK10680 241 DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 325 GCTQVQVTP-LRLPAGFAWRKANVRQQFLRARLEA-VDGRLEVRLFPRQGSAMLTSATWADGLAIVECQR-TLAEGELVQ 401
Cdd:PRK10680 321 GNTASGLPPrQRVRTASRLKKTPGRLDFQRGILQRnADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERgNVEVGEWVE 400
|
....*....
gi 338800245 402 YLPFSELLG 410
Cdd:PRK10680 401 VEPFNALFG 409
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
11-400 |
3.86e-107 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 329.10 E-value: 3.86e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 11 LKPVDEAIAELLARVPAPP-AVEEVALRDALGRVLAEPLDASFPVPPWDNSAMDGYALRAADL-------PAEggaLPLA 82
Cdd:PRK14498 9 LVSLEEAREILESLLSELPlGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTfgaseanPVR---LKLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 83 GRIAAGDAASQQLPAGHAVRIFTGAPLPPGADAVVAQENCRIEGD---RIWLPaVNAGDNVRCLGEETAAGERLIDAGKR 159
Cdd:PRK14498 86 GEVHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDdtvEIYRP-VAPGENVRPAGEDIVAGELILPKGTR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 160 LRPQELGLLATFGVARVKVYRRLRVALLSSGNELREPGEPLDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRD 239
Cdd:PRK14498 165 LTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 240 ALADAASRFDLIITSGGVSVGEEDHLKQAIRELGELHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVTSLVVARPF 319
Cdd:PRK14498 245 ALRKALKECDLVLLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 320 LLRAQGctQVQVTPLRLPAGFAWR--KANVRQQFLRARLEAVDGRLEVRLFPRqGSAMLTSATWADGLAIVECQR-TLAE 396
Cdd:PRK14498 325 LRKLAG--LPPPERATVKARLARRvrSELGREEFVPVSLGRVGDGYVAYPLSR-GSGAITSLVRADGFIEIPANTeGLEA 401
|
....
gi 338800245 397 GELV 400
Cdd:PRK14498 402 GEEV 405
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
13-405 |
4.63e-93 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 286.04 E-value: 4.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 13 PVDEAIAELLARVPAPPAVEEVALRDALGRVLAEPLDASFPVPPWDNSAMDGYALRAAdLPAEGGALPL-AGRIAAGDAA 91
Cdd:PRK14690 24 PVDTALDLLRARLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGA-APEGAQVLPLiEGRAAAGVPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 92 SQQLPAGHAVRIFTGAPLPPGADAVVAQENCRIEGDRIWLPA-VNAGDNVRCLGEETAAGERLIDAGKRLRPQELGLLAT 170
Cdd:PRK14690 103 SGRVPEGMALRILTGAALPEGVDTVVLEEDVAGDGHRIAFHGpLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 171 FGVARVKVYRRLRVALLSSGNELREPGEPLDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADAASRFDL 250
Cdd:PRK14690 183 VGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 251 IITSGGVSVGEEDHLKQAIRELGELHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVTSLVVARPFLLRAQGCTQVQ 330
Cdd:PRK14690 263 ILTSGGASAGDEDHVSALLREAGAMQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEGWSE 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338800245 331 VTPLRLPAGFAWRKANVRQQFLRARLEavDGRLEVrlFPRQGSAMLTSATWADGLA-IVECQRTLAEGELVQYLPF 405
Cdd:PRK14690 343 PQGFTVPAAFEKRKKPGRREYLRARLR--QGHAEV--FRSEGSGRISGLSWAEGLVeLGDGARRIAPGDPVRFIPY 414
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
11-311 |
9.35e-75 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 242.41 E-value: 9.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 11 LKPVDEAIAELLARVPAPPAVEEVALRDALGRVLAEPLDASFPVPPWDNSAMDGYALRAADLPAEggaLPLAGRIAAGDA 90
Cdd:PRK14497 10 LYSIDEAIKVFLSSLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGE---FKVIDKIGIGEF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 91 ASQQLPAGHAVRIFTGAPLPPGADAVVAQENC-RIEGDRIWLPA-VNAGDNVRCLGEETAAGERLIDAGKRLRPQELGLL 168
Cdd:PRK14497 87 KEIHIKECEAVEVDTGSMIPMGADAVIKVENTkVINGNFIKIDKkINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 169 ATFGVARVKVYRRLRVALLSSGNELREPGEPLDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADAASRF 248
