|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
7-436 |
8.44e-151 |
|
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: 433.75 E-value: 8.44e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 7 SVDEHLDDILASVRPLEPIELQLPDAQGCVLVKDVVVEVALPPFDNSSMDGYAVRVADVEGASeefPAVLTVIGDVAAGS 86
Cdd:COG0303 3 SVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAN---PVTLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 87 AglaDDQAVGPGQAARIMTGAPLPAGAEAVVPVEWTDGGTGEgpadamhahsgapegatgeVRVHRPVTAGAHVREAGGD 166
Cdd:COG0303 80 P---PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDR-------------------VTIRKPVAPGENIRRAGED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 167 VEPGALALAAGSVVGPAQIGLLAAIGCATVVVRPRPRVVVLSTGSELVQPGEQLAAGQIYDSNSFALTAAARDAGAIAYR 246
Cdd:COG0303 138 IAAGDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 247 VGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVKEALSSVGDEdepgsgVEFRKLAMQPGKPQGFGSIGpdHTP 326
Cdd:COG0303 218 LGIVPDDPEALRAALREALAEADLVITSGGVSVGDYDLVKEALEELGAE------VLFHKVAMKPGKPLAFGRLG--GKP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 327 LLALPGNPVSSYVSFELFVRPAIRALMGLEDVHRPTARARLDTekALTSPEGRRQFLRGRYDAEEG--TVTPVGGSGSHL 404
Cdd:COG0303 290 VFGLPGNPVSALVTFELFVRPALRKLAGLPPPPPPRVRARLAE--DLPKKPGRTEFLRVRLERDDGelVVEPLGGQGSGL 367
|
410 420 430
....*....|....*....|....*....|..
gi 1988328303 405 IAALAQADALIVVDEDTTSVEPGTETDVILLR 436
Cdd:COG0303 368 LSSLAEADGLIVLPEGVEGVEAGEEVEVLLLD 399
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
8-435 |
2.47e-138 |
|
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: 401.87 E-value: 2.47e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 8 VDEHLDDILASVRPLEPIELQLPDAQGCVLVKDVVVEVALPPFDNSSMDGYAVRVADVEGASEEFPavltVIGDVAAGSA 87
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLR----VVGEIPAGEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 88 GladDQAVGPGQAARIMTGAPLPAGAEAVVPVEWTdggtgegpadamhahsgapEGATGEVRVHRPVTAGAHVREAGGDV 167
Cdd:cd00887 77 P---DGPLGPGEAVRIMTGAPLPEGADAVVMVEDT-------------------EEEGGRVTITKPVKPGQNIRRAGEDI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 168 EPGALALAAGSVVGPAQIGLLAAIGCATVVVRPRPRVVVLSTGSELVQPGEQLAAGQIYDSNSFALTAAARDAGAIAYRV 247
Cdd:cd00887 135 KAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 248 GAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVKEALSSVGDEdepgsgVEFRKLAMQPGKPQGFGSIGpdHTPL 327
Cdd:cd00887 215 GIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKEVLEELGGE------VLFHGVAMKPGKPLAFGRLG--GKPV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 328 LALPGNPVSSYVSFELFVRPAIRALMGLEDVHRPTARARLDteKALTSPEGRRQFLRGRYDAEEG--TVTPVGGSGSHLI 405
Cdd:cd00887 287 FGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRVKARLA--EDLKSKPGRREFLRVRLERDEGglVVAPPGGQGSGLL 364
|
410 420 430
....*....|....*....|....*....|
gi 1988328303 406 AALAQADALIVVDEDTTSVEPGTETDVILL 435
Cdd:cd00887 365 SSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
48-436 |
7.95e-92 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 290.19 E-value: 7.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 48 PPFDNSSMDGYAVRVADVEGASEEFPAVLTVIGDVAAGSAGladDQAVGPGQAARIMTGAPLPAGAEAVVPVEWTDggtg 127
Cdd:PRK14498 54 PPFDRSAMDGYAVRAADTFGASEANPVRLKLGGEVHAGEAP---DVEVEPGEAVEIATGAPIPRGADAVVMVEDTE---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 128 egpadamhahsgapEGATGEVRVHRPVTAGAHVREAGGDVEPGALALAAGSVVGPAQIGLLAAIGCATVVVRPRPRVVVL 207
Cdd:PRK14498 127 --------------EVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGII 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 208 STGSELVQPGEQLAAGQIYDSNSFALTAAARDAGAIAYRVGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVKE 287
