|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
376-782 |
1.82e-165 |
|
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: 483.53 E-value: 1.82e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 376 DKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTQTV 452
Cdd:cd00887 2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 453 MPGQVMRVTTGAPIPCGADAVVQVEDTELiresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 532
Cdd:cd00887 82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE--------EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 533 LLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 612
Cdd:cd00887 154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 613 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 692
Cdd:cd00887 234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELFVRPAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 693 RKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEqyvEL 771
Cdd:cd00887 309 RKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---GL 383
|
410
....*....|.
gi 568979723 772 HKGEVVDVMVI 782
Cdd:cd00887 384 EAGEEVEVLLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
372-785 |
1.94e-150 |
|
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: 445.30 E-value: 1.94e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 372 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF----IIGESQAGEQ 447
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtlrVVGEIAAGSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 448 PTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELiresDDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 527
Cdd:COG0303 81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER----EGDR----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 528 PSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 607
Cdd:COG0303 153 PADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 608 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLF 687
Cdd:COG0303 233 REALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 688 VVPALRKMQGILDPRPTIIKARLSCDV-KLDPRPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTE 766
Cdd:COG0303 308 VRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLERDDGE--LVVEPLGGQGSGLLSSLAEADGLIVLPEGVE 385
|
410
....*....|....*....
gi 568979723 767 qyvELHKGEVVDVMVIGRL 785
Cdd:COG0303 386 ---GVEAGEEVEVLLLDGL 401
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
372-762 |
4.13e-132 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 407.28 E-value: 4.13e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 372 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQ- 450
Cdd:PLN02699 7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 451 TVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEEleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSE 530
Cdd:PLN02699 87 TLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 531 IGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLP-GKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNE 609
Cdd:PLN02699 165 IGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGrGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 610 GISR-ADVIITSGGVSMGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDI---DGVRKII--FALPGNPVSAVVT 683
Cdd:PLN02699 245 AISSgVDILLTSGGVSMGDRDFVKPLL--EKRGTVYFSKVLMKPGKPLTFAEIDAksaPSNSKKMlaFGLPGNPVSCLVC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 684 CNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQE----PLPWAQSTGNQMSSRLMSMRSANGL 758
Cdd:PLN02699 323 FNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPvRPEFHRAIIRWKLNDgsgnPGFVAESTGHQMSSRLLSMKSANAL 402
|
....
gi 568979723 759 LMLP 762
Cdd:PLN02699 403 LELP 406
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
15-182 |
3.20e-65 |
|
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: 213.88 E-value: 3.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRD 94
Cdd:cd00886 1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPA 174
Cdd:cd00886 78 VTPE-------------ATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPE 144
|
....*...
gi 568979723 175 LPHAIDLL 182
Cdd:cd00886 145 LPHLLDLL 152
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
6-183 |
2.33e-59 |
|
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: 198.42 E-value: 2.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 6 MILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTT 85
Cdd:COG0521 1 MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE---AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 86 GGTGFAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLN-VTPLGMLSRPVCGIRGKTLIINLPGSKKGS 164
Cdd:COG0521 78 GGTGLSPRDVTPE-------------ATRPLLDKELPGFGELFRALSLEeIGPSAILSRAVAGIRGGTLIFNLPGSPGAV 144
|
170
....*....|....*....
gi 568979723 165 QECFQFILPALPHAIDLLR 183
Cdd:COG0521 145 REALEAILPELPHAVDLLN 163
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
387-538 |
1.31e-48 |
|
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: 168.13 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 387 PVLGTEI---INYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGeSQAGEQPTQTVMPGQVMRVTTG 463
Cdd:pfam03453 1 PLLGTEEtvpLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP-IAAGEPPGPLLPGGEAVRIMTG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979723 464 APIPCGADAVVQVEDTEliresddGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 538
Cdd:pfam03453 80 APLPEGADAVVMVEDTE-------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
12-183 |
2.41e-47 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 178.85 E-value: 2.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 12 DHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPS--LLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTG 89
Cdd:PLN02699 456 NPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSSSekLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 90 FAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQ 169
Cdd:PLN02699 536 FTPRDVTPE-------------ATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECME 602
|
170
....*....|....
