|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
30-417 |
2.53e-148 |
|
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: 426.52 E-value: 2.53e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 30 PLDEAHGCVLAAPVVSPEDLPAADRSCMDGYAVRAADLFGttegNPAYLECTGTVSIERPADFSIAAGECAAIVTGALLP 109
Cdd:cd00887 21 PLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAG----ASVTLRVVGEIPAGEPPDGPLGPGEAVRIMTGAPLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 110 RGADAVVMVEHTQEMGaGTVEIRKSVAPHEHVMLRGEDAVQGQPALTAGTLLRAQEIGLLAALGVQTVHVHRRPRVGIFS 189
Cdd:cd00887 97 EGADAVVMVEDTEEEG-GRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVAIIS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 190 TGDEVIPAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDMVLLSGGSSVGTRDLTMAA 269
Cdd:cd00887 176 TGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 270 LDSLdGAAVINHGVAISPGKPLILASADGKgqrcAVWGLPGQVTSAQVVMFVLGIPFVHWLAGRRTPfdqsAWASRRAVL 349
Cdd:cd00887 256 LEEL-GGEVLFHGVAMKPGKPLAFGRLGGK----PVFGLPGNPVSALVTFELFVRPALRKLQGAPEP----EPPRVKARL 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78217682 350 ARNIASRQGREDYIRVRLHAEEDGRVTATPVTGKSGLLRTMLQAHGVVRIPAHSEGLDSGTQVDVLLF 417
Cdd:cd00887 327 AEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
18-419 |
1.65e-146 |
|
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: 422.19 E-value: 1.65e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 18 LRGFDHLPALQTPLDEAHGCVLAAPVVSPEDLPAADRSCMDGYAVRAADLFGtteGNPAYLECTGTVSIERPADFSIAAG 97
Cdd:COG0303 12 LAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAG---ANPVTLRVVGEIAAGSPPPGPLGPG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 98 ECAAIVTGALLPRGADAVVMVEHTQEMGaGTVEIRKSVAPHEHVMLRGEDAVQGQPALTAGTLLRAQEIGLLAALGVQTV 177
Cdd:COG0303 89 EAVRIMTGAPLPEGADAVVMQEDTEREG-DRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLASLGIAEV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 178 HVHRRPRVGIFSTGDEVIPAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDMVLLSGG 257
Cdd:COG0303 168 PVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 258 SSVGTRDLTMAALDSLdGAAVINHGVAISPGKPLILASADGKgqrcAVWGLPGQVTSAQVVMFVLGIPFVHWLAGRRTPf 337
Cdd:COG0303 248 VSVGDYDLVKEALEEL-GAEVLFHKVAMKPGKPLAFGRLGGK----PVFGLPGNPVSALVTFELFVRPALRKLAGLPPP- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 338 dqsAWASRRAVLARNIASRQGREDYIRVRLHaEEDGRVTATPVTG-KSGLLRTMLQAHGVVRIPAHSEGLDSGTQVDVLL 416
Cdd:COG0303 322 ---PPPRVRARLAEDLPKKPGRTEFLRVRLE-RDDGELVVEPLGGqGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLL 397
|
...
gi 78217682 417 FGG 419
Cdd:COG0303 398 LDG 400
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
15-418 |
3.07e-133 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 396.51 E-value: 3.07e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 15 IDRLRGFDHLPALQT---PLDEAHGCVLAAPVVSPEDLPAADRSCMDGYAVRAADLFGTTEGNPAYLECTGTVSIERPAD 91
Cdd:PRK14498 16 REILESLLSELPLGTeevPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLKLGGEVHAGEAPD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 92 FSIAAGECAAIVTGALLPRGADAVVMVEHTQEMGAGTVEIRKSVAPHEHVMLRGEDAVQGQPALTAGTLLRAQEIGLLAA 171
Cdd:PRK14498 96 VEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 172 LGVQTVHVHRRPRVGIFSTGDEVIPAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDM 251
Cdd:PRK14498 176 GGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 252 VLLSGGSSVGTRDLTMAALDSLdgAAVINHGVAISPGKPLILASADGKgqrcAVWGLPGQVTSAQVVMFVLGIPFVHWLA 331
Cdd:PRK14498 256 VLLSGGTSAGAGDVTYRVIEEL--GEVLVHGVAIKPGKPTILGVIGGK----PVVGLPGYPVSALTIFEEFVAPLLRKLA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 332 GRRTPFDQSAwasrRAVLARNIASRQGREDYIRVRLhAEEDGRVTATPVTGKSGLLRTMLQAHGVVRIPAHSEGLDSGTQ 411
Cdd:PRK14498 330 GLPPPERATV----KARLARRVRSELGREEFVPVSL-GRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTEGLEAGEE 404
|
....*..
