|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
4-425 |
2.17e-124 |
|
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: 365.95 E-value: 2.17e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 4 LLSIETADRLIGEALAPFGSETVSLLHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRGAQaqgqrtrkqeiPDSF 83
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAN-----------PVTL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 84 VLAATQPAGRPPldlrtivtseNAPLPA--AIAVMTGSVLPHGTDTVIPREDYDLTEGThgtiIRLEDGVHPrkGQHIHS 161
Cdd:COG0303 70 RVVGEIAAGSPP----------PGPLGPgeAVRIMTGAPLPEGADAVVMQEDTEREGDR----VTIRKPVAP--GENIRR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 162 EGSDCAAGTVLLNAGIRLSPPDLAILAANGVAEPRVAIIPSIAIISTGDELVAPDEPVQAWQIRRSNEYAISASLSRKGF 241
Cdd:COG0303 134 AGEDIAAGDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 242 TLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKALAALNVRNVFHKVAQRPGKPFWFGVSDkGQPVFA 321
Cdd:COG0303 214 EVVDLGIVPDDPEALRAALREALAEADLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLG-GKPVFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 322 LPGNPVSALACCSRHVVPALLRAQ---DHALSTRRVVLSEALAPLSGMTRLVPVQLQSDGtGSMRATPHPMPTSGDFNRL 398
Cdd:COG0303 293 LPGNPVSALVTFELFVRPALRKLAglpPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDD-GELVVEPLGGQGSGLLSSL 371
|
410 420
....*....|....*....|....*..
gi 2262111202 399 GMTDGIVSLPPGDRPLQAGDIVTFHEW 425
Cdd:COG0303 372 AEADGLIVLPEGVEGVEAGEEVEVLLL 398
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
7-423 |
7.67e-118 |
|
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: 349.10 E-value: 7.67e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 7 IETADRLIGEALAPFGSETVSLLHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRGAQAqgqrtrkqeipdSFVLA 86
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASV------------TLRVV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 87 ATQPAGRPPldlrtivtseNAPLPA--AIAVMTGSVLPHGTDTVIPREDYDLTEGThgtiIRLEDGVHPrkGQHIHSEGS 164
Cdd:cd00887 69 GEIPAGEPP----------DGPLGPgeAVRIMTGAPLPEGADAVVMVEDTEEEGGR----VTITKPVKP--GQNIRRAGE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 165 DCAAGTVLLNAGIRLSPPDLAILAANGVAEPRVAIIPSIAIISTGDELVAPDEPVQAWQIRRSNEYAISASLSRKGFTLQ 244
Cdd:cd00887 133 DIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 245 SLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKALAALNVRNVFHKVAQRPGKPFWFGVSDkGQPVFALPG 324
Cdd:cd00887 213 DLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGRLG-GKPVFGLPG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 325 NPVSALACCSRHVVPALLRAQ---DHALSTRRVVLSEALAPLSGMTRLVPVQLQSDGtGSMRATPHPMPTSGDFNRLGMT 401
Cdd:cd00887 292 NPVSALVTFELFVRPALRKLQgapEPEPPRVKARLAEDLKSKPGRREFLRVRLERDE-GGLVVAPPGGQGSGLLSSLARA 370
|
410 420
....*....|....*....|..
gi 2262111202 402 DGIVSLPPGDRPLQAGDIVTFH 423
Cdd:cd00887 371 DGLIVIPEGVEGLEAGEEVEVL 392
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
2-423 |
6.93e-62 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 210.84 E-value: 6.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 2 HDLLSIETADRLIGEAL--APFGSETVSLLHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRGAQAQGqrtrkqei 79
Cdd:PRK14498 7 LTLVSLEEAREILESLLseLPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEAN-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 80 pdsfvlaatqpagrpPLDLRTIVTSENAPLPA-------AIAVMTGSVLPHGTDTVIPREDydlTEGTHGTIIRLEDGVH 152
Cdd:PRK14498 79 ---------------PVRLKLGGEVHAGEAPDvevepgeAVEIATGAPIPRGADAVVMVED---TEEVDDDTVEIYRPVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 153 PrkGQHIHSEGSDCAAGTVLLNAGIRLSPPDLAILAANGVAEPRVAIIPSIAIISTGDELVAPDEPVQAWQIRRSNEYAI 232
Cdd:PRK14498 141 P--GENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 233 SASLSRKGFTLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKALAALNvRNVFHKVAQRPGKPFWFGV 312
Cdd:PRK14498 219 AAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEELG-EVLVHGVAIKPGKPTILGV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 313 SDkGQPVFALPGNPVSALACCSRHVVPALLRAQDHALSTRRVV---LSEALAPLSGMTRLVPVQLQSDGTGsMRATPHPM 389
Cdd:PRK14498 298 IG-GKPVVGLPGYPVSALTIFEEFVAPLLRKLAGLPPPERATVkarLARRVRSELGREEFVPVSLGRVGDG-YVAYPLSR 375
|
410 420 430
....*....|....*....|....*....|....
