|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
9-408 |
7.20e-160 |
|
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: 455.41 E-value: 7.20e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 9 VEEAKNIINcNFKLILKTELIDIKECNGRVLSKDITSPLNIPGFKRSMVDGYAVKFRDLQGASESmpslLDLKGEVKMGK 88
Cdd:cd00887 1 VEAARELLL-ALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVT----LRVVGEIPAGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 89 MPVKSLEyPGECMYIPTGGMLPEGTDSVIMIEYIDKMDDaTVLANKSISFGENVLNEDEDVEFGETVLKQGTILKPYGIS 168
Cdd:cd00887 76 PPDGPLG-PGEAVRIMTGAPLPEGADAVVMVEDTEEEGG-RVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 169 MLSSLGITKVQVFCKPRIGIISTGDEIVSPEKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFETVKRAVN 248
Cdd:cd00887 154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 249 ECDLVLVSGGSSVGKKDETAKVIDELGAhGILFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAVVYRILVRYIINAMM 328
Cdd:cd00887 234 EADVVITSGGVSVGDYDFVKEVLEELGG-EVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 329 GFEDVDYP-IPCKFNMNYHKAKGREEYLPVTINNVNGEYIAAPVLS-KSAAISGFTKAWGYIKINKNVEGVYEHEKVYVY 406
Cdd:cd00887 313 GAPEPEPPrVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGqGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVL 392
|
..
gi 736025320 407 KF 408
Cdd:cd00887 393 LL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
6-408 |
2.19e-156 |
|
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: 446.84 E-value: 2.19e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 6 VVSVEEAKNIINCNFKLiLKTELIDIKECNGRVLSKDITSPLNIPGFKRSMVDGYAVKFRDLQGASesmPSLLDLKGEVK 85
Cdd:COG0303 1 MISVEEALALILAAVRP-LGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAN---PVTLRVVGEIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 86 MGKMPVKSLEyPGECMYIPTGGMLPEGTDSVIMIEYIDKmDDATVLANKSISFGENVLNEDEDVEFGETVLKQGTILKPY 165
Cdd:COG0303 77 AGSPPPGPLG-PGEAVRIMTGAPLPEGADAVVMQEDTER-EGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 166 GISMLSSLGITKVQVFCKPRIGIISTGDEIVSPEKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFETVKR 245
Cdd:COG0303 155 DLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALRE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 246 AVNECDLVLVSGGSSVGKKDETAKVIDELGAhGILFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAVVYRILVRYIIN 325
Cdd:COG0303 235 ALAEADLVITSGGVSVGDYDLVKEALEELGA-EVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 326 AMMGFEDVDYP-IPCKFNMNYHKAKGREEYLPVTINNVNGEYIAAPV-LSKSAAISGFTKAWGYIKINKNVEGVYEHEKV 403
Cdd:COG0303 314 KLAGLPPPPPPrVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLgGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEV 393
|
....*
gi 736025320 404 YVYKF 408
Cdd:COG0303 394 EVLLL 398
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
3-408 |
1.78e-154 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 450.43 E-value: 1.78e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 3 FYNVVSVEEAKNIINCNFK-LILKTELIDIKECNGRVLSKDITSPLNIPGFKRSMVDGYAVKFRDLQGASESMPSLLDLK 81
Cdd:PRK14498 6 FLTLVSLEEAREILESLLSeLPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLKLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 82 GEVKMGKMPVKSLEyPGECMYIPTGGMLPEGTDSVIMIEYIDKMDDATVLANKSISFGENVLNEDEDVEFGETVLKQGTI 161
Cdd:PRK14498 86 GEVHAGEAPDVEVE-PGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 162 LKPYGISMLSSLGITKVQVFCKPRIGIISTGDEIVSPEKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFE 241
Cdd:PRK14498 165 LTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 242 TVKRAVNECDLVLVSGGSSVGKKDETAKVIDELGAhgILFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAVVYRILVR 321
Cdd:PRK14498 245 ALRKALKECDLVLLSGGTSAGAGDVTYRVIEELGE--VLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 322 YIINAMMGFEDVDYP-IPCKFNMNYHKAKGREEYLPVTINNVNGEYIAAPVLSKSAAISGFTKAWGYIKINKNVEGVYEH 400
Cdd:PRK14498 323 PLLRKLAGLPPPERAtVKARLARRVRSELGREEFVPVSLGRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTEGLEAG 402
|
....*...
