|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
1-407 |
3.23e-151 |
|
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: 433.75 E-value: 3.23e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 1 MAPLSSALSALRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDG--AWLPISQRIAAGQ- 77
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAnpVTLRVVGEIAAGSp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 78 PTSALASASCARLFTGAEIPEGADVVVMQEEVTLRENEngtteAWLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAM 157
Cdd:COG0303 81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDR-----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 158 LGLLCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALAT 237
Cdd:COG0303 156 LGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGI-VPDDPEALRAALRE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 238 AAEQADLIVTCGGVSVGEEDHVRPAIEALG-SLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLR 316
Cdd:COG0303 235 ALAEADLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRL-----GGKPVFGLPGNPVSALVTFELFVR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 317 PMLGEMLECDAlRALRSLRVRSAFS-ANTAIRQDHLRVTLTPaDDGQLEAHAFPDQNSAVLSSCVGAEALAVIPPHAQ-I 394
Cdd:COG0303 310 PALRKLAGLPP-PPPPRVRARLAEDlPKKPGRTEFLRVRLER-DDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEgV 387
|
410
....*....|...
gi 1062421413 395 SPGDSVECLWLES 407
Cdd:COG0303 388 EAGEEVEVLLLDG 400
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
7-405 |
1.07e-144 |
|
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: 416.89 E-value: 1.07e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 7 ALSALRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDGAW-LPISQRIAAGQ-PTSALAS 84
Cdd:cd00887 4 ARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtLRVVGEIPAGEpPDGPLGP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 85 ASCARLFTGAEIPEGADVVVMQEEVTLRENEngtteAWLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGLLCGQ 164
Cdd:cd00887 84 GEAVRIMTGAPLPEGADAVVMVEDTEEEGGR-----VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 165 GLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALATAAEQADL 244
Cdd:cd00887 159 GIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGI-VPDDPEALREALEEALEEADV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 245 IVTCGGVSVGEEDHVRPAIEAL-GSLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLRPMLGEML 323
Cdd:cd00887 238 VITSGGVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRL-----GGKPVFGLPGNPVSALVTFELFVRPALRKLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 324 eCDALRALRSLRVRSAFS-ANTAIRQDHLRVTLTPaDDGQLEAHAFPDQNSAVLSSCVGAEALAVIPPHAQ-ISPGDSVE 401
Cdd:cd00887 313 -GAPEPEPPRVKARLAEDlKSKPGRREFLRVRLER-DEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEgLEAGEEVE 390
|
....
gi 1062421413 402 CLWL 405
Cdd:cd00887 391 VLLL 394
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
3-378 |
2.37e-92 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 283.91 E-value: 2.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 3 PLSSALSA-LRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDGAWLPISQRIAAGQP-TS 80
Cdd:PRK10680 9 SLETALTEmLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKAFAGQPfHG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 81 ALASASCARLFTGAEIPEGADVVVMQEEVtlRENENGTTeawLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGL 160
Cdd:PRK10680 89 EWPAGTCIRIMTGAPVPEGCEAVVMQEQT--EQTDDGVR---FTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 161 LCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALATAAE 240
Cdd:PRK10680 164 LASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGI-IRDDPHALRAAFIEADS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 241 QADLIVTCGGVSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRILNTQgdsvrVVGLPGNPVSSWVGGWLFLRPMLG 320
Cdd:PRK10680 243 QADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSW-----FCGLPGNPVSAALTFYQLVQPLLA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1062421413 321 EMLECDALRALRSLRVRSA-FSANTAIRQDHLRVTLTPADDGQLEAHAFPDQNSAVLSS 378
Cdd:PRK10680 318 KLSGNTASGLPPRQRVRTAsRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSS 376
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
16-165 |
1.59e-39 |
|
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: 138.08 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 16 PVMPVEQVPV--SKAAGRVLAEDIYAELDVPPADNSQMDGYCARVAdigDGAWLPISQRIAAGQPTSA-LASASCARLFT 92
