|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
6-407 |
1.89e-155 |
|
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440072 [Multi-domain] Cd Length: 401 Bit Score: 444.15 E-value: 1.89e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 6 SVRETFALIETHFSnyPMEKETVPLDQCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDTFGVSesmPAQLRLVGEVKM 85
Cdd:COG0303 3 SVEEALALILAAVR--PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAN---PVTLRVVGEIAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 86 GEKPDFVIRSGESAYVPTGGELPQGADGVVMMEYSEDFGDGdIFLNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRPQDL 165
Cdd:COG0303 78 GSPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDR-VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 166 AMLAGLGLAVVPVQKKLKIGIISTGDEVVGVEETPIGAQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKAV 245
Cdd:COG0303 157 GLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 246 EENDVVAISGGSSVGTKDVTVKVIDGLGApGLLLHGIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIFGKHLIRTM 325
Cdd:COG0303 237 AEADLVITSGGVSVGDYDLVKEALEELGA-EVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 326 EGQKEGFAPFVEAVLGVNYPSNHGREEYLSVSLQKNGEETLAMPV-FGKSGMISLMTKADGYVHIKRESEGLNKGQTVQV 404
Cdd:COG0303 316 AGLPPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLgGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEV 395
|
...
gi 2006062122 405 TLF 407
Cdd:COG0303 396 LLL 398
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
22-407 |
8.06e-153 |
|
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: 437.31 E-value: 8.06e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 22 PMEKETVPLDQCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDTFGVSesmpAQLRLVGEVKMGEKPDFVIRSGESAYV 101
Cdd:cd00887 14 PLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGAS----VTLRVVGEIPAGEPPDGPLGPGEAVRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 102 PTGGELPQGADGVVMMEYSEDFGDGdIFLNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRPQDLAMLAGLGLAVVPVQKK 181
Cdd:cd00887 90 MTGAPLPEGADAVVMVEDTEEEGGR-VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 182 LKIGIISTGDEVVGVEETPIGAQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKAVEENDVVAISGGSSVGT 261
Cdd:cd00887 169 PRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 262 KDVTVKVIDGLGApGLLLHGIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIFGKHLIRTMEGQKEGFAPFVEAVLG 341
Cdd:cd00887 249 YDFVKEVLEELGG-EVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRVKARLA 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006062122 342 VNYPSNHGREEYLSVSL-QKNGEETLAMPVFGKSGMISLMTKADGYVHIKRESEGLNKGQTVQVTLF 407
Cdd:cd00887 328 EDLKSKPGRREFLRVRLeRDEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
3-407 |
3.55e-148 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 434.26 E-value: 3.55e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 3 DVKSVRETFALIETHFSNYPMEKETVPLDQCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDTFGVSESMPAQLRLVGE 82
Cdd:PRK14498 8 TLVSLEEAREILESLLSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLKLGGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 83 VKMGEKPDFVIRSGESAYVPTGGELPQGADGVVMMEYSEDFGDGDIFLNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRP 162
Cdd:PRK14498 88 VHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 163 QDLAMLAGLGLAVVPVQKKLKIGIISTGDEVVGVEETPIGAQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVR 242
Cdd:PRK14498 168 RDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 243 KAVEENDVVAISGGSSVGTKDVTVKVIDGLGApgLLLHGIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIFGKHLI 322
Cdd:PRK14498 248 KALKECDLVLLSGGTSAGAGDVTYRVIEELGE--VLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 323 RTMEGQKEGFAPFVEAVLGVNYPSNHGREEYLSVSLQKNGEETLAMPVFGKSGMISLMTKADGYVHIKRESEGLNKGQTV 402
Cdd:PRK14498 326 RKLAGLPPPERATVKARLARRVRSELGREEFVPVSLGRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTEGLEAGEEV 405
|
....*
gi 2006062122 403 QVTLF 407
Cdd:PRK14498 406 EVELF 410
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
24-172 |
5.61e-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: 160.42 E-value: 5.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 24 EKETVPLD--QCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDTFGVSESMPaqlrlvgeVKMGEKPDFVIRSGESAYV 101