gi 736025320 401 EKVYVYKF 408
Cdd:PRK14498 403 EEVEVELF 410
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
22-174 |
5.38e-45 |
|
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: 152.72 E-value: 5.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 22 LILKTELIDIK--ECNGRVLSKDITSPLNIPGFKRSMVDGYAVKFRDLQGASESMPslldlkgeVKMGKMPVKSLEyPGE 99
Cdd:pfam03453 2 LLGTEETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLP-GGE 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736025320 100 CMYIPTGGMLPEGTDSVIMIEYIDKMDDATVLANKSISFGENVLNEDEDVEFGETVLKQGTILKPYGISMLSSLG 174
Cdd:pfam03453 73 AVRIMTGAPLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
184-321 |
2.10e-39 |
|
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.
Pssm-ID: 272944 [Multi-domain] Cd Length: 148 Bit Score: 138.22 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 184 PRIGIISTGDEIVSPEKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFETVKRAVNECDLVLVSGGSSVGK 263
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736025320 264 KDETAKVIDELGA---HGI------LFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAVVYRILVR 321
Cdd:TIGR00177 81 RDVTPEALEELGEkeiPGFgefrmlSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLIL 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
187-314 |
8.81e-36 |
|
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: 128.09 E-value: 8.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 187 GIISTGDEIVSPekqpqlGEIRDINSYLIYSSVIEDGGQPILYGII--KDNYEELFETVKRAVNECDLVLVSGGSSVGKK 264
Cdd:smart00852 1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 736025320 265 DETAKVIDELGAHGILFHGISIKPGKPTIL---------GKIKDKPIFGLPGHPLSCAV 314
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALV 133
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
9-408 |
7.20e-160 |
|
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: 455.41 E-value: 7.20e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 9 VEEAKNIINcNFKLILKTELIDIKECNGRVLSKDITSPLNIPGFKRSMVDGYAVKFRDLQGASESmpslLDLKGEVKMGK 88
Cdd:cd00887 1 VEAARELLL-ALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVT----LRVVGEIPAGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 89 MPVKSLEyPGECMYIPTGGMLPEGTDSVIMIEYIDKMDDaTVLANKSISFGENVLNEDEDVEFGETVLKQGTILKPYGIS 168
Cdd:cd00887 76 PPDGPLG-PGEAVRIMTGAPLPEGADAVVMVEDTEEEGG-RVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 169 MLSSLGITKVQVFCKPRIGIISTGDEIVSPEKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFETVKRAVN 248
Cdd:cd00887 154 LLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 249 ECDLVLVSGGSSVGKKDETAKVIDELGAhGILFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAVVYRILVRYIINAMM 328
Cdd:cd00887 234 EADVVITSGGVSVGDYDFVKEVLEELGG-EVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 329 GFEDVDYP-IPCKFNMNYHKAKGREEYLPVTINNVNGEYIAAPVLS-KSAAISGFTKAWGYIKINKNVEGVYEHEKVYVY 406
Cdd:cd00887 313 GAPEPEPPrVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGqGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVL 392
|
..
