|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
202-609 |
1.09e-123 |
|
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: 371.06 E-value: 1.09e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 202 EAFQIVDAVMSQWKecVEVLPLEQCIGKVAAQDIRAKEPMPPFPASIKDGYACLSCDGAGVR---KVRSALTAGDEYPQe 278
Cdd:cd00887 3 AARELLLALAPPLG--TETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASvtlRVVGEIPAGEPPDG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 279 sPLVAGECARVNTGAPVPPGADCVVQVEDTRLIkatEDYqteleVEVLVAPAAHQDVRPVGFDIPLGTILLEKGDVIDAA 358
Cdd:cd00887 80 -PLGPGEAVRIMTGAPLPEGADAVVMVEDTEEE---GGR-----VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 359 QIGILAGAGCLEIPVRLCPKVAILSTGNELQEPSEvTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGALAAAIA 438
Cdd:cd00887 151 DIGLLASLGIAEVPVYRRPRVAIISTGDELVEPGE-PLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 439 TALSSADVLVCTGGVSMGERDLLKPVLQhDFGASIHFGRVRMKPGKPSTFATCtykgRTKYIFALPGNPVSAYVCCVLFV 518
Cdd:cd00887 230 EALEEADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRL----GGKPVFGLPGNPVSALVTFELFV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 519 VRALRRCT-RDTSEYARMRVRLAGDVTLDP-RPEYARAVLTFptTDQLPVATVLGNQCSSRLLSVCGASVLLELPAATDT 596
Cdd:cd00887 305 RPALRKLQgAPEPEPPRVKARLAEDLKSKPgRREFLRVRLER--DEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEG 382
|
410
....*....|...
gi 2311241737 597 VKvlaADSTVSAL 609
Cdd:cd00887 383 LE---AGEEVEVL 392
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
197-598 |
1.65e-117 |
|
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: 355.55 E-value: 1.65e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 197 MLEMSEAFQIVDAVMSQWKecVEVLPLEQCIGKVAAQDIRAKEPMPPFPASIKDGYACLSCDGAGVR----KVRSALTAG 272
Cdd:COG0303 1 MISVEEALALILAAVRPLG--TETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANpvtlRVVGEIAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 273 DEYPQesPLVAGECARVNTGAPVPPGADCVVQVEDTRlikATEDYqteleVEVLVAPAAHQDVRPVGFDIPLGTILLEKG 352
Cdd:COG0303 79 SPPPG--PLGPGEAVRIMTGAPLPEGADAVVMQEDTE---REGDR-----VTIRKPVAPGENIRRAGEDIAAGDVLLPAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 353 DVIDAAQIGILAGAGCLEIPVRLCPKVAILSTGNELQEPSEvTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGA 432
Cdd:COG0303 149 TRLTPADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGE-PLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 433 LAAAIATALSSADVLVCTGGVSMGERDLLKPVLQhDFGASIHFGRVRMKPGKPSTFATCtykgRTKYIFALPGNPVSAYV 512
Cdd:COG0303 228 LRAALREALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRL----GGKPVFGLPGNPVSALV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 513 CCVLFVVRALRRCT-RDTSEYARMRVRLAGDVTLDP-RPEYARAVLTfpTTDQLPVATVLGNQCSSRLLSVCGASVLLEL 590
Cdd:COG0303 303 TFELFVRPALRKLAgLPPPPPPRVRARLAEDLPKKPgRTEFLRVRLE--RDDGELVVEPLGGQGSGLLSSLAEADGLIVL 380
|
....*...