gi 78217682 412 VDVLLFG 418
Cdd:PRK14498 405 VEVELFG 411
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
32-173 |
8.64e-50 |
|
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: 165.43 E-value: 8.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 32 DEAHGCVLAAPVVSPEDLPAADRSCMDGYAVRAADLFGTTEGNPaylectgtVSIERPADFSIAAGECAAIVTGALLPRG 111
Cdd:pfam03453 14 LDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLPGGEAVRIMTGAPLPEG 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78217682 112 ADAVVMVEHTQEMGAGTVEIRKSVAPHEHVMLRGEDAVQGQPALTAGTLLRAQEIGLLAALG 173
Cdd:pfam03453 86 ADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
186-322 |
1.75e-24 |
|
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: 98.04 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 186 GIFSTGDEVIPahatprPGQVRDVNSHALQAMARAAGAAVTCYGIV--PDDEKALTAMLARTTAENDMVLLSGGSSVGTR 263
Cdd:smart00852 1 AIISTGDELLS------GGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78217682 264 DLTMAALDSLDGAAVINHGVAISPGKP-----LILASADGKGQRCAVWGLPGQVTSAQVVMFVL 322
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPpgplaNLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
183-325 |
4.50e-21 |
|
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: 88.91 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 183 PRVGIFSTGDEVIPAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDMVLLSGGSSVGT 262
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78217682 263 RDLTMAALDSLDGAAVINHG---------VAISPGKPLILASADGkgqrCAVWGLPGQVTSAQVVMFVLGIP 325
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGFGefrmlsslpVLSRPGKPATAGVRGG----TLIFNLPGNPVSALVTFEVLILP 148
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
30-417 |
2.53e-148 |
|
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: 426.52 E-value: 2.53e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 30 PLDEAHGCVLAAPVVSPEDLPAADRSCMDGYAVRAADLFGttegNPAYLECTGTVSIERPADFSIAAGECAAIVTGALLP 109
Cdd:cd00887 21 PLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAG----ASVTLRVVGEIPAGEPPDGPLGPGEAVRIMTGAPLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 110 RGADAVVMVEHTQEMGaGTVEIRKSVAPHEHVMLRGEDAVQGQPALTAGTLLRAQEIGLLAALGVQTVHVHRRPRVGIFS 189
Cdd:cd00887 97 EGADAVVMVEDTEEEG-GRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVAIIS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 190 TGDEVIPAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDMVLLSGGSSVGTRDLTMAA 269
Cdd:cd00887 176 TGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 270 LDSLdGAAVINHGVAISPGKPLILASADGKgqrcAVWGLPGQVTSAQVVMFVLGIPFVHWLAGRRTPfdqsAWASRRAVL 349
Cdd:cd00887 256 LEEL-GGEVLFHGVAMKPGKPLAFGRLGGK----PVFGLPGNPVSALVTFELFVRPALRKLQGAPEP----EPPRVKARL 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78217682 350 ARNIASRQGREDYIRVRLHAEEDGRVTATPVTGKSGLLRTMLQAHGVVRIPAHSEGLDSGTQVDVLLF 417
Cdd:cd00887 327 AEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
18-419 |
1.65e-146 |
|
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: 422.19 E-value: 1.65e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 18 LRGFDHLPALQTPLDEAHGCVLAAPVVSPEDLPAADRSCMDGYAVRAADLFGtteGNPAYLECTGTVSIERPADFSIAAG 97
Cdd:COG0303 12 LAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAG---ANPVTLRVVGEIAAGSPPPGPLGPG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 98 ECAAIVTGALLPRGADAVVMVEHTQEMGaGTVEIRKSVAPHEHVMLRGEDAVQGQPALTAGTLLRAQEIGLLAALGVQTV 177
