|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
303-709 |
4.48e-166 |
|
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: 482.76 E-value: 4.48e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 303 DKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTQTV 379
Cdd:cd00887 2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 380 MPGQVMRVTTGAPIPCGADAVVQVEDTELiresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 459
Cdd:cd00887 82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE--------EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 460 LLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 539
Cdd:cd00887 154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 540 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 619
Cdd:cd00887 234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELFVRPAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 620 RKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEqyvEL 698
Cdd:cd00887 309 RKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---GL 383
|
410
....*....|.
gi 1039740422 699 HKGEVVDVMVI 709
Cdd:cd00887 384 EAGEEVEVLLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
299-712 |
6.02e-151 |
|
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440072 [Multi-domain] Cd Length: 401 Bit Score: 444.15 E-value: 6.02e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 299 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF----IIGESQAGEQ 374
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtlrVVGEIAAGSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 375 PTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELiresDDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 454
Cdd:COG0303 81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER----EGDR----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 455 PSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 534
Cdd:COG0303 153 PADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 535 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLF 614
Cdd:COG0303 233 REALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 615 VVPALRKMQGILDPRPTIIKARLSCDV-KLDPRPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTE 693
Cdd:COG0303 308 VRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLERDDGE--LVVEPLGGQGSGLLSSLAEADGLIVLPEGVE 385
|
410
....*....|....*....
gi 1039740422 694 qyvELHKGEVVDVMVIGRL 712
Cdd:COG0303 386 ---GVEAGEEVEVLLLDGL 401
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
299-689 |
3.92e-133 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 407.66 E-value: 3.92e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 299 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQ- 377
Cdd:PLN02699 7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 378 TVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEEleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSE 457
Cdd:PLN02699 87 TLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 458 IGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLP-GKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNE 536
Cdd:PLN02699 165 IGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGrGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 537 GISR-ADVIITSGGVSMGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDI---DGVRKII--FALPGNPVSAVVT 610
Cdd:PLN02699 245 AISSgVDILLTSGGVSMGDRDFVKPLL--EKRGTVYFSKVLMKPGKPLTFAEIDAksaPSNSKKMlaFGLPGNPVSCLVC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 611 CNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQE----PLPWAQSTGNQMSSRLMSMRSANGL 685
Cdd:PLN02699 323 FNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPvRPEFHRAIIRWKLNDgsgnPGFVAESTGHQMSSRLLSMKSANAL 402
|
....
gi 1039740422 686 LMLP 689
Cdd:PLN02699 403 LELP 406
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
15-163 |
4.30e-56 |
|
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: 188.07 E-value: 4.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRD 94
Cdd:cd00886 1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039740422 95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKG 163
Cdd:cd00886 78 VTPE-------------ATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKA 133
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
6-163 |
2.91e-51 |
|
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: 175.69 E-value: 2.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 6 MILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTT 85
Cdd:COG0521 1 MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE---AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTT 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039740422 86 GGTGFAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLN-VTPLGMLSRPVCGIRGKTLIINLPGSKKG 163
Cdd:COG0521 78 GGTGLSPRDVTPE-------------ATRPLLDKELPGFGELFRALSLEeIGPSAILSRAVAGIRGGTLIFNLPGSPGA 143
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
314-465 |
6.07e-49 |
|
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: 168.51 E-value: 6.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 314 PVLGTEI---INYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGeSQAGEQPTQTVMPGQVMRVTTG 390
Cdd:pfam03453 1 PLLGTEEtvpLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP-IAAGEPPGPLLPGGEAVRIMTG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039740422 391 APIPCGADAVVQVEDTEliresddGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 465
Cdd:pfam03453 80 APLPEGADAVVMVEDTE-------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
12-159 |
1.78e-40 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 158.05 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 12 DHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPS--LLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTG 89
Cdd:PLN02699 456 NPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSSSekLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 90 FAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPG 159
Cdd:PLN02699 536 FTPRDVTPE-------------ATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPG 592
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
15-166 |
4.61e-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: 130.13 E-value: 4.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 15 IRVGVLTVSDSCFRNLAE-------DRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEkeLNLILTTGG 87
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQE---AGFNVVRLGIVPDDPEEIREILRKAVDE--ADVVLTTGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 88 TGFAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVtplgmLSRP----VCGIRGKTLIINLPGSKKG 163
Cdd:TIGR00177 76 TGVGPRDVTPE-------------ALEELGEKEIPGFGEFRMLSSLPV-----LSRPgkpaTAGVRGGTLIFNLPGNPVS 137
|
...