Cdd:PRK14498 193 STGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVLLSGGTSAGAGDVTYR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 288 ALSSVGDedepgsgVEFRKLAMQPGKPQGFGSIgpDHTPLLALPGNPVSSYVSFELFVRPAIRALMGLEDVHRPTARARL 367
Cdd:PRK14498 273 VIEELGE-------VLVHGVAIKPGKPTILGVI--GGKPVVGLPGYPVSALTIFEEFVAPLLRKLAGLPPPERATVKARL 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988328303 368 DTEkaLTSPEGRRQFLR---GRyDAEEGTVTPVG-GSGShlIAALAQADALIVVDEDTTSVEPGTETDVILLR 436
Cdd:PRK14498 344 ARR--VRSELGREEFVPvslGR-VGDGYVAYPLSrGSGA--ITSLVRADGFIEIPANTEGLEAGEEVEVELFG 411
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
46-192 |
1.72e-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: 133.46 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 46 ALPPFDNSSMDGYAVRVADVEGASEEFPAvltvigdvaagSAGLADDQAVGPGQAARIMTGAPLPAGAEAVVPVEWTDgg 125
Cdd:pfam03453 30 DVPPFDRSAMDGYAVRAADGFGASEVNPI-----------AAGEPPGPLLPGGEAVRIMTGAPLPEGADAVVMVEDTE-- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988328303 126 tgegpadamhahsgapEGATGEVRVHRPVTAGAHVREAGGDVEPGALALAAGSVVGPAQIGLLAAIG 192
Cdd:pfam03453 97 ----------------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
207-347 |
1.02e-36 |
|
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: 131.67 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 207 LSTGSELVQPGEQLAAGQIYDSNSFALTAAARDAGAIAYRVGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVK 286
Cdd:TIGR00177 6 ISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRDVTP 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988328303 287 EALSSVGDEDEPGSGVEFRK----LAMQPGKPQGFGSIGpdHTPLLALPGNPVSSYVSFELFVRP 347
Cdd:TIGR00177 86 EALEELGEKEIPGFGEFRMLsslpVLSRPGKPATAGVRG--GTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
207-344 |
1.72e-27 |
|
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: 106.52 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 207 LSTGSELVQPGeqlaagQIYDSNSFALTA--AARDAGAIAYRVGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDV 284
Cdd:smart00852 3 ISTGDELLSGG------QIRDSNGPMLAAllRELGIEVVRVVVVGGPDDPEAIREALREALAEADVVITTGGTGPGPDDL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988328303 285 VKEALSSVGDEDepgsgVEFRKLAMQPGKPQG-----FGSIG--PDHTPLLALPGNPVSSYVSFELF 344
Cdd:smart00852 77 TPEALAELGGRE-----LLGHGVAMRPGGPPGplanlSGTAPgvRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
7-436 |
8.44e-151 |
|
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: 433.75 E-value: 8.44e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 7 SVDEHLDDILASVRPLEPIELQLPDAQGCVLVKDVVVEVALPPFDNSSMDGYAVRVADVEGASeefPAVLTVIGDVAAGS 86
Cdd:COG0303 3 SVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAN---PVTLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 87 AglaDDQAVGPGQAARIMTGAPLPAGAEAVVPVEWTDGGTGEgpadamhahsgapegatgeVRVHRPVTAGAHVREAGGD 166
Cdd:COG0303 80 P---PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDR-------------------VTIRKPVAPGENIRRAGED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 167 VEPGALALAAGSVVGPAQIGLLAAIGCATVVVRPRPRVVVLSTGSELVQPGEQLAAGQIYDSNSFALTAAARDAGAIAYR 246
Cdd:COG0303 138 IAAGDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 247 VGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVKEALSSVGDEdepgsgVEFRKLAMQPGKPQGFGSIGpdHTP 326
Cdd:COG0303 218 LGIVPDDPEALRAALREALAEADLVITSGGVSVGDYDLVKEALEELGAE------VLFHKVAMKPGKPLAFGRLG--GKP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 327 LLALPGNPVSSYVSFELFVRPAIRALMGLEDVHRPTARARLDTekALTSPEGRRQFLRGRYDAEEG--TVTPVGGSGSHL 404
Cdd:COG0303 290 VFGLPGNPVSALVTFELFVRPALRKLAGLPPPPPPRVRARLAE--DLPKKPGRTEFLRVRLERDDGelVVEPLGGQGSGL 367
|
410 420 430
....*....|....*....|....*....|..