Cdd:pfam03453 5 TEETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLPGGEAVRI 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006062122 102 PTGGELPQGADGVVMMEYSEDFGDGDIFLNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRPQDLAMLAGLG 172
Cdd:pfam03453 77 MTGAPLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
182-317 |
5.76e-31 |
|
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: 115.49 E-value: 5.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 182 LKIGIISTGDEVVGVEETPIGAQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKAVEENDVVAISGGSSVGT 261
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006062122 262 KDVTVKVIDGLGA---PG------LLLHGIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIF 317
Cdd:TIGR00177 81 RDVTPEALEELGEkeiPGfgefrmLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVL 145
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
185-315 |
2.77e-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: 108.06 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 185 GIISTGDEVVgveetpIGAQVRDMNSYGVLALSQGLGLEAALYGIV--KDDFDRIDATVRKAVEENDVVAISGGSSVGTK 262
Cdd:smart00852 1 AIISTGDELL------SGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006062122 263 DVTVKVIDGLGAPGLLLHGIAVKPGKPTIL---------GKVGEKAVMGLPGHPASAFVIFQ 315
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMFE 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
6-407 |
1.89e-155 |
|
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440072 [Multi-domain] Cd Length: 401 Bit Score: 444.15 E-value: 1.89e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 6 SVRETFALIETHFSnyPMEKETVPLDQCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDTFGVSesmPAQLRLVGEVKM 85
Cdd:COG0303 3 SVEEALALILAAVR--PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAN---PVTLRVVGEIAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 86 GEKPDFVIRSGESAYVPTGGELPQGADGVVMMEYSEDFGDGdIFLNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRPQDL 165
Cdd:COG0303 78 GSPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDR-VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 166 AMLAGLGLAVVPVQKKLKIGIISTGDEVVGVEETPIGAQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKAV 245
Cdd:COG0303 157 GLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 246 EENDVVAISGGSSVGTKDVTVKVIDGLGApGLLLHGIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIFGKHLIRTM 325
Cdd:COG0303 237 AEADLVITSGGVSVGDYDLVKEALEELGA-EVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 326 EGQKEGFAPFVEAVLGVNYPSNHGREEYLSVSLQKNGEETLAMPV-FGKSGMISLMTKADGYVHIKRESEGLNKGQTVQV 404
Cdd:COG0303 316 AGLPPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLgGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEV 395
|
...
gi 2006062122 405 TLF 407
Cdd:COG0303 396 LLL 398
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
22-407 |
8.06e-153 |
|
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: 437.31 E-value: 8.06e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 22 PMEKETVPLDQCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDTFGVSesmpAQLRLVGEVKMGEKPDFVIRSGESAYV 101
Cdd:cd00887 14 PLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGAS----VTLRVVGEIPAGEPPDGPLGPGEAVRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 102 PTGGELPQGADGVVMMEYSEDFGDGdIFLNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRPQDLAMLAGLGLAVVPVQKK 181
Cdd:cd00887 90 MTGAPLPEGADAVVMVEDTEEEGGR-VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 182 LKIGIISTGDEVVGVEETPIGAQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKAVEENDVVAISGGSSVGT 261
Cdd:cd00887 169 PRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 262 KDVTVKVIDGLGApGLLLHGIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIFGKHLIRTMEGQKEGFAPFVEAVLG 341
Cdd:cd00887 249 YDFVKEVLEELGG-EVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRVKARLA 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006062122 342 VNYPSNHGREEYLSVSL-QKNGEETLAMPVFGKSGMISLMTKADGYVHIKRESEGLNKGQTVQVTLF 407
Cdd:cd00887 328 EDLKSKPGRREFLRVRLeRDEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
3-407 |
