|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
18-429 |
1.61e-132 |
|
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: 386.85 E-value: 1.61e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 18 EARKIMKQigAQIPRIVESIQVDwSALGRVVAEEVKSSEDMPPVAASTKDGYAVIAHDGIGLK---KMVGVSLAGNIYQG 94
Cdd:cd00887 3 AARELLLA--LAPPLGTETVPLL-EALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASvtlRVVGEIPAGEPPDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 95 AVEIGKCVRISTGGIIPEGADAVIMREYTELvrqdqqsEETEIICKQAVQVGENIRLPGSDVRSSDVIVPFEAQIGSAEF 174
Cdd:cd00887 80 PLGPGEAVRIMTGAPLPEGADAVVMVEDTEE-------EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 175 GILNAFGIRTIKVYKKPVVTVISTGSELVSPMvENVPLGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTEC 254
Cdd:cd00887 153 GLLASLGIAEVPVYRRPRVAIISTGDELVEPG-EPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 255 LEHSDVIVTTGGVSMGEQDYMKNALLHLGFKIEFGRVSMKPGLPCTVATRESaserklKVVLALPGNPASAWVCSHLFAV 334
Cdd:cd00887 232 LEEADVVITSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGRLGG------KPVFGLPGNPVSALVTFELFVR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 335 PLIRDMSGYRRINHTKINVRIAQDIKL-GDRPEFVRAFIEqvgdEDDGHPIAHVTKNQISSNIGNLVGAQVLLELNaasA 413
Cdd:cd00887 306 PALRKLQGAPEPEPPRVKARLAEDLKSkPGRREFLRVRLE----RDEGGLVVAPPGGQGSGLLSSLARADGLIVIP---E 378
|
410
....*....|....*.
gi 25147659 414 DKTVVPKNGLVKALIL 429
Cdd:cd00887 379 GVEGLEAGEEVEVLLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
18-431 |
7.57e-119 |
|
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: 352.08 E-value: 7.57e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 18 EARKImkqIGAQIPRiVESIQVD-WSALGRVVAEEVKSSEDMPPVAASTKDGYAVIAHDGIGLK----KMVGVSLAGNIY 92
Cdd:COG0303 6 EALAL---ILAAVRP-LGTETVPlAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANpvtlRVVGEIAAGSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 93 QGAVEIGKCVRISTGGIIPEGADAVIMREYTELvrqdqqsEETEIICKQAVQVGENIRLPGSDVRSSDVIVPFEAQIGSA 172
Cdd:COG0303 82 PGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER-------EGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 173 EFGILNAFGIRTIKVYKKPVVTVISTGSELVSPmVENVPLGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLT 252
Cdd:COG0303 155 DLGLLASLGIAEVPVYRRPRVAILSTGDELVEP-GEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 253 ECLEHSDVIVTTGGVSMGEQDYMKNALLHLGFKIEFGRVSMKPGLPCTVATRESaserklKVVLALPGNPASAWVCSHLF 332
Cdd:COG0303 234 EALAEADLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLGG------KPVFGLPGNPVSALVTFELF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 333 AVPLIRDMSGYRRINHTKINVRIAQDI-KLGDRPEFVRAFIEQvgdeDDGHPIAHVTKNQISSNIGNLVGAQVLLELnaa 411
Cdd:COG0303 308 VRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLER----DDGELVVEPLGGQGSGLLSSLAEADGLIVL--- 380
|
410 420
....*....|....*....|
gi 25147659 412 SADKTVVPKNGLVKALILSS 431
Cdd:COG0303 381 PEGVEGVEAGEEVEVLLLDG 400
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
18-430 |
4.25e-92 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 291.72 E-value: 4.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 18 EARKIMKQIGAQI-PRIVESIQvdwsALGRVVAEEVKSSEDMPPVAASTKDGYAVIAHDGIGLKKMVGVSLAGNIYQG-A 95
Cdd:PLN02699 12 EALSIVLSVAARLsPVIVPLHE----ALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGvT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 96 VEIGKCVRISTGGIIPEGADAVIMREYTELVRQDQQSEETEIICKQAVQvGENIRLPGSDVRSSDVIVPFEAQIGSAEFG 175
