|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
1-409 |
1.14e-121 |
|
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: 358.63 E-value: 1.14e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 1 MRSITEHLAAAHALAVPGTPVTVPVDRALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADLAGPGPWSLPVAGDVPAGAA 80
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 81 -AREVTPGHALRIMTGAPV---GDehagvRVIPVEDTDIAPGpgplpaVVTVDAVHRDRNHIRRAGENTAVGEEVMPIGT 156
Cdd:COG0303 81 pPGPLGPGEAVRIMTGAPLpegAD-----AVVMQEDTEREGD------RVTIRKPVAPGENIRRAGEDIAAGDVLLPAGT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 157 RIDAGALAALVSCGIPSVTVHPRPRVAVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELGVTATNM-HAGDDTRAFG 235
Cdd:COG0303 150 RLTPADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLgIVPDDPEALR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 236 TLLDELCATHDLVITTGGVSVGAFDVVREVTGS--GDMWFGPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSFCVYAP 313
Cdd:COG0303 230 AALREALAEADLVITSGGVSVGDYDLVKEALEElgAEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 314 GVLATLAGAPTsadlWERPHVTARVADGVtlPASPERAFLAPVRLTYGRDGVTAAPFnrRSTGSHLVGSLAATDGLAVIE 393
Cdd:COG0303 310 PALRKLAGLPP----PPPPRVRARLAEDL--PKKPGRTEFLRVRLERDDGELVVEPL--GGQGSGLLSSLAEADGLIVLP 381
|
410
....*....|....*.
gi 2516283051 394 AGADRPETGSTVRVLL 409
Cdd:COG0303 382 EGVEGVEAGEEVEVLL 397
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
17-409 |
7.57e-117 |
|
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: 346.02 E-value: 7.57e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 17 PGTPVTVPVDRALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADLAGpGPWSLPVAGDVPAGAA-AREVTPGHALRIMTG 95
Cdd:cd00887 14 PLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAG-ASVTLRVVGEIPAGEPpDGPLGPGEAVRIMTG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 96 APVgDEHAGvRVIPVEDTDIAPGpgplpaVVTVDAVHRDRNHIRRAGENTAVGEEVMPIGTRIDAGALAALVSCGIPSVT 175
Cdd:cd00887 93 APL-PEGAD-AVVMVEDTEEEGG------RVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 176 VHPRPRVAVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELGVTATNM-HAGDDTRAFGTLLDELCATHDLVITTGGV 254
Cdd:cd00887 165 VYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLgIVPDDPEALREALEEALEEADVVITSGGV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 255 SVGAFDVVREVTGS--GDMWFGPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSFCVYAPGVLATLAGAPTsadlWERP 332
Cdd:cd00887 245 SVGDYDFVKEVLEElgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPE----PEPP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2516283051 333 HVTARVADGvtLPASPERAFLAPVRLTYGRDGVTAAPFnrRSTGSHLVGSLAATDGLAVIEAGADRPETGSTVRVLL 409
Cdd:cd00887 321 RVKARLAED--LKSKPGRREFLRVRLERDEGGLVVAPP--GGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLL 393
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
20-409 |
1.38e-65 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 220.47 E-value: 1.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 20 PVTVPVDRALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADLAGPG---PWSLPVAGDVPAGAA-AREVTPGHALRIMTG 95
Cdd:PRK14498 30 TEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASeanPVRLKLGGEVHAGEApDVEVEPGEAVEIATG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 96 APVGDEHAGVrvIPVEDTDIApGPGplpAVVTVDAVHRDrNHIRRAGENTAVGEEVMPIGTRIDAGALAALVSCGIPSVT 175
Cdd:PRK14498 110 APIPRGADAV--VMVEDTEEV-DDD---TVEIYRPVAPG-ENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGGVAEVP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 176 VHPRPRVAVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELGVTATNM-HAGDDTRAFGTLLDELCATHDLVITTGGV 254