gi 1988328303 405 IAALAQADALIVVDEDTTSVEPGTETDVILLR 436
Cdd:COG0303 368 LSSLAEADGLIVLPEGVEGVEAGEEVEVLLLD 399
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
8-435 |
2.47e-138 |
|
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: 401.87 E-value: 2.47e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 8 VDEHLDDILASVRPLEPIELQLPDAQGCVLVKDVVVEVALPPFDNSSMDGYAVRVADVEGASEEFPavltVIGDVAAGSA 87
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLR----VVGEIPAGEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 88 GladDQAVGPGQAARIMTGAPLPAGAEAVVPVEWTdggtgegpadamhahsgapEGATGEVRVHRPVTAGAHVREAGGDV 167
Cdd:cd00887 77 P---DGPLGPGEAVRIMTGAPLPEGADAVVMVEDT-------------------EEEGGRVTITKPVKPGQNIRRAGEDI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 168 EPGALALAAGSVVGPAQIGLLAAIGCATVVVRPRPRVVVLSTGSELVQPGEQLAAGQIYDSNSFALTAAARDAGAIAYRV 247
Cdd:cd00887 135 KAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 248 GAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVKEALSSVGDEdepgsgVEFRKLAMQPGKPQGFGSIGpdHTPL 327
Cdd:cd00887 215 GIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKEVLEELGGE------VLFHGVAMKPGKPLAFGRLG--GKPV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 328 LALPGNPVSSYVSFELFVRPAIRALMGLEDVHRPTARARLDteKALTSPEGRRQFLRGRYDAEEG--TVTPVGGSGSHLI 405
Cdd:cd00887 287 FGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRVKARLA--EDLKSKPGRREFLRVRLERDEGglVVAPPGGQGSGLL 364
|
410 420 430
....*....|....*....|....*....|
gi 1988328303 406 AALAQADALIVVDEDTTSVEPGTETDVILL 435
Cdd:cd00887 365 SSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
48-436 |
7.95e-92 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 290.19 E-value: 7.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 48 PPFDNSSMDGYAVRVADVEGASEEFPAVLTVIGDVAAGSAGladDQAVGPGQAARIMTGAPLPAGAEAVVPVEWTDggtg 127
Cdd:PRK14498 54 PPFDRSAMDGYAVRAADTFGASEANPVRLKLGGEVHAGEAP---DVEVEPGEAVEIATGAPIPRGADAVVMVEDTE---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 128 egpadamhahsgapEGATGEVRVHRPVTAGAHVREAGGDVEPGALALAAGSVVGPAQIGLLAAIGCATVVVRPRPRVVVL 207
Cdd:PRK14498 127 --------------EVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGII 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 208 STGSELVQPGEQLAAGQIYDSNSFALTAAARDAGAIAYRVGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVKE 287
Cdd:PRK14498 193 STGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVLLSGGTSAGAGDVTYR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 288 ALSSVGDedepgsgVEFRKLAMQPGKPQGFGSIgpDHTPLLALPGNPVSSYVSFELFVRPAIRALMGLEDVHRPTARARL 367
Cdd:PRK14498 273 VIEELGE-------VLVHGVAIKPGKPTILGVI--GGKPVVGLPGYPVSALTIFEEFVAPLLRKLAGLPPPERATVKARL 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988328303 368 DTEkaLTSPEGRRQFLR---GRyDAEEGTVTPVG-GSGShlIAALAQADALIVVDEDTTSVEPGTETDVILLR 436
Cdd:PRK14498 344 ARR--VRSELGREEFVPvslGR-VGDGYVAYPLSrGSGA--ITSLVRADGFIEIPANTEGLEAGEEVEVELFG 411
