|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
9-415 |
2.29e-159 |
|
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: 454.93 E-value: 2.29e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 9 MTVEAARELLQSRVRPVEPTEVELAEAIGRRLAAPIRTVEPIPHFRRSGMDGYAIRTADIAhasAALPIELEIIEHIPCG 88
Cdd:COG0303 2 ISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLA---GANPVTLRVVGEIAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 89 KEPLYSITEGKAARIMTGGMVPDGADAVIMQEMTEAVEhngrSIVRIQKKIAPGLNITPIGEEAGEGTLVIEAGEKLGAG 168
Cdd:COG0303 79 SPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREG----DRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 169 HTAILAALGYNRVPVYRKPKVAVLSTGTELLRLTDPLQMGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDYPKAERMLyD 248
Cdd:COG0303 155 DLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL-R 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 249 LLASDADLIVTSGGVSVGDYDSMADFFLRWEGTTLFNKIAMRPGSPTTAGAWKDKLLFGLSGNPSACFVGFELFVRPVIQ 328
Cdd:COG0303 234 EALAEADLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 329 QLQGAVVDTAKTVTCLLAADYEKVNAYTRYVRGQWYSSGGNHYAKPVGRDKSSTILSLKDANCLIVIPPTKTGIVSGEIV 408
Cdd:COG0303 314 KLAGLPPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEV 393
|
....*..
gi 1858325166 409 QIIPLDG 415
Cdd:COG0303 394 EVLLLDG 400
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
11-413 |
2.00e-156 |
|
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: 446.94 E-value: 2.00e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 11 VEAARELLQSRVRPVEPTEVELAEAIGRRLAAPIRTVEPIPHFRRSGMDGYAIRTADIAHASAALPIeleiIEHIPCGKE 90
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLRV----VGEIPAGEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 91 PLYSITEGKAARIMTGGMVPDGADAVIMQEMTEAVEhngrSIVRIQKKIAPGLNITPIGEEAGEGTLVIEAGEKLGAGHT 170
Cdd:cd00887 77 PDGPLGPGEAVRIMTGAPLPEGADAVVMVEDTEEEG----GRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 171 AILAALGYNRVPVYRKPKVAVLSTGTELLRLTDPLQMGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDYPKAERMLYDLL 250
Cdd:cd00887 153 GLLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 251 ASdADLIVTSGGVSVGDYDSMADFFLRWEGTTLFNKIAMRPGSPTTAGAWKDKLLFGLSGNPSACFVGFELFVRPVIQQL 330
Cdd:cd00887 233 EE-ADVVITSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 331 QGAVVDTAKTVTCLLAADYEKVNAYTRYVRGQWYSSGGNHYAKPVGRDKSSTILSLKDANCLIVIPPTKTGIVSGEIVQI 410
Cdd:cd00887 312 QGAPEPEPPRVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEV 391
|
...
gi 1858325166 411 IPL 413
Cdd:cd00887 392 LLL 394
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
1-408 |
1.29e-100 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 312.53 E-value: 1.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 1 MNKYHRKAMTVEAARELLQSRVRP--VEPTEVELAEAIGRRLAAPIrtVEPI--PHFRRSGMDGYAIRTADIAHASAALP 76
Cdd:PRK14498 2 KRKIFLTLVSLEEAREILESLLSElpLGTEEVPLEEALGRVLAEDV--YAPIdvPPFDRSAMDGYAVRAADTFGASEANP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 77 IELEIIEHIPCGKEPLYSITEGKAARIMTGGMVPDGADAVIMQEMTEAVEHNGrsiVRIQKKIAPGLNITPIGEEAGEGT 156
Cdd:PRK14498 80 VRLKLGGEVHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDT---VEIYRPVAPGENVRPAGEDIVAGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 157 LVIEAGEKLGAGHTAILAALGYNRVPVYRKPKVAVLSTGTELLRLTDPLQMGKIRNSNAYMLMAQIIAAGAQPLLVGQIP 236
Cdd:PRK14498 157 LILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 237 DDYPKAERMLYDLLAsDADLIVTSGGVSVGDYDSMADFFLRwEGTTLFNKIAMRPGSPTTAGAWKDKLLFGLSGNPSACF 316
Cdd:PRK14498 237 DDEEELEAALRKALK-ECDLVLLSGGTSAGAGDVTYRVIEE-LGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 317 VGFELFVRPVIQQLQGAVVDTAKTVTCLLAADYEKVNAYTRYVRGQWYSSGGNHYAKPVGRdKSSTILSLKDANCLIVIP 396
Cdd:PRK14498 315 TIFEEFVAPLLRKLAGLPPPERATVKARLARRVRSELGREEFVPVSLGRVGDGYVAYPLSR-GSGAITSLVRADGFIEIP 393
|
410
....*....|..
