|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
257-663 |
4.51e-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: 481.22 E-value: 4.51e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 257 DKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTQTV 333
Cdd:cd00887 2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 334 MPGQVMRVTTGAPIPCGADAVVQVEDTELiresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 413
Cdd:cd00887 82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE--------EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 414 LLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 493
Cdd:cd00887 154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 494 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 573
Cdd:cd00887 234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELFVRPAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 574 RKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEqyvEL 652
Cdd:cd00887 309 RKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---GL 383
|
410
....*....|.
gi 1907087789 653 HKGEVVDVMVI 663
Cdd:cd00887 384 EAGEEVEVLLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
253-666 |
7.71e-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: 442.22 E-value: 7.71e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 253 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF----IIGESQAGEQ 328
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtlrVVGEIAAGSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 329 PTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELiresDDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 408
Cdd:COG0303 81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER----EGDR----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 409 PSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 488
Cdd:COG0303 153 PADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 489 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLF 568
Cdd:COG0303 233 REALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 569 VVPALRKMQGILDPRPTIIKARLSCDV-KLDPRPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTE 647
Cdd:COG0303 308 VRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLERDDGE--LVVEPLGGQGSGLLSSLAEADGLIVLPEGVE 385
|
410
....*....|....*....
gi 1907087789 648 qyvELHKGEVVDVMVIGRL 666
Cdd:COG0303 386 ---GVEAGEEVEVLLLDGL 401
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
253-643 |
1.14e-133 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 407.66 E-value: 1.14e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 253 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQ- 331
Cdd:PLN02699 7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 332 TVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEEleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSE 411
Cdd:PLN02699 87 TLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 412 IGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLP-GKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNE 490
Cdd:PLN02699 165 IGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGrGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 491 GISR-ADVIITSGGVSMGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDI---DGVRKII--FALPGNPVSAVVT 564
Cdd:PLN02699 245 AISSgVDILLTSGGVSMGDRDFVKPLL--EKRGTVYFSKVLMKPGKPLTFAEIDAksaPSNSKKMlaFGLPGNPVSCLVC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 565 CNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQE----PLPWAQSTGNQMSSRLMSMRSANGL 639
Cdd:PLN02699 323 FNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPvRPEFHRAIIRWKLNDgsgnPGFVAESTGHQMSSRLLSMKSANAL 402
|
....
gi 1907087789 640 LMLP 643
Cdd:PLN02699 403 LELP 406
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
15-150 |
1.72e-59 |
|
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: 196.54 E-value: 1.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRD 94
Cdd:cd00886 1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907087789 95 VTPEATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKG 150
Cdd:cd00886 78 VTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKA 133
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
6-150 |
1.25e-54 |
|
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: 184.17 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 6 MILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTT 85
Cdd:COG0521 1 MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE---AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTT 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907087789 86 GGTGFAPRDVTPEATKEVIEREAPGMALAMLMGSLN-VTPLGMLSRPVCGIRGKTLIINLPGSKKG 150
Cdd:COG0521 78 GGTGLSPRDVTPEATRPLLDKELPGFGELFRALSLEeIGPSAILSRAVAGIRGGTLIFNLPGSPGA 143
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
268-419 |
8.04e-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: 167.74 E-value: 8.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 268 PVLGTEI---INYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGeSQAGEQPTQTVMPGQVMRVTTG 344
Cdd:pfam03453 1 PLLGTEEtvpLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP-IAAGEPPGPLLPGGEAVRIMTG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907087789 345 APIPCGADAVVQVEDTEliresddGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 419
Cdd:pfam03453 80 APLPEGADAVVMVEDTE-------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
12-146 |
8.69e-44 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 166.91 E-value: 8.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 12 DHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPS--LLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTG 89