Cdd:PRK14497 167 ASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVA 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338800245 249 DLIITSGGVSVGEEDHLKQAIRELGELHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVT 311
Cdd:PRK14497 247 DVLILTGGTSAGEKDFVHQAIRELGNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVV 309
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
5-361 |
1.41e-62 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 213.14 E-value: 1.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 5 GCDTGGLKPVDEAIAELLArVPAPPAVEEVALRDALGRVLAEPLDASFPVPPWDNSAMDGYALRAADLPAEggaLPLAGR 84
Cdd:PLN02699 1 GGGKTEMISVEEALSIVLS-VAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGE---YPVITE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 85 IAAGDAASQ-QLPAGHAVRIFTGAPLPPGADAVVAQENCRIEGD--------RIwLPAVNAGDNVRCLGEETAAGERLID 155
Cdd:PLN02699 77 SRAGNDGLGvTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDpldgskrvRI-LSQASKGQDIRPVGCDIEKDAKVLK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 156 AGKRLRPQELGLLATFGVARVKVYRRLRVALLSSGNELREPGEP-LDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDL 234
Cdd:PLN02699 156 AGERLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 235 GASRDALADA-ASRFDLIITSGGVSVGEEDHLKQAIRELGELHLWRLAIQPGKPLAFGEVNGTPW---------IGLPGN 304
Cdd:PLN02699 236 EELERILDEAiSSGVDILLTSGGVSMGDRDFVKPLLEKRGTVYFSKVLMKPGKPLTFAEIDAKSApsnskkmlaFGLPGN 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 338800245 305 PAAALVTSLVVARPFLLRAQGCTQVQVTPLRLPAGFAWRKANVRQQFLRA--RLEAVDG 361
Cdd:PLN02699 316 PVSCLVCFNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPVRPEFHRAiiRWKLNDG 374
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
26-172 |
1.64e-49 |
|
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: 164.28 E-value: 1.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 26 PAPPAVEEVAL--RDALGRVLAEPLDASFPVPPWDNSAMDGYALRAADLPAEGGALPlagrIAAGDAASQQLPAGHAVRI 103
Cdd:pfam03453 1 PLLGTEETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP----IAAGEPPGPLLPGGEAVRI 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338800245 104 FTGAPLPPGADAVVAQENCRIEGDRI--WLPAVNAGDNVRCLGEETAAGERLIDAGKRLRPQELGLLATFG 172
Cdd:pfam03453 77 MTGAPLPEGADAVVMVEDTEEGGGRTveIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
182-318 |
1.57e-37 |
|
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: 133.21 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 182 LRVALLSSGNELREPGEPLDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADAASRFDLIITSGGVSVGE 261
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338800245 262 EDHLKQAIRELGE-----------LHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVTSLVVARP 318
Cdd:TIGR00177 81 RDVTPEALEELGEkeipgfgefrmLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
185-311 |
1.48e-30 |
|
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: 114.22 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 185 ALLSSGNELREPGepldagQIYNSNRYSLLGVLQSLGCEVHDYPILI--DDLGASRDALADAASRFDLIITSGGVSVGEE 262
Cdd:smart00852 1 AIISTGDELLSGG------QIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 263 DHLKQAIRELG--ELHLWRLAIQPGKP-----LAFGEVNG----TPWIGLPGNPAAALVT 311
Cdd:smart00852 75 DLTPEALAELGgrELLGHGVAMRPGGPpgplaNLSGTAPGvrgkKPVFGLPGNPVAALVM 134
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
185-322 |
3.15e-30 |
|
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: 113.50 E-value: 3.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 185 ALLSSGNELrepgeplDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADAASRFDLIITSGGVSVGEEDH 264