gi 1858325166 397 PTKTGIVSGEIV 408
Cdd:PRK14498 394 ANTEGLEAGEEV 405
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
22-177 |
4.31e-44 |
|
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: 150.41 E-value: 4.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 22 VRPVEPTEVELAEAIGRRLAAPIRTVEPIPHFRRSGMDGYAIRTADIAHASAALPieleiiehIPCGKEPLYSITEGKAA 101
Cdd:pfam03453 3 LGTEETVPLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLPGGEAV 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1858325166 102 RIMTGGMVPDGADAVIMQEMTEAVehnGRSIVRIQKKIAPGLNITPIGEEAGEGTLVIEAGEKLGAGHTAILAALG 177
Cdd:pfam03453 75 RIMTGAPLPEGADAVVMVEDTEEG---GGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
187-325 |
4.27e-34 |
|
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.
Pssm-ID: 272944 [Multi-domain] Cd Length: 148 Bit Score: 124.35 E-value: 4.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 187 PKVAVLSTGTELLRLTDPLQMGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDYPKAERMLYDLLAsDADLIVTSGGVSVG 266
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVD-EADVVLTTGGTGVG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1858325166 267 DYD----SMADFFLRW-EGTTLFNK-----IAMRPGSPTTAGAWKDKLLFGLSGNPSACFVGFELFVRP 325
Cdd:TIGR00177 80 PRDvtpeALEELGEKEiPGFGEFRMlsslpVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
190-322 |
1.71e-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 trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 100.74 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 190 AVLSTGTELLRLtdplqmGKIRNSNAYMLMAQIIAAGAQP--LLVGQIPDDYPKAERMLYDLLAsDADLIVTSGGVSVGD 267
Cdd:smart00852 1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVvrVVVVGGPDDPEAIREALREALA-EADVVITTGGTGPGP 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1858325166 268 YDSMADFFLRWEGTTLFN-KIAMRPGSPTT---------AGAWKDKLLFGLSGNPSACFVGFELF 322
Cdd:smart00852 74 DDLTPEALAELGGRELLGhGVAMRPGGPPGplanlsgtaPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
9-415 |
2.29e-159 |
|
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: 454.93 E-value: 2.29e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 9 MTVEAARELLQSRVRPVEPTEVELAEAIGRRLAAPIRTVEPIPHFRRSGMDGYAIRTADIAhasAALPIELEIIEHIPCG 88
Cdd:COG0303 2 ISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLA---GANPVTLRVVGEIAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 89 KEPLYSITEGKAARIMTGGMVPDGADAVIMQEMTEAVEhngrSIVRIQKKIAPGLNITPIGEEAGEGTLVIEAGEKLGAG 168
Cdd:COG0303 79 SPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREG----DRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 169 HTAILAALGYNRVPVYRKPKVAVLSTGTELLRLTDPLQMGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDYPKAERMLyD 248
Cdd:COG0303 155 DLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAAL-R 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 249 LLASDADLIVTSGGVSVGDYDSMADFFLRWEGTTLFNKIAMRPGSPTTAGAWKDKLLFGLSGNPSACFVGFELFVRPVIQ 328
Cdd:COG0303 234 EALAEADLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 329 QLQGAVVDTAKTVTCLLAADYEKVNAYTRYVRGQWYSSGGNHYAKPVGRDKSSTILSLKDANCLIVIPPTKTGIVSGEIV 408
Cdd:COG0303 314 KLAGLPPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEV 393
|
....*..