Cdd:PLN02699 456 NPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSSSekLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907087789 90 FAPRDVTPEATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPG 146
Cdd:PLN02699 536 FTPRDVTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPG 592
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
15-153 |
3.14e-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: 138.60 E-value: 3.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 15 IRVGVLTVSDSCFRNLAE-------DRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEkeLNLILTTGG 87
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQE---AGFNVVRLGIVPDDPEEIREILRKAVDE--ADVVLTTGG 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 88 TGFAPRDVTPEATKEVIEREAPGMALAMLMGSLNVtplgmLSRP----VCGIRGKTLIINLPGSKKGSQI 153
Cdd:TIGR00177 76 TGVGPRDVTPEALEELGEKEIPGFGEFRMLSSLPV-----LSRPgkpaTAGVRGGTLIFNLPGNPVSALV 140
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
429-571 |
1.41e-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: 128.20 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 429 PVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGE 508
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907087789 509 KDYLKQVLDiDLHAQIHFGR----------VFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVP 571
Cdd:TIGR00177 81 RDVTPEALE-ELGEKEIPGFgefrmlsslpVLSRPGKPATAGVRG----GTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
432-568 |
3.41e-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: 121.16 E-value: 3.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 432 AVMSTGNELLNPeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVG--DNPDDLLNALNEGISRADVIITSGGVSMGEK 509
Cdd:smart00852 1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907087789 510 DYLKQVLDIDLHAQIHFGRVFMKPGLPTT-----FATLDIDGVRKIIFALPGNPVSAVVTCNLF 568
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPPGplanlSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
18-147 |
4.18e-28 |
|
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: 109.60 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 18 GVLTVSDSCFR-NLAEDRSGINLKDLVQDpslLGGTISAYKIV--PDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRD 94
Cdd:smart00852 1 AIISTGDELLSgGQIRDSNGPMLAALLRE---LGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907087789 95 VTPEATKEVIEREAPGMALAMLMGSLnVTPLGMLSRPVCGIRGKTLIINLPGS 147
Cdd:smart00852 76 LTPEALAELGGRELLGHGVAMRPGGP-PGPLANLSGTAPGVRGKKPVFGLPGN 127
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
18-153 |
1.45e-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 trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 102.71 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 18 GVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRDVTP 97
Cdd:pfam00994 1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTP 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907087789 98 EATKEVIEREAPGMALAMLMGSL------NVTPLGMLSrpvcgiRGKTLIINLPGSKKGSQI 153
Cdd:pfam00994 76 EALAELGGRELPGFEELFRGVSLkpgkpvGTAPGAILS------RAGKTVFGLPGSPVAAKV 131
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
257-663 |
4.51e-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: 481.22 E-value: 4.51e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 257 DKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF---IIGESQAGEQPTQTV 333
Cdd:cd00887 2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtlrVVGEIPAGEPPDGPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 334 MPGQVMRVTTGAPIPCGADAVVQVEDTELiresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIG 413
Cdd:cd00887 82 GPGEAVRIMTGAPLPEGADAVVMVEDTEE--------EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 414 LLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGIS 493
Cdd:cd00887 154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 494 RADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 573
Cdd:cd00887 234 EADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELFVRPAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 574 RKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEqyvEL 652
Cdd:cd00887 309 RKLQGAPEPEPPRVKARLAEDLKSKPgRREFLRVRLERDEGG--LVVAPPGGQGSGLLSSLARADGLIVIPEGVE---GL 383
|
410
....*....|.
gi 1907087789 653 HKGEVVDVMVI 663
Cdd:cd00887 384 EAGEEVEVLLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
253-666 |
7.71e-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: 442.22 E-value: 7.71e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 253 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF----IIGESQAGEQ 328
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtlrVVGEIAAGSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 329 PTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELiresDDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 408
Cdd:COG0303 81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER----EGDR----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 409 PSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 488
Cdd:COG0303 153 PADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 489 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLF 568
Cdd:COG0303 233 REALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRLG----GKPVFGLPGNPVSALVTFELF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 569 VVPALRKMQGILDPRPTIIKARLSCDV-KLDPRPEYHRCILTWHHQEplPWAQSTGNQMSSRLMSMRSANGLLMLPPKTE 647
Cdd:COG0303 308 VRPALRKLAGLPPPPPPRVRARLAEDLpKKPGRTEFLRVRLERDDGE--LVVEPLGGQGSGLLSSLAEADGLIVLPEGVE 385
|
410
....*....|....*....