gi 2311241737 591 PAATDTVK 598
Cdd:COG0303 381 PEGVEGVE 388
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
197-614 |
5.60e-103 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 326.38 E-value: 5.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 197 MLEMSEAFQIVDAVmSQWKECVEVlPLEQCIGKVAAQDIRAKEPMPPFPASIKDGYACLSCDGAGVRKVRSALTAGDeYP 276
Cdd:PLN02699 7 MISVEEALSIVLSV-AARLSPVIV-PLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGN-DG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 277 QESPLVAGECARVNTGAPVPPGADCVVQVEDTRLIKATEDYQTEleVEVLVAPAAHQDVRPVGFDIPLGTILLEKGDVID 356
Cdd:PLN02699 84 LGVTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 357 AAQIGILAGAGCLEIPVRLCPKVAILSTGNELQEPSEVTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARD-EPGALAA 435
Cdd:PLN02699 162 ASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDdEEELERI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 436 AIATALSSADVLVCTGGVSMGERDLLKPVLQHDfgASIHFGRVRMKPGKPSTFATCTYK-----GRTKYIFALPGNPVSA 510
Cdd:PLN02699 242 LDEAISSGVDILLTSGGVSMGDRDFVKPLLEKR--GTVYFSKVLMKPGKPLTFAEIDAKsapsnSKKMLAFGLPGNPVSC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 511 YVCCVLFVVRALRRCTRDTSEY-ARMRVRLAGDVTLDP-RPEYARAVLTFPTTDQLP----VATVLGNQCSSRLLSVCGA 584
Cdd:PLN02699 320 LVCFNLFVVPAIRYLAGWSNPHlLRVQARLREPIKLDPvRPEFHRAIIRWKLNDGSGnpgfVAESTGHQMSSRLLSMKSA 399
|
410 420 430
....*....|....*....|....*....|
gi 2311241737 585 SVLLELPAatdTVKVLAADSTVSALIVGRI 614
Cdd:PLN02699 400 NALLELPA---TGNVLSAGTSVSAIIISDI 426
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
5-154 |
1.79e-57 |
|
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: 190.38 E-value: 1.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 5 VVIITVSDTCCKDHAKDQSGPALFQLVKEKFPDADIHTIIlPDEKDLIEKKLKYFCD-TKIDLILTTGGTGLSSRDVTPE 83
Cdd:cd00886 3 AAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIV-PDDKDEIREALIEWADeDGVDLILTTGGTGLAPRDVTPE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2311241737 84 ATKAVIQREIPAISTAMTIESLKKTPMAMLSRAIAGIRDSTLIVNFPGSKKAVIECAEVVMPVLSHALSLL 154
Cdd:cd00886 82 ATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
5-154 |
4.93e-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: 181.85 E-value: 4.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 5 VVIITVSDTCCKDHAKDQSGPALFQLVKEKFPDADIHTIIlPDEKDLIEKKLKYFCDT-KIDLILTTGGTGLSSRDVTPE 83
Cdd:COG0521 12 IAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIV-PDDKDAIRAALRELIDDeGVDLVLTTGGTGLSPRDVTPE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2311241737 84 ATKAVIQREIPAISTAMTIESLKK-TPMAMLSRAIAGIRDSTLIVNFPGSKKAVIECAEVVMPVLSHALSLL 154
Cdd:COG0521 91 ATRPLLDKELPGFGELFRALSLEEiGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHAVDLL 162
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
5-151 |
1.43e-42 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 162.67 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 5 VVIITVSDTCCKDHAKDQSGPALFQLV---KEKFPDADI-HTIILPDEKDLIEKKLKYFCDT-KIDLILTTGGTGLSSRD 79
Cdd:PLN02699 461 VAILTVSDTVSSGAGPDRSGPRAVSVVnssSEKLGGAKVvATAVVPDDVEKIKDVLQKWSDIdRMDLILTLGGTGFTPRD 540
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2311241737 80 VTPEATKAVIQREIPAISTAMTIESLKKTPMAMLSRAIAGIRDSTLIVNFPGSKKAVIECAEVVMPVLSHAL 151
Cdd:PLN02699 541 VTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHAL 612
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
218-367 |
1.53e-41 |
|
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: 147.33 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 218 VEVLPLE--QCIGKVAAQDIRAKEPMPPFPASIKDGYACLSCDGAGVRKVRSALtAGDeyPQESPLVAGECARVNTGAPV 295
Cdd:pfam03453 6 EETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIA-AGE--PPGPLLPGGEAVRIMTGAPL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2311241737 296 PPGADCVVQVEDTRLIKatedyqtELEVEVLVAPAAHQDVRPVGFDIPLGTILLEKGDVIDAAQIGILAGAG 367
Cdd:pfam03453 83 PEGADAVVMVEDTEEGG-------GRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
5-144 |
4.08e-28 |
|
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: 110.10 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 5 VVIITVSDTCCKDHAK-------DQSGPALFQLVKEKFPDADIHTIIlPDEKDLIEKKLKYFCDtKIDLILTTGGTGLSS 77