Cdd:COG0303 89 EAVRIMTGAPLPEGADAVVMQEDTEREG-DRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLASLGIAEV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 178 HVHRRPRVGIFSTGDEVIPAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDMVLLSGG 257
Cdd:COG0303 168 PVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 258 SSVGTRDLTMAALDSLdGAAVINHGVAISPGKPLILASADGKgqrcAVWGLPGQVTSAQVVMFVLGIPFVHWLAGRRTPf 337
Cdd:COG0303 248 VSVGDYDLVKEALEEL-GAEVLFHKVAMKPGKPLAFGRLGGK----PVFGLPGNPVSALVTFELFVRPALRKLAGLPPP- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 338 dqsAWASRRAVLARNIASRQGREDYIRVRLHaEEDGRVTATPVTG-KSGLLRTMLQAHGVVRIPAHSEGLDSGTQVDVLL 416
Cdd:COG0303 322 ---PPPRVRARLAEDLPKKPGRTEFLRVRLE-RDDGELVVEPLGGqGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLL 397
|
...
gi 78217682 417 FGG 419
Cdd:COG0303 398 LDG 400
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
15-418 |
3.07e-133 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 396.51 E-value: 3.07e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 15 IDRLRGFDHLPALQT---PLDEAHGCVLAAPVVSPEDLPAADRSCMDGYAVRAADLFGTTEGNPAYLECTGTVSIERPAD 91
Cdd:PRK14498 16 REILESLLSELPLGTeevPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLKLGGEVHAGEAPD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 92 FSIAAGECAAIVTGALLPRGADAVVMVEHTQEMGAGTVEIRKSVAPHEHVMLRGEDAVQGQPALTAGTLLRAQEIGLLAA 171
Cdd:PRK14498 96 VEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 172 LGVQTVHVHRRPRVGIFSTGDEVIPAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDM 251
Cdd:PRK14498 176 GGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 252 VLLSGGSSVGTRDLTMAALDSLdgAAVINHGVAISPGKPLILASADGKgqrcAVWGLPGQVTSAQVVMFVLGIPFVHWLA 331
Cdd:PRK14498 256 VLLSGGTSAGAGDVTYRVIEEL--GEVLVHGVAIKPGKPTILGVIGGK----PVVGLPGYPVSALTIFEEFVAPLLRKLA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 332 GRRTPFDQSAwasrRAVLARNIASRQGREDYIRVRLhAEEDGRVTATPVTGKSGLLRTMLQAHGVVRIPAHSEGLDSGTQ 411
Cdd:PRK14498 330 GLPPPERATV----KARLARRVRSELGREEFVPVSL-GRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTEGLEAGEE 404
|
....*..
gi 78217682 412 VDVLLFG 418
Cdd:PRK14498 405 VEVELFG 411
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
30-419 |
2.40e-67 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 224.49 E-value: 2.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 30 PLDEAHGCVLAAPVVSPEDLPAADRSCMDGYAVRAADLfgttegNPAYLECTGTVSIERPADFSIAAGECAAIVTGALLP 109
Cdd:PRK14491 222 ALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDL------EPESYTLVGEVLAGHQYDGTLQAGEAVRIMTGAPVP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 110 RGADAVVMVEHTQEMGaGTVEIRKSVAPHEHVMLRGEDAVQGQPALTAGTLLRAQEIGLLAALGVQTVHVHRRPRVGIFS 189
Cdd:PRK14491 296 AGADTVVMRELATQDG-DKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFS 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 190 TGDEVIPAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDMVLLSGGSSVGTRDLTMAA 269
Cdd:PRK14491 375 TGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVSVGDADYIKTA 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 270 LDSLdgaAVINH-GVAISPGKPLilasADGKGQRCAVWGLPGQVTSAQVVMFVLGIPFVHWLAGRRTpfdqsaWASRR-- 346
Cdd:PRK14491 455 LAKL---GQIDFwRINMRPGRPL----AFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKLAGEQN------WQPLLfp 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78217682 347 AVLARNIASRQGREDYIRVRLHAEEDGRVTATpVTGK--SGLLRTMLQAHGVVRIPAHSEGLDSGTQVDVLLFGG 419