Cdd:PLN02699 88 LTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKRVRILSQASK-GQDIRPVGCDIEKDAKVLKAGERLGASEIG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 176 ILNAFGIRTIKVYKKPVVTVISTGSELVSPMVENVPLGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTECL 255
Cdd:PLN02699 167 LLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDEAI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 256 EHS-DVIVTTGGVSMGEQDYMKNALLHLGfKIEFGRVSMKPGLPCTVATRESASERKL-KVVLA--LPGNPASAWVCSHL 331
Cdd:PLN02699 247 SSGvDILLTSGGVSMGDRDFVKPLLEKRG-TVYFSKVLMKPGKPLTFAEIDAKSAPSNsKKMLAfgLPGNPVSCLVCFNL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 332 FAVPLIRDMSGYRRINHTKINVRIAQDIKL-GDRPEFVRAFIEQVGDEDDGHP--IAHVTKNQISSNIGNLVGAQVLLEL 408
Cdd:PLN02699 326 FVVPAIRYLAGWSNPHLLRVQARLREPIKLdPVRPEFHRAIIRWKLNDGSGNPgfVAESTGHQMSSRLLSMKSANALLEL 405
|
410 420
....*....|....*....|..
gi 25147659 409 NAASAdktVVPKNGLVKALILS 430
Cdd:PLN02699 406 PATGN---VLSAGTSVSAIIIS 424
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
30-181 |
2.82e-37 |
|
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: 133.08 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 30 IPRIVESIQVD-WSALGRVVAEEVKSSEDMPPVAASTKDGYAVIAHDGIGLKKMVGVSlAGNIYQGAVEIGKCVRISTGG 108
Cdd:pfam03453 2 LLGTEETVPLEaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIA-AGEPPGPLLPGGEAVRIMTGA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25147659 109 IIPEGADAVIMREYTELVrqdqqsEETEIICKQAVQVGENIRLPGSDVRSSDVIVPFEAQIGSAEFGILNAFG 181
Cdd:pfam03453 81 PLPEGADAVVMVEDTEEG------GGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
195-328 |
5.90e-29 |
|
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: 110.37 E-value: 5.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 195 VISTGSELVSPmvenvplGMVRDSNAPQLVALFKEHGFNVIDGGRVV--DDKEGLDKKLTECLEHSDVIVTTGGVSMGEQ 272
Cdd:smart00852 2 IISTGDELLSG-------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 273 DYMKNALLH-LGFKIEFGRVSMKPGLPCTVAT---RESASERKLKVVLALPGNPASAWVC 328
Cdd:smart00852 75 DLTPEALAElGGRELLGHGVAMRPGGPPGPLAnlsGTAPGVRGKKPVFGLPGNPVAALVM 134
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
191-335 |
1.13e-28 |
|
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: 109.71 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 191 PVVTVISTGSELVSPMvENVPLGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTECLEHSDVIVTTGGVSMG 270
Cdd:TIGR00177 1 PRVAVISVGDELVEGG-QPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25147659 271 EQDYMKNALLHLG----------FKIEFGRVSMKPGLPCTVATRESaserklKVVLALPGNPASAWVCSHLFAVP 335
Cdd:TIGR00177 80 PRDVTPEALEELGekeipgfgefRMLSSLPVLSRPGKPATAGVRGG------TLIFNLPGNPVSALVTFEVLILP 148
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
18-429 |
1.61e-132 |
|
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: 386.85 E-value: 1.61e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 18 EARKIMKQigAQIPRIVESIQVDwSALGRVVAEEVKSSEDMPPVAASTKDGYAVIAHDGIGLK---KMVGVSLAGNIYQG 94
Cdd:cd00887 3 AARELLLA--LAPPLGTETVPLL-EALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASvtlRVVGEIPAGEPPDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 95 AVEIGKCVRISTGGIIPEGADAVIMREYTELvrqdqqsEETEIICKQAVQVGENIRLPGSDVRSSDVIVPFEAQIGSAEF 174
Cdd:cd00887 80 PLGPGEAVRIMTGAPLPEGADAVVMVEDTEE-------EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 175 GILNAFGIRTIKVYKKPVVTVISTGSELVSPMvENVPLGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTEC 254
