|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
19-435 |
3.51e-160 |
|
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: 457.63 E-value: 3.51e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 19 LDVDTVTAFLARLVTPLavaDTEDLALRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDGALLPANAPIdhslTLHVAGT 98
Cdd:COG0303 2 ISVEEALALILAAVRPL---GTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPV----TLRVVGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 99 ALAGSAWRGALGPRDAVRIMTGAMMPAGLDTVIPQEFCKVDGDQVCFPARVlGRGDNRRLAGEDLMQGQPALRRGERLLP 178
Cdd:COG0303 75 IAAGSPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPV-APGENIRRAGEDIAAGDVLLPAGTRLTP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 179 AALGMVASLGMARVNVRRRLRVAYFSTGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQ 258
Cdd:COG0303 154 ADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 259 RAAREADAIVTSGGVSVGAADHTRDVMQQLG-DMAFWRVAMRPGRPLAVGLIPRetaatpVVLFGLPGNPVAAMVAFLAF 337
Cdd:COG0303 234 EALAEADLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGG------KPVFGLPGNPVSALVTFELF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 338 VRPALLRLMGchdAACAPPPLLRARSAGPIRKKPGRTEYQRGVVRQVPGSLpEVRVAAHQGSGVLSSMLEANGLVVLPHE 417
Cdd:COG0303 308 VRPALRKLAG---LPPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDGEL-VVEPLGGQGSGLLSSLAEADGLIVLPEG 383
|
410
....*....|....*...
gi 1241530236 418 QGHVDAGQEVDVMVFEGL 435
Cdd:COG0303 384 VEGVEAGEEVEVLLLDGL 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
21-432 |
8.04e-150 |
|
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: 430.76 E-value: 8.04e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 21 VDTVTAFLARLVTPLAvadTEDLALRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDGALLPANapidhSLTLHVAGTAL 100
Cdd:cd00887 1 VEAARELLLALAPPLG---TETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGA-----SVTLRVVGEIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 101 AGSAWRGALGPRDAVRIMTGAMMPAGLDTVIPQEFCKVDGDQVCFPARVlGRGDNRRLAGEDLMQGQPALRRGERLLPAA 180
Cdd:cd00887 73 AGEPPDGPLGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPV-KPGQNIRRAGEDIKAGDVLLPAGTRLTPAD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 181 LGMVASLGMARVNVRRRLRVAYFSTGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRA 260
Cdd:cd00887 152 IGLLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 261 AREADAIVTSGGVSVGAADHTRDVMQQL-GDMAFWRVAMRPGRPLAVGLIPRetaaTPVvlFGLPGNPVAAMVAFLAFVR 339
Cdd:cd00887 232 LEEADVVITSGGVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRLGG----KPV--FGLPGNPVSALVTFELFVR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 340 PALLRLMGchdAACAPPPLLRARSAGPIRKKPGRTEYQRGVVRQVPGSLpEVRVAAHQGSGVLSSMLEANGLVVLPHEQG 419
Cdd:cd00887 306 PALRKLQG---APEPEPPRVKARLAEDLKSKPGRREFLRVRLERDEGGL-VVAPPGGQGSGLLSSLARADGLIVIPEGVE 381
|
410
....*....|...
gi 1241530236 420 HVDAGQEVDVMVF 432
Cdd:cd00887 382 GLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
31-436 |
4.51e-143 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 420.94 E-value: 4.51e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 31 LVTPlaVADTEDLALRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDGALLPANapidhslTLHVAGTALAGSAWRGALG 110
Cdd:PRK14491 211 LVTP--VTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPE-------SYTLVGEVLAGHQYDGTLQ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 111 PRDAVRIMTGAMMPAGLDTVIPQEFCKVDGDQVCFPARVLgRGDNRRLAGEDLMQGQPALRRGERLLPAALGMVASLGMA 190
Cdd:PRK14491 282 AGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIK-AGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 191 RVNVRRRLRVAYFSTGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRAAREADAIVTS 270
Cdd:PRK14491 361 EVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 271 GGVSVGAADHTRDVMQQLGDMAFWRVAMRPGRPLAVGLIpretAATPVvlFGLPGNPVAAMVAFLAFVRPALLRLMGCHD 350
Cdd:PRK14491 441 GGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQI----GDSPF--FGLPGNPVAVMVSFLQFVEPALRKLAGEQN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 351 AAcapPPLLRARSAGPIRKKPGRTEYQRGVVRQVPGSLPEVRVAAHQGSGVLSSMLEANGLVVLPHEQGHVDAGQEVDVM 430
Cdd:PRK14491 515 WQ---PLLFPAIADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGETVTIQ 591
|
....*.