gi 1907087789 648 qyvELHKGEVVDVMVIGRL 666
Cdd:COG0303 386 ---GVEAGEEVEVLLLDGL 401
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
253-643 |
1.14e-133 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 407.66 E-value: 1.14e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 253 LTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQ- 331
Cdd:PLN02699 7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 332 TVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEEleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSE 411
Cdd:PLN02699 87 TLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 412 IGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLP-GKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNE 490
Cdd:PLN02699 165 IGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGrGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 491 GISR-ADVIITSGGVSMGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDI---DGVRKII--FALPGNPVSAVVT 564
Cdd:PLN02699 245 AISSgVDILLTSGGVSMGDRDFVKPLL--EKRGTVYFSKVLMKPGKPLTFAEIDAksaPSNSKKMlaFGLPGNPVSCLVC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 565 CNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDP-RPEYHRCILTWHHQE----PLPWAQSTGNQMSSRLMSMRSANGL 639
Cdd:PLN02699 323 FNLFVVPAIRYLAGWSNPHLLRVQARLREPIKLDPvRPEFHRAIIRWKLNDgsgnPGFVAESTGHQMSSRLLSMKSANAL 402
|
....
gi 1907087789 640 LMLP 643
Cdd:PLN02699 403 LELP 406
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
267-660 |
6.12e-96 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 308.68 E-value: 6.12e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 267 TPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAAD-------GPGDRFIIGESQAGEQPTQTVMPGQVM 339
Cdd:PRK14498 25 ELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADtfgaseaNPVRLKLGGEVHAGEAPDVEVEPGEAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 340 RVTTGAPIPCGADAVVQVEDTElirESDDGTeeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 419
Cdd:PRK14498 105 EIATGAPIPRGADAVVMVEDTE---EVDDDT----VEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 420 VTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVII 499
Cdd:PRK14498 178 VAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 500 TSGGVSMGEKDYLKQVLDidlhaqiHFGRVF-----MKPGLPTTFATldIDGvrKIIFALPGNPVSAVVTCNLFVVPALR 574
Cdd:PRK14498 258 LSGGTSAGAGDVTYRVIE-------ELGEVLvhgvaIKPGKPTILGV--IGG--KPVVGLPGYPVSALTIFEEFVAPLLR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 575 KMQGILDPRPTIIKARLScdVKLDP---RPEYHRCILTWHHQEPLPWAQSTGnqmSSRLMSMRSANGLLMLPPKTEQyve 651
Cdd:PRK14498 327 KLAGLPPPERATVKARLA--RRVRSelgREEFVPVSLGRVGDGYVAYPLSRG---SGAITSLVRADGFIEIPANTEG--- 398
|
....*....
gi 1907087789 652 LHKGEVVDV 660
Cdd:PRK14498 399 LEAGEEVEV 407
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
267-648 |
7.27e-90 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 291.52 E-value: 7.27e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 267 TPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF-IIGESQAGEQPTQTVMPGQVMRVTTGA 345
Cdd:PRK14491 213 TPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESYtLVGEVLAGHQYDGTLQAGEAVRIMTGA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 346 PIPCGADAVVQVEDTELiresDDGTEELEVRILVqarpGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEV 425
Cdd:PRK14491 293 PVPAGADTVVMRELATQ----DGDKVSFDGGIKA----GQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPV 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 426 NKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVS 505
Cdd:PRK14491 365 FRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVS 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 506 MGEKDYLKQVLdiDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPALRKMQGILDPRPT 585
Cdd:PRK14491 445 VGDADYIKTAL--AKLGQIDFWRINMRPGRPLAFGQIG----DSPFFGLPGNPVAVMVSFLQFVEPALRKLAGEQNWQPL 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907087789 586 IIKARLSCDVKLDP-RPEYHRCILTWHHQEPLPwAQSTGNQMSSRLMSMRSANGLLMLPPKTEQ 648
Cdd:PRK14491 519 LFPAIADETLRSRQgRTEFSRGIYHLGADGRLH-VRTTGKQGSGILSSMSEANCLIEIGPAAET 581
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
253-642 |
3.26e-76 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 250.01 E-value: 3.26e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 253 LTSMDKAFITVL-EMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRF--IIGESQAGeQP 329