Cdd:TIGR00177 3 VAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIV-PDDPEEIREILRKAVD-EADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2311241737 78 RDVTPEATKAVIQREIPAISTAMtieslKKTPMAMLSR----AIAGIRDSTLIVNFPGSKKAVIECAEVVM 144
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGFGEFR-----MLSSLPVLSRpgkpATAGVRGGTLIFNLPGNPVSALVTFEVLI 146
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
7-143 |
3.09e-27 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 106.90 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 7 IITVSDTCCKDHAK-DQSGPALFQLVKEK-FPDADIHTIILPDEKDLIEKKLKYFCDtKIDLILTTGGTGLSSRDVTPEA 84
Cdd:smart00852 2 IISTGDELLSGGQIrDSNGPMLAALLRELgIEVVRVVVVGGPDDPEAIREALREALA-EADVVITTGGTGPGPDDLTPEA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2311241737 85 TKAVIQREIPAISTAMTIESlKKTPMAMLSRAIAGIRDSTLIVNFPGSKKAVIECAEVV 143
Cdd:smart00852 81 LAELGGRELLGHGVAMRPGG-PPGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
380-513 |
3.09e-26 |
|
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: 104.21 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 380 AILSTGNELQEPSEvtlhpshIRDSNRLMLRSLLREHGYASVDSGIA--RDEPGALAAAIATALSSADVLVCTGGVSMGE 457
Cdd:smart00852 1 AIISTGDELLSGGQ-------IRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGP 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2311241737 458 RDLLKPVLQHDFGASIHFGRVRMKPGKPSTFATCTY-----KGRTKYIFALPGNPVSAYVC 513
Cdd:smart00852 74 DDLTPEALAELGGRELLGHGVAMRPGGPPGPLANLSgtapgVRGKKPVFGLPGNPVAALVM 134
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
377-513 |
1.51e-25 |
|
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: 102.78 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 377 PKVAILSTGNELQEPSEvTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGALAAAIATALSSADVLVCTGGVSMG 456
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQ-PLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2311241737 457 ERDLLKPVLQ-------HDFGASIH--FGRVRMKPGKPSTFAtcTYKGrtKYIFALPGNPVSAYVC 513
Cdd:TIGR00177 80 PRDVTPEALEelgekeiPGFGEFRMlsSLPVLSRPGKPATAG--VRGG--TLIFNLPGNPVSALVT 141
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
7-149 |
1.75e-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: 93.85 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 7 IITVSDTCCKDHAKDQSGPALFQLVKEkFPDADIHTIILPDEKDLIEKKLKYFCDtKIDLILTTGGTGLSSRDVTPEATK 86
Cdd:pfam00994 2 IITTGDELLPGQIRDTNGPLLAALLRE-AGAEVIRYGIVPDDPEAIKEALRAAAE-EADVVITTGGTGPGPDDVTPEALA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 87 AVIQREIPAISTAMTIESLK------KTPMAMLSRAiagirdSTLIVNFPGSKKAVIECAE-VVMPVLSH 149
Cdd:pfam00994 80 ELGGRELPGFEELFRGVSLKpgkpvgTAPGAILSRA------GKTVFGLPGSPVAAKVMFElLLLPLLRH 143
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
202-609 |
1.09e-123 |
|
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: 371.06 E-value: 1.09e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 202 EAFQIVDAVMSQWKecVEVLPLEQCIGKVAAQDIRAKEPMPPFPASIKDGYACLSCDGAGVR---KVRSALTAGDEYPQe 278
Cdd:cd00887 3 AARELLLALAPPLG--TETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASvtlRVVGEIPAGEPPDG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 279 sPLVAGECARVNTGAPVPPGADCVVQVEDTRLIkatEDYqteleVEVLVAPAAHQDVRPVGFDIPLGTILLEKGDVIDAA 358
Cdd:cd00887 80 -PLGPGEAVRIMTGAPLPEGADAVVMVEDTEEE---GGR-----VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 359 QIGILAGAGCLEIPVRLCPKVAILSTGNELQEPSEvTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGALAAAIA 438
Cdd:cd00887 151 DIGLLASLGIAEVPVYRRPRVAIISTGDELVEPGE-PLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 439 TALSSADVLVCTGGVSMGERDLLKPVLQhDFGASIHFGRVRMKPGKPSTFATCtykgRTKYIFALPGNPVSAYVCCVLFV 518
Cdd:cd00887 230 EALEEADVVITSGGVSVGDYDFVKEVLE-ELGGEVLFHGVAMKPGKPLAFGRL----GGKPVFGLPGNPVSALVTFELFV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 519 VRALRRCT-RDTSEYARMRVRLAGDVTLDP-RPEYARAVLTFptTDQLPVATVLGNQCSSRLLSVCGASVLLELPAATDT 596
Cdd:cd00887 305 RPALRKLQgAPEPEPPRVKARLAEDLKSKPgRREFLRVRLER--DEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEG 382
|
410
....*....|...