Cdd:cd00887 153 GLLASLGIAEVPVYRRPRVAIISTGDELVEPG-EPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 255 LEHSDVIVTTGGVSMGEQDYMKNALLHLGFKIEFGRVSMKPGLPCTVATRESaserklKVVLALPGNPASAWVCSHLFAV 334
Cdd:cd00887 232 LEEADVVITSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGRLGG------KPVFGLPGNPVSALVTFELFVR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 335 PLIRDMSGYRRINHTKINVRIAQDIKL-GDRPEFVRAFIEqvgdEDDGHPIAHVTKNQISSNIGNLVGAQVLLELNaasA 413
Cdd:cd00887 306 PALRKLQGAPEPEPPRVKARLAEDLKSkPGRREFLRVRLE----RDEGGLVVAPPGGQGSGLLSSLARADGLIVIP---E 378
|
410
....*....|....*.
gi 25147659 414 DKTVVPKNGLVKALIL 429
Cdd:cd00887 379 GVEGLEAGEEVEVLLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
18-431 |
7.57e-119 |
|
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: 352.08 E-value: 7.57e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 18 EARKImkqIGAQIPRiVESIQVD-WSALGRVVAEEVKSSEDMPPVAASTKDGYAVIAHDGIGLK----KMVGVSLAGNIY 92
Cdd:COG0303 6 EALAL---ILAAVRP-LGTETVPlAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANpvtlRVVGEIAAGSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 93 QGAVEIGKCVRISTGGIIPEGADAVIMREYTELvrqdqqsEETEIICKQAVQVGENIRLPGSDVRSSDVIVPFEAQIGSA 172
Cdd:COG0303 82 PGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER-------EGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 173 EFGILNAFGIRTIKVYKKPVVTVISTGSELVSPmVENVPLGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLT 252
Cdd:COG0303 155 DLGLLASLGIAEVPVYRRPRVAILSTGDELVEP-GEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 253 ECLEHSDVIVTTGGVSMGEQDYMKNALLHLGFKIEFGRVSMKPGLPCTVATRESaserklKVVLALPGNPASAWVCSHLF 332
Cdd:COG0303 234 EALAEADLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLGG------KPVFGLPGNPVSALVTFELF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 333 AVPLIRDMSGYRRINHTKINVRIAQDI-KLGDRPEFVRAFIEQvgdeDDGHPIAHVTKNQISSNIGNLVGAQVLLELnaa 411
Cdd:COG0303 308 VRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLER----DDGELVVEPLGGQGSGLLSSLAEADGLIVL--- 380
|
410 420
....*....|....*....|
gi 25147659 412 SADKTVVPKNGLVKALILSS 431
Cdd:COG0303 381 PEGVEGVEAGEEVEVLLLDG 400
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
18-430 |
4.25e-92 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 291.72 E-value: 4.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 18 EARKIMKQIGAQI-PRIVESIQvdwsALGRVVAEEVKSSEDMPPVAASTKDGYAVIAHDGIGLKKMVGVSLAGNIYQG-A 95
Cdd:PLN02699 12 EALSIVLSVAARLsPVIVPLHE----ALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGvT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 96 VEIGKCVRISTGGIIPEGADAVIMREYTELVRQDQQSEETEIICKQAVQvGENIRLPGSDVRSSDVIVPFEAQIGSAEFG 175
Cdd:PLN02699 88 LTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKRVRILSQASK-GQDIRPVGCDIEKDAKVLKAGERLGASEIG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 176 ILNAFGIRTIKVYKKPVVTVISTGSELVSPMVENVPLGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTECL 255
Cdd:PLN02699 167 LLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDEAI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 256 EHS-DVIVTTGGVSMGEQDYMKNALLHLGfKIEFGRVSMKPGLPCTVATRESASERKL-KVVLA--LPGNPASAWVCSHL 331
Cdd:PLN02699 247 SSGvDILLTSGGVSMGDRDFVKPLLEKRG-TVYFSKVLMKPGKPLTFAEIDAKSAPSNsKKMLAfgLPGNPVSCLVCFNL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 332 FAVPLIRDMSGYRRINHTKINVRIAQDIKL-GDRPEFVRAFIEQVGDEDDGHP--IAHVTKNQISSNIGNLVGAQVLLEL 408
Cdd:PLN02699 326 FVVPAIRYLAGWSNPHLLRVQARLREPIKLdPVRPEFHRAIIRWKLNDGSGNPgfVAESTGHQMSSRLLSMKSANALLEL 405
|
410 420
....*....|....*....|..