gi 736025320 407 KF 408
Cdd:cd00887 393 LL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
6-408 |
2.19e-156 |
|
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: 446.84 E-value: 2.19e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 6 VVSVEEAKNIINCNFKLiLKTELIDIKECNGRVLSKDITSPLNIPGFKRSMVDGYAVKFRDLQGASesmPSLLDLKGEVK 85
Cdd:COG0303 1 MISVEEALALILAAVRP-LGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAN---PVTLRVVGEIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 86 MGKMPVKSLEyPGECMYIPTGGMLPEGTDSVIMIEYIDKmDDATVLANKSISFGENVLNEDEDVEFGETVLKQGTILKPY 165
Cdd:COG0303 77 AGSPPPGPLG-PGEAVRIMTGAPLPEGADAVVMQEDTER-EGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 166 GISMLSSLGITKVQVFCKPRIGIISTGDEIVSPEKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFETVKR 245
Cdd:COG0303 155 DLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALRE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 246 AVNECDLVLVSGGSSVGKKDETAKVIDELGAhGILFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAVVYRILVRYIIN 325
Cdd:COG0303 235 ALAEADLVITSGGVSVGDYDLVKEALEELGA-EVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 326 AMMGFEDVDYP-IPCKFNMNYHKAKGREEYLPVTINNVNGEYIAAPV-LSKSAAISGFTKAWGYIKINKNVEGVYEHEKV 403
Cdd:COG0303 314 KLAGLPPPPPPrVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLgGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEV 393
|
....*
gi 736025320 404 YVYKF 408
Cdd:COG0303 394 EVLLL 398
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
3-408 |
1.78e-154 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 450.43 E-value: 1.78e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 3 FYNVVSVEEAKNIINCNFK-LILKTELIDIKECNGRVLSKDITSPLNIPGFKRSMVDGYAVKFRDLQGASESMPSLLDLK 81
Cdd:PRK14498 6 FLTLVSLEEAREILESLLSeLPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLKLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 82 GEVKMGKMPVKSLEyPGECMYIPTGGMLPEGTDSVIMIEYIDKMDDATVLANKSISFGENVLNEDEDVEFGETVLKQGTI 161
Cdd:PRK14498 86 GEVHAGEAPDVEVE-PGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 162 LKPYGISMLSSLGITKVQVFCKPRIGIISTGDEIVSPEKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFE 241
Cdd:PRK14498 165 LTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 242 TVKRAVNECDLVLVSGGSSVGKKDETAKVIDELGAhgILFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAVVYRILVR 321
Cdd:PRK14498 245 ALRKALKECDLVLLSGGTSAGAGDVTYRVIEELGE--VLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 322 YIINAMMGFEDVDYP-IPCKFNMNYHKAKGREEYLPVTINNVNGEYIAAPVLSKSAAISGFTKAWGYIKINKNVEGVYEH 400
Cdd:PRK14498 323 PLLRKLAGLPPPERAtVKARLARRVRSELGREEFVPVSLGRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTEGLEAG 402
|
....*...
gi 736025320 401 EKVYVYKF 408
Cdd:PRK14498 403 EEVEVELF 410
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
5-406 |
1.77e-76 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 247.03 E-value: 1.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 5 NVVSVEEAKNIINCNFKLILKTELIDIKECNGRVLSKDITSPLNIPGFKRSMVDGYAVKfrdlqgaSESMPSLLDLKGEV 84
Cdd:PRK14497 9 SLYSIDEAIKVFLSSLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALK-------SSCTPGEFKVIDKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 85 KMGKMpvKSLEY-PGECMYIPTGGMLPEGTDSVIMIEYIDKMDDATVLANKSISFGENVLNEDEDVEFGETVLKQGTILK 163
Cdd:PRK14497 82 GIGEF--KEIHIkECEAVEVDTGSMIPMGADAVIKVENTKVINGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 164 PYGISMLSSLGITKVQVFCKPRIGIISTGDEIVSPEKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFETV 243
Cdd:PRK14497 160 HEKIGLLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 244 KRAVNECDLVLVSGGSSVGKKDETAKVIDELGAhgILFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAVVYRILV-RY 322
Cdd:PRK14497 240 KRAISVADVLILTGGTSAGEKDFVHQAIRELGN--IIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVIlEY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 323 IINAMMGFEDVDYPIPCKFNM-NYHKA-KGREEYLPVTINNVNGEYIAAPVLSKSAAISGFTKAWGYIKINKNvEGVYEH 400
Cdd:PRK14497 318 LKSLYPSRKEILGLGKIKARLaLRVKAdEHRNTLIPVYLFKSDNSYYALPVPFDSYMVGTFSLTDGYIMLGPN-EEIEEG 396
|
....*.