gi 2311241737 597 VKvlaADSTVSAL 609
Cdd:cd00887 383 LE---AGEEVEVL 392
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
197-598 |
1.65e-117 |
|
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: 355.55 E-value: 1.65e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 197 MLEMSEAFQIVDAVMSQWKecVEVLPLEQCIGKVAAQDIRAKEPMPPFPASIKDGYACLSCDGAGVR----KVRSALTAG 272
Cdd:COG0303 1 MISVEEALALILAAVRPLG--TETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANpvtlRVVGEIAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 273 DEYPQesPLVAGECARVNTGAPVPPGADCVVQVEDTRlikATEDYqteleVEVLVAPAAHQDVRPVGFDIPLGTILLEKG 352
Cdd:COG0303 79 SPPPG--PLGPGEAVRIMTGAPLPEGADAVVMQEDTE---REGDR-----VTIRKPVAPGENIRRAGEDIAAGDVLLPAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 353 DVIDAAQIGILAGAGCLEIPVRLCPKVAILSTGNELQEPSEvTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGA 432
Cdd:COG0303 149 TRLTPADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGE-PLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 433 LAAAIATALSSADVLVCTGGVSMGERDLLKPVLQhDFGASIHFGRVRMKPGKPSTFATCtykgRTKYIFALPGNPVSAYV 512
Cdd:COG0303 228 LRAALREALAEADLVITSGGVSVGDYDLVKEALE-ELGAEVLFHKVAMKPGKPLAFGRL----GGKPVFGLPGNPVSALV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 513 CCVLFVVRALRRCT-RDTSEYARMRVRLAGDVTLDP-RPEYARAVLTfpTTDQLPVATVLGNQCSSRLLSVCGASVLLEL 590
Cdd:COG0303 303 TFELFVRPALRKLAgLPPPPPPRVRARLAEDLPKKPgRTEFLRVRLE--RDDGELVVEPLGGQGSGLLSSLAEADGLIVL 380
|
....*...
gi 2311241737 591 PAATDTVK 598
Cdd:COG0303 381 PEGVEGVE 388
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
197-614 |
5.60e-103 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 326.38 E-value: 5.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 197 MLEMSEAFQIVDAVmSQWKECVEVlPLEQCIGKVAAQDIRAKEPMPPFPASIKDGYACLSCDGAGVRKVRSALTAGDeYP 276
Cdd:PLN02699 7 MISVEEALSIVLSV-AARLSPVIV-PLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGN-DG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 277 QESPLVAGECARVNTGAPVPPGADCVVQVEDTRLIKATEDYQTEleVEVLVAPAAHQDVRPVGFDIPLGTILLEKGDVID 356
Cdd:PLN02699 84 LGVTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR--VRILSQASKGQDIRPVGCDIEKDAKVLKAGERLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 357 AAQIGILAGAGCLEIPVRLCPKVAILSTGNELQEPSEVTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARD-EPGALAA 435
Cdd:PLN02699 162 ASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGTLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDdEEELERI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 436 AIATALSSADVLVCTGGVSMGERDLLKPVLQHDfgASIHFGRVRMKPGKPSTFATCTYK-----GRTKYIFALPGNPVSA 510
Cdd:PLN02699 242 LDEAISSGVDILLTSGGVSMGDRDFVKPLLEKR--GTVYFSKVLMKPGKPLTFAEIDAKsapsnSKKMLAFGLPGNPVSC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 511 YVCCVLFVVRALRRCTRDTSEY-ARMRVRLAGDVTLDP-RPEYARAVLTFPTTDQLP----VATVLGNQCSSRLLSVCGA 584
Cdd:PLN02699 320 LVCFNLFVVPAIRYLAGWSNPHlLRVQARLREPIKLDPvRPEFHRAIIRWKLNDGSGnpgfVAESTGHQMSSRLLSMKSA 399
|
410 420 430
....*....|....*....|....*....|
gi 2311241737 585 SVLLELPAatdTVKVLAADSTVSALIVGRI 614
Cdd:PLN02699 400 NALLELPA---TGNVLSAGTSVSAIIISDI 426
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
218-599 |
1.88e-63 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 219.87 E-value: 1.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 218 VEVLPLEQCIGKVAAQDIRAKEPMPPFPASIKDGYACLSCD-GAGVRKVRSALTAGDEYPQesPLVAGECARVNTGAPVP 296
Cdd:PRK14491 218 TEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDlEPESYTLVGEVLAGHQYDG--TLQAGEAVRIMTGAPVP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 297 PGADCVVQVEDTRLIKATEDYQTELEvevlvapaAHQDVRPVGFDIPLGTILLEKGDVIDAAQIGILAGAGCLEIPVRLC 376