gi 1858325166 409 QIIPLDG 415
Cdd:COG0303 394 EVLLLDG 400
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
11-413 |
2.00e-156 |
|
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: 446.94 E-value: 2.00e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 11 VEAARELLQSRVRPVEPTEVELAEAIGRRLAAPIRTVEPIPHFRRSGMDGYAIRTADIAHASAALPIeleiIEHIPCGKE 90
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLRV----VGEIPAGEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 91 PLYSITEGKAARIMTGGMVPDGADAVIMQEMTEAVEhngrSIVRIQKKIAPGLNITPIGEEAGEGTLVIEAGEKLGAGHT 170
Cdd:cd00887 77 PDGPLGPGEAVRIMTGAPLPEGADAVVMVEDTEEEG----GRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 171 AILAALGYNRVPVYRKPKVAVLSTGTELLRLTDPLQMGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDYPKAERMLYDLL 250
Cdd:cd00887 153 GLLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 251 ASdADLIVTSGGVSVGDYDSMADFFLRWEGTTLFNKIAMRPGSPTTAGAWKDKLLFGLSGNPSACFVGFELFVRPVIQQL 330
Cdd:cd00887 233 EE-ADVVITSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 331 QGAVVDTAKTVTCLLAADYEKVNAYTRYVRGQWYSSGGNHYAKPVGRDKSSTILSLKDANCLIVIPPTKTGIVSGEIVQI 410
Cdd:cd00887 312 QGAPEPEPPRVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEV 391
|
...
gi 1858325166 411 IPL 413
Cdd:cd00887 392 LLL 394
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
1-408 |
1.29e-100 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 312.53 E-value: 1.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 1 MNKYHRKAMTVEAARELLQSRVRP--VEPTEVELAEAIGRRLAAPIrtVEPI--PHFRRSGMDGYAIRTADIAHASAALP 76
Cdd:PRK14498 2 KRKIFLTLVSLEEAREILESLLSElpLGTEEVPLEEALGRVLAEDV--YAPIdvPPFDRSAMDGYAVRAADTFGASEANP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 77 IELEIIEHIPCGKEPLYSITEGKAARIMTGGMVPDGADAVIMQEMTEAVEHNGrsiVRIQKKIAPGLNITPIGEEAGEGT 156
Cdd:PRK14498 80 VRLKLGGEVHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDT---VEIYRPVAPGENVRPAGEDIVAGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 157 LVIEAGEKLGAGHTAILAALGYNRVPVYRKPKVAVLSTGTELLRLTDPLQMGKIRNSNAYMLMAQIIAAGAQPLLVGQIP 236
Cdd:PRK14498 157 LILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 237 DDYPKAERMLYDLLAsDADLIVTSGGVSVGDYDSMADFFLRwEGTTLFNKIAMRPGSPTTAGAWKDKLLFGLSGNPSACF 316
Cdd:PRK14498 237 DDEEELEAALRKALK-ECDLVLLSGGTSAGAGDVTYRVIEE-LGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 317 VGFELFVRPVIQQLQGAVVDTAKTVTCLLAADYEKVNAYTRYVRGQWYSSGGNHYAKPVGRdKSSTILSLKDANCLIVIP 396
Cdd:PRK14498 315 TIFEEFVAPLLRKLAGLPPPERATVKARLARRVRSELGREEFVPVSLGRVGDGYVAYPLSR-GSGAITSLVRADGFIEIP 393
|
410
....*....|..
gi 1858325166 397 PTKTGIVSGEIV 408
Cdd:PRK14498 394 ANTEGLEAGEEV 405
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
7-417 |
7.53e-86 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 273.03 E-value: 7.53e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 7 KAMTVEAARELLQSRVRPVEPTE-VELAEAIGRRLAAPIrtVEPI--PHFRRSGMDGYAIRTADIAHASAALPIELEIIE 83
Cdd:PRK14491 197 AFLSVSQGLDKILSLVTPVTETEdVALDELDGRVLAQDV--ISPVnvPQHTNSAMDGYAFRSDDLEPESYTLVGEVLAGH 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 84 HIPcgkEPLysiTEGKAARIMTGGMVPDGADAVIMQEmtEAVEHNGrsIVRIQKKIAPGLNITPIGEEAGEGTLVIEAGE 163
Cdd:PRK14491 275 QYD---GTL---QAGEAVRIMTGAPVPAGADTVVMRE--LATQDGD--KVSFDGGIKAGQNVRLAGEDLAQGQVALAAGT 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 164 KLGAGHTAILAALGYNRVPVYRKPKVAVLSTGTELLRLTDPLQMGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDypkaE 243
Cdd:PRK14491 345 RLSAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDS----E 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 244 RMLYDLL---ASDADLIVTSGGVSVGDydsmADFF---LRWEGTTLFNKIAMRPGSPTTAGAWKDKLLFGLSGNPSACFV 317
Cdd:PRK14491 421 AALEATLeqaAAQADVVISSGGVSVGD----ADYIktaLAKLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMV 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 318 GFELFVRPVIQQLQGAVVDTAKTVTCLLAADYEKVNAYTRYVRGQWY-SSGGNHYAKPVGRDKSSTILSLKDANCLIVIP 396
Cdd:PRK14491 497 SFLQFVEPALRKLAGEQNWQPLLFPAIADETLRSRQGRTEFSRGIYHlGADGRLHVRTTGKQGSGILSSMSEANCLIEIG 576
|
410 420
....*....|....*....|.