gi 1039740422 164 SQI 166
Cdd:TIGR00177 138 ALV 140
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
475-617 |
1.03e-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: 128.97 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 475 PVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGE 554
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039740422 555 KDYLKQVLDiDLHAQIHFGR----------VFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVP 617
Cdd:TIGR00177 81 RDVTPEALE-ELGEKEIPGFgefrmlsslpVLSRPGKPATAGVRG----GTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
478-614 |
2.00e-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: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 478 AVMSTGNELLNPeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVG--DNPDDLLNALNEGISRADVIITSGGVSMGEK 555
Cdd:smart00852 1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039740422 556 DYLKQVLDIDLHAQIHFGRVFMKPGLPTT-----FATLDIDGVRKIIFALPGNPVSAVVTCNLF 614
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPPGplanlSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
18-160 |
3.91e-25 |
|
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: 101.51 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 18 GVLTVSDSCFR-NLAEDRSGINLKDLVQDpslLGGTISAYKIV--PDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRD 94
Cdd:smart00852 1 AIISTGDELLSgGQIRDSNGPMLAALLRE---LGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039740422 95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLnVTPLGMLSRPVCGIRGKTLIINLPGS 160
Cdd:smart00852 76 LTPE-------------ALAELGGRELLGHGVAMRPGGP-PGPLANLSGTAPGVRGKKPVFGLPGN 127
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
18-166 |
1.55e-22 |
|
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: 94.24 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 18 GVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRDVTP 97
Cdd:pfam00994 1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTP 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039740422 98 EkfptfpfcglqkgATKEVIEREAPGMALAMLMGSL------NVTPLGMLSrpvcgiRGKTLIINLPGSKKGSQI 166
Cdd:pfam00994 76 E-------------ALAELGGRELPGFEELFRGVSLkpgkpvGTAPGAILS------RAGKTVFGLPGSPVAAKV 131
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
303-709 |
4.48e-166 |
|
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: 482.76 E-value: 4.48e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 303 DKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTQTV 379
Cdd:cd00887 2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 380 MPGQVMRVTTGAPIPCGADAVVQVEDTELiresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 459
Cdd:cd00887 82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE--------EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 460 LLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 539
Cdd:cd00887 154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 540 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 619
Cdd:cd00887 234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELFVRPAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 620 RKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEqyvEL 698
Cdd:cd00887 309 RKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---GL 383
|
410
....*....|.
gi 1039740422 699 HKGEVVDVMVI 709
Cdd:cd00887 384 EAGEEVEVLLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
299-712 |
6.02e-151 |
|
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440072 [Multi-domain] Cd Length: 401 Bit Score: 444.15 E-value: 6.02e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 299 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF----IIGESQAGEQ 374
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtlrVVGEIAAGSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 375 PTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELiresDDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 454
Cdd:COG0303 81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER----EGDR----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 455 PSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 534
Cdd:COG0303 153 PADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 535 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLF 614
Cdd:COG0303 233 REALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 615 VVPALRKMQGILDPRPTIIKARLSCDV-KLDPRPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTE 693
Cdd:COG0303 308 VRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLERDDGE--LVVEPLGGQGSGLLSSLAEADGLIVLPEGVE 385
|
410
....*....|....*....