gi 25147659 409 NAASAdktVVPKNGLVKALILS 430
Cdd:PLN02699 406 PATGN---VLSAGTSVSAIIIS 424
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
14-384 |
9.41e-69 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 229.72 E-value: 9.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 14 KELPEARKIMKQIGAQIPRIVESIQVDwSALGRVVAEEVKSSEDMPPVAASTKDGYAVIAHDGIG--------LKKMVGV 85
Cdd:PRK14498 10 VSLEEAREILESLLSELPLGTEEVPLE-EALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGaseanpvrLKLGGEV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 86 SlAGNIYQGAVEIGKCVRISTGGIIPEGADAVIMREYTelvrqdQQSEETEIICKQAVQVGENIRLPGSDVRSSDVIVPF 165
Cdd:PRK14498 89 H-AGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDT------EEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 166 EAQIGSAEFGILNAFGIRTIKVYKKPVVTVISTGSELVSPMvENVPLGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKE 245
Cdd:PRK14498 162 GTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPG-EPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 246 GLDKKLTECLEHSDVIVTTGGVSMGEQDYMKNALLHLGfKIEFGRVSMKPGLPCTVATRESaserklKVVLALPGNPASA 325
Cdd:PRK14498 241 ELEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEELG-EVLVHGVAIKPGKPTILGVIGG------KPVVGLPGYPVSA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25147659 326 WVCSHLFAVPLIRDMSGYRRINHTKINVRIAQDI--KLGdRPEFVRAFIEQVGDEDDGHPI 384
Cdd:PRK14498 314 LTIFEEFVAPLLRKLAGLPPPERATVKARLARRVrsELG-REEFVPVSLGRVGDGYVAYPL 373
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
43-419 |
3.40e-58 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 200.61 E-value: 3.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 43 ALGRVVAEEVKSSEDMPPVAASTKDGYAvIAHDGIGLK--KMVGVSLAGNIYQGAVEIGKCVRISTGGIIPEGADAVIMR 120
Cdd:PRK14491 226 LDGRVLAQDVISPVNVPQHTNSAMDGYA-FRSDDLEPEsyTLVGEVLAGHQYDGTLQAGEAVRIMTGAPVPAGADTVVMR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 121 EYTELvRQDQQSEETEIickqavQVGENIRLPGSDVRSSDVIVPFEAQIGSAEFGILNAFGIRTIKVYKKPVVTVISTGS 200
Cdd:PRK14491 305 ELATQ-DGDKVSFDGGI------KAGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTGD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 201 ELVSPMVENVPlGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTECLEHSDVIVTTGGVSMGEQDYMKNALL 280
Cdd:PRK14491 378 EVQAPGETLKP-NCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVSVGDADYIKTALA 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 281 HLGfKIEFGRVSMKPGLPCTVATRESaserklKVVLALPGNPASAWVCSHLFAVPLIRDMSGYRRINHTKINVRIAQDI- 359
Cdd:PRK14491 457 KLG-QIDFWRINMRPGRPLAFGQIGD------SPFFGLPGNPVAVMVSFLQFVEPALRKLAGEQNWQPLLFPAIADETLr 529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25147659 360 KLGDRPEFVRAFIEQvgdEDDGHpiAHV--TKNQISSNIGNLVGAQVLLELnaASADKTVVP 419
Cdd:PRK14491 530 SRQGRTEFSRGIYHL---GADGR--LHVrtTGKQGSGILSSMSEANCLIEI--GPAAETVNA 584
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
43-344 |
1.39e-51 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 178.75 E-value: 1.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 43 ALGRVVAEEVKSSEDMPPVAASTKDGYAVIAHD---GIGLKkMVGVSLAGNIYQGAVEIGKCVRISTGGIIPEGADAVIM 119
