|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
17-443 |
8.69e-168 |
|
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: 477.27 E-value: 8.69e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 17 SVSEHLDDILGSVRPLEPIELQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAVRVADIAGASeefPAVLTVIGDVAAGQ 96
Cdd:COG0303 3 SVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAN---PVTLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 97 GEQPTVGAGEAARIMTGAPLPPGAEAVVPVEWTDgglgegpVSGmrahsaapdgafGEVRVHRPAEARAHVRARGSDVQA 176
Cdd:COG0303 80 PPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTE-------REG------------DRVTIRKPVAPGENIRRAGEDIAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 177 GDRALAAGTVLGAPQIGLLAAIGRGTVKVRPRPRVVVMSTGSELIQPGEELAKGQIYDSNSFSLTAAAREAGAIAYRVGA 256
Cdd:COG0303 141 GDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 257 VADDAETLRSTIEDQLIRADLIVTTGGVSVGAYDVVKEALssvgdeDEAGSGIEFRKLAMQPGKPQGFGSIGpdHTPLLA 336
Cdd:COG0303 221 VPDDPEALRAALREALAEADLVITSGGVSVGDYDLVKEAL------EELGAEVLFHKVAMKPGKPLAFGRLG--GKPVFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 337 LPGNPVSSYVSFEIFVRPAVRALMGLPDVHRPTARAVLSADkaLTSPKGKRQFLRGQYDAEAGS--VRPVGGAGSHLVAA 414
Cdd:COG0303 293 LPGNPVSALVTFELFVRPALRKLAGLPPPPPPRVRARLAED--LPKKPGRTEFLRVRLERDDGElvVEPLGGQGSGLLSS 370
|
410 420
....*....|....*....|....*....
gi 2240240455 415 LAHANALIVVPEDTASVEPGADVEVVLLG 443
Cdd:COG0303 371 LAEADGLIVLPEGVEGVEAGEEVEVLLLD 399
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
25-442 |
6.24e-155 |
|
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: 444.24 E-value: 6.24e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 25 ILGSVRPLEPIELQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAVRVADIAGASEEFPavltVIGDVAAGQGEQPTVGA 104
Cdd:cd00887 8 LLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLR----VVGEIPAGEPPDGPLGP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 105 GEAARIMTGAPLPPGAEAVVPVEWTDGglgEGpvsgmrahsaapdgafGEVRVHRPAEARAHVRARGSDVQAGDRALAAG 184
Cdd:cd00887 84 GEAVRIMTGAPLPEGADAVVMVEDTEE---EG----------------GRVTITKPVKPGQNIRRAGEDIKAGDVLLPAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 185 TVLGAPQIGLLAAIGRGTVKVRPRPRVVVMSTGSELIQPGEELAKGQIYDSNSFSLTAAAREAGAIAYRVGAVADDAETL 264
Cdd:cd00887 145 TRLTPADIGLLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 265 RSTIEDQLIRADLIVTTGGVSVGAYDVVKEALSSVGDEdeagsgIEFRKLAMQPGKPQGFGSIGpdHTPLLALPGNPVSS 344
Cdd:cd00887 225 REALEEALEEADVVITSGGVSVGDYDFVKEVLEELGGE------VLFHGVAMKPGKPLAFGRLG--GKPVFGLPGNPVSA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 345 YVSFEIFVRPAVRALMGLPDVHRPTARAVLSADkaLTSPKGKRQFLRGQYDAEAG--SVRPVGGAGSHLVAALAHANALI 422
Cdd:cd00887 297 LVTFELFVRPALRKLQGAPEPEPPRVKARLAED--LKSKPGRREFLRVRLERDEGglVVAPPGGQGSGLLSSLARADGLI 374
|
410 420
....*....|....*....|
gi 2240240455 423 VVPEDTASVEPGADVEVVLL 442
Cdd:cd00887 375 VIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
30-443 |
1.10e-103 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 321.39 E-value: 1.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 30 RPLEPIELQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAVRVADIAGASEEFPAVLTVIGDVAAGQGEQPTVGAGEAAR 109
Cdd:PRK14498 26 LPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLKLGGEVHAGEAPDVEVEPGEAVE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 110 IMTGAPLPPGAEAVVPVEWTDgglgegpvsgmrahsaaPDGAfGEVRVHRPAEARAHVRARGSDVQAGDRALAAGTVLGA 189