gi 1039740422 694 qyvELHKGEVVDVMVIGRL 712
Cdd:COG0303 386 ---GVEAGEEVEVLLLDGL 401
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
299-689 |
3.92e-133 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 407.66 E-value: 3.92e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 299 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQ- 377
Cdd:PLN02699 7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 378 TVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEEleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSE 457
Cdd:PLN02699 87 TLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 458 IGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLP-GKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNE 536
Cdd:PLN02699 165 IGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGrGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 537 GISR-ADVIITSGGVSMGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDI---DGVRKII--FALPGNPVSAVVT 610
Cdd:PLN02699 245 AISSgVDILLTSGGVSMGDRDFVKPLL--EKRGTVYFSKVLMKPGKPLTFAEIDAksaPSNSKKMlaFGLPGNPVSCLVC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 611 CNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQE----PLPWAQSTGNQMSSRLMSMRSANGL 685
Cdd:PLN02699 323 FNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPvRPEFHRAIIRWKLNDgsgnPGFVAESTGHQMSSRLLSMKSANAL 402
|
....
gi 1039740422 686 LMLP 689
Cdd:PLN02699 403 LELP 406
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
313-706 |
5.36e-96 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 309.84 E-value: 5.36e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 313 TPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAAD-------GPGDRFIIGESQAGEQPTQTVMPGQVM 385
Cdd:PRK14498 25 ELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADtfgaseaNPVRLKLGGEVHAGEAPDVEVEPGEAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 386 RVTTGAPIPCGADAVVQVEDTElirESDDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 465
Cdd:PRK14498 105 EIATGAPIPRGADAVVMVEDTE---EVDDDT----VEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 466 VTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVII 545
Cdd:PRK14498 178 VAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 546 TSGGVSMGEKDYLKQVLDidlhaqiHFGRVF-----MKPGLPTTFATldIDGvrKIIFALPGNPVSAVVTCNLFVVPALR 620
Cdd:PRK14498 258 LSGGTSAGAGDVTYRVIE-------ELGEVLvhgvaIKPGKPTILGV--IGG--KPVVGLPGYPVSALTIFEEFVAPLLR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 621 KMQGILDPRPTIIKARLScdVKLDP---RPEYHRCILTWHHQEPLPWAQSTGnqmSSRLMSMRSANGLLMLPPKTEQyve 697
Cdd:PRK14498 327 KLAGLPPPERATVKARLA--RRVRSelgREEFVPVSLGRVGDGYVAYPLSRG---SGAITSLVRADGFIEIPANTEG--- 398
|
....*....
gi 1039740422 698 LHKGEVVDV 706
Cdd:PRK14498 399 LEAGEEVEV 407
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
313-694 |
1.05e-89 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 292.29 E-value: 1.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 313 TPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF-IIGESQAGEQPTQTVMPGQVMRVTTGA 391
Cdd:PRK14491 213 TPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESYtLVGEVLAGHQYDGTLQAGEAVRIMTGA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 392 PIPCGADAVVQVEDTELiresDDGTEELEVRILVqarpGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEV 471
Cdd:PRK14491 293 PVPAGADTVVMRELATQ----DGDKVSFDGGIKA----GQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPV 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 472 NKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVS 551
Cdd:PRK14491 365 FRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVS 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 552 MGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPALRKMQGILDPRPT 631
Cdd:PRK14491 445 VGDADYIKTAL--AKLGQIDFWRINMRPGRPLAFGQIG----DSPFFGLPGNPVAVMVSFLQFVEPALRKLAGEQNWQPL 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039740422 632 IIKARLSCDVKLDP-RPEYHRCILTWHHQEPLPwAQSTGNQMSSRLMSMRSANGLLMLPPKTEQ 694
Cdd:PRK14491 519 LFPAIADETLRSRQgRTEFSRGIYHLGADGRLH-VRTTGKQGSGILSSMSEANCLIEIGPAAET 581
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
299-688 |
7.69e-76 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 250.01 E-value: 7.69e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 299 LTSMDKAFITVL-EMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF--IIGESQAGeQP 375