gi 736025320 401 EKVYVY 406
Cdd:PRK14497 397 KEVEVD 402
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
8-409 |
3.20e-64 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 216.02 E-value: 3.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 8 SVEEAKNIINCNFKLILKTELIDIKECNGRVLSKDITSPLNIPGFKRSMVDGYAVKFRDLqgasesMPSLLDLKGEVKMG 87
Cdd:PRK14491 200 SVSQGLDKILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDL------EPESYTLVGEVLAG 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 88 KMPVKSLEyPGECMYIPTGGMLPEGTDSVIMIEYIdKMDDATVLANKSISFGENVLNEDEDVEFGETVLKQGTILKPYGI 167
Cdd:PRK14491 274 HQYDGTLQ-AGEAVRIMTGAPVPAGADTVVMRELA-TQDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQ 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 168 SMLSSLGITKVQVFCKPRIGIISTGDEIVSPEKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFETVKRAV 247
Cdd:PRK14491 352 GLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 248 NECDLVLVSGGSSVGKKDETAKVIDELGAhgILFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAVVYRILVRYIINAM 327
Cdd:PRK14491 432 AQADVVISSGGVSVGDADYIKTALAKLGQ--IDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 328 MG---FEDVDYPIPCKFNMnyHKAKGREEY------------LPVTINNVNGeyiaapvlskSAAISGFTKAWGYIKINK 392
Cdd:PRK14491 510 AGeqnWQPLLFPAIADETL--RSRQGRTEFsrgiyhlgadgrLHVRTTGKQG----------SGILSSMSEANCLIEIGP 577
|
410
....*....|....*..
gi 736025320 393 NVEGVYEHEKVYVYKFQ 409
Cdd:PRK14491 578 AAETVNAGETVTIQPLA 594
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
26-336 |
3.12e-61 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 203.40 E-value: 3.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 26 TELIDIKECNGRVLSKDITSPLNIPGFKRSMVDGYAVKFRDLQGaseSMPslLDLKGEVKMGKmPVKSlEYP-GECMYIP 104
Cdd:PRK10680 27 TETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLAS---GQP--LPVAGKAFAGQ-PFHG-EWPaGTCIRIM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 105 TGGMLPEGTDSVIMIEYIDKMDDAtVLANKSISFGENVLNEDEDVEFGETVLKQGTILKPYGISMLSSLGITKVQVFCKP 184
Cdd:PRK10680 100 TGAPVPEGCEAVVMQEQTEQTDDG-VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 185 RIGIISTGDEIVSPEKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFETVKRAVNECDLVLVSGGSSVGKK 264
Cdd:PRK10680 179 RVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEA 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736025320 265 DETAKVIDELGAhgILFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAVVYRILVRYIINAMMGFEDVDYP 336
Cdd:PRK10680 259 DYTKTILEELGE--IAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNTASGLP 328
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
9-390 |
4.46e-51 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 177.03 E-value: 4.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 9 VEEAKNIINCNFKLILKTELIDIKECNGRVLSKDITSPLNIPGFKRSMVDGYAVKfrdlQGASESMPSLLDLKGEVKMGk 88
Cdd:PRK14690 25 VDTALDLLRARLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFA----GAAPEGAQVLPLIEGRAAAG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 89 MPVKSLEYPGECMYIPTGGMLPEGTDSVIMIEYIdKMDDATVLANKSISFGENVLNEDEDVEFGETVLKQGTILKPYGIS 168
Cdd:PRK14690 100 VPFSGRVPEGMALRILTGAALPEGVDTVVLEEDV-AGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 169 MLSSLGITKVQVFCKPRIGIISTGDEIVSPEKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFETVKRAVN 248
Cdd:PRK14690 179 LLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 249 ECDLVLVSGGSSVGKKDETAKVIDELGAhgILFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAVVYRILVRYIINAMM 328
Cdd:PRK14690 259 EADVILTSGGASAGDEDHVSALLREAGA--MQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLA 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736025320 329 G---FEDVDYPIPCKFNMNyhKAKGREEYLPVTINNVNGEYIAApvlSKSAAISGFTKAWGYIKI 390
Cdd:PRK14690 337 GegwSEPQGFTVPAAFEKR--KKPGRREYLRARLRQGHAEVFRS---EGSGRISGLSWAEGLVEL 396
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
6-340 |
1.16e-47 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 172.30 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 6 VVSVEEAKNIINCNFKLILKTElIDIKECNGRVLSKDITSPLNIPGFKRSMVDGYAVKfrdlqgASESmPSLLDLKGEVK 85
Cdd:PLN02699 7 MISVEEALSIVLSVAARLSPVI-VPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVV------ASDG-PGEYPVITESR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 86 MGKMPVKSLEYPGECMYIPTGGMLPEGTDSVIMIEYIDKMDDATVLANK-----SISFGENVLNEDEDVEFGETVLKQGT 160
Cdd:PLN02699 79 AGNDGLGVTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKRvrilsQASKGQDIRPVGCDIEKDAKVLKAGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 161 ILKPYGISMLSSLGITKVQVFCKPRIGIISTGDEIVSP-EKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEEL 239
Cdd:PLN02699 159 RLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPtTGTLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 240 FETVKRAVNE-CDLVLVSGGSSVGKKDETAKVIDELGAhgILFHGISIKPGKPTILGKIKDKP---------IFGLPGHP 309
Cdd:PLN02699 239 ERILDEAISSgVDILLTSGGVSMGDRDFVKPLLEKRGT--VYFSKVLMKPGKPLTFAEIDAKSapsnskkmlAFGLPGNP 316
|
330 340 350
....*....|....*....|....*....|.
gi 736025320 310 LSCAVVYRILVRYIINAMMGFEDvdyPIPCK 340
Cdd:PLN02699 317 VSCLVCFNLFVVPAIRYLAGWSN---PHLLR 344
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
22-174 |
5.38e-45 |
|
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: 152.72 E-value: 5.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 22 LILKTELIDIK--ECNGRVLSKDITSPLNIPGFKRSMVDGYAVKFRDLQGASESMPslldlkgeVKMGKMPVKSLEyPGE 99
Cdd:pfam03453 2 LLGTEETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLP-GGE 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736025320 100 CMYIPTGGMLPEGTDSVIMIEYIDKMDDATVLANKSISFGENVLNEDEDVEFGETVLKQGTILKPYGISMLSSLG 174
Cdd:pfam03453 73 AVRIMTGAPLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
184-321 |
2.10e-39 |
|
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.
Pssm-ID: 272944 [Multi-domain] Cd Length: 148 Bit Score: 138.22 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 184 PRIGIISTGDEIVSPEKQPQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFETVKRAVNECDLVLVSGGSSVGK 263
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736025320 264 KDETAKVIDELGA---HGI------LFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAVVYRILVR 321
Cdd:TIGR00177 81 RDVTPEALEELGEkeiPGFgefrmlSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLIL 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
187-314 |
8.81e-36 |
|
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: 128.09 E-value: 8.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 187 GIISTGDEIVSPekqpqlGEIRDINSYLIYSSVIEDGGQPILYGII--KDNYEELFETVKRAVNECDLVLVSGGSSVGKK 264
Cdd:smart00852 1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 736025320 265 DETAKVIDELGAHGILFHGISIKPGKPTIL---------GKIKDKPIFGLPGHPLSCAV 314
Cdd:smart00852 75 DLTPEALAELGGRELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALV 133
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
187-324 |
6.52e-35 |
|
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: 125.82 E-value: 6.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 187 GIISTGDEIVSpekqpqlGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFETVKRAVNECDLVLVSGGSSVGKKDE 266