Cdd:PRK14498 106 IATGAPIPRGADAVVMVEDTE-----------------EVDD-DTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 190 PQIGLLAAIGRGTVKVRPRPRVVVMSTGSELIQPGEELAKGQIYDSNSFSLTAAAREAGAIAYRVGAVADDAETLRSTIE 269
Cdd:PRK14498 168 RDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 270 DQLIRADLIVTTGGVSVGAYDVVKEALSSVGDedeagsgIEFRKLAMQPGKPQGFGSIgpDHTPLLALPGNPVSSYVSFE 349
Cdd:PRK14498 248 KALKECDLVLLSGGTSAGAGDVTYRVIEELGE-------VLVHGVAIKPGKPTILGVI--GGKPVVGLPGYPVSALTIFE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 350 IFVRPAVRALMGLPDVHRPTARAVLSadKALTSPKGKRQFLR---GQyDAEAGSVRPVG-GAGShlVAALAHANALIVVP 425
Cdd:PRK14498 319 EFVAPLLRKLAGLPPPERATVKARLA--RRVRSELGREEFVPvslGR-VGDGYVAYPLSrGSGA--ITSLVRADGFIEIP 393
|
410
....*....|....*...
gi 2240240455 426 EDTASVEPGADVEVVLLG 443
Cdd:PRK14498 394 ANTEGLEAGEEVEVELFG 411
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
33-199 |
3.28e-48 |
|
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of these contains the conserved DGXA motif. This region is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this region is uncertain.
Pssm-ID: 460923 [Multi-domain] Cd Length: 147 Bit Score: 161.97 E-value: 3.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 33 EPIELQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAVRVADIAGASEEFPavltvigdVAAGQGEQPTVGAGEAARIMT 112
Cdd:pfam03453 7 ETVPLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLPGGEAVRIMT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 113 GAPLPPGAEAVVPVEWTDGGLGEgpvsgmrahsaapdgafgEVRVHRPAEARAHVRARGSDVQAGDRALAAGTVLGAPQI 192
Cdd:pfam03453 79 GAPLPEGADAVVMVEDTEEGGGR------------------TVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEI 140
|
....*..
gi 2240240455 193 GLLAAIG 199
Cdd:pfam03453 141 GLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
209-354 |
2.17e-37 |
|
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: 133.60 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 209 PRVVVMSTGSELIQPGEELAKGQIYDSNSFSLTAAAREAGAIAYRVGAVADDAETLRSTIEDQLIRADLIVTTGGVSVGA 288
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 289 YDVVKEALSSVGDEDEAGSGIEFRK----LAMQPGKPQGFGSIGpdHTPLLALPGNPVSSYVSFEIFVRP 354
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGFGEFRMLsslpVLSRPGKPATAGVRG--GTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
213-349 |
8.89e-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: 104.59 E-value: 8.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 213 VMSTGSELIQPGeelakgQIYDSNSFSLTA--AAREAGAIAYRVGAVADDAETLRSTIEDQLIRADLIVTTGGVSVGAYD 290
Cdd:smart00852 2 IISTGDELLSGG------QIRDSNGPMLAAllRELGIEVVRVVVVGGPDDPEAIREALREALAEADVVITTGGTGPGPDD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2240240455 291 VVKEALSSVGDEDeagsgIEFRKLAMQPGKPQG-----FGSIG--PDHTPLLALPGNPVSSYVSFE 349
Cdd:smart00852 76 LTPEALAELGGRE-----LLGHGVAMRPGGPPGplanlSGTAPgvRGKKPVFGLPGNPVAALVMFE 136
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
17-443 |
8.69e-168 |
|
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: 477.27 E-value: 8.69e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 17 SVSEHLDDILGSVRPLEPIELQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAVRVADIAGASeefPAVLTVIGDVAAGQ 96
Cdd:COG0303 3 SVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAN---PVTLRVVGEIAAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 97 GEQPTVGAGEAARIMTGAPLPPGAEAVVPVEWTDgglgegpVSGmrahsaapdgafGEVRVHRPAEARAHVRARGSDVQA 176