3.55e-148 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 434.26 E-value: 3.55e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 3 DVKSVRETFALIETHFSNYPMEKETVPLDQCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDTFGVSESMPAQLRLVGE 82
Cdd:PRK14498 8 TLVSLEEAREILESLLSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLKLGGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 83 VKMGEKPDFVIRSGESAYVPTGGELPQGADGVVMMEYSEDFGDGDIFLNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRP 162
Cdd:PRK14498 88 VHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 163 QDLAMLAGLGLAVVPVQKKLKIGIISTGDEVVGVEETPIGAQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVR 242
Cdd:PRK14498 168 RDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 243 KAVEENDVVAISGGSSVGTKDVTVKVIDGLGApgLLLHGIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIFGKHLI 322
Cdd:PRK14498 248 KALKECDLVLLSGGTSAGAGDVTYRVIEELGE--VLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 323 RTMEGQKEGFAPFVEAVLGVNYPSNHGREEYLSVSLQKNGEETLAMPVFGKSGMISLMTKADGYVHIKRESEGLNKGQTV 402
Cdd:PRK14498 326 RKLAGLPPPERATVKARLARRVRSELGREEFVPVSLGRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTEGLEAGEEV 405
|
....*
gi 2006062122 403 QVTLF 407
Cdd:PRK14498 406 EVELF 410
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
6-402 |
4.85e-71 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 234.12 E-value: 4.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 6 SVRETFALIETHFSnyPM-EKETVPLDQCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDTfgvsesMPAQLRLVGEVK 84
Cdd:PRK14491 200 SVSQGLDKILSLVT--PVtETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDL------EPESYTLVGEVL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 85 MGEKPDFVIRSGESAYVPTGGELPQGADGVVMMEYSEDFGDGDIFlNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRPQD 164
Cdd:PRK14491 272 AGHQYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSF-DGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 165 LAMLAGLGLAVVPVQKKLKIGIISTGDEVVGVEETPIGAQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKA 244
Cdd:PRK14491 351 QGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 245 VEENDVVAISGGSSVGTKDVTVKVIDGLGAPGLLLhgIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIFGKHLIRT 324
Cdd:PRK14491 431 AAQADVVISSGGVSVGDADYIKTALAKLGQIDFWR--INMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRK 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 325 MEGQKEGFAPFVEAVLGVNYPSNHGREEYLSVSLQKNGEETLAMPVFGK--SGMISLMTKADGYVHIKRESEGLNKGQTV 402
Cdd:PRK14491 509 LAGEQNWQPLLFPAIADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKqgSGILSSMSEANCLIEIGPAAETVNAGETV 588
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
14-406 |
2.22e-66 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 220.45 E-value: 2.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 14 IETHFSNYPMEKETVPLD--QCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDTfgvsesmPAQLRLVGEVKMGEKPDF 91
Cdd:PRK14497 17 IKVFLSSLNFKPKIVKVEvkDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCT-------PGEFKVIDKIGIGEFKEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 92 VIRSGESAYVPTGGELPQGADGVVMMEYSEDFGDGDIFLNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRPQDLAMLAGL 171
Cdd:PRK14497 90 HIKECEAVEVDTGSMIPMGADAVIKVENTKVINGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 172 GLAVVPVQKKLKIGIISTGDEVV--GVEETPigAQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKAVEEND 249
Cdd:PRK14497 170 GISSVKVYEKPKIYLIATGDELVepGNSLSP--GKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVAD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 250 VVAISGGSSVGTKDVTVKVIDGLGApgLLLHGIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIFGKHLIRTMEGQK 329
Cdd:PRK14497 248 VLILTGGTSAGEKDFVHQAIRELGN--IIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPSR 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006062122 330 EGFAPF--VEAVLGVNYPSNHGREEYLSVSLQKNGEETLAMPVFGKSGMISLMTKADGYVHIKrESEGLNKGQTVQVTL 406
Cdd:PRK14497 326 KEILGLgkIKARLALRVKADEHRNTLIPVYLFKSDNSYYALPVPFDSYMVGTFSLTDGYIMLG-PNEEIEEGKEVEVDL 403
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
24-407 |
3.40e-54 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 184.91 E-value: 3.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 24 EKETVPLDQCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDtfgVSESMPaqLRLVGEVKMGEKPDFVIRSGESAYVPT 103