Cdd:pfam03453 2 LLGTEETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAA---DGFGASEVNPIAAGEPPGPlLPGGEAVRIMT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062421413 93 GAEIPEGADVVVMQEEVTLRENENGTTEAwlpgPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGLLCGQG 165
Cdd:pfam03453 79 GAPLPEGADAVVMVEDTEEGGGRTVEIRA----PVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-310 |
5.07e-31 |
|
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: 115.38 E-value: 5.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 178 ALFATGDELiepgqpLEPGQIYNSNRVMLSQMLSDFGADVVLAPLN-VADTFEATRDALATAAEQADLIVTCGGVSVGEE 256
Cdd:smart00852 1 AIISTGDEL------LSGGQIRDSNGPMLAALLRELGIEVVRVVVVgGPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062421413 257 DHVRPAIEALGSLDL--WRLAIKPGKP-----LALGRILNTQGDSVrVVGLPGNPVSSWVG 310
Cdd:smart00852 75 DLTPEALAELGGRELlgHGVAMRPGGPpgplaNLSGTAPGVRGKKP-VFGLPGNPVAALVM 134
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
175-317 |
6.16e-30 |
|
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: 112.80 E-value: 6.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 175 VRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVlAPLNVADTFEATRDALATAAEQADLIVTCGGVSVG 254
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVV-RLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062421413 255 EEDHVRPAIEALG-----------SLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLRP 317
Cdd:TIGR00177 80 PRDVTPEALEELGekeipgfgefrMLSSLPVLSRPGKPATAGVR-----GGTLIFNLPGNPVSALVTFEVLILP 148
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
1-407 |
3.23e-151 |
|
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: 433.75 E-value: 3.23e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 1 MAPLSSALSALRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDG--AWLPISQRIAAGQ- 77
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAnpVTLRVVGEIAAGSp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 78 PTSALASASCARLFTGAEIPEGADVVVMQEEVTLRENEngtteAWLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAM 157
Cdd:COG0303 81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDR-----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 158 LGLLCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALAT 237
Cdd:COG0303 156 LGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGI-VPDDPEALRAALRE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 238 AAEQADLIVTCGGVSVGEEDHVRPAIEALG-SLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLR 316
Cdd:COG0303 235 ALAEADLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRL-----GGKPVFGLPGNPVSALVTFELFVR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 317 PMLGEMLECDAlRALRSLRVRSAFS-ANTAIRQDHLRVTLTPaDDGQLEAHAFPDQNSAVLSSCVGAEALAVIPPHAQ-I 394
Cdd:COG0303 310 PALRKLAGLPP-PPPPRVRARLAEDlPKKPGRTEFLRVRLER-DDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEgV 387
|
410
....*....|...
gi 1062421413 395 SPGDSVECLWLES 407
Cdd:COG0303 388 EAGEEVEVLLLDG 400
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
7-405 |
1.07e-144 |
|
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: 416.89 E-value: 1.07e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 7 ALSALRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDGAW-LPISQRIAAGQ-PTSALAS 84
Cdd:cd00887 4 ARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtLRVVGEIPAGEpPDGPLGP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 85 ASCARLFTGAEIPEGADVVVMQEEVTLRENEngtteAWLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGLLCGQ 164
Cdd:cd00887 84 GEAVRIMTGAPLPEGADAVVMVEDTEEEGGR-----VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 165 GLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALATAAEQADL 244
Cdd:cd00887 159 GIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGI-VPDDPEALREALEEALEEADV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 245 IVTCGGVSVGEEDHVRPAIEAL-GSLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLRPMLGEML 323
Cdd:cd00887 238 VITSGGVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRL-----GGKPVFGLPGNPVSALVTFELFVRPALRKLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 324 eCDALRALRSLRVRSAFS-ANTAIRQDHLRVTLTPaDDGQLEAHAFPDQNSAVLSSCVGAEALAVIPPHAQ-ISPGDSVE 401
Cdd:cd00887 313 -GAPEPEPPRVKARLAEDlKSKPGRREFLRVRLER-DEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEgLEAGEEVE 390
|
....