Cdd:PRK14498 183 VYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYgIVPDDEEELEAALRKALKECDLVLLSGGT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 255 SVGAFDVVREVTGS-GDMWFGPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSFCVYAPGVLATLAGAPTSadlwERPH 333
Cdd:PRK14498 263 SAGAGDVTYRVIEElGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLRKLAGLPPP----ERAT 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2516283051 334 VTARVADGVtlpASPE--RAFLaPVRLTYGRDGVTAAPFNRrstGSHLVGSLAATDGLAVIEAGADRPETGSTVRVLL 409
Cdd:PRK14498 339 VKARLARRV---RSELgrEEFV-PVSLGRVGDGYVAYPLSR---GSGAITSLVRADGFIEIPANTEGLEAGEEVEVEL 409
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
180-308 |
5.38e-32 |
|
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: 118.57 E-value: 5.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 180 PRVAVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELGVTATNM-HAGDDTRAFGTLLDELCATHDLVITTGGVSVGA 258
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLgIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2516283051 259 FDVVREVTGS-GDMWF-----------GPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSF 308
Cdd:TIGR00177 81 RDVTPEALEElGEKEIpgfgefrmlssLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTF 142
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
16-170 |
2.03e-26 |
|
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: 103.42 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 16 VPGTPVTVPVD--RALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADLAGPGPWSLPVAGDVPagaaAREVTPGHALRIM 93
Cdd:pfam03453 2 LLGTEETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIAAGEPP----GPLLPGGEAVRIM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 94 TGAPV---GDehagvRVIPVEDTDiapgpGPLPAVVTVDAVHRDRNHIRRAGENTAVGEEVMPIGTRIDAGALAALVSCG 170
Cdd:pfam03453 78 TGAPLpegAD-----AVVMVEDTE-----EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
183-308 |
1.10e-23 |
|
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: 95.73 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 183 AVLSSGDELVDPGttpgagQLPDSNRPMITALLAELGVTATNMH---AGDDTRAFGTLLDELCATHDLVITTGGVSVGAF 259
Cdd:smart00852 1 AIISTGDELLSGG------QIRDSNGPMLAALLRELGIEVVRVVvvgGPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2516283051 260 DVVREVT---GSGDMWFGPVAQRPGAPQGL---------GTRGGAVLMCLPGNPVAAFVSF 308
Cdd:smart00852 75 DLTPEALaelGGRELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMF 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
1-409 |
1.14e-121 |
|
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: 358.63 E-value: 1.14e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 1 MRSITEHLAAAHALAVPGTPVTVPVDRALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADLAGPGPWSLPVAGDVPAGAA 80
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 81 -AREVTPGHALRIMTGAPV---GDehagvRVIPVEDTDIAPGpgplpaVVTVDAVHRDRNHIRRAGENTAVGEEVMPIGT 156
Cdd:COG0303 81 pPGPLGPGEAVRIMTGAPLpegAD-----AVVMQEDTEREGD------RVTIRKPVAPGENIRRAGEDIAAGDVLLPAGT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 157 RIDAGALAALVSCGIPSVTVHPRPRVAVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELGVTATNM-HAGDDTRAFG 235
Cdd:COG0303 150 RLTPADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLgIVPDDPEALR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 236 TLLDELCATHDLVITTGGVSVGAFDVVREVTGS--GDMWFGPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSFCVYAP 313
Cdd:COG0303 230 AALREALAEADLVITSGGVSVGDYDLVKEALEElgAEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 314 GVLATLAGAPTsadlWERPHVTARVADGVtlPASPERAFLAPVRLTYGRDGVTAAPFnrRSTGSHLVGSLAATDGLAVIE 393
Cdd:COG0303 310 PALRKLAGLPP----PPPPRVRARLAEDL--PKKPGRTEFLRVRLERDDGELVVEPL--GGQGSGLLSSLAEADGLIVLP 381
|
410
....*....|....*.