Cdd:PRK10680 7 LMSLETALTEMLsRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPlpVAGKAFAG-QP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 376 TQTVMP-GQVMRVTTGAPIPCGADAVVQVEDTELireSDDGteeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 454
Cdd:PRK10680 86 FHGEWPaGTCIRIMTGAPVPEGCEAVVMQEQTEQ---TDDG-----VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 455 PSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 534
Cdd:PRK10680 158 TAELPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 535 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLhAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLF 614
Cdd:PRK10680 238 IEADSQADVVISSGGVSVGEADYTKTILE-EL-GEIAFWKLAIKPGKPFAFGKLS----NSWFCGLPGNPVSAALTFYQL 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039740422 615 VVPALRKMQGILDPRPTI-IKARLSCDVKLDP-RPEYHRCILTWHHQEPLPwAQSTGNQMSSRLMSMRSANGLLML 688
Cdd:PRK10680 312 VQPLLAKLSGNTASGLPPrQRVRTASRLKKTPgRLDFQRGILQRNADGELE-VTTTGHQGSHIFSSFSLGNCFIVL 386
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
311-708 |
2.34e-68 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 233.93 E-value: 2.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 311 EMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQTVMPGQVMRVTTG 390
Cdd:PRK14497 23 SLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGEFKVIDKIGIGEFKEIHIKECEAVEVDTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 391 APIPCGADAVVQVEDTELIresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVE 470
Cdd:PRK14497 103 SMIPMGADAVIKVENTKVI-------NGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 471 VNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGV 550
Cdd:PRK14497 176 VYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 551 SMGEKDYLKQVL----DIDLHAqihfgrVFMKPGLPTTFATldIDGvrKIIFALPGNPVSAVVTCNLFVVPALRKMQG-- 624
Cdd:PRK14497 256 SAGEKDFVHQAIrelgNIIVHG------LKIKPGKPTILGI--VDG--KPVIGLPGNIVSTMVVLNMVILEYLKSLYPsr 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 625 --ILDPRPtiIKARLSCDVKLDprpeYHRCIL---------TWHHQEPLPWAqstgnqmSSRLMSMRSANGLLMLPPKTe 693
Cdd:PRK14497 326 keILGLGK--IKARLALRVKAD----EHRNTLipvylfksdNSYYALPVPFD-------SYMVGTFSLTDGYIMLGPNE- 391
|
410
....*....|....*
gi 1039740422 694 qyvELHKGEVVDVMV 708
Cdd:PRK14497 392 ---EIEEGKEVEVDL 403
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
15-163 |
4.30e-56 |
|
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: 188.07 E-value: 4.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRD 94
Cdd:cd00886 1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039740422 95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKG 163
Cdd:cd00886 78 VTPE-------------ATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKA 133
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
6-163 |
2.91e-51 |
|
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: 175.69 E-value: 2.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 6 MILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTT 85
Cdd:COG0521 1 MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE---AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTT 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039740422 86 GGTGFAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLN-VTPLGMLSRPVCGIRGKTLIINLPGSKKG 163
Cdd:COG0521 78 GGTGLSPRDVTPE-------------ATRPLLDKELPGFGELFRALSLEeIGPSAILSRAVAGIRGGTLIFNLPGSPGA 143
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
314-465 |
6.07e-49 |
|
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: 168.51 E-value: 6.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 314 PVLGTEI---INYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGeSQAGEQPTQTVMPGQVMRVTTG 390
Cdd:pfam03453 1 PLLGTEEtvpLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP-IAAGEPPGPLLPGGEAVRIMTG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039740422 391 APIPCGADAVVQVEDTEliresddGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 465
Cdd:pfam03453 80 APLPEGADAVVMVEDTE-------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
300-689 |
1.85e-48 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 176.26 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 300 TSMDKAFITVLE-MTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDR---FIIGESQAGEQP 375
Cdd:PRK14690 23 TPVDTALDLLRArLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQvlpLIEGRAAAGVPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 376 TQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELiresddGTEELEVRILVQArpGQDIRPIGHDIKRGECVLAKGTHMGP 455