gi 1062421413 402 CLWL 405
Cdd:cd00887 391 VLLL 394
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
3-378 |
2.37e-92 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 283.91 E-value: 2.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 3 PLSSALSA-LRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDGAWLPISQRIAAGQP-TS 80
Cdd:PRK10680 9 SLETALTEmLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKAFAGQPfHG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 81 ALASASCARLFTGAEIPEGADVVVMQEEVtlRENENGTTeawLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGL 160
Cdd:PRK10680 89 EWPAGTCIRIMTGAPVPEGCEAVVMQEQT--EQTDDGVR---FTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 161 LCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALATAAE 240
Cdd:PRK10680 164 LASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGI-IRDDPHALRAAFIEADS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 241 QADLIVTCGGVSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRILNTQgdsvrVVGLPGNPVSSWVGGWLFLRPMLG 320
Cdd:PRK10680 243 QADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSW-----FCGLPGNPVSAALTFYQLVQPLLA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1062421413 321 EMLECDALRALRSLRVRSA-FSANTAIRQDHLRVTLTPADDGQLEAHAFPDQNSAVLSS 378
Cdd:PRK10680 318 KLSGNTASGLPPRQRVRTAsRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSS 376
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
16-400 |
4.98e-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: 4.98e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 16 PVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDGAWlPISQRIAAGQPTSALASASCA-RLFTGA 94
Cdd:PRK14491 214 PVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESY-TLVGEVLAGHQYDGTLQAGEAvRIMTGA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 95 EIPEGADVVVMQEEVTLRENE---NGTTEAwlpgpripGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGLLCGQGLSYVSV 171
Cdd:PRK14491 293 PVPAGADTVVMRELATQDGDKvsfDGGIKA--------GQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPV 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 172 RHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVlaPLNVA-DTFEATRDALATAAEQADLIVTCGG 250
Cdd:PRK14491 365 FRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVI--DLGIIeDSEAALEATLEQAAAQADVVISSGG 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 251 VSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRIlntqGDSVrVVGLPGNPVSSWVGGWLFLRPML----GE----- 321
Cdd:PRK14491 443 VSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQI----GDSP-FFGLPGNPVAVMVSFLQFVEPALrklaGEqnwqp 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 322 -MLECDALRALRSLRVRSAFSantairqdhlRVTLTPADDGQLEAHAFPDQNSAVLSSCVGAEALAVI-PPHAQISPGDS 399
Cdd:PRK14491 518 lLFPAIADETLRSRQGRTEFS----------RGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIgPAAETVNAGET 587
|
.
gi 1062421413 400 V 400
Cdd:PRK14491 588 V 588
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
8-401 |
2.37e-83 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 267.08 E-value: 2.37e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 8 LSALREccPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADI-----GDGAWLPISQRIAAGQ-PTSA 81
Cdd:PRK14498 20 ESLLSE--LPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTfgaseANPVRLKLGGEVHAGEaPDVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 82 LASASCARLFTGAEIPEGADVVVMQEEVTLRENENGTTEAwlpgPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGLL 161
Cdd:PRK14498 98 VEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYR----PVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 162 CGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALATAAEQ 241
Cdd:PRK14498 174 AAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGI-VPDDEEELEAALRKALKE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 242 ADLIVTCGGVSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLRPMLGE 321
Cdd:PRK14498 253 CDLVLLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVI-----GGKPVVGLPGYPVSALTIFEEFVAPLLRK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 322 ML-----ECDALRALRSLRVRSAFSantaiRQDHLRVTLTPADDGQLeahAFP-DQNSAVLSSCVGAEALAVIPPHAQ-I 394
Cdd:PRK14498 328 LAglpppERATVKARLARRVRSELG-----REEFVPVSLGRVGDGYV---AYPlSRGSGAITSLVRADGFIEIPANTEgL 399
|
....*..
gi 1062421413 395 SPGDSVE 401
Cdd:PRK14498 400 EAGEEVE 406
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
3-400 |
7.67e-73 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 234.04 E-value: 7.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 3 PLSSALSALRE-CCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDGAWLPISQ-RIAAGQPTS 80
Cdd:PRK14690 24 PVDTALDLLRArLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQVLPLIEgRAAAGVPFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 81 ALASASCA-RLFTGAEIPEGADVVVMQEEVTLrenenGTTEAWLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLG 159
Cdd:PRK14690 104 GRVPEGMAlRILTGAALPEGVDTVVLEEDVAG-----DGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 160 LLCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFG-ADVVLAplNVADTFEATRDALATA 238
Cdd:PRK14690 179 LLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGhAPVDLG--RVGDDRAALAARLDRA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 239 AEQADLIVTCGGVSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRilnTQGdsVRVVGLPGNPVSSWVGGWLFLRPM 318
Cdd:PRK14690 257 AAEADVILTSGGASAGDEDHVSALLREAGAMQSWRIALKPGRPLALGL---WQG--VPVFGLPGNPVAALVCTLVFARPA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 319 LGeMLECDALRALRSLRVRSAFSANT-AIRQDHLRVTLTpadDGQLEahAFPDQNSAVLSSCVGAEALAVIPPHA-QISP 396
Cdd:PRK14690 332 MS-LLAGEGWSEPQGFTVPAAFEKRKkPGRREYLRARLR---QGHAE--VFRSEGSGRISGLSWAEGLVELGDGArRIAP 405
|
....