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
2-428 |
6.32e-80 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 258.39 E-value: 6.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 2 SSRIWSVDEHLDDILASVRPLEPIE-LQLPDAQGCVLVKDVVVEVALPPFDNSSMDGYAVRVADVEgaseefPAVLTVIG 80
Cdd:PRK14491 195 SPAFLSVSQGLDKILSLVTPVTETEdVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLE------PESYTLVG 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 81 DVAAGSAglaDDQAVGPGQAARIMTGAPLPAGAEAVVPVEWT--DGGTgegpadamhahsgapegatgeVRVHRPVTAGA 158
Cdd:PRK14491 269 EVLAGHQ---YDGTLQAGEAVRIMTGAPVPAGADTVVMRELAtqDGDK---------------------VSFDGGIKAGQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 159 HVREAGGDVEPGALALAAGSVVGPAQIGLLAAIGCATVVVRPRPRVVVLSTGSELVQPGEQLAAGQIYDSNSFALTAAAR 238
Cdd:PRK14491 325 NVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAK 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 239 DAGAIAYRVGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVKEALSSVGDedepgsgVEFRKLAMQPGKPQGFG 318
Cdd:PRK14491 405 KLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVSVGDADYIKTALAKLGQ-------IDFWRINMRPGRPLAFG 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 319 SIGpdHTPLLALPGNPVSSYVSFELFVRPAIRALMGlEDVHRPTaRARLDTEKALTSPEGRRQFLRGRYD-AEEG--TVT 395
Cdd:PRK14491 478 QIG--DSPFFGLPGNPVAVMVSFLQFVEPALRKLAG-EQNWQPL-LFPAIADETLRSRQGRTEFSRGIYHlGADGrlHVR 553
|
410 420 430
....*....|....*....|....*....|...
gi 1988328303 396 PVGGSGSHLIAALAQADALIVVDEDTTSVEPGT 428
Cdd:PRK14491 554 TTGKQGSGILSSMSEANCLIEIGPAAETVNAGE 586
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
2-432 |
1.54e-72 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 233.83 E-value: 1.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 2 SSRIWSVDEHLDDILASVRPLEPIE-LQLPDAQGCVLVKDVVVEVALPPFDNSSMDGYAVRVADVEGAseefpAVLTVIG 80
Cdd:PRK10680 4 TAGLMSLETALTEMLSRVTPLTATEtLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASG-----QPLPVAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 81 DVAAGsaglADDQAVGP-GQAARIMTGAPLPAGAEAVVPVEWTDGgTGEGpadamhahsgapegatgeVRVHRPVTAGAH 159
Cdd:PRK10680 79 KAFAG----QPFHGEWPaGTCIRIMTGAPVPEGCEAVVMQEQTEQ-TDDG------------------VRFTAEVRSGQN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 160 VREAGGDVEPGALALAAGSVVGPAQIGLLAAIGCATVVVRPRPRVVVLSTGSELVQPGEQLAAGQIYDSNSFALTAAARD 239
Cdd:PRK10680 136 IRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 240 AGAIAYRVGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVKEALSSVGDedepgsgVEFRKLAMQPGKPQGFGS 319
Cdd:PRK10680 216 LGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEADYTKTILEELGE-------IAFWKLAIKPGKPFAFGK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 320 IgpDHTPLLALPGNPVSSYVSFELFVRPAIRALMGLEDVHRPtARARLDTEKALTSPEGRRQFLRG---RYDAEEGTVTP 396
Cdd:PRK10680 289 L--SNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNTASGLP-PRQRVRTASRLKKTPGRLDFQRGilqRNADGELEVTT 365
|
410 420 430
....*....|....*....|....*....|....*.