gi 1858325166 397 PTKTGIVSGEIVQIIPLDGAL 417
Cdd:PRK14491 577 PAAETVNAGETVTIQPLAGLL 597
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
9-411 |
2.42e-70 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 233.94 E-value: 2.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 9 MTVEAARELLQSRVRPVEPTEVELAEAIGRRLAAPIRTVEPIPHFRRSGMDGYAIRTADiahasaaLPIELEIIEHIPCG 88
Cdd:PLN02699 8 ISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASD-------GPGEYPVITESRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 89 KEPL-YSITEGKAARIMTGGMVPDGADAVIMQEMTEAVEH--NGRSIVRIQKKIAPGLNITPIGEEAGEGTLVIEAGEKL 165
Cdd:PLN02699 81 NDGLgVTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDplDGSKRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 166 GAGHTAILAALGYNRVPVYRKPKVAVLSTGTELLRLTDP-LQMGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDYPKAER 244
Cdd:PLN02699 161 GASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 245 MLYDLLASDADLIVTSGGVSVGDYDSMADFFLRwEGTTLFNKIAMRPGSPTT---------AGAWKDKLLFGLSGNPSAC 315
Cdd:PLN02699 241 ILDEAISSGVDILLTSGGVSMGDRDFVKPLLEK-RGTVYFSKVLMKPGKPLTfaeidaksaPSNSKKMLAFGLPGNPVSC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 316 FVGFELFVRPVIQQLQG-AVVDTAKTVTCL---LAADYEKVNAYTRYVRGQWYSSGGN--HYAKPVGRDKSSTILSLKDA 389
Cdd:PLN02699 320 LVCFNLFVVPAIRYLAGwSNPHLLRVQARLrepIKLDPVRPEFHRAIIRWKLNDGSGNpgFVAESTGHQMSSRLLSMKSA 399
|
410 420
....*....|....*....|..
gi 1858325166 390 NCLIVIPPTKTGIVSGEIVQII 411
Cdd:PLN02699 400 NALLELPATGNVLSAGTSVSAI 421
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
9-412 |
2.56e-62 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 206.48 E-value: 2.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 9 MTVEAARELLQSRVRPVEPTE-VELAEAIGRRLAAPIrtVEPI--PHFRRSGMDGYAIRTADIAhASAALPIELEIIEHI 85
Cdd:PRK10680 8 MSLETALTEMLSRVTPLTATEtLPLVQCFGRITASDI--VSPLdvPGFDNSAMDGYAVRLADLA-SGQPLPVAGKAFAGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 86 PC-GKEPlysitEGKAARIMTGGMVPDGADAVIMQEMTEAVEHNgrsiVRIQKKIAPGLNITPIGEEAGEGTLVIEAGEK 164
Cdd:PRK10680 85 PFhGEWP-----AGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDG----VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 165 LGAGHTAILAALGYNRVPVYRKPKVAVLSTGTELLRLTDPLQMGKIRNSN--AYMLMAQiiAAGAQPLLVGQIPDDyPKA 242
Cdd:PRK10680 156 LTTAELPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNrlAVHLMLE--QLGCEVINLGIIRDD-PHA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 243 ERMLYDLLASDADLIVTSGGVSVGDydsmADF---FLRWEGTTLFNKIAMRPGSPTTAGAWKDKLLFGLSGNPSACFVGF 319
Cdd:PRK10680 233 LRAAFIEADSQADVVISSGGVSVGE----ADYtktILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 320 ELFVRPVIQQLQG------AVVDTAKTVTCLlaadyEKVNAYTRYVRGQWYSSG-GNHYAKPVGRDKSSTILSLKDANCL 392
Cdd:PRK10680 309 YQLVQPLLAKLSGntasglPPRQRVRTASRL-----KKTPGRLDFQRGILQRNAdGELEVTTTGHQGSHIFSSFSLGNCF 383
|
410 420