gi 568979723 170 FILPALPHAIDLLR 183
Cdd:PLN02699 603 ALLPALKHALKQIK 616
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
15-173 |
3.36e-38 |
|
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: 138.99 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 15 IRVGVLTVSDSCFRNLAE-------DRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEkeLNLILTTGG 87
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQE---AGFNVVRLGIVPDDPEEIREILRKAVDE--ADVVLTTGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 88 TGFAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVtplgmLSRP----VCGIRGKTLIINLPGSKKG 163
Cdd:TIGR00177 76 TGVGPRDVTPE-------------ALEELGEKEIPGFGEFRMLSSLPV-----LSRPgkpaTAGVRGGTLIFNLPGNPVS 137
|
170
....*....|.
gi 568979723 164 SQECFQ-FILP 173
Cdd:TIGR00177 138 ALVTFEvLILP 148
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
548-690 |
9.67e-35 |
|
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: 129.36 E-value: 9.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 548 PVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGE 627
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979723 628 KDYLKQVLDiDLHAQIHFGR----------VFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVP 690
Cdd:TIGR00177 81 RDVTPEALE-ELGEKEIPGFgefrmlsslpVLSRPGKPATAGVRG----GTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
551-687 |
1.77e-32 |
|
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: 122.31 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 551 AVMSTGNELLNPeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVG--DNPDDLLNALNEGISRADVIITSGGVSMGEK 628
Cdd:smart00852 1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568979723 629 DYLKQVLDIDLHAQIHFGRVFMKPGLPTT-----FATLDIDGVRKIIFALPGNPVSAVVTCNLF 687
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPPGplanlSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
18-171 |
4.78e-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: 106.90 E-value: 4.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 18 GVLTVSDSCFR-NLAEDRSGINLKDLVQDpslLGGTISAYKIV--PDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRD 94
Cdd:smart00852 1 AIISTGDELLSgGQIRDSNGPMLAALLRE---LGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDD 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568979723 95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLnVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFI 171
Cdd:smart00852 76 LTPE-------------ALAELGGRELLGHGVAMRPGGP-PGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
18-177 |
8.20e-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 trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 106.56 E-value: 8.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 18 GVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRDVTP 97
Cdd:pfam00994 1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 98 EkfptfpfcglqkgATKEVIEREAPGMALAMLMGSL------NVTPLGMLSrpvcgiRGKTLIINLPGSKKGSQECFQ-F 170
Cdd:pfam00994 76 E-------------ALAELGGRELPGFEELFRGVSLkpgkpvGTAPGAILS------RAGKTVFGLPGSPVAAKVMFElL 136
|
....*..
gi 568979723 171 ILPALPH 177
Cdd:pfam00994 137 LLPLLRH 143
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
376-782 |
1.82e-165 |
|
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: 483.53 E-value: 1.82e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 376 DKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTQTV 452
Cdd:cd00887 2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 453 MPGQVMRVTTGAPIPCGADAVVQVEDTELiresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 532
Cdd:cd00887 82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE--------EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 533 LLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 612
Cdd:cd00887 154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 613 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 692
Cdd:cd00887 234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELFVRPAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 693 RKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEqyvEL 771
Cdd:cd00887 309 RKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---GL 383
|
410
....*....|.
gi 568979723 772 HKGEVVDVMVI 782
Cdd:cd00887 384 EAGEEVEVLLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
372-785 |
1.94e-150 |
|
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: 445.30 E-value: 1.94e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 372 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF----IIGESQAGEQ 447
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtlrVVGEIAAGSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 448 PTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELiresDDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 527
Cdd:COG0303 81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER----EGDR----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 528 PSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 607
Cdd:COG0303 153 PADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 608 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLF 687
Cdd:COG0303 233 REALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 688 VVPALRKMQGILDPRPTIIKARLSCDV-KLDPRPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTE 766
Cdd:COG0303 308 VRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLERDDGE--LVVEPLGGQGSGLLSSLAEADGLIVLPEGVE 385
|
410
....*....|....*....