Cdd:PRK10680 35 CFGRITASDIVSPLDVPGFDNSAMDGYAVRLADlasGQPLP-VAGKAFAGQPFHGEWPAGTCIRIMTGAPVPEGCEAVVM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 120 REYTELVrqdqqseETEIICKQAVQVGENIRLPGSDVRSSDVIVPFEAQIGSAEFGILNAFGIRTIKVYKKPVVTVISTG 199
Cdd:PRK10680 114 QEQTEQT-------DDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVRVALFSTG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 200 SELVSPmveNVPL--GMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTECLEHSDVIVTTGGVSMGEQDYMKN 277
Cdd:PRK10680 187 DELQLP---GQPLgdGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEADYTKT 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25147659 278 ALLHLGfKIEFGRVSMKPGLPCTVATRESASerklkvVLALPGNPASAWVCSHLFAVPLIRDMSGYR 344
Cdd:PRK10680 264 ILEELG-EIAFWKLAIKPGKPFAFGKLSNSW------FCGLPGNPVSAALTFYQLVQPLLAKLSGNT 323
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
12-360 |
1.57e-48 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 173.84 E-value: 1.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 12 PKKELPEARKIMKQIGAQIPRIVESIQVD-WSALGRVVAEEVKSSEDMPPVAASTKDGYAVIAHDGIGLKKMVGVSLAGN 90
Cdd:PRK14497 6 GDESLYSIDEAIKVFLSSLNFKPKIVKVEvKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGEFKVIDKIGIGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 91 IYQgaVEIGKC--VRISTGGIIPEGADAVIMREYTELVRQDQqseeteIICKQAVQVGENIRLPGSDV-RSSDVIVPFEa 167
Cdd:PRK14497 86 FKE--IHIKECeaVEVDTGSMIPMGADAVIKVENTKVINGNF------IKIDKKINFGQNIGWIGSDIpKGSIILRKGE- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 168 QIGSAEFGILNAFGIRTIKVYKKPVVTVISTGSELVSPMVENVPlGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGL 247
Cdd:PRK14497 157 VISHEKIGLLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSP-GKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 248 DKKLTECLEHSDVIVTTGGVSMGEQDYMKNALLHLGFKIEFGrVSMKPGLPCTVAtresasERKLKVVLALPGNPASAWV 327
Cdd:PRK14497 236 KNEIKRAISVADVLILTGGTSAGEKDFVHQAIRELGNIIVHG-LKIKPGKPTILG------IVDGKPVIGLPGNIVSTMV 308
|
330 340 350
....*....|....*....|....*....|....*
gi 25147659 328 CSHLFAVPLIRDMSGYRR--INHTKINVRIAQDIK 360
Cdd:PRK14497 309 VLNMVILEYLKSLYPSRKeiLGLGKIKARLALRVK 343
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
43-408 |
3.56e-47 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 167.40 E-value: 3.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 43 ALGRVVAEEVKSSEDMPPVAASTKDGYAVIAHDGIGLKKMV---GVSLAGNIYQGAVEIGKCVRISTGGIIPEGADAVIM 119
Cdd:PRK14690 50 ALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQVLPlieGRAAAGVPFSGRVPEGMALRILTGAALPEGVDTVVL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 120 REytelvrqDQQSEETEIICKQAVQVGENIRLPGSDVRSSDVIVPFEAQIGSAEFGILNAFGIRTIKVYKKPVVTVISTG 199
Cdd:PRK14690 130 EE-------DVAGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRVAVLSTG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 200 SELVSPMvENVPLGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTECLEHSDVIVTTGGVSMGEQDYMkNAL 279
Cdd:PRK14690 203 DELVEPG-ALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGASAGDEDHV-SAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 280 LHLGFKIEFGRVSMKPGLPCTVATRESaserklKVVLALPGNPASAWVCSHLFAVPLIRDMSGYRRINHTKINVRIA-QD 358