Cdd:PRK14690 103 SGRVPEGMALRILTGAALPEGVDTVVLEEDVAG------DGHRIAFHGPLKM--GANTRKAGEDVIAGDVALPAGRRLTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 456 SEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALN 535
Cdd:PRK14690 175 ADLALLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 536 EGISRADVIITSGGVSMGEKDYLKQVLDIDlhAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFV 615
Cdd:PRK14690 255 RAAAEADVILTSGGASAGDEDHVSALLREA--GAMQSWRIALKPGRPLALGLWQ----GVPVFGLPGNPVAALVCTLVFA 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039740422 616 VPALRKM--QGILDPRPTIIKARLSCDvKLDPRPEYHRCILTWHHQEPLpwaQSTGnqmSSRLMSMRSANGLLMLP 689
Cdd:PRK14690 329 RPAMSLLagEGWSEPQGFTVPAAFEKR-KKPGRREYLRARLRQGHAEVF---RSEG---SGRISGLSWAEGLVELG 397
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
477-619 |
4.03e-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: 4.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 477 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKD 556
Cdd:cd00758 2 VAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039740422 557 YLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 619
Cdd:cd00758 75 VTPEALAELGEREAHGKGVALAPGSRTAFGIIG----KVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
12-159 |
1.78e-40 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 158.05 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 12 DHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPS--LLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTG 89
Cdd:PLN02699 456 NPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSSSekLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 90 FAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPG 159
Cdd:PLN02699 536 FTPRDVTPE-------------ATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPG 592
|
|
| mogA |
PRK09417 |
molybdenum cofactor biosynthesis protein MogA; Provisional |
15-162 |
5.11e-36 |
|
molybdenum cofactor biosynthesis protein MogA; Provisional
Pssm-ID: 181837 [Multi-domain] Cd Length: 193 Bit Score: 134.31 E-value: 5.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 15 IRVGVLTVSDSCFRNLAEDRSGINLKDLvqdpslLGGTISA-----YKIVPDEIEEIKETLIDWCDEKELNLILTTGGTG 89
Cdd:PRK09417 4 LKIGLVSISDRASSGVYEDKGIPALEEW------LASALTSpfeieTRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039740422 90 FAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKK 162
Cdd:PRK09417 78 PARRDVTPE-------------ATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPK 137
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
15-166 |
4.61e-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: 130.13 E-value: 4.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 15 IRVGVLTVSDSCFRNLAE-------DRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEkeLNLILTTGG 87
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQE---AGFNVVRLGIVPDDPEEIREILRKAVDE--ADVVLTTGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 88 TGFAPRDVTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVtplgmLSRP----VCGIRGKTLIINLPGSKKG 163
Cdd:TIGR00177 76 TGVGPRDVTPE-------------ALEELGEKEIPGFGEFRMLSSLPV-----LSRPgkpaTAGVRGGTLIFNLPGNPVS 137
|
...
gi 1039740422 164 SQI 166
Cdd:TIGR00177 138 ALV 140
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
16-165 |
6.07e-35 |
|
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: 129.00 E-value: 6.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 16 RVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEkeLNLILTTGGTGFAPRDV 95
Cdd:cd00758 1 RVAIVTVSDELSQGQIEDTNGPALEALLED---LGCEVIYAGVVPDDADSIRAALIEASRE--ADLVLTTGGTGVGRRDV 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 96 TPEkfptfpfcglqkgATKEVIEREAPGmalamlmgslNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQ 165
Cdd:cd00758 76 TPE-------------ALAELGEREAHG----------KGVALAPGSRTAFGIIGKVLIINLPGSPKSAL 122
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
475-617 |
1.03e-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: 128.97 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 475 PVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGE 554
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039740422 555 KDYLKQVLDiDLHAQIHFGR----------VFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVP 617
Cdd:TIGR00177 81 RDVTPEALE-ELGEKEIPGFgefrmlsslpVLSRPGKPATAGVRG----GTLIFNLPGNPVSALVTFEVLILP 148
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
15-163 |