....*....|....*....|
gi 1858325166 393 IVIPPTKTGIVSGEIVQIIP 412
Cdd:PRK10680 384 IVLERERGNVEVGEWVEVEP 403
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
12-410 |
7.68e-51 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 179.62 E-value: 7.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 12 EAARELLQSRVRPVEPTEVELAEAIGRRLAAPIRTVEPIPHFRRSGMDGYAIRtadiahaSAALPIELEIIEHIPCGKEP 91
Cdd:PRK14497 15 EAIKVFLSSLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALK-------SSCTPGEFKVIDKIGIGEFK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 92 LYSITEGKAARIMTGGMVPDGADAVIMQEMTEAVEHNgrsIVRIQKKIAPGLNITPIGEEAGEGTLVIEAGEKLGAGHTA 171
Cdd:PRK14497 88 EIHIKECEAVEVDTGSMIPMGADAVIKVENTKVINGN---FIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 172 ILAALGYNRVPVYRKPKVAVLSTGTELLRLTDPLQMGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDYPKAERMLYDLLa 251
Cdd:PRK14497 165 LLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAI- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 252 SDADLIVTSGGVSVGDYDSMADfFLRWEGTTLFNKIAMRPGSPTTAGAWKDKLLFGLSGNPSACFVGFELFVRPVIQQLQ 331
Cdd:PRK14497 244 SVADVLILTGGTSAGEKDFVHQ-AIRELGNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 332 GAVVDTAK--TVTCLLA----ADYEKVNAYTRYVrgqwYSSGGNHYAKPVGRDkSSTILSLKDANCLIVIPPTkTGIVSG 405
Cdd:PRK14497 323 PSRKEILGlgKIKARLAlrvkADEHRNTLIPVYL----FKSDNSYYALPVPFD-SYMVGTFSLTDGYIMLGPN-EEIEEG 396
|
....*
gi 1858325166 406 EIVQI 410
Cdd:PRK14497 397 KEVEV 401
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
11-412 |
2.41e-50 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 175.49 E-value: 2.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 11 VEAARELLQSRVRPVEPTE-VELAEAIGRRLAAPIRTVEPIPHFRRSGMDGYAIRTADIAHASAALPIELEIIEHIPCGK 89
Cdd:PRK14690 25 VDTALDLLRARLGPVTDIKeLDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQVLPLIEGRAAAGVPFSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 90 eplySITEGKAARIMTGGMVPDGADAVIMQEmteAVEHNGRSIVrIQKKIAPGLNITPIGEEAGEGTLVIEAGEKLGAGH 169
Cdd:PRK14690 105 ----RVPEGMALRILTGAALPEGVDTVVLEE---DVAGDGHRIA-FHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPAD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 170 TAILAALGYNRVPVYRKPKVAVLSTGTELLRLTDPLQMGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDYpKAERMLYDL 249
Cdd:PRK14690 177 LALLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDR-AALAARLDR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 250 LASDADLIVTSGGVSVGDYDSMADFfLRWEGTTLFNKIAMRPGSPTTAGAWKDKLLFGLSGNPSACFVGFELFVRPVIQQ 329
Cdd:PRK14690 256 AAAEADVILTSGGASAGDEDHVSAL-LREAGAMQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 330 LQGAVVDTAKTVTCLLAADYEKVNAYTRYVRGQWYSSggnhYAKPVGRDKSSTILSLKDANCLIVIPPTKTGIVSGEIVQ 409
Cdd:PRK14690 335 LAGEGWSEPQGFTVPAAFEKRKKPGRREYLRARLRQG----HAEVFRSEGSGRISGLSWAEGLVELGDGARRIAPGDPVR 410
|
...