Cdd:PRK14491 296 AGADTVVMRELATQDGDKVSFDGGIK--------AGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRR 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 377 PKVAILSTGNELQEPSEvTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGALAAAIATALSSADVLVCTGGVSMG 456
Cdd:PRK14491 368 PKVAVFSTGDEVQAPGE-TLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVSVG 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 457 ERDLLKPVLQHDfgASIHFGRVRMKPGKPSTFAtctyKGRTKYIFALPGNPVSAYVCCVLFVVRALRRCTRDTSeYARMR 536
Cdd:PRK14491 447 DADYIKTALAKL--GQIDFWRINMRPGRPLAFG----QIGDSPFFGLPGNPVAVMVSFLQFVEPALRKLAGEQN-WQPLL 519
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2311241737 537 VRLAGDVTLDPRP---EYARAVLTFPTTDQLPVATVlGNQCSSRLLSVCGASVLLELPAATDTVKV 599
Cdd:PRK14491 520 FPAIADETLRSRQgrtEFSRGIYHLGADGRLHVRTT-GKQGSGILSSMSEANCLIEIGPAAETVNA 584
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
202-543 |
4.32e-60 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 211.61 E-value: 4.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 202 EAFQIVDAVMSQWKECVEVLPLEQCIGKVAAQDIRAKEPMPPFPASIKDGYACLSCD--GAG----VR-KVRSALTAGDE 274
Cdd:PRK14498 14 EAREILESLLSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADtfGASeanpVRlKLGGEVHAGEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 275 YPQEspLVAGECARVNTGAPVPPGADCVVQVEDTRlikaTEDYQTeleVEVLVAPAAHQDVRPVGFDIPLGTILLEKGDV 354
Cdd:PRK14498 94 PDVE--VEPGEAVEIATGAPIPRGADAVVMVEDTE----EVDDDT---VEIYRPVAPGENVRPAGEDIVAGELILPKGTR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 355 IDAAQIGILAGAGCLEIPVRLCPKVAILSTGNELQEPSEvTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGALA 434
Cdd:PRK14498 165 LTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGE-PLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 435 AAIATALSSADVLVCTGGVSMGERDLLKPVLQhDFGaSIHFGRVRMKPGKPSTFATCtykgRTKYIFALPGNPVSAYVCC 514
Cdd:PRK14498 244 AALRKALKECDLVLLSGGTSAGAGDVTYRVIE-ELG-EVLVHGVAIKPGKPTILGVI----GGKPVVGLPGYPVSALTIF 317
|
330 340 350
....*....|....*....|....*....|
gi 2311241737 515 VLFVVRALRRCT-RDTSEYARMRVRLAGDV 543
Cdd:PRK14498 318 EEFVAPLLRKLAgLPPPERATVKARLARRV 347
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
5-154 |
1.79e-57 |
|
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: 190.38 E-value: 1.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 5 VVIITVSDTCCKDHAKDQSGPALFQLVKEKFPDADIHTIIlPDEKDLIEKKLKYFCD-TKIDLILTTGGTGLSSRDVTPE 83
Cdd:cd00886 3 AAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIV-PDDKDEIREALIEWADeDGVDLILTTGGTGLAPRDVTPE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2311241737 84 ATKAVIQREIPAISTAMTIESLKKTPMAMLSRAIAGIRDSTLIVNFPGSKKAVIECAEVVMPVLSHALSLL 154
Cdd:cd00886 82 ATRPLLDKELPGFGEAFRALSLEETGTAMLSRAVAGIRGGTLIFNLPGSPKAVREALEVILPELPHLLDLL 152
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
5-154 |
4.93e-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: 181.85 E-value: 4.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 5 VVIITVSDTCCKDHAKDQSGPALFQLVKEKFPDADIHTIIlPDEKDLIEKKLKYFCDT-KIDLILTTGGTGLSSRDVTPE 83
Cdd:COG0521 12 IAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIV-PDDKDAIRAALRELIDDeGVDLVLTTGGTGLSPRDVTPE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2311241737 84 ATKAVIQREIPAISTAMTIESLKK-TPMAMLSRAIAGIRDSTLIVNFPGSKKAVIECAEVVMPVLSHALSLL 154
Cdd:COG0521 91 ATRPLLDKELPGFGELFRALSLEEiGPSAILSRAVAGIRGGTLIFNLPGSPGAVREALEAILPELPHAVDLL 162
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
218-575 |
1.59e-50 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 180.29 E-value: 1.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 218 VEVLPLEQCIGKVAAQDIRAKEPMPPFPASIKDGYACLSCDGAGVR--KVRSALTAGDEYPQESPlvAGECARVNTGAPV 295