gi 2516283051 394 AGADRPETGSTVRVLL 409
Cdd:COG0303 382 EGVEGVEAGEEVEVLL 397
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
17-409 |
7.57e-117 |
|
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: 346.02 E-value: 7.57e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 17 PGTPVTVPVDRALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADLAGpGPWSLPVAGDVPAGAA-AREVTPGHALRIMTG 95
Cdd:cd00887 14 PLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAG-ASVTLRVVGEIPAGEPpDGPLGPGEAVRIMTG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 96 APVgDEHAGvRVIPVEDTDIAPGpgplpaVVTVDAVHRDRNHIRRAGENTAVGEEVMPIGTRIDAGALAALVSCGIPSVT 175
Cdd:cd00887 93 APL-PEGAD-AVVMVEDTEEEGG------RVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 176 VHPRPRVAVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELGVTATNM-HAGDDTRAFGTLLDELCATHDLVITTGGV 254
Cdd:cd00887 165 VYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLgIVPDDPEALREALEEALEEADVVITSGGV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 255 SVGAFDVVREVTGS--GDMWFGPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSFCVYAPGVLATLAGAPTsadlWERP 332
Cdd:cd00887 245 SVGDYDFVKEVLEElgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPE----PEPP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2516283051 333 HVTARVADGvtLPASPERAFLAPVRLTYGRDGVTAAPFnrRSTGSHLVGSLAATDGLAVIEAGADRPETGSTVRVLL 409
Cdd:cd00887 321 RVKARLAED--LKSKPGRREFLRVRLERDEGGLVVAPP--GGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLL 393
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
20-409 |
1.38e-65 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 220.47 E-value: 1.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 20 PVTVPVDRALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADLAGPG---PWSLPVAGDVPAGAA-AREVTPGHALRIMTG 95
Cdd:PRK14498 30 TEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASeanPVRLKLGGEVHAGEApDVEVEPGEAVEIATG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 96 APVGDEHAGVrvIPVEDTDIApGPGplpAVVTVDAVHRDrNHIRRAGENTAVGEEVMPIGTRIDAGALAALVSCGIPSVT 175
Cdd:PRK14498 110 APIPRGADAV--VMVEDTEEV-DDD---TVEIYRPVAPG-ENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGGVAEVP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 176 VHPRPRVAVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELGVTATNM-HAGDDTRAFGTLLDELCATHDLVITTGGV 254
Cdd:PRK14498 183 VYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYgIVPDDEEELEAALRKALKECDLVLLSGGT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 255 SVGAFDVVREVTGS-GDMWFGPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSFCVYAPGVLATLAGAPTSadlwERPH 333
Cdd:PRK14498 263 SAGAGDVTYRVIEElGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLRKLAGLPPP----ERAT 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2516283051 334 VTARVADGVtlpASPE--RAFLaPVRLTYGRDGVTAAPFNRrstGSHLVGSLAATDGLAVIEAGADRPETGSTVRVLL 409
Cdd:PRK14498 339 VKARLARRV---RSELgrEEFV-PVSLGRVGDGYVAYPLSR---GSGAITSLVRADGFIEIPANTEGLEAGEEVEVEL 409
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
19-408 |
8.09e-57 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 196.37 E-value: 8.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 19 TPVT----VPVDRALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADLaGPGPWSLPvaGDVPAGAA-AREVTPGHALRIM 93
Cdd:PRK14491 213 TPVTetedVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDL-EPESYTLV--GEVLAGHQyDGTLQAGEAVRIM 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 94 TGAPVGdehAGV-RVIPVEDTDIAPGpgplpaVVTVDAVHRDRNHIRRAGENTAVGEEVMPIGTRIDAGALAALVSCGIP 172
Cdd:PRK14491 290 TGAPVP---AGAdTVVMRELATQDGD------KVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 173 SVTVHPRPRVAVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELGVTATNMH-AGDDTRAFGTLLDELCATHDLVITT 251
Cdd:PRK14491 361 EVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGiIEDSEAALEATLEQAAAQADVVISS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 252 GGVSVGAFDVVREVTGS-GDMWFGPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSFCVYAPGVLATLAGAPTsadlWE 330
Cdd:PRK14491 441 GGVSVGDADYIKTALAKlGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKLAGEQN----WQ 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 331 RPHVTArVADgVTLPASPERA-FLAPVrLTYGRDGVtaapFNRRST---GSHLVGSLAATDGLAVIEAGADRPETGSTVR 406
Cdd:PRK14491 517 PLLFPA-IAD-ETLRSRQGRTeFSRGI-YHLGADGR----LHVRTTgkqGSGILSSMSEANCLIEIGPAAETVNAGETVT 589
|
..