Cdd:pfam00994 1 AIITTGDEL-------LPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 265 LKQAIRELGEL-------HLWRLAIQPGKPLAFG-----EVNGTPWIGLPGNPAAALVTSLVVARPFLLR 322
Cdd:pfam00994 74 TPEALAELGGRelpgfeeLFRGVSLKPGKPVGTApgailSRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
183-320 |
1.28e-24 |
|
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: 98.18 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 183 RVALLSSGNELrepgeplDAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADAASRFDLIITSGGVSVGEE 262
Cdd:cd00758 1 RVAIVTVSDEL-------SQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 263 DHLKQAIRELG--ELHLWRLAIQPGKPLAFGEVNGTPWIGLPGNPAAALVTSLVVARPFL 320
Cdd:cd00758 74 DVTPEALAELGerEAHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
335-405 |
2.09e-13 |
|
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: 64.94 E-value: 2.09e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338800245 335 RLPAGFAWRKANVRQQFLRARLEAVDGRLEVRLFPRQGSAMLTSATWADGLAIV-ECQRTLAEGELVQYLPF 405
Cdd:pfam03454 1 KARLARDLKSDPGRREFVRVRLHEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVpEGTEGLEAGEEVEVILL 72
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
165-303 |
1.70e-09 |
|
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: 58.71 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 165 LGLLATFGVARVKVYRRLRVALLSSGNELrEPGEPLDAGqiynsnRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADA 244
Cdd:cd03522 143 EALARDGPLLRVAPFRPLRVGLIVTGSEV-YGGRIEDKF------GPVLRARLAALGVELVEQVIVPHDEAAIAAAIAEA 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338800245 245 ASRF-DLIITSGGVSVGEEDHLKQAIRELG-ELHLWRLAIQPGKPLAFGEVNGTPWIGLPG 303
Cdd:cd03522 216 LEAGaELLILTGGASVDPDDVTPAAIRAAGgEVIRYGMPVDPGNLLLLGYLGGVPVIGLPG 276
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
217-308 |
2.40e-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: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 217 LQSLGCEVHDYPILIDDLGASRDALADAASR--FDLIITSGGVSVGEEDHLKQAIREL--------GELhLWRLAIQPGK 286
Cdd:COG0521 38 LEEAGHEVVARRIVPDDKDAIRAALRELIDDegVDLVLTTGGTGLSPRDVTPEATRPLldkelpgfGEL-FRALSLEEIG 116
|
90 100
....*....|....*....|....*...
gi 338800245 287 PLAF------GEVNGTPWIGLPGNPAAA 308
Cdd:COG0521 117 PSAIlsravaGIRGGTLIFNLPGSPGAV 144
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
217-308 |
2.78e-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: 40.92 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 217 LQSLGCEVHDYPILIDDLGASRDALADAASRF--DLIITSGGVSVGEEDHLKQAIRELGELHLwrlaiqPGkplaFGEV- 293
Cdd:cd00886 29 LEEAGHEVVAYEIVPDDKDEIREALIEWADEDgvDLILTTGGTGLAPRDVTPEATRPLLDKEL------PG----FGEAf 98
|
90 100 110
....*....|....*....|....*....|....*.
gi 338800245 294 ---------------------NGTPWIGLPGNPAAA 308
Cdd:cd00886 99 ralsleetgtamlsravagirGGTLIFNLPGSPKAV 134
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
183-256 |
5.12e-03 |
|
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: 37.46 E-value: 5.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338800245 183 RVALLSSGNELrepgepLdAGQIYNSNRYSLLGVLQSLGCEVHDYPILIDDLGASRDALADAASRFDLIITSGG 256
Cdd:cd00885 1 TAEIIAIGDEL------L-SGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
217-308 |
8.38e-03 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 38.00 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338800245 217 LQSLGCEVHDYPILIDDLGASRDALADA-ASRFDLIITSGGVSVGEEDHLKQAIRELGELHL------WRLAIQPGKPLA 289
Cdd:PRK03604 184 LEEAGFEVSHYTIIPDEPAEIAAAVAAWiAEGYALIITTGGTGLGPRDVTPEALAPLLERRLpgiaeaLRSWGQGRTPTA 263
|
90 100
....*....|....*....|....*
gi 338800245 290 F------GEVNGTPWIGLPGNPAAA 308
Cdd:PRK03604 264 MlsrlvaGMIGNSLVVALPGSPGGA 288
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