Cdd:COG0303 80 PPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTE-------REG------------DRVTIRKPVAPGENIRRAGEDIAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 177 GDRALAAGTVLGAPQIGLLAAIGRGTVKVRPRPRVVVMSTGSELIQPGEELAKGQIYDSNSFSLTAAAREAGAIAYRVGA 256
Cdd:COG0303 141 GDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 257 VADDAETLRSTIEDQLIRADLIVTTGGVSVGAYDVVKEALssvgdeDEAGSGIEFRKLAMQPGKPQGFGSIGpdHTPLLA 336
Cdd:COG0303 221 VPDDPEALRAALREALAEADLVITSGGVSVGDYDLVKEAL------EELGAEVLFHKVAMKPGKPLAFGRLG--GKPVFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 337 LPGNPVSSYVSFEIFVRPAVRALMGLPDVHRPTARAVLSADkaLTSPKGKRQFLRGQYDAEAGS--VRPVGGAGSHLVAA 414
Cdd:COG0303 293 LPGNPVSALVTFELFVRPALRKLAGLPPPPPPRVRARLAED--LPKKPGRTEFLRVRLERDDGElvVEPLGGQGSGLLSS 370
|
410 420
....*....|....*....|....*....
gi 2240240455 415 LAHANALIVVPEDTASVEPGADVEVVLLG 443
Cdd:COG0303 371 LAEADGLIVLPEGVEGVEAGEEVEVLLLD 399
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
25-442 |
6.24e-155 |
|
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: 444.24 E-value: 6.24e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 25 ILGSVRPLEPIELQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAVRVADIAGASEEFPavltVIGDVAAGQGEQPTVGA 104
Cdd:cd00887 8 LLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLR----VVGEIPAGEPPDGPLGP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 105 GEAARIMTGAPLPPGAEAVVPVEWTDGglgEGpvsgmrahsaapdgafGEVRVHRPAEARAHVRARGSDVQAGDRALAAG 184
Cdd:cd00887 84 GEAVRIMTGAPLPEGADAVVMVEDTEE---EG----------------GRVTITKPVKPGQNIRRAGEDIKAGDVLLPAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 185 TVLGAPQIGLLAAIGRGTVKVRPRPRVVVMSTGSELIQPGEELAKGQIYDSNSFSLTAAAREAGAIAYRVGAVADDAETL 264
Cdd:cd00887 145 TRLTPADIGLLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 265 RSTIEDQLIRADLIVTTGGVSVGAYDVVKEALSSVGDEdeagsgIEFRKLAMQPGKPQGFGSIGpdHTPLLALPGNPVSS 344
Cdd:cd00887 225 REALEEALEEADVVITSGGVSVGDYDFVKEVLEELGGE------VLFHGVAMKPGKPLAFGRLG--GKPVFGLPGNPVSA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 345 YVSFEIFVRPAVRALMGLPDVHRPTARAVLSADkaLTSPKGKRQFLRGQYDAEAG--SVRPVGGAGSHLVAALAHANALI 422
Cdd:cd00887 297 LVTFELFVRPALRKLQGAPEPEPPRVKARLAED--LKSKPGRREFLRVRLERDEGglVVAPPGGQGSGLLSSLARADGLI 374
|
410 420
....*....|....*....|
gi 2240240455 423 VVPEDTASVEPGADVEVVLL 442
Cdd:cd00887 375 VIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
30-443 |
1.10e-103 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 321.39 E-value: 1.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 30 RPLEPIELQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAVRVADIAGASEEFPAVLTVIGDVAAGQGEQPTVGAGEAAR 109
Cdd:PRK14498 26 LPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLKLGGEVHAGEAPDVEVEPGEAVE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 110 IMTGAPLPPGAEAVVPVEWTDgglgegpvsgmrahsaaPDGAfGEVRVHRPAEARAHVRARGSDVQAGDRALAAGTVLGA 189
Cdd:PRK14498 106 IATGAPIPRGADAVVMVEDTE-----------------EVDD-DTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 190 PQIGLLAAIGRGTVKVRPRPRVVVMSTGSELIQPGEELAKGQIYDSNSFSLTAAAREAGAIAYRVGAVADDAETLRSTIE 269
Cdd:PRK14498 168 RDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 270 DQLIRADLIVTTGGVSVGAYDVVKEALSSVGDedeagsgIEFRKLAMQPGKPQGFGSIgpDHTPLLALPGNPVSSYVSFE 349
Cdd:PRK14498 248 KALKECDLVLLSGGTSAGAGDVTYRVIEELGE-------VLVHGVAIKPGKPTILGVI--GGKPVVGLPGYPVSALTIFE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 350 IFVRPAVRALMGLPDVHRPTARAVLSadKALTSPKGKRQFLR---GQyDAEAGSVRPVG-GAGShlVAALAHANALIVVP 425
Cdd:PRK14498 319 EFVAPLLRKLAGLPPPERATVKARLA--RRVRSELGREEFVPvslGR-VGDGYVAYPLSrGSGA--ITSLVRADGFIEIP 393
|
410
....*....|....*...