gi 2516283051 407 VL 408
Cdd:PRK14491 590 IQ 591
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
22-407 |
6.15e-50 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 173.74 E-value: 6.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 22 TVPVDRALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADLAGPGPwsLPVAGDVPAGAAAREVTP-GHALRIMTGAPVGd 100
Cdd:PRK10680 29 TLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQP--LPVAGKAFAGQPFHGEWPaGTCIRIMTGAPVP- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 101 ehAGVR-VIPVEDTDIApGPGplpavVTVDAVHRDRNHIRRAGENTAVGEEVMPIGTRIDAGALAALVSCGIPSVTVHPR 179
Cdd:PRK10680 106 --EGCEaVVMQEQTEQT-DDG-----VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 180 PRVAVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELGVTATNMHA-GDDTRAFGTLLDELCATHDLVITTGGVSVGA 258
Cdd:PRK10680 178 VRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIiRDDPHALRAAFIEADSQADVVISSGGVSVGE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 259 FDVVREVTGS-GDMWFGPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSFCVYAPGVLATLAGAPTSAdlwERPHVTAR 337
Cdd:PRK10680 258 ADYTKTILEElGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNTASG---LPPRQRVR 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2516283051 338 VAdgVTLPASPERAFLAPVRLTYGRDGvtaaPFNRRST---GSHLVGSLAATDGLAVIEAGADRPETGSTVRV 407
Cdd:PRK10680 335 TA--SRLKKTPGRLDFQRGILQRNADG----ELEVTTTghqGSHIFSSFSLGNCFIVLERERGNVEVGEWVEV 401
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
22-408 |
3.12e-46 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 164.32 E-value: 3.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 22 TVPVDRALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDAdlAGPGPWSLPV-AGDVPAGAAAREVTP-GHALRIMTGAPVG 99
Cdd:PRK14690 44 ELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGA--APEGAQVLPLiEGRAAAGVPFSGRVPeGMALRILTGAALP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 100 dehAGVRVIPVEDtDIAPGPGPlpavVTVDAVHRDRNHIRRAGENTAVGEEVMPIGTRIDAGALAALVSCGIPSVTVHPR 179
Cdd:PRK14690 122 ---EGVDTVVLEE-DVAGDGHR----IAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 180 PRVAVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELGVTATNM-HAGDDTRAFGTLLDELCATHDLVITTGGVSVGA 258
Cdd:PRK14690 194 LRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLgRVGDDRAALAARLDRAAAEADVILTSGGASAGD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 259 FDVVRE-VTGSGDMWFGPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSFCVYAPGVLATLAGAPtsadlWERPHvtar 337
Cdd:PRK14690 274 EDHVSAlLREAGAMQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEG-----WSEPQ---- 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2516283051 338 vadGVTLPAS------PERAFLAPVRLTYGRDGVTaapfnrRSTGSHLVGSLAATDGLAVIEAGADRPETGSTVRVL 408
Cdd:PRK14690 345 ---GFTVPAAfekrkkPGRREYLRARLRQGHAEVF------RSEGSGRISGLSWAEGLVELGDGARRIAPGDPVRFI 412
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
20-349 |
1.64e-39 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 149.58 E-value: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 20 PVTVPVDRALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADlaGPGPWslPVAGDVPAGAAAREVT--PGHALRIMTGAP 97
Cdd:PLN02699 26 PVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASD--GPGEY--PVITESRAGNDGLGVTltPGTVAYVTTGGP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 98 VGDehAGVRVIPVEDTDIAPGPGPLPAVVTVDAVHRDRNHIRRAGENTAVGEEVMPIGTRIDAGALAALVSCGIPSVTVH 177
Cdd:PLN02699 102 IPD--GADAVVQVEDTEVVEDPLDGSKRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASEIGLLATVGVTMVKVY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 178 PRPRVAVLSSGDELVDPGT-TPGAGQLPDSNRPMITALLAELGVTATNMH-AGDDTRAFGTLLDE-LCATHDLVITTGGV 254
Cdd:PLN02699 180 PRPTVAILSTGDELVEPTTgTLGRGQIRDSNRAMLLAAAIQQQCKVVDLGiARDDEEELERILDEaISSGVDILLTSGGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 255 SVGAFDVVREVTGS-GDMWFGPVAQRPGAP--------QGLGTRGGAVL-MCLPGNPVAAFVSFCVYAPGVLATLAGapt 324
Cdd:PLN02699 260 SMGDRDFVKPLLEKrGTVYFSKVLMKPGKPltfaeidaKSAPSNSKKMLaFGLPGNPVSCLVCFNLFVVPAIRYLAG--- 336
|
330 340
....*....|....*....|....*....