Cdd:pfam00994 1 AIITTGDELLP-------GQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736025320 267 TAKVIDELGA-----HGILFHGISIKPGKPTILGKI-----KDKPIFGLPGHPLSCAVVYRILVRYII 324
Cdd:pfam00994 74 TPEALAELGGrelpgFEELFRGVSLKPGKPVGTAPGailsrAGKTVFGLPGSPVAAKVMFELLLLPLL 141
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
185-314 |
1.02e-32 |
|
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: 119.76 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 185 RIGIISTGDEIvspekqpQLGEIRDINSYLIYSSVIEDGGQPILYGIIKDNYEELFETVKRAVNECDLVLVSGGSSVGKK 264
Cdd:cd00758 1 RVAIVTVSDEL-------SQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 736025320 265 DETAKVIDELGAHGILFHGISIKPGKPTILGKIKDKPIFGLPGHPLSCAV 314
Cdd:cd00758 74 DVTPEALAELGEREAHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALT 123
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
344-408 |
8.37e-11 |
|
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: 57.62 E-value: 8.37e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736025320 344 NYHKAKGREEYLPVTINNVNGEYIAAPVLSK-SAAISGFTKAWGYIKINKNVEGVYEHEKVYVYKF 408
Cdd:pfam03454 7 DLKSDPGRREFVRVRLHEEDGRYYAEPIGKQgSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
185-309 |
1.00e-07 |
|
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: 51.27 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 185 RIGIISTGDEIVSPEKQPQLGEirdinsyLIYSSVIEDGGQPILYGIIKDNYEELFETVKRAVNE--CDLVLVSGGSSVG 262
Cdd:COG0521 11 RIAVLTVSDRRSRGEREDTSGP-------ALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDegVDLVLTTGGTGLS 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 736025320 263 KKDET----AKVID-ELGAHGILFHGISIKPGKPT-IL-----GKIKDKPIFGLPGHP 309
Cdd:COG0521 84 PRDVTpeatRPLLDkELPGFGELFRALSLEEIGPSaILsravaGIRGGTLIFNLPGSP 141
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
214-309 |
1.78e-07 |
|
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: 50.17 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 214 LIYSSVIEDGGQPILYGIIKDNYEELFETVKRAVNE--CDLVLVSGGSSVGKKDET----AKVID-ELGAHGILFHGISI 286
Cdd:cd00886 24 ALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEdgVDLILTTGGTGLAPRDVTpeatRPLLDkELPGFGEAFRALSL 103
|
90 100
....*....|....*....|....*...
gi 736025320 287 KPGKPTIL-----GKIKDKPIFGLPGHP 309
Cdd:cd00886 104 EETGTAMLsravaGIRGGTLIFNLPGSP 131
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
185-258 |
2.57e-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: 2.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736025320 185 RIGIISTGDEIVSpekqpqlGEIRDINS-YLiySSVIEDGGQPILYG-IIKDNYEELFETVKRAVNECDLVLVSGG 258
Cdd:cd00885 1 TAEIIAIGDELLS-------GQIVDTNAaFL--AKELAELGIEVYRVtVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
164-329 |
1.54e-05 |
|
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. There this domain is presumed to bind molybdopterin. The exact function of this subgroup is unknown.
Pssm-ID: 239599 Cd Length: 312 Bit Score: 46.39 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 164 PYGIS---------MLSSLGITKVQVFCKPRIGIISTGDEIvspekqpqlgeirdinsyliYSSVIEDGGQPIL------ 228
Cdd:cd03522 131 PLAVPealveraeaLARDGPLLRVAPFRPLRVGLIVTGSEV--------------------YGGRIEDKFGPVLrarlaa 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736025320 229 YG-------IIKDNYEELFETVKRAVNEC-DLVLVSGGSSVGKKDETAKVIDELGAHgILFHGISIKPGKPTILGKIKDK 300
Cdd:cd03522 191 LGvelveqvIVPHDEAAIAAAIAEALEAGaELLILTGGASVDPDDVTPAAIRAAGGE-VIRYGMPVDPGNLLLLGYLGGV 269
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 736025320 301 PIFGLPGhplsCA----------VVYRILVRYIIN----AMMG 329
Cdd:cd03522 270 PVIGLPG----CArspklngfdlVLPRLLAGERVTradiAAMG 308
|
|
| |