gi 568979723 767 qyvELHKGEVVDVMVIGRL 785
Cdd:COG0303 386 ---GVEAGEEVEVLLLDGL 401
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
372-762 |
4.13e-132 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 407.28 E-value: 4.13e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 372 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQ- 450
Cdd:PLN02699 7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 451 TVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEEleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSE 530
Cdd:PLN02699 87 TLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 531 IGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLP-GKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNE 609
Cdd:PLN02699 165 IGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGrGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 610 GISR-ADVIITSGGVSMGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDI---DGVRKII--FALPGNPVSAVVT 683
Cdd:PLN02699 245 AISSgVDILLTSGGVSMGDRDFVKPLL--EKRGTVYFSKVLMKPGKPLTFAEIDAksaPSNSKKMlaFGLPGNPVSCLVC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 684 CNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQE----PLPWAQSTGNQMSSRLMSMRSANGL 758
Cdd:PLN02699 323 FNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPvRPEFHRAIIRWKLNDgsgnPGFVAESTGHQMSSRLLSMKSANAL 402
|
....
gi 568979723 759 LMLP 762
Cdd:PLN02699 403 LELP 406
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
386-779 |
1.00e-95 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 311.38 E-value: 1.00e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 386 TPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAAD-------GPGDRFIIGESQAGEQPTQTVMPGQVM 458
Cdd:PRK14498 25 ELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADtfgaseaNPVRLKLGGEVHAGEAPDVEVEPGEAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 459 RVTTGAPIPCGADAVVQVEDTElirESDDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 538
Cdd:PRK14498 105 EIATGAPIPRGADAVVMVEDTE---EVDDDT----VEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 539 VTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVII 618
Cdd:PRK14498 178 VAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 619 TSGGVSMGEKDYLKQVLDidlhaqiHFGRVF-----MKPGLPTTFATldIDGvrKIIFALPGNPVSAVVTCNLFVVPALR 693
Cdd:PRK14498 258 LSGGTSAGAGDVTYRVIE-------ELGEVLvhgvaIKPGKPTILGV--IGG--KPVVGLPGYPVSALTIFEEFVAPLLR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 694 KMQGILDPRPTIIKARLScdVKLDP---RPEYHRCILTWHHQEPLPWAQSTGnqmSSRLMSMRSANGLLMLPPKTEQyve 770
Cdd:PRK14498 327 KLAGLPPPERATVKARLA--RRVRSelgREEFVPVSLGRVGDGYVAYPLSRG---SGAITSLVRADGFIEIPANTEG--- 398
|
....*....
gi 568979723 771 LHKGEVVDV 779
Cdd:PRK14498 399 LEAGEEVEV 407
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
386-767 |
8.10e-89 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 291.90 E-value: 8.10e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 386 TPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF-IIGESQAGEQPTQTVMPGQVMRVTTGA 464
Cdd:PRK14491 213 TPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESYtLVGEVLAGHQYDGTLQAGEAVRIMTGA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 465 PIPCGADAVVQVEDTELiresDDGTEELEVRILVqarpGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEV 544
Cdd:PRK14491 293 PVPAGADTVVMRELATQ----DGDKVSFDGGIKA----GQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPV 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 545 NKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVS 624
Cdd:PRK14491 365 FRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVS 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 625 MGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPALRKMQGILDPRPT 704
Cdd:PRK14491 445 VGDADYIKTAL--AKLGQIDFWRINMRPGRPLAFGQIG----DSPFFGLPGNPVAVMVSFLQFVEPALRKLAGEQNWQPL 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568979723 705 IIKARLSCDVKLDP-RPEYHRCILTWHHQEPLPwAQSTGNQMSSRLMSMRSANGLLMLPPKTEQ 767