gi 2240240455 426 EDTASVEPGADVEVVLLG 443
Cdd:PRK14498 394 ANTEGLEAGEEVEVELFG 411
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
17-437 |
4.69e-95 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 298.07 E-value: 4.69e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 17 SVSEHLDDILGSVRPLEPIE-LQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAVRVADIAgaseefPAVLTVIGDVAAG 95
Cdd:PRK14491 200 SVSQGLDKILSLVTPVTETEdVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLE------PESYTLVGEVLAG 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 96 QGEQPTVGAGEAARIMTGAPLPPGAEAVVPVEwtdgglgegpvsgmrahSAAPDGafGEVRVHRPAEARAHVRARGSDVQ 175
Cdd:PRK14491 274 HQYDGTLQAGEAVRIMTGAPVPAGADTVVMRE-----------------LATQDG--DKVSFDGGIKAGQNVRLAGEDLA 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 176 AGDRALAAGTVLGAPQIGLLAAIGRGTVKVRPRPRVVVMSTGSELIQPGEELAKGQIYDSNSFSLTAAAREAGAIAYRVG 255
Cdd:PRK14491 335 QGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLG 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 256 AVADDAETLRSTIEDQLIRADLIVTTGGVSVGAYDVVKEALSSVGDedeagsgIEFRKLAMQPGKPQGFGSIGpdHTPLL 335
Cdd:PRK14491 415 IIEDSEAALEATLEQAAAQADVVISSGGVSVGDADYIKTALAKLGQ-------IDFWRINMRPGRPLAFGQIG--DSPFF 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 336 ALPGNPVSSYVSFEIFVRPAVRALMGLPDVHRPTARAVlsADKALTSPKGKRQFLRGQYD-AEAG--SVRPVGGAGSHLV 412
Cdd:PRK14491 486 GLPGNPVAVMVSFLQFVEPALRKLAGEQNWQPLLFPAI--ADETLRSRQGRTEFSRGIYHlGADGrlHVRTTGKQGSGIL 563
|
410 420
....*....|....*....|....*
gi 2240240455 413 AALAHANALIVVPEDTASVEPGADV 437
Cdd:PRK14491 564 SSMSEANCLIEIGPAAETVNAGETV 588
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
17-439 |
8.95e-80 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 252.71 E-value: 8.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 17 SVSEHLDDILGSVRPLEPIE-LQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAVRVADIAGAseefpAVLTVIGDVAAG 95
Cdd:PRK10680 9 SLETALTEMLSRVTPLTATEtLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASG-----QPLPVAGKAFAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 96 ---QGEQPtvgAGEAARIMTGAPLPPGAEAVVpvewtdgglgegpvsgMRAHSAAPDGAfgeVRVHRPAEARAHVRARGS 172
Cdd:PRK10680 84 qpfHGEWP---AGTCIRIMTGAPVPEGCEAVV----------------MQEQTEQTDDG---VRFTAEVRSGQNIRRRGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 173 DVQAGDRALAAGTVLGAPQIGLLAAIGRGTVKVRPRPRVVVMSTGSELIQPGEELAKGQIYDSNSFSLTAAAREAGAIAY 252
Cdd:PRK10680 142 DISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 253 RVGAVADDAETLRSTIEDQLIRADLIVTTGGVSVGAYDVVKEALSSVGDedeagsgIEFRKLAMQPGKPQGFGSIgpDHT 332
Cdd:PRK10680 222 NLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEADYTKTILEELGE-------IAFWKLAIKPGKPFAFGKL--SNS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 333 PLLALPGNPVSSYVSFEIFVRPAVRALMGLPDVHRPTARAVLSADKALTSPkGKRQFLRG--QYDAEAG-SVRPVGGAGS 409