1.72e-33 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 130.83 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCdEKELNLILTTGGTGFAPRD 94
Cdd:PRK03604 156 TSAAVLVLSDSIAAGTKEDRSGKLIVEGLEE---AGFEVSHYTIIPDEPAEIAAAVAAWI-AEGYALIITTGGTGLGPRD 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039740422 95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKG 163
Cdd:PRK03604 232 VTPE-------------ALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGG 287
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
478-621 |
5.19e-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: 5.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 478 AVMSTGNELLnpeddllPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDY 557
Cdd:pfam00994 1 AIITTGDELL-------PGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039740422 558 LKQVL------DIDLHAQIhFGRVFMKPGLPTTFATL-DIDGVRKIIFALPGNPVSAVVTCNLFVVPALRK 621
Cdd:pfam00994 74 TPEALaelggrELPGFEEL-FRGVSLKPGKPVGTAPGaILSRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
478-614 |
2.00e-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: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 478 AVMSTGNELLNPeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVG--DNPDDLLNALNEGISRADVIITSGGVSMGEK 555
Cdd:smart00852 1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039740422 556 DYLKQVLDIDLHAQIHFGRVFMKPGLPTT-----FATLDIDGVRKIIFALPGNPVSAVVTCNLF 614
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPPGplanlSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
18-160 |
3.91e-25 |
|
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: 101.51 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 18 GVLTVSDSCFR-NLAEDRSGINLKDLVQDpslLGGTISAYKIV--PDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRD 94
Cdd:smart00852 1 AIISTGDELLSgGQIRDSNGPMLAALLRE---LGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039740422 95 VTPEkfptfpfcglqkgATKEVIEREAPGMALAMLMGSLnVTPLGMLSRPVCGIRGKTLIINLPGS 160
Cdd:smart00852 76 LTPE-------------ALAELGGRELLGHGVAMRPGGP-PGPLANLSGTAPGVRGKKPVFGLPGN 127
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
18-166 |
1.55e-22 |
|
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: 94.24 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 18 GVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRDVTP 97
Cdd:pfam00994 1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTP 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039740422 98 EkfptfpfcglqkgATKEVIEREAPGMALAMLMGSL------NVTPLGMLSrpvcgiRGKTLIINLPGSKKGSQI 166
Cdd:pfam00994 76 E-------------ALAELGGRELPGFEELFRGVSLkpgkpvGTAPGAILS------RAGKTVFGLPGSPVAAKV 131
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
634-709 |
1.85e-19 |
|
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: 82.66 E-value: 1.85e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039740422 634 KARLSCDVKLDP-RPEYHRCILtwHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVElhkGEVVDVMVI 709
Cdd:pfam03454 1 KARLARDLKSDPgRREFVRVRL--HEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEA---GEEVEVILL 72
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
477-549 |
3.63e-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: 3.63e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039740422 477 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 549
Cdd:COG1058 2 AEIITIGDELLS-------GRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGG 67
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
477-549 |
6.23e-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: 6.23e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039740422 477 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 549
Cdd:cd00885 2 AEIIAIGDELLS-------GQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
485-550 |
9.96e-07 |
|
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: 9.96e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039740422 485 ELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGV 550
Cdd:TIGR00200 4 EIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGL 69
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
479-562 |
2.58e-06 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 50.56 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 479 VMSTGNELLNpeddllpGKIRDSNRSTL---LATIQ-EHGYPTInlgiVGDNPDDLLNALNEGISRADVIITSGGVSMGE 554
Cdd:PRK00549 5 IIAVGTELLL-------GQIVNTNAQFLsekLAELGiDVYHQTV----VGDNPERLLSALEIAEERSDLIITTGGLGPTK 73
|
....*...