gi 2262111202 390 pTSGDFNRLGMTDGIVSLPPGDRPLQAGDIVTFH 423
Cdd:PRK14498 376 -GSGAITSLVRADGFIEIPANTEGLEAGEEVEVE 408
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
24-191 |
1.37e-31 |
|
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: 117.67 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 24 ETVSL--LHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRGAqaqgqrtrkqeiPDSFVLAATQPAGRPPldlrti 101
Cdd:pfam03453 7 ETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGA------------SEVNPIAAGEPPGPLL------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 102 vtsenaPLPAAIAVMTGSVLPHGTDTVIPREDydlTEGTHGTIIRLEDGVHPrkGQHIHSEGSDCAAGTVLLNAGIRLSP 181
Cdd:pfam03453 69 ------PGGEAVRIMTGAPLPEGADAVVMVED---TEEGGGRTVEIRAPVAP--GENVRRAGEDIKAGEVVLPAGTRLTP 137
|
170
....*....|
gi 2262111202 182 PDLAILAANG 191
Cdd:pfam03453 138 AEIGLLASLG 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
208-332 |
1.11e-26 |
|
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: 103.82 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 208 TGDELVAPDepvqawQIRRSNEYAISASLSRKGFTL--QSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVP 285
Cdd:smart00852 5 TGDELLSGG------QIRDSNGPMLAALLRELGIEVvrVVVVGGPDDPEAIREALREALAEADVVITTGGTGPGPDDLTP 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2262111202 286 KALA-ALNVRNVFHKVAQRPGKPF--------WFGVSDKGQPVFALPGNPVSALAC 332
Cdd:smart00852 79 EALAeLGGRELLGHGVAMRPGGPPgplanlsgTAPGVRGKKPVFGLPGNPVAALVM 134
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
208-332 |
2.42e-26 |
|
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: 103.55 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 208 TGDELVAPDEPVQAWQIRRSNEYAISASLSRKGFTLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKA 287
Cdd:TIGR00177 8 VGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRDVTPEA 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2262111202 288 LAAL----------NVRNVFHKVAQRPGKPFWFGVSdKGQPVFALPGNPVSALAC 332
Cdd:TIGR00177 88 LEELgekeipgfgeFRMLSSLPVLSRPGKPATAGVR-GGTLIFNLPGNPVSALVT 141
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
4-425 |
2.17e-124 |
|
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: 365.95 E-value: 2.17e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 4 LLSIETADRLIGEALAPFGSETVSLLHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRGAQaqgqrtrkqeiPDSF 83
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAN-----------PVTL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 84 VLAATQPAGRPPldlrtivtseNAPLPA--AIAVMTGSVLPHGTDTVIPREDYDLTEGThgtiIRLEDGVHPrkGQHIHS 161
Cdd:COG0303 70 RVVGEIAAGSPP----------PGPLGPgeAVRIMTGAPLPEGADAVVMQEDTEREGDR----VTIRKPVAP--GENIRR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 162 EGSDCAAGTVLLNAGIRLSPPDLAILAANGVAEPRVAIIPSIAIISTGDELVAPDEPVQAWQIRRSNEYAISASLSRKGF 241
Cdd:COG0303 134 AGEDIAAGDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 242 TLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKALAALNVRNVFHKVAQRPGKPFWFGVSDkGQPVFA 321
Cdd:COG0303 214 EVVDLGIVPDDPEALRAALREALAEADLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLG-GKPVFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 322 LPGNPVSALACCSRHVVPALLRAQ---DHALSTRRVVLSEALAPLSGMTRLVPVQLQSDGtGSMRATPHPMPTSGDFNRL 398
Cdd:COG0303 293 LPGNPVSALVTFELFVRPALRKLAglpPPPPPRVRARLAEDLPKKPGRTEFLRVRLERDD-GELVVEPLGGQGSGLLSSL 371
|
410 420
....*....|....*....|....*..