gi 1988328303 397 VGGSGSHLIAALAQADALIVVDEDTTSVEPGTETDV 432
Cdd:PRK10680 366 TGHQGSHIFSSFSLGNCFIVLERERGNVEVGEWVEV 401
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
7-436 |
1.26e-53 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 189.64 E-value: 1.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 7 SVDEHLDDILASVRPLEPIELQLPDAQGCVLVKDVVVEVALPPFDNSSMDGYAVRVADVEGaseEFPavltVIGDVAAGS 86
Cdd:PLN02699 9 SVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPG---EYP----VITESRAGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 87 AGLadDQAVGPGQAARIMTGAPLPAGAEAVVPVEWTDGGTGegpadamhahsgaPEGATGEVRVHRPVTAGAHVREAGGD 166
Cdd:PLN02699 82 DGL--GVTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVED-------------PLDGSKRVRILSQASKGQDIRPVGCD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 167 VEPGALALAAGSVVGPAQIGLLAAIGCATVVVRPRPRVVVLSTGSELVQPGEQ-LAAGQIYDSNSFALTAAARDAGAIAY 245
Cdd:PLN02699 147 IEKDAKVLKAGERLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 246 RVGAVSDDAETLRATIEDQLIR-ADIVVTTGGVSVGAYDVVKEALSSVGDedepgsgVEFRKLAMQPGKPQGFGSIGPDH 324
Cdd:PLN02699 227 DLGIARDDEEELERILDEAISSgVDILLTSGGVSMGDRDFVKPLLEKRGT-------VYFSKVLMKPGKPLTFAEIDAKS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 325 TP-----LLA--LPGNPVSSYVSFELFVRPAIRALMGLEDVHRPTARARLdtEKALTSPEGRRQFLRG--RYDAEEGTVT 395
Cdd:PLN02699 300 APsnskkMLAfgLPGNPVSCLVCFNLFVVPAIRYLAGWSNPHLLRVQARL--REPIKLDPVRPEFHRAiiRWKLNDGSGN 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1988328303 396 P--VGGSGSHLIA----ALAQADALIVVDEDTTSVEPGTETDVILLR 436
Cdd:PLN02699 378 PgfVAESTGHQMSsrllSMKSANALLELPATGNVLSAGTSVSAIIIS 424
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
3-434 |
1.22e-45 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 165.75 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 3 SRIWSVDEHLDDILASVRPL-EPIELQLPDAQGCVLVKDVVVEVALPPFDNSSMDGYAVRvadvegaSEEFPAVLTVIGD 81
Cdd:PRK14497 8 ESLYSIDEAIKVFLSSLNFKpKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALK-------SSCTPGEFKVIDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 82 VaagSAGLADDQAVGPGQAARIMTGAPLPAGAEAVVPVEwtDGGTGEGPadamhahsgapegatgEVRVHRPVTAGAHVR 161
Cdd:PRK14497 81 I---GIGEFKEIHIKECEAVEVDTGSMIPMGADAVIKVE--NTKVINGN----------------FIKIDKKINFGQNIG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 162 EAGGDVEPGALALAAGSVVGPAQIGLLAAIGCATVVVRPRPRVVVLSTGSELVQPGEQLAAGQIYDSNSFALTAAARDAG 241
Cdd:PRK14497 140 WIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 242 AIAYRVGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVKEALSSVGDedepgsgVEFRKLAMQPGKPQGFGSIg 321
Cdd:PRK14497 220 YKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKDFVHQAIRELGN-------IIVHGLKIKPGKPTILGIV- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 322 pDHTPLLALPGNPVSSYVSFELFVRPAIRALMGLEdvhrpTARARLDTEKAltspegrRQFLRGRYDAEEGTVTPV---G 398
Cdd:PRK14497 292 -DGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPSR-----KEILGLGKIKA-------RLALRVKADEHRNTLIPVylfK 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1988328303 399 GSGSH----------LIAALAQADALIVVdEDTTSVEPGTETDVIL 434