gi 1062421413 397 GDSV 400
Cdd:PRK14690 406 GDPV 409
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
11-401 |
7.61e-53 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 184.63 E-value: 7.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 11 LRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCA---------RVAD-IGDGAWLPIsqRIAAGQpts 80
Cdd:PRK14497 21 LSSLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALkssctpgefKVIDkIGIGEFKEI--HIKECE--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 81 alasasCARLFTGAEIPEGADVVVMQEEVTLREnengtteawlpGPRIP-------GDNIRRQGRDVTRGTRLIAAGTRL 153
Cdd:PRK14497 96 ------AVEVDTGSMIPMGADAVIKVENTKVIN-----------GNFIKidkkinfGQNIGWIGSDIPKGSIILRKGEVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 154 DAAMLGLLCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRD 233
Cdd:PRK14497 159 SHEKIGLLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSL-LSDDKESIKN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 234 ALATAAEQADLIVTCGGVSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWvggwl 313
Cdd:PRK14497 238 EIKRAISVADVLILTGGTSAGEKDFVHQAIRELGNIIVHGLKIKPGKPTILGIV-----DGKPVIGLPGNIVSTM----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 314 flrpMLGEMLECDALRALRSLRVR-------SAFSANtAIRQDHLRVTLTPA----DDGQLEAHAFPdQNSAVLSSCVGA 382
Cdd:PRK14497 308 ----VVLNMVILEYLKSLYPSRKEilglgkiKARLAL-RVKADEHRNTLIPVylfkSDNSYYALPVP-FDSYMVGTFSLT 381
|
410
....*....|....*....
gi 1062421413 383 EALAVIPPHAQISPGDSVE 401
Cdd:PRK14497 382 DGYIMLGPNEEIEEGKEVE 400
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
1-403 |
3.10e-45 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 165.76 E-value: 3.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 1 MAPLSSALSALRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYcARVADIGDGAWlPISQRIAAGQPTS 80
Cdd:PLN02699 7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGY-AVVASDGPGEY-PVITESRAGNDGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 81 A--LASASCARLFTGAEIPEGADVVVMQEEVTLRENENGTTEAwlpgPRI-----PGDNIRRQGRDVTRGTRLIAAGTRL 153
Cdd:PLN02699 85 GvtLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR----VRIlsqasKGQDIRPVGCDIEKDAKVLKAGERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 154 DAAMLGLLCGQGLSYVSVRHKVRVALFATGDELIEPGQP-LEPGQIYNSNRVMLSQMLSDFGADVVlaPLNVA-DTFEAT 231
Cdd:PLN02699 161 GASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVV--DLGIArDDEEEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 232 RDALATA-AEQADLIVTCGGVSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRILNTQGDS----VRVVGLPGNPVS 306
Cdd:PLN02699 239 ERILDEAiSSGVDILLTSGGVSMGDRDFVKPLLEKRGTVYFSKVLMKPGKPLTFAEIDAKSAPSnskkMLAFGLPGNPVS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 307 SWVGGWLFLRPMLGEMLECDALRALR-SLRVRSAFSANtAIRQDHLRVTLT-PADDGQLE----AHAFPDQNSAVLSSCV 380
Cdd:PLN02699 319 CLVCFNLFVVPAIRYLAGWSNPHLLRvQARLREPIKLD-PVRPEFHRAIIRwKLNDGSGNpgfvAESTGHQMSSRLLSMK 397
|
410 420
....*....|....*....|....