Cdd:PRK14491 519 LFPAIADETLRSRQgRTEFSRGIYHLGADGRLH-VRTTGKQGSGILSSMSEANCLIEIGPAAET 581
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
372-761 |
3.26e-75 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 250.01 E-value: 3.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 372 LTSMDKAFITVL-EMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF--IIGESQAGeQP 448
Cdd:PRK10680 7 LMSLETALTEMLsRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPlpVAGKAFAG-QP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 449 TQTVMP-GQVMRVTTGAPIPCGADAVVQVEDTELireSDDGteeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 527
Cdd:PRK10680 86 FHGEWPaGTCIRIMTGAPVPEGCEAVVMQEQTEQ---TDDG-----VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 528 PSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 607
Cdd:PRK10680 158 TAELPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 608 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLhAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLF 687
Cdd:PRK10680 238 IEADSQADVVISSGGVSVGEADYTKTILE-EL-GEIAFWKLAIKPGKPFAFGKLS----NSWFCGLPGNPVSAALTFYQL 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568979723 688 VVPALRKMQGILDPRPTI-IKARLSCDVKLDP-RPEYHRCILTWHHQEPLPwAQSTGNQMSSRLMSMRSANGLLML 761
Cdd:PRK10680 312 VQPLLAKLSGNTASGLPPrQRVRTASRLKKTPgRLDFQRGILQRNADGELE-VTTTGHQGSHIFSSFSLGNCFIVL 386
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
369-781 |
3.58e-68 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 235.09 E-value: 3.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 369 PFPLTSMDKaFITVLEMTPvlGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQP 448
Cdd:PRK14497 11 YSIDEAIKV-FLSSLNFKP--KIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGEFKVIDKIGIGEFK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 449 TQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELIresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGP 528
Cdd:PRK14497 88 EIHIKECEAVEVDTGSMIPMGADAVIKVENTKVI-------NGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 529 SEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALN 608
Cdd:PRK14497 161 EKIGLLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 609 EGISRADVIITSGGVSMGEKDYLKQVL----DIDLHAqihfgrVFMKPGLPTTFATldIDGvrKIIFALPGNPVSAVVTC 684
Cdd:PRK14497 241 RAISVADVLILTGGTSAGEKDFVHQAIrelgNIIVHG------LKIKPGKPTILGI--VDG--KPVIGLPGNIVSTMVVL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 685 NLFVVPALRKMQG----ILDPRPtiIKARLSCDVKLDprpeYHRCIL---------TWHHQEPLPWAqstgnqmSSRLMS 751
Cdd:PRK14497 311 NMVILEYLKSLYPsrkeILGLGK--IKARLALRVKAD----EHRNTLipvylfksdNSYYALPVPFD-------SYMVGT 377
|
410 420 430
....*....|....*....|....*....|
gi 568979723 752 MRSANGLLMLPPKTeqyvELHKGEVVDVMV 781
Cdd:PRK14497 378 FSLTDGYIMLGPNE----EIEEGKEVEVDL 403
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
15-182 |
3.20e-65 |
|
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: 213.88 E-value: 3.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRD 94
Cdd:cd00886 1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPA 174
Cdd:cd00886 78 VTPE-------------ATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPE 144
|
....*...
gi 568979723 175 LPHAIDLL 182
Cdd:cd00886 145 LPHLLDLL 152
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
6-183 |
2.33e-59 |
|
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: 198.42 E-value: 2.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 6 MILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTT 85
Cdd:COG0521 1 MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE---AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 86 GGTGFAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLN-VTPLGMLSRPVCGIRGKTLIINLPGSKKGS 164
Cdd:COG0521 78 GGTGLSPRDVTPE-------------ATRPLLDKELPGFGELFRALSLEeIGPSAILSRAVAGIRGGTLIFNLPGSPGAV 144
|
170
....*....|....*....