Cdd:PRK10680 293 WFCGLPGNPVSAALTFYQLVQPLLAKLSGNTASGLPPRQRVRTASRLKKTP-GRLDFQRGilQRNADGElEVTTTGHQGS 371
|
410 420 430
....*....|....*....|....*....|
gi 2240240455 410 HLVAALAHANALIVVPEDTASVEPGADVEV 439
Cdd:PRK10680 372 HIFSSFSLGNCFIVLERERGNVEVGEWVEV 401
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
17-442 |
6.09e-61 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 209.67 E-value: 6.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 17 SVSEHLDDILGSVRPLEPIELQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAVRVADIAGaseEFPavltVIGDVAAGQ 96
Cdd:PLN02699 9 SVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPG---EYP----VITESRAGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 97 -GEQPTVGAGEAARIMTGAPLPPGAEAVVPVEwtDGGLGEGPVSGMRahsaapdgafgEVRVHRPAEARAHVRARGSDVQ 175
Cdd:PLN02699 82 dGLGVTLTPGTVAYVTTGGPIPDGADAVVQVE--DTEVVEDPLDGSK-----------RVRILSQASKGQDIRPVGCDIE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 176 AGDRALAAGTVLGAPQIGLLAAIGRGTVKVRPRPRVVVMSTGSELIQPGEE-LAKGQIYDSNSFSLTAAAREAGAIAYRV 254
Cdd:PLN02699 149 KDAKVLKAGERLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 255 GAVADDAETLRSTIEDQLIR-ADLIVTTGGVSVGAYDVVKEALSSVGDedeagsgIEFRKLAMQPGKPQGFGSIGPDHTP 333
Cdd:PLN02699 229 GIARDDEEELERILDEAISSgVDILLTSGGVSMGDRDFVKPLLEKRGT-------VYFSKVLMKPGKPLTFAEIDAKSAP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 334 -----LLA--LPGNPVSSYVSFEIFVRPAVRALMGLPDVHRPTARAVLSadKALTSPKGKRQFLRG--QYDAEAGSVRP- 403
Cdd:PLN02699 302 snskkMLAfgLPGNPVSCLVCFNLFVVPAIRYLAGWSNPHLLRVQARLR--EPIKLDPVRPEFHRAiiRWKLNDGSGNPg 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2240240455 404 -----VGGAGSHLVAALAHANALIVVPEDTASVEPGADVEVVLL 442
Cdd:PLN02699 380 fvaesTGHQMSSRLLSMKSANALLELPATGNVLSAGTSVSAIII 423
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
11-362 |
1.25e-54 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 190.41 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 11 GQEHVWSVSEHLDDILGSVRPL-EPIELQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAVRvadiagaSEEFPAVLTVI 89
Cdd:PRK14497 6 GDESLYSIDEAIKVFLSSLNFKpKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALK-------SSCTPGEFKVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 90 GDVAAGQGEQPTVGAGEAARIMTGAPLPPGAEAVVPVEwtDGGLGEGPvsgmrahsaapdgafgEVRVHRPAEARAHVRA 169
Cdd:PRK14497 79 DKIGIGEFKEIHIKECEAVEVDTGSMIPMGADAVIKVE--NTKVINGN----------------FIKIDKKINFGQNIGW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 170 RGSDVQAGDRALAAGTVLGAPQIGLLAAIGRGTVKVRPRPRVVVMSTGSELIQPGEELAKGQIYDSNSFSLTAAAREAGA 249
Cdd:PRK14497 141 IGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 250 IAYRVGAVADDAETLRSTIEDQLIRADLIVTTGGVSVGAYDVVKEALSSVGDedeagsgIEFRKLAMQPGKPQGFGSIgp 329
Cdd:PRK14497 221 KIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKDFVHQAIRELGN-------IIVHGLKIKPGKPTILGIV-- 291
|
330 340 350
....*....|....*....|....*....|...