Cdd:PRK10680 7 LMSLETALTEMLsRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPlpVAGKAFAG-QP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 330 TQTVMP-GQVMRVTTGAPIPCGADAVVQVEDTELireSDDGteeleVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMG 408
Cdd:PRK10680 86 FHGEWPaGTCIRIMTGAPVPEGCEAVVMQEQTEQ---TDDG-----VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 409 PSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNAL 488
Cdd:PRK10680 158 TAELPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 489 NEGISRADVIITSGGVSMGEKDYLKQVLDiDLhAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLF 568
Cdd:PRK10680 238 IEADSQADVVISSGGVSVGEADYTKTILE-EL-GEIAFWKLAIKPGKPFAFGKLS----NSWFCGLPGNPVSAALTFYQL 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907087789 569 VVPALRKMQGILDPRPTI-IKARLSCDVKLDP-RPEYHRCILTWHHQEPLPwAQSTGNQMSSRLMSMRSANGLLML 642
Cdd:PRK10680 312 VQPLLAKLSGNTASGLPPrQRVRTASRLKKTPgRLDFQRGILQRNADGELE-VTTTGHQGSHIFSSFSLGNCFIVL 386
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
265-662 |
1.23e-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: 1.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 265 EMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQTVMPGQVMRVTTG 344
Cdd:PRK14497 23 SLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGEFKVIDKIGIGEFKEIHIKECEAVEVDTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 345 APIPCGADAVVQVEDTELIresddgtEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVE 424
Cdd:PRK14497 103 SMIPMGADAVIKVENTKVI-------NGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 425 VNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGV 504
Cdd:PRK14497 176 VYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 505 SMGEKDYLKQVL----DIDLHAqihfgrVFMKPGLPTTFATldIDGvrKIIFALPGNPVSAVVTCNLFVVPALRKMQG-- 578
Cdd:PRK14497 256 SAGEKDFVHQAIrelgNIIVHG------LKIKPGKPTILGI--VDG--KPVIGLPGNIVSTMVVLNMVILEYLKSLYPsr 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 579 --ILDPRPtiIKARLSCDVKLDprpeYHRCIL---------TWHHQEPLPWAqstgnqmSSRLMSMRSANGLLMLPPKTe 647
Cdd:PRK14497 326 keILGLGK--IKARLALRVKAD----EHRNTLipvylfksdNSYYALPVPFD-------SYMVGTFSLTDGYIMLGPNE- 391
|
410
....*....|....*
gi 1907087789 648 qyvELHKGEVVDVMV 662
Cdd:PRK14497 392 ---EIEEGKEVEVDL 403
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
15-150 |
1.72e-59 |
|
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: 196.54 E-value: 1.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRD 94
Cdd:cd00886 1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEE---AGHEVVAYEIVPDDKDEIREALIEWADEDGVDLILTTGGTGLAPRD 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907087789 95 VTPEATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKG 150
Cdd:cd00886 78 VTPEATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKA 133
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
6-150 |
1.25e-54 |
|
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: 184.17 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 6 MILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTT 85
Cdd:COG0521 1 MSSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEE---AGHEVVARRIVPDDKDAIRAALRELIDDEGVDLVLTT 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907087789 86 GGTGFAPRDVTPEATKEVIEREAPGMALAMLMGSLN-VTPLGMLSRPVCGIRGKTLIINLPGSKKG 150
Cdd:COG0521 78 GGTGLSPRDVTPEATRPLLDKELPGFGELFRALSLEeIGPSAILSRAVAGIRGGTLIFNLPGSPGA 143
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
268-419 |
8.04e-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: 167.74 E-value: 8.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 268 PVLGTEI---INYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGeSQAGEQPTQTVMPGQVMRVTTG 344
Cdd:pfam03453 1 PLLGTEEtvpLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP-IAAGEPPGPLLPGGEAVRIMTG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907087789 345 APIPCGADAVVQVEDTEliresddGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVG 419
Cdd:pfam03453 80 APLPEGADAVVMVEDTE-------EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
254-643 |
1.25e-48 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 175.88 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 254 TSMDKAFITVLE-MTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDR---FIIGESQAGEQP 329
Cdd:PRK14690 23 TPVDTALDLLRArLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQvlpLIEGRAAAGVPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 330 TQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELiresddGTEELEVRILVQArpGQDIRPIGHDIKRGECVLAKGTHMGP 409