Cdd:PRK10680 27 TETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQplPVAGKAFAGQPFHGEWP--AGTCIRIMTGAPV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 296 PPGADCVVQVEDTRlikatedyQTELEVEVLVAPAAHQDVRPVGFDIPLGTILLEKGDVIDAAQIGILAGAGCLEIPVRL 375
Cdd:PRK10680 105 PEGCEAVVMQEQTE--------QTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 376 CPKVAILSTGNELQEPSEvTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGALAAAIATALSSADVLVCTGGVSM 455
Cdd:PRK10680 177 KVRVALFSTGDELQLPGQ-PLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 456 GERDLLKPVLQhDFGaSIHFGRVRMKPGKPSTFAtctyKGRTKYIFALPGNPVSAYVCCVLFVVRALRRCTRDTSEY--A 533
Cdd:PRK10680 256 GEADYTKTILE-ELG-EIAFWKLAIKPGKPFAFG----KLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNTASGlpP 329
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2311241737 534 RMRVRLAGDVTLDP-RPEYARAVLTFPTTDQLPVATVlGNQCS 575
Cdd:PRK10680 330 RQRVRTASRLKKTPgRLDFQRGILQRNADGELEVTTT-GHQGS 371
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
215-546 |
1.31e-42 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 161.13 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 215 KECVEVLPLEQCIGKVAAQDIRAKEPMPPFPASIKDGYACLSCDGAGVRKVRSALTAGdEYpQESPLVAGECARVNTGAP 294
Cdd:PRK14497 27 KPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGEFKVIDKIGIG-EF-KEIHIKECEAVEVDTGSM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 295 VPPGADCVVQVEDTRLIKATEdyqteleVEVLVAPAAHQDVRPVGFDIPLGTILLEKGDVIDAAQIGILAGAGCLEIPVR 374
Cdd:PRK14497 105 IPMGADAVIKVENTKVINGNF-------IKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVY 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 375 LCPKVAILSTGNELQEPSEvTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGALAAAIATALSSADVLVCTGGVS 454
Cdd:PRK14497 178 EKPKIYLIATGDELVEPGN-SLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 455 MGERDLLKPVLQhDFGASIHFGrVRMKPGKPSTFATCtyKGrtKYIFALPGNPVSAYVC---CVLFVVRALRRCTRDTSE 531
Cdd:PRK14497 257 AGEKDFVHQAIR-ELGNIIVHG-LKIKPGKPTILGIV--DG--KPVIGLPGNIVSTMVVlnmVILEYLKSLYPSRKEILG 330
|
330
....*....|....*
gi 2311241737 532 YARMRVRLAGDVTLD 546
Cdd:PRK14497 331 LGKIKARLALRVKAD 345
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
5-151 |
1.43e-42 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 162.67 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 5 VVIITVSDTCCKDHAKDQSGPALFQLV---KEKFPDADI-HTIILPDEKDLIEKKLKYFCDT-KIDLILTTGGTGLSSRD 79
Cdd:PLN02699 461 VAILTVSDTVSSGAGPDRSGPRAVSVVnssSEKLGGAKVvATAVVPDDVEKIKDVLQKWSDIdRMDLILTLGGTGFTPRD 540
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2311241737 80 VTPEATKAVIQREIPAISTAMTIESLKKTPMAMLSRAIAGIRDSTLIVNFPGSKKAVIECAEVVMPVLSHAL 151
Cdd:PLN02699 541 VTPEATKEVIQKETPGLLYVMMQESLKVTPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHAL 612
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
218-367 |
1.53e-41 |
|
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: 147.33 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 218 VEVLPLE--QCIGKVAAQDIRAKEPMPPFPASIKDGYACLSCDGAGVRKVRSALtAGDeyPQESPLVAGECARVNTGAPV 295
Cdd:pfam03453 6 EETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIA-AGE--PPGPLLPGGEAVRIMTGAPL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2311241737 296 PPGADCVVQVEDTRLIKatedyqtELEVEVLVAPAAHQDVRPVGFDIPLGTILLEKGDVIDAAQIGILAGAG 367
Cdd:pfam03453 83 PEGADAVVMVEDTEEGG-------GRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
4-155 |
2.35e-38 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 143.93 E-value: 2.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 4 AVVIITVSDTCCKDHAKDQSGPALfqlvKEKFPDADI---HTIILPDEKDLIEKKLKYFCDTKIDLILTTGGTGLSSRDV 80
Cdd:PRK03604 157 SAAVLVLSDSIAAGTKEDRSGKLI----VEGLEEAGFevsHYTIIPDEPAEIAAAVAAWIAEGYALIITTGGTGLGPRDV 232