Cdd:PRK14497 359 SDNSYyalpvpfdsyMVGTFSLTDGYIML-GPNEEIEEGKEVEVDL 403
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
8-427 |
5.44e-44 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 158.93 E-value: 5.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 8 VDEHLDDILASVRPLEPIE-LQLPDAQGCVLVKDVVVEVALPPFDNSSMDGYAVRVADVEGASeefpaVLTVIGDVAAgs 86
Cdd:PRK14690 25 VDTALDLLRARLGPVTDIKeLDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQ-----VLPLIEGRAA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 87 AGLADDQAVGPGQAARIMTGAPLPAGAEAVVPVEWTDGGTGEgpadamhahsgapegatgeVRVHRPVTAGAHVREAGGD 166
Cdd:PRK14690 98 AGVPFSGRVPEGMALRILTGAALPEGVDTVVLEEDVAGDGHR-------------------IAFHGPLKMGANTRKAGED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 167 VEPGALALAAGSVVGPAQIGLLAAIGCATVVVRPRPRVVVLSTGSELVQPGEQLAAGQIYDSNSFALTAAARDAGAIAYR 246
Cdd:PRK14690 159 VIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 247 VGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVKEALSsvgdedEPGSGVEFRkLAMQPGKPQGFGSIgpDHTP 326
Cdd:PRK14690 239 LGRVGDDRAALAARLDRAAAEADVILTSGGASAGDEDHVSALLR------EAGAMQSWR-IALKPGRPLALGLW--QGVP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 327 LLALPGNPVSSYVSFELFVRPAIRALMGlEDVHRP---TARARLDTEKAltspEGRRQFLRGRydAEEGTVTPVGGSGSH 403
Cdd:PRK14690 310 VFGLPGNPVAALVCTLVFARPAMSLLAG-EGWSEPqgfTVPAAFEKRKK----PGRREYLRAR--LRQGHAEVFRSEGSG 382
|
410 420
....*....|....*....|....
gi 1988328303 404 LIAALAQADALIVVDEDTTSVEPG 427
Cdd:PRK14690 383 RISGLSWAEGLVELGDGARRIAPG 406
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
46-192 |
1.72e-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: 133.46 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 46 ALPPFDNSSMDGYAVRVADVEGASEEFPAvltvigdvaagSAGLADDQAVGPGQAARIMTGAPLPAGAEAVVPVEWTDgg 125
Cdd:pfam03453 30 DVPPFDRSAMDGYAVRAADGFGASEVNPI-----------AAGEPPGPLLPGGEAVRIMTGAPLPEGADAVVMVEDTE-- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988328303 126 tgegpadamhahsgapEGATGEVRVHRPVTAGAHVREAGGDVEPGALALAAGSVVGPAQIGLLAAIG 192
Cdd:pfam03453 97 ----------------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
207-347 |
1.02e-36 |
|
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: 131.67 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 207 LSTGSELVQPGEQLAAGQIYDSNSFALTAAARDAGAIAYRVGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVK 286
Cdd:TIGR00177 6 ISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRDVTP 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988328303 287 EALSSVGDEDEPGSGVEFRK----LAMQPGKPQGFGSIGpdHTPLLALPGNPVSSYVSFELFVRP 347
Cdd:TIGR00177 86 EALEELGEKEIPGFGEFRMLsslpVLSRPGKPATAGVRG--GTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
207-351 |
1.29e-33 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 123.13 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 207 LSTGSELVqpgeqlaAGQIYDSNSFALTAAARDAGAIAYRVGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVK 286