gi 2262111202 399 GMTDGIVSLPPGDRPLQAGDIVTFHEW 425
Cdd:COG0303 372 AEADGLIVLPEGVEGVEAGEEVEVLLL 398
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
7-423 |
7.67e-118 |
|
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: 349.10 E-value: 7.67e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 7 IETADRLIGEALAPFGSETVSLLHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRGAQAqgqrtrkqeipdSFVLA 86
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASV------------TLRVV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 87 ATQPAGRPPldlrtivtseNAPLPA--AIAVMTGSVLPHGTDTVIPREDYDLTEGThgtiIRLEDGVHPrkGQHIHSEGS 164
Cdd:cd00887 69 GEIPAGEPP----------DGPLGPgeAVRIMTGAPLPEGADAVVMVEDTEEEGGR----VTITKPVKP--GQNIRRAGE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 165 DCAAGTVLLNAGIRLSPPDLAILAANGVAEPRVAIIPSIAIISTGDELVAPDEPVQAWQIRRSNEYAISASLSRKGFTLQ 244
Cdd:cd00887 133 DIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 245 SLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKALAALNVRNVFHKVAQRPGKPFWFGVSDkGQPVFALPG 324
Cdd:cd00887 213 DLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGRLG-GKPVFGLPG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 325 NPVSALACCSRHVVPALLRAQ---DHALSTRRVVLSEALAPLSGMTRLVPVQLQSDGtGSMRATPHPMPTSGDFNRLGMT 401
Cdd:cd00887 292 NPVSALVTFELFVRPALRKLQgapEPEPPRVKARLAEDLKSKPGRREFLRVRLERDE-GGLVVAPPGGQGSGLLSSLARA 370
|
410 420
....*....|....*....|..
gi 2262111202 402 DGIVSLPPGDRPLQAGDIVTFH 423
Cdd:cd00887 371 DGLIVIPEGVEGLEAGEEVEVL 392
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
2-423 |
6.93e-62 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 210.84 E-value: 6.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 2 HDLLSIETADRLIGEAL--APFGSETVSLLHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRGAQAQGqrtrkqei 79
Cdd:PRK14498 7 LTLVSLEEAREILESLLseLPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEAN-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 80 pdsfvlaatqpagrpPLDLRTIVTSENAPLPA-------AIAVMTGSVLPHGTDTVIPREDydlTEGTHGTIIRLEDGVH 152
Cdd:PRK14498 79 ---------------PVRLKLGGEVHAGEAPDvevepgeAVEIATGAPIPRGADAVVMVED---TEEVDDDTVEIYRPVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 153 PrkGQHIHSEGSDCAAGTVLLNAGIRLSPPDLAILAANGVAEPRVAIIPSIAIISTGDELVAPDEPVQAWQIRRSNEYAI 232
Cdd:PRK14498 141 P--GENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 233 SASLSRKGFTLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKALAALNvRNVFHKVAQRPGKPFWFGV 312
Cdd:PRK14498 219 AAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEELG-EVLVHGVAIKPGKPTILGV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 313 SDkGQPVFALPGNPVSALACCSRHVVPALLRAQDHALSTRRVV---LSEALAPLSGMTRLVPVQLQSDGTGsMRATPHPM 389
Cdd:PRK14498 298 IG-GKPVVGLPGYPVSALTIFEEFVAPLLRKLAGLPPPERATVkarLARRVRSELGREEFVPVSLGRVGDG-YVAYPLSR 375
|
410 420 430
....*....|....*....|....*....|....