Cdd:PRK14690 281 LREAGAMQSWRIALKPGRPLALGLWQG------VPVFGLPGNPVAALVCTLVFARPAMSLLAGEGWSEPQGFTVPAAfEK 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 25147659 359 IKLGDRPEFVRAFIEqvgdedDGHpiAHVTKNQISSNIGNLVGAQVLLEL 408
Cdd:PRK14690 355 RKKPGRREYLRARLR------QGH--AEVFRSEGSGRISGLSWAEGLVEL 396
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
30-181 |
2.82e-37 |
|
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: 133.08 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 30 IPRIVESIQVD-WSALGRVVAEEVKSSEDMPPVAASTKDGYAVIAHDGIGLKKMVGVSlAGNIYQGAVEIGKCVRISTGG 108
Cdd:pfam03453 2 LLGTEETVPLEaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIA-AGEPPGPLLPGGEAVRIMTGA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25147659 109 IIPEGADAVIMREYTELVrqdqqsEETEIICKQAVQVGENIRLPGSDVRSSDVIVPFEAQIGSAEFGILNAFG 181
Cdd:pfam03453 81 PLPEGADAVVMVEDTEEG------GGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
195-338 |
3.00e-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: 116.58 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 195 VISTGSELVSpmvenvplGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTECLEHSDVIVTTGGVSMGEQDY 274
Cdd:pfam00994 2 IITTGDELLP--------GQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 275 MKNALLHLG------FKIEFGRVSMKPGLPCTVATRESASeRKLKVVLALPGNPASAWVCSHLFAVPLIR 338
Cdd:pfam00994 74 TPEALAELGgrelpgFEELFRGVSLKPGKPVGTAPGAILS-RAGKTVFGLPGSPVAAKVMFELLLLPLLR 142
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
195-328 |
5.90e-29 |
|
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: 110.37 E-value: 5.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 195 VISTGSELVSPmvenvplGMVRDSNAPQLVALFKEHGFNVIDGGRVV--DDKEGLDKKLTECLEHSDVIVTTGGVSMGEQ 272
Cdd:smart00852 2 IISTGDELLSG-------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 273 DYMKNALLH-LGFKIEFGRVSMKPGLPCTVAT---RESASERKLKVVLALPGNPASAWVC 328
Cdd:smart00852 75 DLTPEALAElGGRELLGHGVAMRPGGPPGPLAnlsGTAPGVRGKKPVFGLPGNPVAALVM 134
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
191-335 |
1.13e-28 |
|
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: 109.71 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 191 PVVTVISTGSELVSPMvENVPLGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTECLEHSDVIVTTGGVSMG 270
Cdd:TIGR00177 1 PRVAVISVGDELVEGG-QPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25147659 271 EQDYMKNALLHLG----------FKIEFGRVSMKPGLPCTVATRESaserklKVVLALPGNPASAWVCSHLFAVP 335
Cdd:TIGR00177 80 PRDVTPEALEELGekeipgfgefRMLSSLPVLSRPGKPATAGVRGG------TLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
193-337 |
2.74e-20 |
|
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: 86.24 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 193 VTVISTGSELVspmvenvpLGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTECLEHSDVIVTTGGVSMGEQ 272
Cdd:cd00758 2 VAIVTVSDELS--------QGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25147659 273 DYMKNALLHLGFK-IEFGRVSMKPGLPCTVATRESaserklKVVLALPGNPASAWVCSHLFAVPLI 337