gi 1039740422 555 KDYLKQVL 562
Cdd:PRK00549 74 DDLTKETV 81
|
|
| PRK03673 |
PRK03673 |
nicotinamide mononucleotide deamidase-related protein YfaY; |
477-549 |
5.09e-06 |
|
nicotinamide mononucleotide deamidase-related protein YfaY;
Pssm-ID: 179629 [Multi-domain] Cd Length: 396 Bit Score: 49.31 E-value: 5.09e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039740422 477 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 549
Cdd:PRK03673 4 VEMLSTGDEVLH-------GQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGG 69
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
39-159 |
5.23e-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: 46.33 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 39 LKDLVQDpslLGGTISAYKIVPDEIEEIKETL---IDWCDekelnLILTTGGTGFAPRDVtpekfptfpfcglqkgaTKE 115
Cdd:cd00887 200 LAALLRE---LGAEVVDLGIVPDDPEALREALeeaLEEAD-----VVITSGGVSVGDYDF-----------------VKE 254
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1039740422 116 VIEREAPGmalaMLMGSLNVTPlGmlsRPV-CGIRGKTLIINLPG 159
Cdd:cd00887 255 VLEELGGE----VLFHGVAMKP-G---KPLaFGRLGGKPVFGLPG 291
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
475-549 |
7.42e-05 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 45.00 E-value: 7.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039740422 475 PVVAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 549
Cdd:PRK01215 4 WFAWIITIGNELLI-------GRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGG 71
|
|
| PRK03670 |
PRK03670 |
competence damage-inducible protein A; Provisional |
485-550 |
4.09e-04 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 167581 Cd Length: 252 Bit Score: 42.86 E-value: 4.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039740422 485 ELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRA-DVIITSGGV 550
Cdd:PRK03670 4 EIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKpEVLVISGGL 70
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
510-619 |
8.37e-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: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 510 IQEHGYPTINLGIVGDNPDDLLNALNEGISR--ADVIITSGGVSMGEKDY----LKQVLDIDLHAqihFGRVF----MKP 579
Cdd:COG0521 38 LEEAGHEVVARRIVPDDKDAIRAALRELIDDegVDLVLTTGGTGLSPRDVtpeaTRPLLDKELPG---FGELFralsLEE 114
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1039740422 580 GLPTTFATLDIDGVRK--IIFALPGNPvSAVVTCNLFVVPAL 619
Cdd:COG0521 115 IGPSAILSRAVAGIRGgtLIFNLPGSP-GAVREALEAILPEL 155
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
16-150 |
2.29e-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: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 16 RVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELnLILTTGGTGFAPRDV 95
Cdd:cd03522 161 RVGLIVTGSEVYGGRIEDKFGPVLRARLAA---LGVELVEQVIVPHDEAAIAAAIAEALEAGAE-LLILTGGASVDPDDV 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039740422 96 TPekfptfpfCGLqKGATKEVIEREAPGMALAMLMgslnvtpLGML-SRPVCGIRG 150
Cdd:cd03522 237 TP--------AAI-RAAGGEVIRYGMPVDPGNLLL-------LGYLgGVPVIGLPG 276
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
49-159 |
2.78e-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: 40.84 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 49 LGGTISAYKIVPDEIEEIKETL---IDWCDekelnLILTTGGTGFAPRDVtpekfptfpfcglqkgaTKEVIEREapGMA 125
Cdd:COG0303 211 AGAEVVDLGIVPDDPEALRAALreaLAEAD-----LVITSGGVSVGDYDL-----------------VKEALEEL--GAE 266
|
90 100 110
....*....|....*....|....*....|....*
gi 1039740422 126 LamLMGSLNVTPlGmlsRPV-CGIRGKTLIINLPG 159
Cdd:COG0303 267 V--LFHKVAMKP-G---KPLaFGRLGGKPVFGLPG 295
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
496-619 |
9.42e-03 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 38.77 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039740422 496 GKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISR-ADVIITSGGVSMGEKDY----LKQVLDIDLHAQI 570
Cdd:PRK03604 170 GTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAEgYALIITTGGTGLGPRDVtpeaLAPLLERRLPGIA 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1039740422 571 HFGRVFMKPGLPTTFATLDIDGV--RKIIFALPGNPvSAVVTCNLFVVPAL 619
Cdd:PRK03604 250 EALRSWGQGRTPTAMLSRLVAGMigNSLVVALPGSP-GGASDALAVLLPAL 299
|
|
|