gi 2516283051 325 sadlWERPH---VTARVADGVTL-PASPE 349
Cdd:PLN02699 337 ----WSNPHllrVQARLREPIKLdPVRPE 361
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
17-412 |
1.80e-37 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 142.64 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 17 PGTpVTVPVDRALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADLAGpgpwSLPVAGDVPAGAAAR-EVTPGHALRIMTG 95
Cdd:PRK14497 28 PKI-VKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPG----EFKVIDKIGIGEFKEiHIKECEAVEVDTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 96 APVgDEHAGVrVIPVEDTDIAPGPgplpaVVTVDAVHRDRNHIRRAGENTAVGEEVMPIGTRIDAGALAALVSCGIPSVT 175
Cdd:PRK14497 103 SMI-PMGADA-VIKVENTKVINGN-----FIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 176 VHPRPRVAVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELG---VTATnmHAGDDTRAFGTLLDELCATHDLVITTG 252
Cdd:PRK14497 176 VYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGykiVGLS--LLSDDKESIKNEIKRAISVADVLILTG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 253 GVSVGAFD----VVREVtgsGDMWFGPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSFCVYAPGVLATLAGAPTsaDL 328
Cdd:PRK14497 254 GTSAGEKDfvhqAIREL---GNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPSRK--EI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 329 WERPHVTARVADGVTlpASPERAFLAPVRLTYGRDGVTA--APFNrrstgSHLVGSLAATDGLAVIEAGADRPEtGSTVR 406
Cdd:PRK14497 329 LGLGKIKARLALRVK--ADEHRNTLIPVYLFKSDNSYYAlpVPFD-----SYMVGTFSLTDGYIMLGPNEEIEE-GKEVE 400
|
....*.
gi 2516283051 407 VLLRRL 412
Cdd:PRK14497 401 VDLKKL 406
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
180-308 |
5.38e-32 |
|
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: 118.57 E-value: 5.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 180 PRVAVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELGVTATNM-HAGDDTRAFGTLLDELCATHDLVITTGGVSVGA 258
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLgIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2516283051 259 FDVVREVTGS-GDMWF-----------GPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSF 308
Cdd:TIGR00177 81 RDVTPEALEElGEKEIpgfgefrmlssLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTF 142
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
16-170 |
2.03e-26 |
|
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: 103.42 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 16 VPGTPVTVPVD--RALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADLAGPGPWSLPVAGDVPagaaAREVTPGHALRIM 93
Cdd:pfam03453 2 LLGTEETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIAAGEPP----GPLLPGGEAVRIM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 94 TGAPV---GDehagvRVIPVEDTDiapgpGPLPAVVTVDAVHRDRNHIRRAGENTAVGEEVMPIGTRIDAGALAALVSCG 170
Cdd:pfam03453 78 TGAPLpegAD-----AVVMVEDTE-----EGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
183-308 |
1.10e-23 |
|
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: 95.73 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 183 AVLSSGDELVDPGttpgagQLPDSNRPMITALLAELGVTATNMH---AGDDTRAFGTLLDELCATHDLVITTGGVSVGAF 259
Cdd:smart00852 1 AIISTGDELLSGG------QIRDSNGPMLAALLRELGIEVVRVVvvgGPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2516283051 260 DVVREVT---GSGDMWFGPVAQRPGAPQGL---------GTRGGAVLMCLPGNPVAAFVSF 308
Cdd:smart00852 75 DLTPEALaelGGRELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMF 135
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
183-308 |