gi 2262111202 390 pTSGDFNRLGMTDGIVSLPPGDRPLQAGDIVTFH 423
Cdd:PRK14498 376 -GSGAITSLVRADGFIEIPANTEGLEAGEEVEVE 408
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
3-345 |
2.89e-47 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 170.95 E-value: 2.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 3 DLLSIETADRLIGEALAPF-GSETVSLLHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRgaqaqgqrtrkqeiPD 81
Cdd:PRK14491 197 AFLSVSQGLDKILSLVTPVtETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLE--------------PE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 82 SFVLAATQPAGRPpldlrtivtsENAPLPAAIAV--MTGSVLPHGTDTVIPREDYDLTEGThgtiIRLEDGVhpRKGQHI 159
Cdd:PRK14491 263 SYTLVGEVLAGHQ----------YDGTLQAGEAVriMTGAPVPAGADTVVMRELATQDGDK----VSFDGGI--KAGQNV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 160 HSEGSDCAAGTVLLNAGIRLSPPDLAILAANGVAEPRVAIIPSIAIISTGDELVAPDEPVQAWQIRRSNEYAISASLSRK 239
Cdd:PRK14491 327 RLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKL 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 240 GFTLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKALAALNVRNvFHKVAQRPGKPFWFGVSDkGQPV 319
Cdd:PRK14491 407 GCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVSVGDADYIKTALAKLGQID-FWRINMRPGRPLAFGQIG-DSPF 484
|
330 340
....*....|....*....|....*.
gi 2262111202 320 FALPGNPVSALACCSRHVVPALLRAQ 345
Cdd:PRK14491 485 FGLPGNPVAVMVSFLQFVEPALRKLA 510
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
3-343 |
1.22e-45 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 162.57 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 3 DLLSIETA-DRLIGEALAPFGSETVSLLHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRGAQAqgqrtrkqeIPd 81
Cdd:PRK10680 6 GLMSLETAlTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQP---------LP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 82 sfvLAATQPAGRPpldlrtivTSENAPLPAAIAVMTGSVLPHGTDTVIPREDYDLTEgthgtiirleDGV---HP-RKGQ 157
Cdd:PRK10680 76 ---VAGKAFAGQP--------FHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTD----------DGVrftAEvRSGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 158 HIHSEGSDCAAGTVLLNAGIRLSPPDLAILAANGVAEPRVAIIPSIAIISTGDELVAPDEPVQAWQIRRSNEYAISASLS 237
Cdd:PRK10680 135 NIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 238 RKGFTLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKALAALNVRNvFHKVAQRPGKPFWFGVSDKGQ 317
Cdd:PRK10680 215 QLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEADYTKTILEELGEIA-FWKLAIKPGKPFAFGKLSNSW 293
|
330 340
....*....|....*....|....*.
gi 2262111202 318 pVFALPGNPVSALACCSRHVVPALLR 343
Cdd:PRK10680 294 -FCGLPGNPVSAALTFYQLVQPLLAK 318
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
3-411 |
1.13e-38 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 146.49 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 3 DLLSIETADRLIGEALAPF-GSETVSLLHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRGAQAQGQRTRKQEIPD 81
Cdd:PRK14497 9 SLYSIDEAIKVFLSSLNFKpKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGEFKVIDKIGIGEFKE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 82 SfvlaatqpagrppldlrTIVTSEnaplpaAIAVMTGSVLPHGTDTVIPREDYDLTEGThgtiiRLEDGVHPRKGQHIHS 161