Cdd:cd00758 74 DVTPEALAELGEReAHGKGVALAPGSRTAFGIIGK------VLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
192-325 |
8.07e-07 |
|
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: 48.63 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 192 VVTVISTGSElvspmvenvplGMVRDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTECLE--HSDVIVTTGGVSM 269
Cdd:cd00886 5 VLTVSDTRSA-----------GEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADedGVDLILTTGGTGL 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25147659 270 GEQDYMKNALLHL------GFKIEFGRVSMKPGlPCTVATRESASERKLKVVLALPGNPASA 325
Cdd:cd00886 74 APRDVTPEATRPLldkelpGFGEAFRALSLEET-GTAMLSRAVAGIRGGTLIFNLPGSPKAV 134
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
192-325 |
8.70e-06 |
|
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: 45.88 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 192 VVTVISTGSELVSPmvenvplgmvrDSNAPQLVALFKEHGFNVIDGGRVVDDKEGLDKKLTECLEHS--DVIVTTGGVSM 269
Cdd:COG0521 14 VLTVSDRRSRGERE-----------DTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEgvDLVLTTGGTGL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25147659 270 GEQDYMKNALLHL------GFKIEFGRVSMKPGLPCTVATRESASERKLKVVLALPGNPASA 325
Cdd:COG0521 83 SPRDVTPEATRPLldkelpGFGELFRALSLEEIGPSAILSRAVAGIRGGTLIFNLPGSPGAV 144
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
195-266 |
1.64e-05 |
|
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: 45.17 E-value: 1.64e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25147659 195 VISTGSELVSpmvenvplGMVRDSNAPQLVALFKEHGFNViDGGRVV-DDKEGLDKKLTECLEHSDVIVTTGG 266
Cdd:cd00885 4 IIAIGDELLS--------GQIVDTNAAFLAKELAELGIEV-YRVTVVgDDEDRIAEALRRASERADLVITTGG 67
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
352-410 |
9.52e-04 |
|
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: 37.59 E-value: 9.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 352 NVRIAQDIKL-GDRPEFVRAFIeqvgDEDDGHPIAHVTKNQISSNIGNLVGAQVLLELNA 410
Cdd:pfam03454 1 KARLARDLKSdPGRREFVRVRL----HEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPE 56
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
162-273 |
3.21e-03 |
|
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: 39.45 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147659 162 IVPF---EAQIGSAEfGILNAFGIRTIKVYKKPVVTVISTGSElvspmvenVPLGMVRDSNAPQLVALFKEHGFNVIDGG 238
Cdd:cd03522 129 IIPLavpEALVERAE-ALARDGPLLRVAPFRPLRVGLIVTGSE--------VYGGRIEDKFGPVLRARLAALGVELVEQV 199
|
90 100 110
....*....|....*....|....*....|....*.
gi 25147659 239 RVVDDKEGLDKKLTECLE-HSDVIVTTGGVSMGEQD 273
Cdd:cd03522 200 IVPHDEAAIAAAIAEALEaGAELLILTGGASVDPDD 235
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
195-266 |
5.95e-03 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 38.62 E-value: 5.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25147659 195 VISTGSELVspmvenvpLGMVRDSNAP----QLVALFKEHGFNVIDGgrvvDDKEGLDKKLTECLEHSDVIVTTGG 266
Cdd:PRK00549 5 IIAVGTELL--------LGQIVNTNAQflseKLAELGIDVYHQTVVG----DNPERLLSALEIAEERSDLIITTGG 68
|
|
| |