gi 1241530236 431 VFEGLI 436
Cdd:PRK14491 592 PLAGLL 597
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
42-188 |
1.80e-40 |
|
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: 141.55 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 42 DLALRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDgallpANAPIDHSLTLHVAgtalAGSAWRGALGPRDAVRIMTGA 121
Cdd:pfam03453 10 PLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVR-----AADGFGASEVNPIA----AGEPPGPLLPGGEAVRIMTGA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1241530236 122 MMPAGLDTVIPQEFCKVDGDQVCFPARVLGRGDNRRLAGEDLMQGQPALRRGERLLPAALGMVASLG 188
Cdd:pfam03453 81 PLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
203-340 |
2.65e-34 |
|
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: 125.12 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 203 FSTGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRAAREADAIVTSGGVSVGAADHTR 282
Cdd:TIGR00177 6 ISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRDVTP 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1241530236 283 DVMQQLGDMAFW-----------RVAMRPGRPLAVGLIPRetaaTPVvlFGLPGNPVAAMVAFLAFVRP 340
Cdd:TIGR00177 86 EALEELGEKEIPgfgefrmlsslPVLSRPGKPATAGVRGG----TLI--FNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
201-334 |
2.47e-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 trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 121.93 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 201 AYFSTGDEILclgdtpREGAVYDSNRYTLFGLLTRLGCEVIDLGLV--HDDPATLAATLQRAAREADAIVTSGGVSVGAA 278
Cdd:smart00852 1 AIISTGDELL------SGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1241530236 279 DHTRDVMQQLGD--MAFWRVAMRPGRPLAVGLIPRETAAT---PVVLFGLPGNPVAAMVAF 334
Cdd:smart00852 75 DLTPEALAELGGreLLGHGVAMRPGGPPGPLANLSGTAPGvrgKKPVFGLPGNPVAALVMF 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
19-435 |
3.51e-160 |
|
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: 457.63 E-value: 3.51e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 19 LDVDTVTAFLARLVTPLavaDTEDLALRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDGALLPANAPIdhslTLHVAGT 98
Cdd:COG0303 2 ISVEEALALILAAVRPL---GTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPV----TLRVVGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 99 ALAGSAWRGALGPRDAVRIMTGAMMPAGLDTVIPQEFCKVDGDQVCFPARVlGRGDNRRLAGEDLMQGQPALRRGERLLP 178
Cdd:COG0303 75 IAAGSPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPV-APGENIRRAGEDIAAGDVLLPAGTRLTP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 179 AALGMVASLGMARVNVRRRLRVAYFSTGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQ 258
Cdd:COG0303 154 ADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 259 RAAREADAIVTSGGVSVGAADHTRDVMQQLG-DMAFWRVAMRPGRPLAVGLIPRetaatpVVLFGLPGNPVAAMVAFLAF 337
Cdd:COG0303 234 EALAEADLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRLGG------KPVFGLPGNPVSALVTFELF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 338 VRPALLRLMGchdAACAPPPLLRARSAGPIRKKPGRTEYQRGVVRQVPGSLpEVRVAAHQGSGVLSSMLEANGLVVLPHE 417
Cdd:COG0303 308 VRPALRKLAG---LPPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDGEL-VVEPLGGQGSGLLSSLAEADGLIVLPEG 383
|
410
....*....|....*...