4.10e-22 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 91.54 E-value: 4.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 183 AVLSSGDELVdpgttpgAGQLPDSNRPMITALLAELGVTATNM-HAGDDTRAFGTLLDELCATHDLVITTGGVSVGAFDV 261
Cdd:pfam00994 1 AIITTGDELL-------PGQIRDTNGPLLAALLREAGAEVIRYgIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 262 VREVTGS--------GDMWFGPVAQRPGAPQGLGT-----RGGAVLMCLPGNPVAAFVSF 308
Cdd:pfam00994 74 TPEALAElggrelpgFEELFRGVSLKPGKPVGTAPgailsRAGKTVFGLPGSPVAAKVMF 133
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
181-308 |
1.55e-19 |
|
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: 83.93 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 181 RVAVLSSGDELVdpgttpgAGQLPDSNRPMITALLAELGVTATNMH-AGDDTRAFGTLLDELCATHDLVITTGGVSVGAF 259
Cdd:cd00758 1 RVAIVTVSDELS-------QGQIEDTNGPALEALLEDLGCEVIYAGvVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2516283051 260 DVVREVT---GSGDMWFGPVAQRPGAPQGLGTRGGAVLMCLPGNPVAAFVSF 308
Cdd:cd00758 74 DVTPEALaelGEREAHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTF 125
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
335-409 |
1.65e-06 |
|
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: 45.29 E-value: 1.65e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2516283051 335 TARVADGVTLPasPERAFLAPVRLTYGRDGVTAAPFnrRSTGSHLVGSLAATDGLAVIEAGADRPETGSTVRVLL 409
Cdd:pfam03454 1 KARLARDLKSD--PGRREFVRVRLHEEDGRYYAEPI--GKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVIL 71
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
181-253 |
1.25e-04 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 43.18 E-value: 1.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2516283051 181 RVAVLSSGDELVdpgttpgAGQLPDSNRPMITALLAELGVTATNMHA-GDDTRAFGTLLDELCATHDLVITTGG 253
Cdd:COG1058 1 KAEIITIGDELL-------SGRIVDTNAAWLARELAELGIDVYRITTvGDDPERIVEALREALARADLVITTGG 67
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
23-412 |
2.47e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 43.32 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 23 VPVDRALGLVLAAPPVAQLPVPPFSNSAVDGFLVRDADLAGPGPWSLPVAGDVPAGAAAREVTPGHALRIMTGAPVGDEH 102
Cdd:COG3321 845 VPVDWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAA 924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 103 AGVRVIPVEDTDIAPGPGPLPAVVTVDAVHRDRNHIRRAGENTAVGEEVMPIGTRIDAGALAALVSCGIPSVTVHPRPRV 182
Cdd:COG3321 925 ALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALAL 1004
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 183 AVLSSGDELVDPGTTPGAGQLPDSNRPMITALLAELGVTATNMHAGDDTRAFGTLLDELCATHDLVITTGGVSVGAFDVV 262
Cdd:COG3321 1005 LAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAAL 1084
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 263 REVTGSGDMWFGPVAQRPGAPQGLGTRGGAVLMcLPGNPVAAFVSFCVYAPGVLATLAGAPTSADLWERPHVTARVADGV 342
Cdd:COG3321 1085 ALAAALAAAALALALAALAAALLLLALLAALAL-AAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAAL 1163
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516283051 343 TLPASPERAFLAPVRLTYGRDGVTAAPFNRRSTGSHLVGSLAATDGLAVIEAGADRPETGSTVRVLLRRL 412
Cdd:COG3321 1164 AAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAAL 1233
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
181-253 |
1.14e-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: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2516283051 181 RVAVLSSGDELVdpgttpgAGQLPDSNRPMITALLAELGVTATNMHA-GDDTRAFGTLLDELCATHDLVITTGG 253
Cdd:cd00885 1 TAEIIAIGDELL-------SGQIVDTNAAFLAKELAELGIEVYRVTVvGDDEDRIAEALRRASERADLVITTGG 67
|
|
| |