Cdd:PRK14690 103 SGRVPEGMALRILTGAALPEGVDTVVLEEDVAG------DGHRIAFHGPLKM--GANTRKAGEDVIAGDVALPAGRRLTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 410 SEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALN 489
Cdd:PRK14690 175 ADLALLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 490 EGISRADVIITSGGVSMGEKDYLKQVLDIDlhAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFV 569
Cdd:PRK14690 255 RAAAEADVILTSGGASAGDEDHVSALLREA--GAMQSWRIALKPGRPLALGLWQ----GVPVFGLPGNPVAALVCTLVFA 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907087789 570 VPALRKM--QGILDPRPTIIKARLSCDvKLDPRPEYHRCILTWHHQEPLpwaQSTGnqmSSRLMSMRSANGLLMLP 643
Cdd:PRK14690 329 RPAMSLLagEGWSEPQGFTVPAAFEKR-KKPGRREYLRARLRQGHAEVF---RSEG---SGRISGLSWAEGLVELG 397
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
12-146 |
8.69e-44 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 166.91 E-value: 8.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 12 DHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPS--LLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTG 89
Cdd:PLN02699 456 NPEVKVAILTVSDTVSSGAGPDRSGPRAVSVVNSSSekLGGAKVVATAVVPDDVEKIKDVLQKWSDIDRMDLILTLGGTG 535
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907087789 90 FAPRDVTPEATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPG 146
Cdd:PLN02699 536 FTPRDVTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPG 592
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
431-573 |
6.45e-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: 145.56 E-value: 6.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 431 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKD 510
Cdd:cd00758 2 VAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907087789 511 YLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVPAL 573
Cdd:cd00758 75 VTPEALAELGEREAHGKGVALAPGSRTAFGIIG----KVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| mogA |
PRK09417 |
molybdenum cofactor biosynthesis protein MogA; Provisional |
15-149 |
2.59e-39 |
|
molybdenum cofactor biosynthesis protein MogA; Provisional
Pssm-ID: 181837 [Multi-domain] Cd Length: 193 Bit Score: 143.17 E-value: 2.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 15 IRVGVLTVSDSCFRNLAEDRSGINLKDLvqdpslLGGTISA-----YKIVPDEIEEIKETLIDWCDEKELNLILTTGGTG 89
Cdd:PRK09417 4 LKIGLVSISDRASSGVYEDKGIPALEEW------LASALTSpfeieTRLIPDEQDLIEQTLIELVDEMGCDLVLTTGGTG 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 90 FAPRDVTPEATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKK 149
Cdd:PRK09417 78 PARRDVTPEATLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPK 137
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
15-153 |
3.14e-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: 138.60 E-value: 3.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 15 IRVGVLTVSDSCFRNLAE-------DRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEkeLNLILTTGG 87
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQE---AGFNVVRLGIVPDDPEEIREILRKAVDE--ADVVLTTGG 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 88 TGFAPRDVTPEATKEVIEREAPGMALAMLMGSLNVtplgmLSRP----VCGIRGKTLIINLPGSKKGSQI 153
Cdd:TIGR00177 76 TGVGPRDVTPEALEELGEKEIPGFGEFRMLSSLPV-----LSRPgkpaTAGVRGGTLIFNLPGNPVSALV 140
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
16-152 |
5.45e-38 |
|
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: 137.47 E-value: 5.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 16 RVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEkeLNLILTTGGTGFAPRDV 95
Cdd:cd00758 1 RVAIVTVSDELSQGQIEDTNGPALEALLED---LGCEVIYAGVVPDDADSIRAALIEASRE--ADLVLTTGGTGVGRRDV 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907087789 96 TPEATKEVIEREAPGmalamlmgslNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQ 152
Cdd:cd00758 76 TPEALAELGEREAHG----------KGVALAPGSRTAFGIIGKVLIINLPGSPKSAL 122
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
15-150 |
1.19e-36 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 139.69 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 15 IRVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCdEKELNLILTTGGTGFAPRD 94
Cdd:PRK03604 156 TSAAVLVLSDSIAAGTKEDRSGKLIVEGLEE---AGFEVSHYTIIPDEPAEIAAAVAAWI-AEGYALIITTGGTGLGPRD 231
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907087789 95 VTPEATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKG 150
Cdd:PRK03604 232 VTPEALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGG 287
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
429-571 |