Cdd:PRK10680 26 ATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLAD---LASGQP--LPVAGKAFAGQPFHGEWPAGTCIRIMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 104 GGELPQGADGVVMMEYSEDFGDGDIFlNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRPQDLAMLAGLGLAVVPVQKKLK 183
Cdd:PRK10680 101 GAPVPEGCEAVVMQEQTEQTDDGVRF-TAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 184 IGIISTGDEVVGVEEtPIGA-QVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKAVEENDVVAISGGSSVGTK 262
Cdd:PRK10680 180 VALFSTGDELQLPGQ-PLGDgQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 263 DVTVKVIDGLGAPGLLlhGIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIFGKHLIRTMEGQKE-GFAPFVEAVLG 341
Cdd:PRK10680 259 DYTKTILEELGEIAFW--KLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNTAsGLPPRQRVRTA 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006062122 342 VNYPSNHGREEYLSVSLQKNGEETLAMPVFGKSG--MISLMTKADGYVHIKRESEGLNKGQTVQVTLF 407
Cdd:PRK10680 337 SRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGshIFSSFSLGNCFIVLERERGNVEVGEWVEVEPF 404
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
26-389 |
2.89e-49 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 172.02 E-value: 2.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 26 ETVPLDQCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDTFGvSESMPAQlrlVGEVKMGEKPDFVIRSGESAYVPTGG 105
Cdd:PRK14690 43 KELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEG-AQVLPLI---EGRAAAGVPFSGRVPEGMALRILTGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 106 ELPQGADGVVMMEySEDFGDGDIFLNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRPQDLAMLAGLGLAVVPVQKKLKIG 185
Cdd:PRK14690 119 ALPEGVDTVVLEE-DVAGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRVA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 186 IISTGDEVVGVEETPIGAQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKAVEENDVVAISGGSSVGTKDVT 265
Cdd:PRK14690 198 VLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGASAGDEDHV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 266 VKVIDGLGApgLLLHGIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIFGKHLIRTMEGqkEGFAPFVEAVLGVNYP 345
Cdd:PRK14690 278 SALLREAGA--MQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAG--EGWSEPQGFTVPAAFE 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2006062122 346 SNH--GREEYLSVSLQKNGEETLAMPvfgKSGMISLMTKADGYVHI 389
Cdd:PRK14690 354 KRKkpGRREYLRARLRQGHAEVFRSE---GSGRISGLSWAEGLVEL 396
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
24-172 |
5.61e-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: 160.42 E-value: 5.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 24 EKETVPLD--QCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDTFGVSESMPaqlrlvgeVKMGEKPDFVIRSGESAYV 101
Cdd:pfam03453 5 TEETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLPGGEAVRI 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006062122 102 PTGGELPQGADGVVMMEYSEDFGDGDIFLNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRPQDLAMLAGLG 172
Cdd:pfam03453 77 MTGAPLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
27-330 |
4.41e-40 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 151.12 E-value: 4.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 27 TVPLDQCLGRILSRDIAAREDMPAFHRSSVDGYAVTSKDTfgvsesmPAQLRLVGEVKMG-EKPDFVIRSGESAYVPTGG 105
Cdd:PLN02699 28 IVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDG-------PGEYPVITESRAGnDGLGVTLTPGTVAYVTTGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 106 ELPQGADGVVMMEYSEDFGDG-----DIFLNKSVAPGNNVIFRGDDVAVDQVVLQKGRRIRPQDLAMLAGLGLAVVPVQK 180
Cdd:PLN02699 101 PIPDGADAVVQVEDTEVVEDPldgskRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASEIGLLATVGVTMVKVYP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 181 KLKIGIISTGDEVVGVEETPIG-AQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKAVEEN-DVVAISGGSS 258
Cdd:PLN02699 181 RPTVAILSTGDELVEPTTGTLGrGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDEAISSGvDILLTSGGVS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 259 VGTKDVTVKVIDGLGApgLLLHGIAVKPGKPTILGKVGEKA---------VMGLPGHPASAFVIFQIFGKHLIRTMEGQK 329
Cdd:PLN02699 261 MGDRDFVKPLLEKRGT--VYFSKVLMKPGKPLTFAEIDAKSapsnskkmlAFGLPGNPVSCLVCFNLFVVPAIRYLAGWS 338
|
.