Cdd:PRK14491 522 AIADETLRSRQGRTEFSRGIYHLGADGRLHVR-TTGKqgSGILSSMSEANCLIEIGPAAETVNAGETVTIQPLAG 595
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
24-385 |
1.10e-56 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 191.84 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 24 LPALQT-PLDEAHGCVLAAPVVSPEDLPAADRSCMDGYAVRAADLfgtTEGNPayLECTGTVSIERPADFSIAAGECAAI 102
Cdd:PRK10680 24 LTATETlPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADL---ASGQP--LPVAGKAFAGQPFHGEWPAGTCIRI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 103 VTGALLPRGADAVVMVEHTQEMGAGtVEIRKSVAPHEHVMLRGEDAVQGQPALTAGTLLRAQEIGLLAALGVQTVHVHRR 182
Cdd:PRK10680 99 MTGAPVPEGCEAVVMQEQTEQTDDG-VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 183 PRVGIFSTGDEVIPAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDMVLLSGGSSVGT 262
Cdd:PRK10680 178 VRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 263 RDLTMAALDSLDGAAVINhgVAISPGKPLilasADGKGQRCAVWGLPGQVTSAQVVMFVLGIPFVHWLAGrrtpfdQSAW 342
Cdd:PRK10680 258 ADYTKTILEELGEIAFWK--LAIKPGKPF----AFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSG------NTAS 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 78217682 343 A---SRRAVLARNIASRQGREDYIRVRLHAEEDGRVTATpVTGKSG 385
Cdd:PRK10680 326 GlppRQRVRTASRLKKTPGRLDFQRGILQRNADGELEVT-TTGHQG 370
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
36-416 |
5.93e-50 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 177.31 E-value: 5.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 36 GCVLAAPVVSPEDLPAADRSCMDGYAVRAADlfgttegNPAYLECTGTVSIERPADFSIAAGECAAIVTGALLPRGADAV 115
Cdd:PRK14497 40 GYVSAEDLMSPIDYPPFSRSTVDGYALKSSC-------TPGEFKVIDKIGIGEFKEIHIKECEAVEVDTGSMIPMGADAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 116 VMVEHTQEMGAGTVEIRKSVAPHEHVMLRGEDAVQGQPALTAGTLLRAQEIGLLAALGVQTVHVHRRPRVGIFSTGDEVI 195
Cdd:PRK14497 113 IKVENTKVINGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPKIYLIATGDELV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 196 PAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDMVLLSGGSSVGTRDLTMAALDSLdg 275
Cdd:PRK14497 193 EPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKDFVHQAIREL-- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 276 AAVINHGVAISPGKPLILASADGKgqrcAVWGLPGQVTSAQVV--MFVLGIPFVHWLAGRRTPFDQSAwasrRAVLARNI 353
Cdd:PRK14497 271 GNIIVHGLKIKPGKPTILGIVDGK----PVIGLPGNIVSTMVVlnMVILEYLKSLYPSRKEILGLGKI----KARLALRV 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78217682 354 ASRQGREDYIRVRLhAEEDGRVTATPVTGKSGLLRTMLQAHGVVRIPAHSEgLDSGTQVDVLL 416
Cdd:PRK14497 343 KADEHRNTLIPVYL-FKSDNSYYALPVPFDSYMVGTFSLTDGYIMLGPNEE-IEEGKEVEVDL 403
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
32-173 |
8.64e-50 |
|
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: 165.43 E-value: 8.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 32 DEAHGCVLAAPVVSPEDLPAADRSCMDGYAVRAADLFGTTEGNPaylectgtVSIERPADFSIAAGECAAIVTGALLPRG 111
Cdd:pfam03453 14 LDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLPGGEAVRIMTGAPLPEG 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78217682 112 ADAVVMVEHTQEMGAGTVEIRKSVAPHEHVMLRGEDAVQGQPALTAGTLLRAQEIGLLAALG 173
Cdd:pfam03453 86 ADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
23-416 |