1.41e-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: 128.20 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 429 PVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGE 508
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907087789 509 KDYLKQVLDiDLHAQIHFGR----------VFMKPGLPTTFATLDidgvRKIIFALPGNPVSAVVTCNLFVVP 571
Cdd:TIGR00177 81 RDVTPEALE-ELGEKEIPGFgefrmlsslpVLSRPGKPATAGVRG----GTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
432-575 |
9.23e-33 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 123.13 E-value: 9.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 432 AVMSTGNELLnpeddllPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDY 511
Cdd:pfam00994 1 AIITTGDELL-------PGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907087789 512 LKQVL------DIDLHAQIhFGRVFMKPGLPTTFATL-DIDGVRKIIFALPGNPVSAVVTCNLFVVPALRK 575
Cdd:pfam00994 74 TPEALaelggrELPGFEEL-FRGVSLKPGKPVGTAPGaILSRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
432-568 |
3.41e-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: 121.16 E-value: 3.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 432 AVMSTGNELLNPeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVG--DNPDDLLNALNEGISRADVIITSGGVSMGEK 509
Cdd:smart00852 1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907087789 510 DYLKQVLDIDLHAQIHFGRVFMKPGLPTT-----FATLDIDGVRKIIFALPGNPVSAVVTCNLF 568
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPPGplanlSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
18-147 |
4.18e-28 |
|
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: 109.60 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 18 GVLTVSDSCFR-NLAEDRSGINLKDLVQDpslLGGTISAYKIV--PDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRD 94
Cdd:smart00852 1 AIISTGDELLSgGQIRDSNGPMLAALLRE---LGIEVVRVVVVggPDDPEAIREALREALAEADV--VITTGGTGPGPDD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907087789 95 VTPEATKEVIEREAPGMALAMLMGSLnVTPLGMLSRPVCGIRGKTLIINLPGS 147
Cdd:smart00852 76 LTPEALAELGGRELLGHGVAMRPGGP-PGPLANLSGTAPGVRGKKPVFGLPGN 127
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
18-153 |
1.45e-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 trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 102.71 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 18 GVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELnlILTTGGTGFAPRDVTP 97
Cdd:pfam00994 1 AIITTGDELLPGQIRDTNGPLLAALLRE---AGAEVIRYGIVPDDPEAIKEALRAAAEEADV--VITTGGTGPGPDDVTP 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907087789 98 EATKEVIEREAPGMALAMLMGSL------NVTPLGMLSrpvcgiRGKTLIINLPGSKKGSQI 153
Cdd:pfam00994 76 EALAELGGRELPGFEELFRGVSLkpgkpvGTAPGAILS------RAGKTVFGLPGSPVAAKV 131
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
588-663 |
1.81e-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: 1.81e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907087789 588 KARLSCDVKLDP-RPEYHRCILtwHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVElhkGEVVDVMVI 663
Cdd:pfam03454 1 KARLARDLKSDPgRREFVRVRL--HEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEA---GEEVEVILL 72
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
431-503 |
4.56e-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: 63.59 E-value: 4.56e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907087789 431 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 503
Cdd:COG1058 2 AEIITIGDELLS-------GRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGG 67
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
431-503 |
7.90e-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: 60.96 E-value: 7.90e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907087789 431 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 503
Cdd:cd00885 2 AEIIAIGDELLS-------GQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
439-504 |
9.49e-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: 9.49e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907087789 439 ELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGV 504
Cdd:TIGR00200 4 EIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGL 69
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
39-146 |
1.67e-06 |
|
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: 50.96 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 39 LKDLVQDpslLGGTISAYKIVPDEIEEIKETL---IDWCDekelnLILTTGGTGFAPRDVtpeaTKEVIEREAPGmalaM 115
Cdd:cd00887 200 LAALLRE---LGAEVVDLGIVPDDPEALREALeeaLEEAD-----VVITSGGVSVGDYDF----VKEVLEELGGE----V 263
|
90 100 110
....*....|....*....|....*....|..