gi 1858325166 410 IIP 412
Cdd:PRK14690 411 FIP 413
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
22-177 |
4.31e-44 |
|
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: 150.41 E-value: 4.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 22 VRPVEPTEVELAEAIGRRLAAPIRTVEPIPHFRRSGMDGYAIRTADIAHASAALPieleiiehIPCGKEPLYSITEGKAA 101
Cdd:pfam03453 3 LGTEETVPLEALDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLPGGEAV 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1858325166 102 RIMTGGMVPDGADAVIMQEMTEAVehnGRSIVRIQKKIAPGLNITPIGEEAGEGTLVIEAGEKLGAGHTAILAALG 177
Cdd:pfam03453 75 RIMTGAPLPEGADAVVMVEDTEEG---GGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
187-325 |
4.27e-34 |
|
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.
Pssm-ID: 272944 [Multi-domain] Cd Length: 148 Bit Score: 124.35 E-value: 4.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 187 PKVAVLSTGTELLRLTDPLQMGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDYPKAERMLYDLLAsDADLIVTSGGVSVG 266
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVD-EADVVLTTGGTGVG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1858325166 267 DYD----SMADFFLRW-EGTTLFNK-----IAMRPGSPTTAGAWKDKLLFGLSGNPSACFVGFELFVRP 325
Cdd:TIGR00177 80 PRDvtpeALEELGEKEiPGFGEFRMlsslpVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
190-327 |
1.09e-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: 101.56 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 190 AVLSTGTELLRltdplqmGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDYPKAERMLyDLLASDADLIVTSGGVSVGDYD 269
Cdd:pfam00994 1 AIITTGDELLP-------GQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEAL-RAAAEEADVVITTGGTGPGPDD 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1858325166 270 ----SMADFFLR--WEGTTLFNKIAMRPGSPTTAGAW-----KDKLLFGLSGNPSACFVGFELFVRPVI 327
Cdd:pfam00994 73 vtpeALAELGGRelPGFEELFRGVSLKPGKPVGTAPGailsrAGKTVFGLPGSPVAAKVMFELLLLPLL 141
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
190-322 |
1.71e-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 trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 100.74 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 190 AVLSTGTELLRLtdplqmGKIRNSNAYMLMAQIIAAGAQP--LLVGQIPDDYPKAERMLYDLLAsDADLIVTSGGVSVGD 267
Cdd:smart00852 1 AIISTGDELLSG------GQIRDSNGPMLAALLRELGIEVvrVVVVGGPDDPEAIREALREALA-EADVVITTGGTGPGP 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1858325166 268 YDSMADFFLRWEGTTLFN-KIAMRPGSPTT---------AGAWKDKLLFGLSGNPSACFVGFELF 322
Cdd:smart00852 74 DDLTPEALAELGGRELLGhGVAMRPGGPPGplanlsgtaPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
188-327 |
1.30e-18 |
|
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: 81.62 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858325166 188 KVAVLSTGTELLRltdplqmGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDYPKAERMLyDLLASDADLIVTSGGVSVGD 267
Cdd:cd00758 1 RVAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAAL-IEASREADLVLTTGGTGVGR 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1858325166 268 YDSMADFFLRW-EGTTLFNKIAMRPGSPTTAGAWKDKLLFGLSGNPSACFVGFELFVRPVI 327
Cdd:cd00758 73 RDVTPEALAELgEREAHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
345-413 |
1.51e-13 |
|
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: 65.33 E-value: 1.51e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1858325166 345 LAADYEKVNAYTRYVRGQWYSSGGNHYAKPVGRDKSSTILSLKDANCLIVIPPTKTGIVSGEIVQIIPL 413
Cdd:pfam03454 4 LARDLKSDPGRREFVRVRLHEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
188-262 |
1.38e-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: 1.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1858325166 188 KVAVLSTGTELLrltdplqMGKIRNSNAYMLMAQIIAAGAQPLLVGQIPDDypkAERML--YDLLASDADLIVTSGG 262
Cdd:cd00885 1 TAEIIAIGDELL-------SGQIVDTNAAFLAKELAELGIEVYRVTVVGDD---EDRIAeaLRRASERADLVITTGG 67
|
|
| |