gi 568979723 165 QECFQFILPALPHAIDLLR 183
Cdd:COG0521 145 REALEAILPELPHAVDLLN 163
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
387-538 |
1.31e-48 |
|
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: 168.13 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 387 PVLGTEI---INYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGeSQAGEQPTQTVMPGQVMRVTTG 463
Cdd:pfam03453 1 PLLGTEEtvpLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP-IAAGEPPGPLLPGGEAVRIMTG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979723 464 APIPCGADAVVQVEDTEliresddGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 538
Cdd:pfam03453 80 APLPEGADAVVMVEDTE-------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
373-762 |
1.50e-48 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 177.42 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 373 TSMDKAFITVLE-MTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDR---FIIGESQAGEQP 448
Cdd:PRK14690 23 TPVDTALDLLRArLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQvlpLIEGRAAAGVPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 449 TQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELiresddGTEELEVRILVQArpGQDIRPIGHDIKRGECVLAKGTHMGP 528
Cdd:PRK14690 103 SGRVPEGMALRILTGAALPEGVDTVVLEEDVAG------DGHRIAFHGPLKM--GANTRKAGEDVIAGDVALPAGRRLTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 529 SEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALN 608
Cdd:PRK14690 175 ADLALLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 609 EGISRADVIITSGGVSMGEKDYLKQVLDIDlhAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFV 688
Cdd:PRK14690 255 RAAAEADVILTSGGASAGDEDHVSALLREA--GAMQSWRIALKPGRPLALGLWQ----GVPVFGLPGNPVAALVCTLVFA 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568979723 689 VPALRKM--QGILDPRPTIIKARLScDVKLDPRPEYHRCILTWHHQEPLpwaQSTGnqmSSRLMSMRSANGLLMLP 762
Cdd:PRK14690 329 RPAMSLLagEGWSEPQGFTVPAAFE-KRKKPGRREYLRARLRQGHAEVF---RSEG---SGRISGLSWAEGLVELG 397
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
12-183 |
2.41e-47 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 178.85 E-value: 2.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 12 DHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPS--LLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTG 89
Cdd:PLN02699 456 NPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSSSekLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 90 FAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQ 169
Cdd:PLN02699 536 FTPRDVTPE-------------ATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECME 602
|
170
....*....|....
gi 568979723 170 FILPALPHAIDLLR 183
Cdd:PLN02699 603 ALLPALKHALKQIK 616
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
550-692 |
5.68e-41 |
|
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: 146.33 E-value: 5.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 550 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKD 629
Cdd:cd00758 2 VAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979723 630 YLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 692
Cdd:cd00758 75 VTPEALAELGEREAHGKGVALAPGSRTAFGIIG----KVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| mogA |
PRK09417 |
molybdenum cofactor biosynthesis protein MogA; Provisional |
15-182 |
6.10e-40 |
|
molybdenum cofactor biosynthesis protein MogA; Provisional
Pssm-ID: 181837 [Multi-domain] Cd Length: 193 Bit Score: 145.87 E-value: 6.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 15 IRVGVLTVSDSCFRNLAEDRSGINLKDLvqdpslLGGTISA-----YKIVPDEIEEIKETLIDWCDEKELNLILTTGGTG 89
Cdd:PRK09417 4 LKIGLVSISDRASSGVYEDKGIPALEEW------LASALTSpfeieTRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 90 FAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQ 169
Cdd:PRK09417 78 PARRDVTPE-------------ATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLE 144
|
170 180
....*....|....*....|....*
gi 568979723 170 F------------ILPALPHAIDLL 182
Cdd:PRK09417 145 GlkdadgnvvvpgIFAAVPYCIDLI 169
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
15-184 |
2.17e-39 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 148.17 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCdEKELNLILTTGGTGFAPRD 94
Cdd:PRK03604 156 TSAAVLVLSDSIAAGTKEDRSGKLIVEGLEE---AGFEVSHYTIIPDEPAEIAAAVAAWI-AEGYALIITTGGTGLGPRD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPA 174
Cdd:PRK03604 232 VTPE-------------ALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPA 298
|
170
....*....|
gi 568979723 175 LPHAIDLLRD 184
Cdd:PRK03604 299 LFHAFAMVKG 308
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
16-175 |
5.39e-39 |
|
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: 140.94 E-value: 5.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 16 RVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEkeLNLILTTGGTGFAPRDV 95
Cdd:cd00758 1 RVAIVTVSDELSQGQIEDTNGPALEALLED---LGCEVIYAGVVPDDADSIRAALIEASRE--ADLVLTTGGTGVGRRDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 96 TPEkfptfpfcglqkgATKEVIEREAPGmalamlmgslNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECF-QFILPA 174
Cdd:cd00758 76 TPE-------------ALAELGEREAHG----------KGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFeALVLPA 132
|
.
gi 568979723 175 L 175
Cdd:cd00758 133 L 133
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
15-173 |
3.36e-38 |
|
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: 138.99 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 15 IRVGVLTVSDSCFRNLAE-------DRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEkeLNLILTTGG 87
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQE---AGFNVVRLGIVPDDPEEIREILRKAVDE--ADVVLTTGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 88 TGFAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVtplgmLSRP----VCGIRGKTLIINLPGSKKG 163
Cdd:TIGR00177 76 TGVGPRDVTPE-------------ALEELGEKEIPGFGEFRMLSSLPV-----LSRPgkpaTAGVRGGTLIFNLPGNPVS 137
|
170
....*....|.