gi 2240240455 330 DHTPLLALPGNPVSSYVSFEIFVRPAVRALMGL 362
Cdd:PRK14497 292 DGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPS 324
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
22-443 |
7.48e-50 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 174.72 E-value: 7.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 22 LDDILGSVRPLEpiELQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAvrvadIAGASEEFPAVLTVI-GDVAAGQGEQP 100
Cdd:PRK14690 32 LRARLGPVTDIK--ELDLSDALGHVLAHDAVALRSNPPQANSAVDGYG-----FAGAAPEGAQVLPLIeGRAAAGVPFSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 101 TVGAGEAARIMTGAPLPPGAEAVVPVEWTDGGLGEgpvsgmrahsaapdgafgeVRVHRPAEARAHVRARGSDVQAGDRA 180
Cdd:PRK14690 105 RVPEGMALRILTGAALPEGVDTVVLEEDVAGDGHR-------------------IAFHGPLKMGANTRKAGEDVIAGDVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 181 LAAGTVLGAPQIGLLAAIGRGTVKVRPRPRVVVMSTGSELIQPGEELAKGQIYDSNSFSLTAAAREAGAIAYRVGAVADD 260
Cdd:PRK14690 166 LPAGRRLTPADLALLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 261 AETLRSTIEDQLIRADLIVTTGGVSVGAYDVVKEALSsvgdedEAGSGIEFRkLAMQPGKPQGFGSIgpDHTPLLALPGN 340
Cdd:PRK14690 246 RAALAARLDRAAAEADVILTSGGASAGDEDHVSALLR------EAGAMQSWR-IALKPGRPLALGLW--QGVPVFGLPGN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 341 PVSSYVSFEIFVRPAVRALMGlPDVHRPTARAVLSADKALTSPkGKRQFLRGQydAEAGSVRPVGGAGSHLVAALAHANA 420
Cdd:PRK14690 317 PVAALVCTLVFARPAMSLLAG-EGWSEPQGFTVPAAFEKRKKP-GRREYLRAR--LRQGHAEVFRSEGSGRISGLSWAEG 392
|
410 420
....*....|....*....|...
gi 2240240455 421 LIVVPEDTASVEPGADVEVVLLG 443
Cdd:PRK14690 393 LVELGDGARRIAPGDPVRFIPYG 415
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
33-199 |
3.28e-48 |
|
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of these contains the conserved DGXA motif. This region is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this region is uncertain.
Pssm-ID: 460923 [Multi-domain] Cd Length: 147 Bit Score: 161.97 E-value: 3.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 33 EPIELQLLDAQGCVLVEDVTVPVSLPPFDNSSMDGYAVRVADIAGASEEFPavltvigdVAAGQGEQPTVGAGEAARIMT 112
Cdd:pfam03453 7 ETVPLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLPGGEAVRIMT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 113 GAPLPPGAEAVVPVEWTDGGLGEgpvsgmrahsaapdgafgEVRVHRPAEARAHVRARGSDVQAGDRALAAGTVLGAPQI 192
Cdd:pfam03453 79 GAPLPEGADAVVMVEDTEEGGGR------------------TVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEI 140
|
....*..