8.78e-46 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 167.68 E-value: 8.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 23 HLPALQTPLDEAHGCVLAAPVVSPEDLPAADRSCMDGYAVRAADlfgtteGNPAYLECTGTVSIERPADFSIAAGECAAI 102
Cdd:PLN02699 23 RLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASD------GPGEYPVITESRAGNDGLGVTLTPGTVAYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 103 VTGALLPRGADAVVMVEHTQEMGAGTVE---IRKSVAPHEHVMLR--GEDAVQGQPALTAGTLLRAQEIGLLAALGVQTV 177
Cdd:PLN02699 97 TTGGPIPDGADAVVQVEDTEVVEDPLDGskrVRILSQASKGQDIRpvGCDIEKDAKVLKAGERLGASEIGLLATVGVTMV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 178 HVHRRPRVGIFSTGDEVI-PAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAEN-DMVLLS 255
Cdd:PLN02699 177 KVYPRPTVAILSTGDELVePTTGTLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDEAISSGvDILLTS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 256 GGSSVGTRDLTMAALDSLdgAAVINHGVAISPGKPLILA-----SADGKGQRCAVWGLPGQVTSAQVVMFVLGIPFVHWL 330
Cdd:PLN02699 257 GGVSMGDRDFVKPLLEKR--GTVYFSKVLMKPGKPLTFAeidakSAPSNSKKMLAFGLPGNPVSCLVCFNLFVVPAIRYL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 331 AGRRTPFDQSAwasrRAVLARNIASRQGREDYIRVRLHAE-EDGRVTATPV---TGK--SGLLRTMLQAHGVVRIPAHSE 404
Cdd:PLN02699 335 AGWSNPHLLRV----QARLREPIKLDPVRPEFHRAIIRWKlNDGSGNPGFVaesTGHqmSSRLLSMKSANALLELPATGN 410
|
410
....*....|..
gi 78217682 405 GLDSGTQVDVLL 416
Cdd:PLN02699 411 VLSAGTSVSAII 422
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
31-418 |
1.67e-41 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 151.61 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 31 LDEAHGCVLAAPVVSPEDLPAADRSCMDGYAVRAAdlfgTTEGNPAYLECTGTVSIERPADFSIAAGECAAIVTGALLPR 110
Cdd:PRK14690 47 LSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGA----APEGAQVLPLIEGRAAAGVPFSGRVPEGMALRILTGAALPE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 111 GADAVVMVEHTQeMGAGTVEIRKSVAPHEHVMLRGEDAVQGQPALTAGTLLRAQEIGLLAALGVQTVHVHRRPRVGIFST 190
Cdd:PRK14690 123 GVDTVVLEEDVA-GDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRVAVLST 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 191 GDEVIPAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDMVLLSGGSSVGTRDLTMAAL 270
Cdd:PRK14690 202 GDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGASAGDEDHVSALL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 271 DslDGAAVINHGVAISPGKPLILASADGKgqrcAVWGLPGQVTSAQVVMFVLGIPFVHWLAGR--RTP--FDQSAWASRR 346
Cdd:PRK14690 282 R--EAGAMQSWRIALKPGRPLALGLWQGV----PVFGLPGNPVAALVCTLVFARPAMSLLAGEgwSEPqgFTVPAAFEKR 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78217682 347 avlarniaSRQGREDYIRVRLhaeEDGRVTATPVTGkSGLLRTMLQAHGVVRIPAHSEGLDSGTQVDVLLFG 418
Cdd:PRK14690 356 --------KKPGRREYLRARL---RQGHAEVFRSEG-SGRISGLSWAEGLVELGDGARRIAPGDPVRFIPYG 415
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
186-322 |
1.75e-24 |
|
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: 98.04 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 186 GIFSTGDEVIPahatprPGQVRDVNSHALQAMARAAGAAVTCYGIV--PDDEKALTAMLARTTAENDMVLLSGGSSVGTR 263
Cdd:smart00852 1 AIISTGDELLS------GGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78217682 264 DLTMAALDSLDGAAVINHGVAISPGKP-----LILASADGKGQRCAVWGLPGQVTSAQVVMFVL 322
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPpgplaNLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
186-328 |
1.57e-21 |
|