gi 568979723 164 SQECFQ-FILP 173
Cdd:TIGR00177 138 ALVTFEvLILP 148
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
548-690 |
9.67e-35 |
|
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: 129.36 E-value: 9.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 548 PVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGE 627
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979723 628 KDYLKQVLDiDLHAQIHFGR----------VFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVP 690
Cdd:TIGR00177 81 RDVTPEALE-ELGEKEIPGFgefrmlsslpVLSRPGKPATAGVRG----GTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
551-694 |
5.70e-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: 123.90 E-value: 5.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 551 AVMSTGNELLnpeddllPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDY 630
Cdd:pfam00994 1 AIITTGDELL-------PGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568979723 631 LKQVL------DIDLHAQIhFGRVFMKPGLPTTFATL-DIDGVRKIIFALPGNPVSAVVTCNLFVVPALRK 694
Cdd:pfam00994 74 TPEALaelggrELPGFEEL-FRGVSLKPGKPVGTAPGaILSRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
551-687 |
1.77e-32 |
|
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: 122.31 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 551 AVMSTGNELLNPeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVG--DNPDDLLNALNEGISRADVIITSGGVSMGEK 628
Cdd:smart00852 1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568979723 629 DYLKQVLDIDLHAQIHFGRVFMKPGLPTT-----FATLDIDGVRKIIFALPGNPVSAVVTCNLF 687
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPPGplanlSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
18-171 |
4.78e-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: 106.90 E-value: 4.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 18 GVLTVSDSCFR-NLAEDRSGINLKDLVQDpslLGGTISAYKIV--PDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRD 94
Cdd:smart00852 1 AIISTGDELLSgGQIRDSNGPMLAALLRE---LGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDD 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568979723 95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLnVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFI 171
Cdd:smart00852 76 LTPE-------------ALAELGGRELLGHGVAMRPGGP-PGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
18-177 |
8.20e-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 trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 106.56 E-value: 8.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 18 GVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRDVTP 97
Cdd:pfam00994 1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 98 EkfptfpfcglqkgATKEVIEREAPGMALAMLMGSL------NVTPLGMLSrpvcgiRGKTLIINLPGSKKGSQECFQ-F 170
Cdd:pfam00994 76 E-------------ALAELGGRELPGFEELFRGVSLkpgkpvGTAPGAILS------RAGKTVFGLPGSPVAAKVMFElL 136
|
....*..
gi 568979723 171 ILPALPH 177
Cdd:pfam00994 137 LLPLLRH 143
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
707-782 |
9.19e-20 |
|
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: 83.81 E-value: 9.19e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568979723 707 KARLSCDVKLDP-RPEYHRCILtwHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVElhkGEVVDVMVI 782
Cdd:pfam03454 1 KARLARDLKSDPgRREFVRVRL--HEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEA---GEEVEVILL 72
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
550-622 |
3.81e-11 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 63.98 E-value: 3.81e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979723 550 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 622
Cdd:COG1058 2 AEIITIGDELLS-------GRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGG 67
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
550-622 |
6.71e-11 |
|
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: 61.73 E-value: 6.71e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979723 550 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 622
Cdd:cd00885 2 AEIIAIGDELLS-------GQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
558-623 |
1.06e-06 |
|
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 161761 [Multi-domain] Cd Length: 413 Bit Score: 51.83 E-value: 1.06e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568979723 558 ELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGV 623
Cdd:TIGR00200 4 EIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGL 69
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
552-635 |
2.49e-06 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 50.56 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 552 VMSTGNELLNpeddllpGKIRDSNRSTL---LATIQ-EHGYPTInlgiVGDNPDDLLNALNEGISRADVIITSGGVSMGE 627
Cdd:PRK00549 5 IIAVGTELLL-------GQIVNTNAQFLsekLAELGiDVYHQTV----VGDNPERLLSALEIAEERSDLIITTGGLGPTK 73
|
....*...