Cdd:PRK14497 89 I-----------------HIKECE------AVEVDTGSMIPMGADAVIKVENTKVINGN-----FIKIDKKINFGQNIGW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 162 EGSDCAAGTVLLNAGIRLSPPDLAILAANGVAEPRVAIIPSIAIISTGDELVAPDEPVQAWQIRRSNEYAISASLSRKGF 241
Cdd:PRK14497 141 IGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 242 TLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKALAALNvRNVFHKVAQRPGKPFWFGVSDkGQPVFA 321
Cdd:PRK14497 221 KIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKDFVHQAIRELG-NIIVHGLKIKPGKPTILGIVD-GKPVIG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 322 LPGNPVSALACCSRhVVPALLRAQdHALSTRRVVLSEALAPLSGMTR-------LVPVQL-QSDgtGSMRATPHPMPTS- 392
Cdd:PRK14497 299 LPGNIVSTMVVLNM-VILEYLKSL-YPSRKEILGLGKIKARLALRVKadehrntLIPVYLfKSD--NSYYALPVPFDSYm 374
|
410 420
....*....|....*....|
gi 2262111202 393 -GDFNrlgMTDGIVSLPPGD 411
Cdd:PRK14497 375 vGTFS---LTDGYIMLGPNE 391
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
3-341 |
8.21e-37 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 139.28 E-value: 8.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 3 DLLSIETADRLIGEALAPF-GSETVSLLHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRGAQAqgqrtrkqeIPd 81
Cdd:PRK14690 21 DWTPVDTALDLLRARLGPVtDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQV---------LP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 82 sfvLAATQPAGRPPLDLRTivtsenaPLPAAIAVMTGSVLPHGTDTVIPREDydLTEGTHGTIIR--LEDGVHPRKGqhi 159
Cdd:PRK14690 91 ---LIEGRAAAGVPFSGRV-------PEGMALRILTGAALPEGVDTVVLEED--VAGDGHRIAFHgpLKMGANTRKA--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 160 hseGSDCAAGTVLLNAGIRLSPPDLAILAANGVAEPRVAIIPSIAIISTGDELVAPDEPVQAWQIRRSNEYAISASLSRK 239
Cdd:PRK14690 156 ---GEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 240 GFTLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKALAALNVRNVFhKVAQRPGKPFWFGVSdKGQPV 319
Cdd:PRK14690 233 GHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGASAGDEDHVSALLREAGAMQSW-RIALKPGRPLALGLW-QGVPV 310
|
330 340
....*....|....*....|..
gi 2262111202 320 FALPGNPVSALACCSRHVVPAL 341
Cdd:PRK14690 311 FGLPGNPVAALVCTLVFARPAM 332
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
4-341 |
4.52e-36 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 140.33 E-value: 4.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 4 LLSIETADRLIGEALAPFGSETVSLLHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRGaqaqgqrtrkqEIPdsf 83
Cdd:PLN02699 7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPG-----------EYP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 84 VLAATQpAGRPPLDLrtIVTsenaplPAAIA-VMTGSVLPHGTDTVIPREDYDLTEGTHGTIIRLEDGVHPRKGQHIHSE 162
Cdd:PLN02699 73 VITESR-AGNDGLGV--TLT------PGTVAyVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKRVRILSQASKGQDIRPV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 163 GSDCAAGTVLLNAGIRLSPPDLAILAANGVAEPRVAIIPSIAIISTGDELVAP-DEPVQAWQIRRSNEYAISASLSRKGF 241
Cdd:PLN02699 144 GCDIEKDAKVLKAGERLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPtTGTLGRGQIRDSNRAMLLAAAIQQQC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 242 TLQSLSLVPDNLAAVTDHFREVLETH-DVLVISGGVSMGQFDFVPKALAALNVRNvFHKVAQRPGKPFWFG-VSDKGQP- 318
Cdd:PLN02699 224 KVVDLGIARDDEEELERILDEAISSGvDILLTSGGVSMGDRDFVKPLLEKRGTVY-FSKVLMKPGKPLTFAeIDAKSAPs 302
|
330 340
....*....|....*....|....*....