gi 2240240455 193 GLLAAIG 199
Cdd:pfam03453 141 GLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
209-354 |
2.17e-37 |
|
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: 133.60 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 209 PRVVVMSTGSELIQPGEELAKGQIYDSNSFSLTAAAREAGAIAYRVGAVADDAETLRSTIEDQLIRADLIVTTGGVSVGA 288
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 289 YDVVKEALSSVGDEDEAGSGIEFRK----LAMQPGKPQGFGSIGpdHTPLLALPGNPVSSYVSFEIFVRP 354
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGFGEFRMLsslpVLSRPGKPATAGVRG--GTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
224-358 |
1.95e-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 trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 120.05 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 224 GEELAKGQIYDSNSFSLTAAAREAGAIAYRVGAVADDAETLRSTIEDQLIRADLIVTTGGVSVGAYDVVKEALSSVGDED 303
Cdd:pfam00994 6 GDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAELGGRE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2240240455 304 EAGSGIEFRKLAMQPGKPQGFG---SIGPDHTPLLALPGNPVSSYVSFEIFVRPAVRA 358
Cdd:pfam00994 86 LPGFEELFRGVSLKPGKPVGTApgaILSRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
213-349 |
8.89e-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: 104.59 E-value: 8.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 213 VMSTGSELIQPGeelakgQIYDSNSFSLTA--AAREAGAIAYRVGAVADDAETLRSTIEDQLIRADLIVTTGGVSVGAYD 290
Cdd:smart00852 2 IISTGDELLSGG------QIRDSNGPMLAAllRELGIEVVRVVVVGGPDDPEAIREALREALAEADVVITTGGTGPGPDD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2240240455 291 VVKEALSSVGDEDeagsgIEFRKLAMQPGKPQG-----FGSIG--PDHTPLLALPGNPVSSYVSFE 349
Cdd:smart00852 76 LTPEALAELGGRE-----LLGHGVAMRPGGPPGplanlSGTAPgvRGKKPVFGLPGNPVAALVMFE 136
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
210-356 |
4.55e-24 |
|
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: 97.03 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 210 RVVVMSTGSELIQpgeelakGQIYDSNSFSLTAAAREAGAIAYRVGAVADDAETLRSTIEDQLIRADLIVTTGGVSVGAY 289
Cdd:cd00758 1 RVAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2240240455 290 DVVKEALSSVGDEDEAGSGIefrklAMQPGKPQGFGSIGpdHTPLLALPGNPVSSYVSFEIFVRPAV 356
Cdd:cd00758 74 DVTPEALAELGEREAHGKGV-----ALAPGSRTAFGIIG--KVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
371-442 |
8.83e-15 |
|
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: 68.79 E-value: 8.83e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2240240455 371 RAVLSADkaLTSPKGKRQFLRGQYDAEAG--SVRPVGGAGSHLVAALAHANALIVVPEDTASVEPGADVEVVLL 442
Cdd:pfam03454 1 KARLARD--LKSDPGRREFVRVRLHEEDGryYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
219-283 |
3.53e-06 |
|
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.
Pssm-ID: 238450 [Multi-domain] Cd Length: 170 Bit Score: 47.09 E-value: 3.53e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2240240455 219 ELIQPGEELAKGQIYDSNSFSLTAAAREAGAIAYRVGAVADDAETLRSTIEDQLIRADLIVTTGG 283
Cdd:cd00885 3 EIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
252-341 |
3.32e-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: 41.26 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240240455 252 YRVgaVADDAETLRSTIEDQLIR--ADLIVTTGGVSVGAYDVVKEALSSVGDEDEAGSGIEFRKLAMQpgkpqgfgSIGP 329
Cdd:COG0521 48 RRI--VPDDKDAIRAALRELIDDegVDLVLTTGGTGLSPRDVTPEATRPLLDKELPGFGELFRALSLE--------EIGP 117
|
90 100
....*....|....*....|....
gi 2240240455 330 ------------DHTPLLALPGNP 341
Cdd:COG0521 118 sailsravagirGGTLIFNLPGSP 141
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
257-317 |
4.61e-03 |
|
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: 37.46 E-value: 4.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2240240455 257 VADDAETLRSTIED--QLIRADLIVTTGGVSVGAYDVVKEALSSVGDEDEAGSGIEFRKLAMQ 317
Cdd:cd00886 42 VPDDKDEIREALIEwaDEDGVDLILTTGGTGLAPRDVTPEATRPLLDKELPGFGEAFRALSLE 104
|
|
|