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: 90.00 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 186 GIFSTGDEVIPahatprpGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDMVLLSGGSSVGTRDL 265
Cdd:pfam00994 1 AIITTGDELLP-------GQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78217682 266 TMAAL-----DSLDGAAVINHGVAISPGKPLILAS-ADGKGQRCAVWGLPGQVTSAQVVMFVLGIPFVH 328
Cdd:pfam00994 74 TPEALaelggRELPGFEELFRGVSLKPGKPVGTAPgAILSRAGKTVFGLPGSPVAAKVMFELLLLPLLR 142
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
183-325 |
4.50e-21 |
|
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: 88.91 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 183 PRVGIFSTGDEVIPAHATPRPGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDMVLLSGGSSVGT 262
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78217682 263 RDLTMAALDSLDGAAVINHG---------VAISPGKPLILASADGkgqrCAVWGLPGQVTSAQVVMFVLGIP 325
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGFGefrmlsslpVLSRPGKPATAGVRGG----TLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
184-327 |
2.64e-17 |
|
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: 77.77 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 184 RVGIFSTGDEVIPahatprpGQVRDVNSHALQAMARAAGAAVTCYGIVPDDEKALTAMLARTTAENDMVLLSGGSSVGTR 263
Cdd:cd00758 1 RVAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78217682 264 DLTMAALDSLDGAAVINHGVAISPGKPLILASADGKgqrcAVWGLPGQVTSAQVVMFVLGIPFV 327
Cdd:cd00758 74 DVTPEALAELGEREAHGKGVALAPGSRTAFGIIGKV----LIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
346-417 |
2.04e-15 |
|
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: 70.72 E-value: 2.04e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78217682 346 RAVLARNIASRQGREDYIRVRLHaEEDGRVTATPV-TGKSGLLRTMLQAHGVVRIPAHSEGLDSGTQVDVLLF 417
Cdd:pfam03454 1 KARLARDLKSDPGRREFVRVRLH-EEDGRYYAEPIgKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
230-316 |
2.75e-05 |
|
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. There this domain is presumed to bind molybdopterin. The exact function of this subgroup is unknown.
Pssm-ID: 239599 Cd Length: 312 Bit Score: 45.62 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 230 IVPDDEKALTAMLARTTAEN-DMVLLSGGSSVGTRDLTMAALDSLdGAAVINHGVAISPGKPLILASADGKgqrcAVWGL 308
Cdd:cd03522 200 IVPHDEAAIAAAIAEALEAGaELLILTGGASVDPDDVTPAAIRAA-GGEVIRYGMPVDPGNLLLLGYLGGV----PVIGL 274
|
....*...
gi 78217682 309 PGQVTSAQ 316
Cdd:cd03522 275 PGCARSPK 282
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
184-287 |
3.14e-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: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 184 RVGIFSTGDEVIPahatprpGQVRDVNSHALqamaraaGAAVTCYGI-------VPDDEKALTAMLARTTAENDMVLLSG 256
Cdd:cd00885 1 TAEIIAIGDELLS-------GQIVDTNAAFL-------AKELAELGIevyrvtvVGDDEDRIAEALRRASERADLVITTG 66
|
90 100 110
....*....|....*....|....*....|...
gi 78217682 257 GssVG-TR-DLTMAALdsldgAAVINHGVAISP 287
Cdd:cd00885 67 G--LGpTHdDLTREAV-----AKAFGRPLVLDE 92
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
184-270 |
6.70e-03 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 38.17 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78217682 184 RVGIFSTGDEVIPahatprpGQVRDVNSHALqamaraaGAAVTCYGI-------VPDDEKALTAMLARTTAENDMVLLSG 256
Cdd:COG1058 1 KAEIITIGDELLS-------GRIVDTNAAWL-------ARELAELGIdvyrittVGDDPERIVEALREALARADLVITTG 66
|
90
....*....|....*.
gi 78217682 257 GssVG-TR-DLTMAAL 270
Cdd:COG1058 67 G--LGpTPdDLTREAV 80
|
|
| |