gi 1241530236 418 QGHVDAGQEVDVMVFEGL 435
Cdd:COG0303 384 VEGVEAGEEVEVLLLDGL 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
21-432 |
8.04e-150 |
|
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: 430.76 E-value: 8.04e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 21 VDTVTAFLARLVTPLAvadTEDLALRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDGALLPANapidhSLTLHVAGTAL 100
Cdd:cd00887 1 VEAARELLLALAPPLG---TETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGA-----SVTLRVVGEIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 101 AGSAWRGALGPRDAVRIMTGAMMPAGLDTVIPQEFCKVDGDQVCFPARVlGRGDNRRLAGEDLMQGQPALRRGERLLPAA 180
Cdd:cd00887 73 AGEPPDGPLGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPV-KPGQNIRRAGEDIKAGDVLLPAGTRLTPAD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 181 LGMVASLGMARVNVRRRLRVAYFSTGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRA 260
Cdd:cd00887 152 IGLLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 261 AREADAIVTSGGVSVGAADHTRDVMQQL-GDMAFWRVAMRPGRPLAVGLIPRetaaTPVvlFGLPGNPVAAMVAFLAFVR 339
Cdd:cd00887 232 LEEADVVITSGGVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRLGG----KPV--FGLPGNPVSALVTFELFVR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 340 PALLRLMGchdAACAPPPLLRARSAGPIRKKPGRTEYQRGVVRQVPGSLpEVRVAAHQGSGVLSSMLEANGLVVLPHEQG 419
Cdd:cd00887 306 PALRKLQG---APEPEPPRVKARLAEDLKSKPGRREFLRVRLERDEGGL-VVAPPGGQGSGLLSSLARADGLIVIPEGVE 381
|
410
....*....|...
gi 1241530236 420 HVDAGQEVDVMVF 432
Cdd:cd00887 382 GLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
31-436 |
4.51e-143 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 420.94 E-value: 4.51e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 31 LVTPlaVADTEDLALRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDGALLPANapidhslTLHVAGTALAGSAWRGALG 110
Cdd:PRK14491 211 LVTP--VTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPE-------SYTLVGEVLAGHQYDGTLQ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 111 PRDAVRIMTGAMMPAGLDTVIPQEFCKVDGDQVCFPARVLgRGDNRRLAGEDLMQGQPALRRGERLLPAALGMVASLGMA 190
Cdd:PRK14491 282 AGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIK-AGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 191 RVNVRRRLRVAYFSTGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRAAREADAIVTS 270
Cdd:PRK14491 361 EVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 271 GGVSVGAADHTRDVMQQLGDMAFWRVAMRPGRPLAVGLIpretAATPVvlFGLPGNPVAAMVAFLAFVRPALLRLMGCHD 350
Cdd:PRK14491 441 GGVSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQI----GDSPF--FGLPGNPVAVMVSFLQFVEPALRKLAGEQN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 351 AAcapPPLLRARSAGPIRKKPGRTEYQRGVVRQVPGSLPEVRVAAHQGSGVLSSMLEANGLVVLPHEQGHVDAGQEVDVM 430
Cdd:PRK14491 515 WQ---PLLFPAIADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGETVTIQ 591
|
....*.
gi 1241530236 431 VFEGLI 436
Cdd:PRK14491 592 PLAGLL 597
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
22-436 |
1.24e-119 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 354.78 E-value: 1.24e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 22 DTVTAFLARlVTPLAvaDTEDLALRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDGALLPANAPidhsltLHVAGTALA 101
Cdd:PRK10680 12 TALTEMLSR-VTPLT--ATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQP------LPVAGKAFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 102 GSAWRGALGPRDAVRIMTGAMMPAGLDTVIPQEFCKVDGDQVCFPARVlGRGDNRRLAGEDLMQGQPALRRGERLLPAAL 181
Cdd:PRK10680 83 GQPFHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAEV-RSGQNIRRRGEDISQGAVVFPAGTRLTTAEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 182 GMVASLGMARVNVRRRLRVAYFSTGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRAA 261
Cdd:PRK10680 162 PVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 262 READAIVTSGGVSVGAADHTRDVMQQLGDMAFWRVAMRPGRPLAVGLIPRETaatpvvLFGLPGNPVAAMVAFLAFVRPA 341