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2311241737 81 TPEATKAVIQREIPAISTAMTIESLKKTPMAMLSRAIAGIRDSTLIVNFPGSKKAVIECAEVVMPVLSHALSLLA 155
Cdd:PRK03604 233 TPEALAPLLERRLPGIAEALRSWGQGRTPTAMLSRLVAGMIGNSLVVALPGSPGGASDALAVLLPALFHAFAMVK 307
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
218-591 |
3.87e-37 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 143.13 E-value: 3.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 218 VEVLPLEQCIGKVAAQDIRAKEPMPPFPASIKDGY--ACLSCDGAGVRKVRSALTAGDeYPQESPLVAGECARVNTGAPV 295
Cdd:PRK14690 42 IKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYgfAGAAPEGAQVLPLIEGRAAAG-VPFSGRVPEGMALRILTGAAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 296 PPGADCVVQVEDTRLIKATEDYQTELEVEvlvapaahQDVRPVGFDIPLGTILLEKGDVIDAAQIGILAGAGCLEIPVRL 375
Cdd:PRK14690 121 PEGVDTVVLEEDVAGDGHRIAFHGPLKMG--------ANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 376 CPKVAILSTGNELQEPSEvTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGALAAAIATALSSADVLVCTGGVSM 455
Cdd:PRK14690 193 PLRVAVLSTGDELVEPGA-LAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGASA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 456 GERDLLKPVLQHdfGASIHFGRVRMKPGKPstFATCTYKGrtKYIFALPGNPVSAYVCCVLFVVRALRRCTRDT-SEYAR 534
Cdd:PRK14690 272 GDEDHVSALLRE--AGAMQSWRIALKPGRP--LALGLWQG--VPVFGLPGNPVAALVCTLVFARPAMSLLAGEGwSEPQG 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2311241737 535 MRVRLAGDVTLDP-RPEYARAVLTFPTtdqlpvATVLGNQCSSRLLSVCGASVLLELP 591
Cdd:PRK14690 346 FTVPAAFEKRKKPgRREYLRARLRQGH------AEVFRSEGSGRISGLSWAEGLVELG 397
|
|
| mogA |
PRK09417 |
molybdenum cofactor biosynthesis protein MogA; Provisional |
7-143 |
9.01e-36 |
|
molybdenum cofactor biosynthesis protein MogA; Provisional
Pssm-ID: 181837 [Multi-domain] Cd Length: 193 Bit Score: 133.16 E-value: 9.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 7 IITVSDTCCKDHAKDQSGPALFQLVKEKFPDA-DIHTIILPDEKDLIEKKLKYFCDTK-IDLILTTGGTGLSSRDVTPEA 84
Cdd:PRK09417 8 LVSISDRASSGVYEDKGIPALEEWLASALTSPfEIETRLIPDEQDLIEQTLIELVDEMgCDLVLTTGGTGPARRDVTPEA 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2311241737 85 TKAVIQREIPAISTAMTIESLKKTPMAMLSRAIAGIRDSTLIVNFPGSKKAVIECAEVV 143
Cdd:PRK09417 88 TLAVADKEMPGFGEQMRQISLKFVPTAILSRQVAVIRGQSLIINLPGQPKSIKETLEGL 146
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
5-144 |
4.08e-28 |
|
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: 110.10 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 5 VVIITVSDTCCKDHAK-------DQSGPALFQLVKEKFPDADIHTIIlPDEKDLIEKKLKYFCDtKIDLILTTGGTGLSS 77
Cdd:TIGR00177 3 VAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIV-PDDPEEIREILRKAVD-EADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2311241737 78 RDVTPEATKAVIQREIPAISTAMtieslKKTPMAMLSR----AIAGIRDSTLIVNFPGSKKAVIECAEVVM 144
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGFGEFR-----MLSSLPVLSRpgkpATAGVRGGTLIFNLPGNPVSALVTFEVLI 146
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
7-143 |
3.09e-27 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 106.90 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 7 IITVSDTCCKDHAK-DQSGPALFQLVKEK-FPDADIHTIILPDEKDLIEKKLKYFCDtKIDLILTTGGTGLSSRDVTPEA 84
Cdd:smart00852 2 IISTGDELLSGGQIrDSNGPMLAALLRELgIEVVRVVVVGGPDDPEAIREALREALA-EADVVITTGGTGPGPDDLTPEA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2311241737 85 TKAVIQREIPAISTAMTIESlKKTPMAMLSRAIAGIRDSTLIVNFPGSKKAVIECAEVV 143
Cdd:smart00852 81 LAELGGRELLGHGVAMRPGG-PPGPLANLSGTAPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
380-513 |
3.09e-26 |
|
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: 104.21 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 380 AILSTGNELQEPSEvtlhpshIRDSNRLMLRSLLREHGYASVDSGIA--RDEPGALAAAIATALSSADVLVCTGGVSMGE 457