gi 1062421413 381 GAEALAVIPP-HAQISPGDSVECL 403
Cdd:PLN02699 398 SANALLELPAtGNVLSAGTSVSAI 421
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
16-165 |
1.59e-39 |
|
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: 138.08 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 16 PVMPVEQVPV--SKAAGRVLAEDIYAELDVPPADNSQMDGYCARVAdigDGAWLPISQRIAAGQPTSA-LASASCARLFT 92
Cdd:pfam03453 2 LLGTEETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAA---DGFGASEVNPIAAGEPPGPlLPGGEAVRIMT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062421413 93 GAEIPEGADVVVMQEEVTLRENENGTTEAwlpgPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGLLCGQG 165
Cdd:pfam03453 79 GAPLPEGADAVVMVEDTEEGGGRTVEIRA----PVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-310 |
5.07e-31 |
|
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: 115.38 E-value: 5.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 178 ALFATGDELiepgqpLEPGQIYNSNRVMLSQMLSDFGADVVLAPLN-VADTFEATRDALATAAEQADLIVTCGGVSVGEE 256
Cdd:smart00852 1 AIISTGDEL------LSGGQIRDSNGPMLAALLRELGIEVVRVVVVgGPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062421413 257 DHVRPAIEALGSLDL--WRLAIKPGKP-----LALGRILNTQGDSVrVVGLPGNPVSSWVG 310
Cdd:smart00852 75 DLTPEALAELGGRELlgHGVAMRPGGPpgplaNLSGTAPGVRGKKP-VFGLPGNPVAALVM 134
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-319 |
6.70e-31 |
|
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: 115.42 E-value: 6.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 178 ALFATGDELIepgqplePGQIYNSNRVMLSQMLSDFGADVVlAPLNVADTFEATRDALATAAEQADLIVTCGGVSVGEED 257
Cdd:pfam00994 1 AIITTGDELL-------PGQIRDTNGPLLAALLREAGAEVI-RYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDD 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062421413 258 HVRPAIEALG-------SLDLWRLAIKPGKPLALGRILNTQGDSVRVVGLPGNPVSSWVGGWLFLRPML 319
Cdd:pfam00994 73 VTPEALAELGgrelpgfEELFRGVSLKPGKPVGTAPGAILSRAGKTVFGLPGSPVAAKVMFELLLLPLL 141
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
175-317 |
6.16e-30 |
|
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: 112.80 E-value: 6.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 175 VRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVlAPLNVADTFEATRDALATAAEQADLIVTCGGVSVG 254
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVV-RLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062421413 255 EEDHVRPAIEALG-----------SLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLRP 317
Cdd:TIGR00177 80 PRDVTPEALEELGekeipgfgefrMLSSLPVLSRPGKPATAGVR-----GGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
176-319 |
3.13e-22 |
|
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: 91.64 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 176 RVALFATGDELIepgqplePGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALATAAEQADLIVTCGGVSVGE 255
Cdd:cd00758 1 RVAIVTVSDELS-------QGQIEDTNGPALEALLEDLGCEVIYAGV-VPDDADSIRAALIEASREADLVLTTGGTGVGR 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062421413 256 EDHVRPAIEALGSLDLW--RLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLRPML 319
Cdd:cd00758 73 RDVTPEALAELGEREAHgkGVALAPGSRTAFGII-----GKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
347-401 |
2.53e-07 |
|
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: 47.61 E-value: 2.53e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1062421413 347 RQDHLRVTLTpADDGQLEAHAFPDQNSAVLSSCVGAEALAVIPPH-AQISPGDSVE 401
Cdd:pfam03454 14 RREFVRVRLH-EEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGtEGLEAGEEVE 68
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
176-250 |
5.32e-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: 46.32 E-value: 5.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062421413 176 RVALFATGDELIepgqplePGQIYNSNRVMLSQMLSDFGADVVLApLNVADTFEATRDALATAAEQADLIVTCGG 250
Cdd:cd00885 1 TAEIIAIGDELL-------SGQIVDTNAAFLAKELAELGIEVYRV-TVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
181-250 |
6.87e-04 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 41.70 E-value: 6.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 181 ATGDELIEpgqplepGQIYNSNRVMLSQMLSDFGADVVLApLNVADTFEATRDALATAAEQADLIVTCGG 250
Cdd:PRK00549 7 AVGTELLL-------GQIVNTNAQFLSEKLAELGIDVYHQ-TVVGDNPERLLSALEIAEERSDLIITTGG 68
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
210-302 |
1.09e-03 |
|
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: 40.61 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 210 LSDFGADVVLAPLnVADTFEATRDALATAAEQADLIVTC-GGVSVGEEDHVRPAIEALG-SLDLWRLAIKPGKPLALGRI 287
Cdd:cd03522 188 LAALGVELVEQVI-VPHDEAAIAAAIAEALEAGAELLILtGGASVDPDDVTPAAIRAAGgEVIRYGMPVDPGNLLLLGYL 266
|
90
....*....|....*
gi 1062421413 288 lntqgDSVRVVGLPG 302
Cdd:cd03522 267 -----GGVPVIGLPG 276
|
|
|