Cdd:PRK10680 242 SQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSW------FCGLPGNPVSAALTFYQLVQPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 342 LLRLMGCHdaACAPPPLLRARSAGPIRKKPGRTEYQRGVVRQVPGSLPEVRVAAHQGSGVLSSMLEANGLVVLPHEQGHV 421
Cdd:PRK10680 316 LAKLSGNT--ASGLPPRQRVRTASRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNV 393
|
410
....*....|....*
gi 1241530236 422 DAGQEVDVMVFEGLI 436
Cdd:PRK10680 394 EVGEWVEVEPFNALF 408
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
21-427 |
1.57e-83 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 262.55 E-value: 1.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 21 VDTVTAFLARLVTPlaVADTEDLALRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDGALlPANApidHSLTLhVAGTAL 100
Cdd:PRK14690 25 VDTALDLLRARLGP--VTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAA-PEGA---QVLPL-IEGRAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 101 AGSAWRGALGPRDAVRIMTGAMMPAGLDTVIPQEFCKVDGDQVCFPARvLGRGDNRRLAGEDLMQGQPALRRGERLLPAA 180
Cdd:PRK14690 98 AGVPFSGRVPEGMALRILTGAALPEGVDTVVLEEDVAGDGHRIAFHGP-LKMGANTRKAGEDVIAGDVALPAGRRLTPAD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 181 LGMVASLGMARVNVRRRLRVAYFSTGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRA 260
Cdd:PRK14690 177 LALLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 261 AREADAIVTSGGVSVGAADHTRDVMQQLGDMAFWRVAMRPGRPLAVGLipreTAATPVvlFGLPGNPVAAMVAFLAFVRP 340
Cdd:PRK14690 257 AAEADVILTSGGASAGDEDHVSALLREAGAMQSWRIALKPGRPLALGL----WQGVPV--FGLPGNPVAALVCTLVFARP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 341 ALLRLMGchdAACAPPPLLRARSAGPIRKKPGRTEYQRGVVRQvpgslPEVRVAAHQGSGVLSSMLEANGLVVLPHEQGH 420
Cdd:PRK14690 331 AMSLLAG---EGWSEPQGFTVPAAFEKRKKPGRREYLRARLRQ-----GHAEVFRSEGSGRISGLSWAEGLVELGDGARR 402
|
....*..
gi 1241530236 421 VDAGQEV 427
Cdd:PRK14690 403 IAPGDPV 409
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
34-432 |
2.90e-82 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 265.15 E-value: 2.90e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 34 PLAVADTEDLALRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDGALLpANAPIDHSLTLHVAGTALAGSAWRGALGPRD 113
Cdd:PRK14498 24 SELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADT-FGASEANPVRLKLGGEVHAGEAPDVEVEPGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 114 AVRIMTGAMMPAGLDTVIPQEFCKVDGDQV------CFParvlgrGDNRRLAGEDLMQGQPALRRGERLLPAALGMVASL 187
Cdd:PRK14498 103 AVEIATGAPIPRGADAVVMVEDTEEVDDDTveiyrpVAP------GENVRPAGEDIVAGELILPKGTRLTPRDIGALAAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 188 GMARVNVRRRLRVAYFSTGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRAAREADAI 267
Cdd:PRK14498 177 GVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 268 VTSGGVSVGAADHTRDVMQQLGDMAFWRVAMRPGRPLAVGLIpretAATPVVlfGLPGNPVAAMVAFLAFVRPALLRLMG 347
Cdd:PRK14498 257 LLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVI----GGKPVV--GLPGYPVSALTIFEEFVAPLLRKLAG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 348 CHDaacAPPPLLRARSAGPIRKKPGRTEYQRGVVRQVPGSLpeVRVAAHQGSGVLSSMLEANGLVVLPHEQGHVDAGQEV 427
Cdd:PRK14498 331 LPP---PERATVKARLARRVRSELGREEFVPVSLGRVGDGY--VAYPLSRGSGAITSLVRADGFIEIPANTEGLEAGEEV 405
|
....*
gi 1241530236 428 DVMVF 432
Cdd:PRK14498 406 EVELF 410
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
45-436 |
3.20e-55 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 193.88 E-value: 3.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 45 LRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDGALLPANAPidhsltlhVAGTALAGSAWRG-ALGPRDAVRIMTGAMM 123
Cdd:PLN02699 31 LHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYP--------VITESRAGNDGLGvTLTPGTVAYVTTGGPI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 124 PAGLDTVIPQEFCKVDGDQVCFPARV-----LGRGDNRRLAGEDLMQGQPALRRGERLLPAALGMVASLGMARVNVRRRL 198