Cdd:smart00852 1 AIISTGDELLSGGQ-------IRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGP 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2311241737 458 RDLLKPVLQHDFGASIHFGRVRMKPGKPSTFATCTY-----KGRTKYIFALPGNPVSAYVC 513
Cdd:smart00852 74 DDLTPEALAELGGRELLGHGVAMRPGGPPGPLANLSgtapgVRGKKPVFGLPGNPVAALVM 134
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
380-524 |
9.91e-26 |
|
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: 103.10 E-value: 9.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 380 AILSTGNELqepsevtlHPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGALAAAIATALSSADVLVCTGGVSMGERD 459
Cdd:pfam00994 1 AIITTGDEL--------LPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDD 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2311241737 460 LLKPVLQHDF-----GASIHFGRVRMKPGKPSTFATCTYKGRT-KYIFALPGNPVSAYVCCVLFVVRALRR 524
Cdd:pfam00994 73 VTPEALAELGgrelpGFEELFRGVSLKPGKPVGTAPGAILSRAgKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
377-513 |
1.51e-25 |
|
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: 102.78 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 377 PKVAILSTGNELQEPSEvTLHPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGALAAAIATALSSADVLVCTGGVSMG 456
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQ-PLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2311241737 457 ERDLLKPVLQ-------HDFGASIH--FGRVRMKPGKPSTFAtcTYKGrtKYIFALPGNPVSAYVC 513
Cdd:TIGR00177 80 PRDVTPEALEelgekeiPGFGEFRMlsSLPVLSRPGKPATAG--VRGG--TLIFNLPGNPVSALVT 141
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
5-147 |
2.76e-25 |
|
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: 101.27 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 5 VVIITVSDTCCKDHAKDQSGPALFQLVKEKFPDAdIHTIILPDEKDLIEKKLKYFCDtKIDLILTTGGTGLSSRDVTPEA 84
Cdd:cd00758 2 VAIVTVSDELSQGQIEDTNGPALEALLEDLGCEV-IYAGVVPDDADSIRAALIEASR-EADLVLTTGGTGVGRRDVTPEA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2311241737 85 TKAVIQREIPAistamtieslKKTPMAMLSRAIAGIRDSTLIVNFPGSKKAVIECAEV-VMPVL 147
Cdd:cd00758 80 LAELGEREAHG----------KGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEAlVLPAL 133
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
7-149 |
1.75e-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: 93.85 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 7 IITVSDTCCKDHAKDQSGPALFQLVKEkFPDADIHTIILPDEKDLIEKKLKYFCDtKIDLILTTGGTGLSSRDVTPEATK 86
Cdd:pfam00994 2 IITTGDELLPGQIRDTNGPLLAALLRE-AGAEVIRYGIVPDDPEAIKEALRAAAE-EADVVITTGGTGPGPDDVTPEALA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 87 AVIQREIPAISTAMTIESLK------KTPMAMLSRAiagirdSTLIVNFPGSKKAVIECAE-VVMPVLSH 149
Cdd:pfam00994 80 ELGGRELPGFEELFRGVSLKpgkpvgTAPGAILSRA------GKTVFGLPGSPVAAKVMFElLLLPLLRH 143
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
378-522 |
5.16e-21 |
|
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: 89.32 E-value: 5.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311241737 378 KVAILSTGNELQepsevtlhPSHIRDSNRLMLRSLLREHGYASVDSGIARDEPGALAAAIATALSSADVLVCTGGVSMGE 457
Cdd:cd00758 1 RVAIVTVSDELS--------QGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGR 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2311241737 458 RDLLKPVLQHDFGASIHFGRVRMKPGKPSTFATctyKGRTKyIFALPGNPVSAYVCCVLFVVRAL 522
Cdd:cd00758 73 RDVTPEALAELGEREAHGKGVALAPGSRTAFGI---IGKVL-IINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
536-599 |
9.99e-07 |
|
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: 46.45 E-value: 9.99e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2311241737 536 RVRLAGDVTLDP-RPEYARAVLTFPttDQLPVATVLGNQCSSRLLSVCGASVLLELPAATDTVKV 599
Cdd:pfam03454 1 KARLARDLKSDPgRREFVRVRLHEE--DGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEA 63
|
|
| |