gi 2262111202 319 ------VFALPGNPVSALACCSRHVVPAL 341
Cdd:PLN02699 303 nskkmlAFGLPGNPVSCLVCFNLFVVPAI 331
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
24-191 |
1.37e-31 |
|
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: 117.67 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 24 ETVSL--LHSAGRILRQEIRAERALPPYDRVILDGIAIRWQDTRGAqaqgqrtrkqeiPDSFVLAATQPAGRPPldlrti 101
Cdd:pfam03453 7 ETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGA------------SEVNPIAAGEPPGPLL------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 102 vtsenaPLPAAIAVMTGSVLPHGTDTVIPREDydlTEGTHGTIIRLEDGVHPrkGQHIHSEGSDCAAGTVLLNAGIRLSP 181
Cdd:pfam03453 69 ------PGGEAVRIMTGAPLPEGADAVVMVED---TEEGGGRTVEIRAPVAP--GENVRRAGEDIKAGEVVLPAGTRLTP 137
|
170
....*....|
gi 2262111202 182 PDLAILAANG 191
Cdd:pfam03453 138 AEIGLLASLG 147
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
208-332 |
1.11e-26 |
|
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: 103.82 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 208 TGDELVAPDepvqawQIRRSNEYAISASLSRKGFTL--QSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVP 285
Cdd:smart00852 5 TGDELLSGG------QIRDSNGPMLAALLRELGIEVvrVVVVGGPDDPEAIREALREALAEADVVITTGGTGPGPDDLTP 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2262111202 286 KALA-ALNVRNVFHKVAQRPGKPF--------WFGVSDKGQPVFALPGNPVSALAC 332
Cdd:smart00852 79 EALAeLGGRELLGHGVAMRPGGPPgplanlsgTAPGVRGKKPVFGLPGNPVAALVM 134
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
208-332 |
2.42e-26 |
|
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: 103.55 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 208 TGDELVAPDEPVQAWQIRRSNEYAISASLSRKGFTLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKA 287
Cdd:TIGR00177 8 VGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRDVTPEA 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2262111202 288 LAAL----------NVRNVFHKVAQRPGKPFWFGVSdKGQPVFALPGNPVSALAC 332
Cdd:TIGR00177 88 LEELgekeipgfgeFRMLSSLPVLSRPGKPATAGVR-GGTLIFNLPGNPVSALVT 141
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
208-343 |
2.35e-24 |
|
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: 97.70 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 208 TGDELVApdepvqaWQIRRSNEYAISASLSRKGFTLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKA 287
Cdd:pfam00994 5 TGDELLP-------GQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEA 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2262111202 288 LAALNVRN------VFHKVAQRPGKPF----WFGVSDKGQPVFALPGNPVSALACCSRHVVPALLR 343
Cdd:pfam00994 78 LAELGGRElpgfeeLFRGVSLKPGKPVgtapGAILSRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
212-341 |
1.66e-17 |
|
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: 78.54 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 212 LVAPDEpVQAWQIRRSNEYAISASLSRKGFTLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKALAAL 291
Cdd:cd00758 5 VTVSDE-LSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALAEL 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2262111202 292 -NVRNVFHKVAQRPGKPFWFGVSDKgQPVFALPGNPVSALACCSRHVVPAL 341
Cdd:cd00758 84 gEREAHGKGVALAPGSRTAFGIIGK-VLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
353-425 |
4.00e-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: 44.14 E-value: 4.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2262111202 353 RVVLSEALAPLSGMTRLVPVQLQSDGtGSMRATPHPMPTSGDFNRLGMTDGIVSLPPGDRPLQAGDIVTFHEW 425
Cdd:pfam03454 1 KARLARDLKSDPGRREFVRVRLHEED-GRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
208-275 |
1.06e-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: 43.56 E-value: 1.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2262111202 208 TGDELVAPdepvqawQIRRSNEYAISASLSRKGFTLQSLSLVPDNLAAVTDHFREVLETHDVLVISGG 275
Cdd:COG1058 7 IGDELLSG-------RIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGG 67
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
208-275 |
4.49e-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: 37.85 E-value: 4.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2262111202 208 TGDELVAPdepvqawQIRRSNEYAISASLSRKGFTLQSLSLVPDNLAAVTDHFREVLETHDVLVISGG 275
Cdd:cd00885 7 IGDELLSG-------QIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
221-303 |
9.45e-03 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 37.68 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2262111202 221 AWQIRRSNEYAI-------SASLSRK----GFTLQSLSLVPDNLAAVTDHFREVLETHDVLVISGGVSMGQFDFVPKALA 289
Cdd:PRK01215 6 AWIITIGNELLIgrtvntnASWIARRltylGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGFA 85
|
90
....*....|....*
gi 2262111202 290 -ALNVRNVFHKVAQR 303
Cdd:PRK01215 86 kALGVELELNEDALR 100
|
|
| |