Cdd:PLN02699 103 PDGADAVVQVEDTEVVEDPLDGSKRVrilsqASKGQDIRPVGCDIEKDAKVLKAGERLGASEIGLLATVGVTMVKVYPRP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 199 RVAYFSTGDEIL-----CLGdtprEGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRA-AREADAIVTSGG 272
Cdd:PLN02699 183 TVAILSTGDELVepttgTLG----RGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDEAiSSGVDILLTSGG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 273 VSVGAADHTRDVMQQLGDMAFWRVAMRPGRPLAVGLI---PRETAATPVVLFGLPGNPVAAMVAFLAFVRPALLRLMGCH 349
Cdd:PLN02699 259 VSMGDRDFVKPLLEKRGTVYFSKVLMKPGKPLTFAEIdakSAPSNSKKMLAFGLPGNPVSCLVCFNLFVVPAIRYLAGWS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 350 DaacaPPPL-LRARSAGPIRKKPGRTEYQRGVVRQV-------PGSLPEvrVAAHQGSGVLSSMLEANGLVVLPHEQGHV 421
Cdd:PLN02699 339 N----PHLLrVQARLREPIKLDPVRPEFHRAIIRWKlndgsgnPGFVAE--STGHQMSSRLLSMKSANALLELPATGNVL 412
|
410
....*....|....*
gi 1241530236 422 DAGQEVDVMVFEGLI 436
Cdd:PLN02699 413 SAGTSVSAIIISDIS 427
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
40-334 |
1.69e-42 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 157.28 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 40 TEDLALRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDGALLPANapidhsltLHVAGTALAGSAWRGALGPRDAVRIMT 119
Cdd:PRK14497 30 IVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGE--------FKVIDKIGIGEFKEIHIKECEAVEVDT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 120 GAMMPAGLDTVIPQEFCKVDGDQVCFPARVLGRGDNRRLAGEDLMQGQPALRRGERLLPAALGMVASLGMARVNVRRRLR 199
Cdd:PRK14497 102 GSMIPMGADAVIKVENTKVINGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 200 VAYFSTGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRAAREADAIVTSGGVSVGAAD 279
Cdd:PRK14497 182 IYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKD 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1241530236 280 HTRDVMQQLGDMAFWRVAMRPGRPLAVGLIpretAATPVvlFGLPGNPVAAMVAF 334
Cdd:PRK14497 262 FVHQAIRELGNIIVHGLKIKPGKPTILGIV----DGKPV--IGLPGNIVSTMVVL 310
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
42-188 |
1.80e-40 |
|
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: 141.55 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 42 DLALRDALGRVLAADLVSPVSVPPHDNSAMDGYAFDgallpANAPIDHSLTLHVAgtalAGSAWRGALGPRDAVRIMTGA 121
Cdd:pfam03453 10 PLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVR-----AADGFGASEVNPIA----AGEPPGPLLPGGEAVRIMTGA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1241530236 122 MMPAGLDTVIPQEFCKVDGDQVCFPARVLGRGDNRRLAGEDLMQGQPALRRGERLLPAALGMVASLG 188
Cdd:pfam03453 81 PLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
204-344 |
3.23e-35 |
|
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: 127.36 E-value: 3.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 204 STGDEILclgdtprEGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRAAREADAIVTSGGVSVGAADHTRD 283
Cdd:pfam00994 4 TTGDELL-------PGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPE 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1241530236 284 VMQQLGD-------MAFWRVAMRPGRPLAVGLIPRETAAtPVVLFGLPGNPVAAMVAFLAFVRPALLR 344
Cdd:pfam00994 77 ALAELGGrelpgfeELFRGVSLKPGKPVGTAPGAILSRA-GKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
203-340 |
2.65e-34 |
|
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: 125.12 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 203 FSTGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRAAREADAIVTSGGVSVGAADHTR 282
Cdd:TIGR00177 6 ISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRDVTP 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1241530236 283 DVMQQLGDMAFW-----------RVAMRPGRPLAVGLIPRetaaTPVvlFGLPGNPVAAMVAFLAFVRP 340
Cdd:TIGR00177 86 EALEELGEKEIPgfgefrmlsslPVLSRPGKPATAGVRGG----TLI--FNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
201-334 |
2.47e-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 trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 121.93 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 201 AYFSTGDEILclgdtpREGAVYDSNRYTLFGLLTRLGCEVIDLGLV--HDDPATLAATLQRAAREADAIVTSGGVSVGAA 278