gi 568979723 628 KDYLKQVL 635
Cdd:PRK00549 74 DDLTKETV 81
|
|
| PRK03673 |
PRK03673 |
nicotinamide mononucleotide deamidase-related protein YfaY; |
550-622 |
4.74e-06 |
|
nicotinamide mononucleotide deamidase-related protein YfaY;
Pssm-ID: 179629 [Multi-domain] Cd Length: 396 Bit Score: 49.70 E-value: 4.74e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979723 550 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 622
Cdd:PRK03673 4 VEMLSTGDEVLH-------GQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGG 69
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
39-190 |
1.42e-05 |
|
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: 48.26 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 39 LKDLVQDpslLGGTISAYKIVPDEIEEIKETL---IDWCDekelnLILTTGGTGFAPRDVtpekfptfpfcglqkgaTKE 115
Cdd:cd00887 200 LAALLRE---LGAEVVDLGIVPDDPEALREALeeaLEEAD-----VVITSGGVSVGDYDF-----------------VKE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 116 VIEREAPGmalaMLMGSLNVTPlGmlsRPV-CGIRGKTLIINLPG---SkkgSQECF-QFILPALPHAIDLLRDAIVKVK 190
Cdd:cd00887 255 VLEELGGE----VLFHGVAMKP-G---KPLaFGRLGGKPVFGLPGnpvS---ALVTFeLFVRPALRKLQGAPEPEPPRVK 323
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
548-622 |
6.74e-05 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 45.39 E-value: 6.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979723 548 PVVAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 622
Cdd:PRK01215 4 WFAWIITIGNELLI-------GRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGG 71
|
|
| PRK03670 |
PRK03670 |
competence damage-inducible protein A; Provisional |
558-623 |
4.56e-04 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 167581 Cd Length: 252 Bit Score: 42.86 E-value: 4.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568979723 558 ELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRA-DVIITSGGV 623
Cdd:PRK03670 4 EIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKpEVLVISGGL 70
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
583-692 |
8.13e-04 |
|
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440287 [Multi-domain] Cd Length: 169 Bit Score: 40.87 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 583 IQEHGYPTINLGIVGDNPDDLLNALNEGISR--ADVIITSGGVSMGEKDY----LKQVLDIDLHAqihFGRVF----MKP 652
Cdd:COG0521 38 LEEAGHEVVARRIVPDDKDAIRAALRELIDDegVDLVLTTGGTGLSPRDVtpeaTRPLLDKELPG---FGELFralsLEE 114
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568979723 653 GLPTTFATLDIDGVRK--IIFALPGNPvSAVVTCNLFVVPAL 692
Cdd:COG0521 115 IGPSAILSRAVAGIRGgtLIFNLPGSP-GAVREALEAILPEL 155
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
49-175 |
1.18e-03 |
|
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: 42.00 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 49 LGGTISAYKIVPDEIEEIKETL---IDWCDekelnLILTTGGTGFAPRDVtpekfptfpfcglqkgaTKEVIEREapGMA 125
Cdd:COG0303 211 AGAEVVDLGIVPDDPEALRAALreaLAEAD-----LVITSGGVSVGDYDL-----------------VKEALEEL--GAE 266
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568979723 126 LamLMGSLNVTPlGmlsRPV-CGIRGKTLIINLPG---SkkgSQECF-QFILPAL 175
Cdd:COG0303 267 V--LFHKVAMKP-G---KPLaFGRLGGKPVFGLPGnpvS---ALVTFeLFVRPAL 312
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
16-150 |
2.65e-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: 40.61 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979723 16 RVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELnLILTTGGTGFAPRDV 95
Cdd:cd03522 161 RVGLIVTGSEVYGGRIEDKFGPVLRARLAA---LGVELVEQVIVPHDEAAIAAAIAEALEAGAE-LLILTGGASVDPDDV 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568979723 96 TPekfptfpfCGLqKGATKEVIEREAPGMALAMLMgslnvtpLGML-SRPVCGIRG 150
Cdd:cd03522 237 TP--------AAI-RAAGGEVIRYGMPVDPGNLLL-------LGYLgGVPVIGLPG 276
|
|
|