gi 2006062122 330 E 330
Cdd:PLN02699 339 N 339
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
182-317 |
5.76e-31 |
|
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: 115.49 E-value: 5.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 182 LKIGIISTGDEVVGVEETPIGAQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKAVEENDVVAISGGSSVGT 261
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006062122 262 KDVTVKVIDGLGA---PG------LLLHGIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIF 317
Cdd:TIGR00177 81 RDVTPEALEELGEkeiPGfgefrmLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVL 145
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
185-315 |
2.77e-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: 108.06 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 185 GIISTGDEVVgveetpIGAQVRDMNSYGVLALSQGLGLEAALYGIV--KDDFDRIDATVRKAVEENDVVAISGGSSVGTK 262
Cdd:smart00852 1 AIISTGDELL------SGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006062122 263 DVTVKVIDGLGAPGLLLHGIAVKPGKPTIL---------GKVGEKAVMGLPGHPASAFVIFQ 315
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMFE 136
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
185-324 |
1.31e-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: 101.17 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 185 GIISTGDEVVGveetpigAQVRDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKAVEENDVVAISGGSSVGTKDV 264
Cdd:pfam00994 1 AIITTGDELLP-------GQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 265 TVKVIDGLGAPGL-----LLHGIAVKPGKPTILGKV-----GEKAVMGLPGHPASAFVIFQIFGKHLIRT 324
Cdd:pfam00994 74 TPEALAELGGRELpgfeeLFRGVSLKPGKPVGTAPGailsrAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
183-322 |
3.60e-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: 96.64 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 183 KIGIISTGDEVVGVEETpigaqvrDMNSYGVLALSQGLGLEAALYGIVKDDFDRIDATVRKAVEENDVVAISGGSSVGTK 262
Cdd:cd00758 1 RVAIVTVSDELSQGQIE-------DTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 263 DVTVKVIDGLGAPGLLLHGIAVKPGKPTILGKVGEKAVMGLPGHPASAFVIFQIFGKHLI 322
Cdd:cd00758 74 DVTPEALAELGEREAHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
338-407 |
1.22e-10 |
|
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: 56.85 E-value: 1.22e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006062122 338 AVLGVNYPSNHGREEYLSVSLQKNGEETLAMPV-FGKSGMISLMTKADGYVHIKRESEGLNKGQTVQVTLF 407
Cdd:pfam03454 2 ARLARDLKSDPGRREFVRVRLHEEDGRYYAEPIgKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
165-305 |
7.51e-06 |
|
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: 47.54 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 165 LAMLAGLG-LAVVPVqKKLKIGIISTGDEV-VGVEETPIGAQVRdmnsyGVLAlsqGLGLEAALYGIVKDDFDRIDATVR 242
Cdd:cd03522 143 EALARDGPlLRVAPF-RPLRVGLIVTGSEVyGGRIEDKFGPVLR-----ARLA---ALGVELVEQVIVPHDEAAIAAAIA 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006062122 243 KAVEENDVVAI-SGGSSVGTKDVTVKVIDGLGAPgLLLHGIAVKPGKPTILGKVGEKAVMGLPG 305
Cdd:cd03522 214 EALEAGAELLIlTGGASVDPDDVTPAAIRAAGGE-VIRYGMPVDPGNLLLLGYLGGVPVIGLPG 276
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
180-273 |
1.91e-05 |
|
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: 44.72 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 180 KKLKIGIISTGDEV-VGVEETPIGAQVRDMnsygvlaLsQGLGLEAALYGIVKDDFDRIDATVRKAVEEN--DVVAISGG 256
Cdd:COG0521 8 VPLRIAVLTVSDRRsRGEREDTSGPALVEL-------L-EEAGHEVVARRIVPDDKDAIRAALRELIDDEgvDLVLTTGG 79
|
90 100
....*....|....*....|....*
gi 2006062122 257 SSVGTKDVTV--------KVIDGLG 273
Cdd:COG0521 80 TGLSPRDVTPeatrplldKELPGFG 104
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
182-310 |
1.21e-04 |
|
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: 42.08 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 182 LKIGIISTGDEV-VGVEETPIGAQVRDMnsygvlaLSQGlGLEAALYGIVKDDFDRIDATVRKAVEEN--DVVAISGGSS 258
Cdd:cd00886 1 LRAAVLTVSDTRsAGEAEDRSGPALVEL-------LEEA-GHEVVAYEIVPDDKDEIREALIEWADEDgvDLILTTGGTG 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006062122 259 VGTKDVTV--------KVIDGLgapGLLLHGIAVKPGKPTIL-----GKVGEKAVMGLPGHPASA 310
Cdd:cd00886 73 LAPRDVTPeatrplldKELPGF---GEAFRALSLEETGTAMLsravaGIRGGTLIFNLPGSPKAV 134
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
183-269 |
1.24e-03 |
|
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: 39.39 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006062122 183 KIGIISTGDEVVgveetpIGaQVRDMNSygvlalsQGLGLEAALYGI-------VKDDFDRIDATVRKAVEENDVVAISG 255
Cdd:cd00885 1 TAEIIAIGDELL------SG-QIVDTNA-------AFLAKELAELGIevyrvtvVGDDEDRIAEALRRASERADLVITTG 66
|
90
....*....|....*.
gi 2006062122 256 GssVG-TK-DVTVKVI 269
Cdd:cd00885 67 G--LGpTHdDLTREAV 80
|
|
| |