Cdd:smart00852 1 AIISTGDELL------SGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1241530236 279 DHTRDVMQQLGD--MAFWRVAMRPGRPLAVGLIPRETAAT---PVVLFGLPGNPVAAMVAF 334
Cdd:smart00852 75 DLTPEALAELGGreLLGHGVAMRPGGPPGPLANLSGTAPGvrgKKPVFGLPGNPVAALVMF 135
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
208-342 |
4.22e-26 |
|
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: 102.42 E-value: 4.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 208 EILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRAAREADAIVTSGGVSVGAADHTRDVMQQ 287
Cdd:cd00758 3 AIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALAE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1241530236 288 LGDMAFW--RVAMRPGRPLAVGLIPRetaatpVVLFGLPGNPVAAMVAFLAFVRPAL 342
Cdd:cd00758 83 LGEREAHgkGVALAPGSRTAFGIIGK------VLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
360-432 |
5.94e-17 |
|
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: 74.96 E-value: 5.94e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1241530236 360 RARSAGPIRKKPGRTEYQRGVVRQVPGsLPEVRVAAHQGSGVLSSMLEANGLVVLPHEQGHVDAGQEVDVMVF 432
Cdd:pfam03454 1 KARLARDLKSDPGRREFVRVRLHEEDG-RYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
204-306 |
1.17e-06 |
|
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: 48.25 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 204 STGDEILcLGDTPregavyDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRAAREADAIVTSGGvsVGAA--DHT 281
Cdd:cd00885 6 AIGDELL-SGQIV------DTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG--LGPThdDLT 76
|
90 100
....*....|....*....|....*
gi 1241530236 282 RDVMQQlgdmAFwrvamrpGRPLAV 306
Cdd:cd00885 77 REAVAK----AF-------GRPLVL 90
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
232-342 |
2.69e-05 |
|
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440287 [Multi-domain] Cd Length: 169 Bit Score: 44.34 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 232 LLTRLGCEVIDLGLVHDDPATLAATLQRAA--READAIVTSGGVSVGAADHTRDVMQQLGDM-------AFWRVAMRPGR 302
Cdd:COG0521 37 LLEEAGHEVVARRIVPDDKDAIRAALRELIddEGVDLVLTTGGTGLSPRDVTPEATRPLLDKelpgfgeLFRALSLEEIG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1241530236 303 PLAVglIPRETA----ATPVvlFGLPGNPVAAMVAfLAFVRPAL 342
Cdd:COG0521 117 PSAI--LSRAVAgirgGTLI--FNLPGSPGAVREA-LEAILPEL 155
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
232-342 |
1.41e-04 |
|
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.
Pssm-ID: 238451 [Multi-domain] Cd Length: 152 Bit Score: 42.08 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 232 LLTRLGCEVIDLGLVHDDPATLAATLQRAARE--ADAIVTSGGVSVGAADHTRDVMQQLGD-------MAFWRVAMRPGr 302
Cdd:cd00886 28 LLEEAGHEVVAYEIVPDDKDEIREALIEWADEdgVDLILTTGGTGLAPRDVTPEATRPLLDkelpgfgEAFRALSLEET- 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1241530236 303 PLAVglIPRETA----ATPVvlFGLPGNPVAAMVAfLAFVRPAL 342
Cdd:cd00886 107 GTAM--LSRAVAgirgGTLI--FNLPGSPKAVREA-LEVILPEL 145
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
204-290 |
1.43e-04 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 43.39 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241530236 204 STGDEILCLGDTPREGAVYDSNRYTLFGLLTRLGCEVIDLGLVHDDPATLAATLQRAARE-ADAIVTSGGVSVGAADHTR 282
Cdd:PRK03604 155 RTSAAVLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAEgYALIITTGGTGLGPRDVTP 234
|
....*...
gi 1241530236 283 DVMQQLGD 290
Cdd:PRK03604 235 EALAPLLE 242
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
233-289 |
2.03e-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: 39.84 E-value: 2.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1241530236 233 LTRLGCEVIDLGLVHDDPATLAATLQRAARE-ADAIVTSGGVSVGAADHTRDVMQQLG 289
Cdd:cd03522 188 LAALGVELVEQVIVPHDEAAIAAAIAEALEAgAELLILTGGASVDPDDVTPAAIRAAG 245
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