Cdd:pfam00994 3 ITTGDELL-------PGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTP 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988328303 287 EALSSVGDEDEPGSGVEFRKLAMQPGKPQGFG---SIGPDHTPLLALPGNPVSSYVSFELFVRPAIRA 351
Cdd:pfam00994 76 EALAELGGRELPGFEELFRGVSLKPGKPVGTApgaILSRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
207-344 |
1.72e-27 |
|
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: 106.52 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 207 LSTGSELVQPGeqlaagQIYDSNSFALTA--AARDAGAIAYRVGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDV 284
Cdd:smart00852 3 ISTGDELLSGG------QIRDSNGPMLAAllRELGIEVVRVVVVGGPDDPEAIREALREALAEADVVITTGGTGPGPDDL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988328303 285 VKEALSSVGDEDepgsgVEFRKLAMQPGKPQG-----FGSIG--PDHTPLLALPGNPVSSYVSFELF 344
Cdd:smart00852 77 TPEALAELGGRE-----LLGHGVAMRPGGPPGplanlSGTAPgvRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
207-349 |
1.21e-23 |
|
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: 95.49 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 207 LSTGSELVQpgeqlaaGQIYDSNSFALTAAARDAGAIAYRVGAVSDDAETLRATIEDQLIRADIVVTTGGVSVGAYDVVK 286
Cdd:cd00758 5 VTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTP 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988328303 287 EALSSVGDEDEPGSGVefrklAMQPGKPQGFGSIGpdHTPLLALPGNPVSSYVSFELFVRPAI 349
Cdd:cd00758 78 EALAELGEREAHGKGV-----ALAPGSRTAFGIIG--KVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
364-435 |
1.10e-16 |
|
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: 74.18 E-value: 1.10e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988328303 364 RARLDTekALTSPEGRRQFLRGRYDAEEG--TVTPVGGSGSHLIAALAQADALIVVDEDTTSVEPGTETDVILL 435
Cdd:pfam03454 1 KARLAR--DLKSDPGRREFVRVRLHEEDGryYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
245-334 |
3.58e-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: 43.95 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 245 YRVgaVSDDAETLRATIEDQLIR--ADIVVTTGGVSVGAYDVVKEALSSVGDEDEPGSGVEFRKLAMQpgkpqgfgSIGP 322
Cdd:COG0521 48 RRI--VPDDKDAIRAALRELIDDegVDLVLTTGGTGLSPRDVTPEATRPLLDKELPGFGELFRALSLE--------EIGP 117
|
90 100
....*....|....*....|....
gi 1988328303 323 ------------DHTPLLALPGNP 334
Cdd:COG0521 118 sailsravagirGGTLIFNLPGSP 141
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
207-276 |
4.16e-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: 44.01 E-value: 4.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988328303 207 LSTGSELVqpgeqlaAGQIYDSNSFALTAAARDAGAIAYRVGAVSDDAETLRATIEDQLIRADIVVTTGG 276
Cdd:cd00885 5 IAIGDELL-------SGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
250-310 |
1.44e-03 |
|
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.
Pssm-ID: 238451 [Multi-domain] Cd Length: 152 Bit Score: 39.00 E-value: 1.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988328303 250 VSDDAETLRATIED--QLIRADIVVTTGGVSVGAYDVVKEALSSVGDEDEPGSGVEFRKLAMQ 310
Cdd:cd00886 42 VPDDKDEIREALIEwaDEDGVDLILTTGGTGLAPRDVTPEATRPLLDKELPGFGEAFRALSLE 104
|
|
| |