gi 1907087789 116 LMGSLNVTPlGmlsRPV-CGIRGKTLIINLPG 146
Cdd:cd00887 264 LFHGVAMKP-G---KPLaFGRLGGKPVFGLPG 291
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
433-516 |
2.78e-06 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 50.17 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 433 VMSTGNELLNpeddllpGKIRDSNRSTL---LATIQ-EHGYPTInlgiVGDNPDDLLNALNEGISRADVIITSGGVSMGE 508
Cdd:PRK00549 5 IIAVGTELLL-------GQIVNTNAQFLsekLAELGiDVYHQTV----VGDNPERLLSALEIAEERSDLIITTGGLGPTK 73
|
....*...
gi 1907087789 509 KDYLKQVL 516
Cdd:PRK00549 74 DDLTKETV 81
|
|
| PRK03673 |
PRK03673 |
nicotinamide mononucleotide deamidase-related protein YfaY; |
431-503 |
5.26e-06 |
|
nicotinamide mononucleotide deamidase-related protein YfaY;
Pssm-ID: 179629 [Multi-domain] Cd Length: 396 Bit Score: 49.31 E-value: 5.26e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907087789 431 VAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 503
Cdd:PRK03673 4 VEMLSTGDEVLH-------GQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGG 69
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
16-137 |
1.94e-05 |
|
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. There this domain is presumed to bind molybdopterin. The exact function of this subgroup is unknown.
Pssm-ID: 239599 Cd Length: 312 Bit Score: 47.16 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 16 RVGVLTVSDSCFRNLAEDRSGINLKDLVQDpslLGGTISAYKIVPDEIEEIKETLIDWCDEKELnLILTTGGTGFAPRDV 95
Cdd:cd03522 161 RVGLIVTGSEVYGGRIEDKFGPVLRARLAA---LGVELVEQVIVPHDEAAIAAAIAEALEAGAE-LLILTGGASVDPDDV 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907087789 96 TPEATK----EVIEREAPGMALAMLMgslnvtpLGML-SRPVCGIRG 137
Cdd:cd03522 237 TPAAIRaaggEVIRYGMPVDPGNLLL-------LGYLgGVPVIGLPG 276
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
429-503 |
7.40e-05 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 45.00 E-value: 7.40e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907087789 429 PVVAVMSTGNELLNpeddllpGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGG 503
Cdd:PRK01215 4 WFAWIITIGNELLI-------GRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGG 71
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
49-146 |
8.38e-05 |
|
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: 45.47 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 49 LGGTISAYKIVPDEIEEIKETL---IDWCDekelnLILTTGGTGFAPRDVtpeaTKEVIEREapGMALamLMGSLNVTPl 125
Cdd:COG0303 211 AGAEVVDLGIVPDDPEALRAALreaLAEAD-----LVITSGGVSVGDYDL----VKEALEEL--GAEV--LFHKVAMKP- 276
|
90 100
....*....|....*....|..
gi 1907087789 126 GmlsRPV-CGIRGKTLIINLPG 146
Cdd:COG0303 277 G---KPLaFGRLGGKPVFGLPG 295
|
|
| PRK03670 |
PRK03670 |
competence damage-inducible protein A; Provisional |
439-504 |
4.35e-04 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 167581 Cd Length: 252 Bit Score: 42.48 E-value: 4.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907087789 439 ELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRA-DVIITSGGV 504
Cdd:PRK03670 4 EIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKpEVLVISGGL 70
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
464-573 |
9.71e-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: 40.49 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907087789 464 IQEHGYPTINLGIVGDNPDDLLNALNEGISR--ADVIITSGGVSMGEKDY----LKQVLDIDLHAqihFGRVF----MKP 533
Cdd:COG0521 38 LEEAGHEVVARRIVPDDKDAIRAALRELIDDegVDLVLTTGGTGLSPRDVtpeaTRPLLDKELPG---FGELFralsLEE 114
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907087789 534 GLPTTFATLDIDGVRK--IIFALPGNPvSAVVTCNLFVVPAL 573
Cdd:COG0521 115 IGPSAILSRAVAGIRGgtLIFNLPGSP-GAVREALEAILPEL 155
|
|
|