|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
1-416 |
0e+00 |
|
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: 526.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 1 MLSVRDAADIIFNLVQPLDpqqdTEVVDLFAANGRILATPVTSPLDFPHWDNSAMDGYAVRYEDVHNASteqPVNLEIVE 80
Cdd:COG0303 1 MISVEEALALILAAVRPLG----TETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAN---PVTLRVVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 81 EIPAGYQPKLTLQPGQAARIFTGAVIPQGADTVVMQEMTHREDHRVLILTTPQLGEFVRRKASYYQAGTQLLPAGIKLTA 160
Cdd:COG0303 74 EIAAGSPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 161 AEIAVLAASQCPQIRVYRRPRVAIFSTGDELVTVNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTIK 240
Cdd:COG0303 154 ADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 241 QAITNADIVISSGGVSVGDYDYVDKILDGLGAKIHIRAVAMRPGKPLTVATFSNfyspvpspqsPIYFGLPGNPAAVLVT 320
Cdd:COG0303 234 EALAEADLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLGG----------KPVFGLPGNPVSALVT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 321 FWRFVQPVIQKLGGIAEGGKPEFmKVRSRDELRSDGKRETYIWGRLHLIDGVYEFHKAGGsHSSGNLINLAQTNALAVLP 400
Cdd:COG0303 304 FELFVRPALRKLAGLPPPPPPRV-RARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGG-QGSGLLSSLAEADGLIVLP 381
|
410
....*....|....*.
gi 427365491 401 VDTTLIPPGEKVDILL 416
Cdd:COG0303 382 EGVEGVEAGEEVEVLL 397
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
6-416 |
1.47e-174 |
|
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: 493.16 E-value: 1.47e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 6 DAADIIFNLVQPLDPqqdTEVVDLFAANGRILATPVTSPLDFPHWDNSAMDGYAVRYEDVHNASTEqpvnLEIVEEIPAG 85
Cdd:cd00887 2 EAARELLLALAPPLG---TETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVT----LRVVGEIPAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 86 YQPKLTLQPGQAARIFTGAVIPQGADTVVMQEMTHREDHRVLILTTPQLGEFVRRKASYYQAGTQLLPAGIKLTAAEIAV 165
Cdd:cd00887 75 EPPDGPLGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 166 LAASQCPQIRVYRRPRVAIFSTGDELVTVNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTIKQAITN 245
Cdd:cd00887 155 LASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 246 ADIVISSGGVSVGDYDYVDKILDGLGAKIHIRAVAMRPGKPLTVATFSNfySPVpspqspiyFGLPGNPAAVLVTFWRFV 325
Cdd:cd00887 235 ADVVITSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGRLGG--KPV--------FGLPGNPVSALVTFELFV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 326 QPVIQKLGGIAEgGKPEFMKVRSRDELRSDGKRETYIWGRLHLIDGVYEFHKAGGsHSSGNLINLAQTNALAVLPVDTTL 405
Cdd:cd00887 305 RPALRKLQGAPE-PEPPRVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGG-QGSGLLSSLARADGLIVIPEGVEG 382
|
410
....*....|.
gi 427365491 406 IPPGEKVDILL 416
Cdd:cd00887 383 LEAGEEVEVLL 393
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
1-416 |
4.36e-112 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 342.19 E-value: 4.36e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 1 MLSVRDAADIIFNLVQPldPQQDTEVVDLFAANGRILATPVTSPLDFPHWDNSAMDGYAVRYEDVHNASTEQPVNLEIVE 80
Cdd:PRK14498 9 LVSLEEAREILESLLSE--LPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLKLGG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 81 EIPAGYQPKLTLQPGQAARIFTGAVIPQGADTVVMQEMTHREDHR-VLILT--TPqlGEFVRRKASYYQAGTQLLPAGIK 157
Cdd:PRK14498 87 EVHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDtVEIYRpvAP--GENVRPAGEDIVAGELILPKGTR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 158 LTAAEIAVLAASQCPQIRVYRRPRVAIFSTGDELVTVNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQ 237
Cdd:PRK14498 165 LTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 238 TIKQAITNADIVISSGGVSVGDYDYVDKILDGLGaKIHIRAVAMRPGKPLTVATFSNfySPVpspqspiyFGLPGNPAAV 317
Cdd:PRK14498 245 ALRKALKECDLVLLSGGTSAGAGDVTYRVIEELG-EVLVHGVAIKPGKPTILGVIGG--KPV--------VGLPGYPVSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 318 LVTFWRFVQPVIQKLGGIAEgGKPEFMKVRSRDELRSDGKRETYIwgRLHLIDG-----VYEFHKaggshSSGNLINLAQ 392
Cdd:PRK14498 314 LTIFEEFVAPLLRKLAGLPP-PERATVKARLARRVRSELGREEFV--PVSLGRVgdgyvAYPLSR-----GSGAITSLVR 385
|
410 420
....*....|....*....|....
gi 427365491 393 TNALAVLPVDTTLIPPGEKVDILL 416
Cdd:PRK14498 386 ADGFIEIPANTEGLEAGEEVEVEL 409
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
20-168 |
7.96e-52 |
|
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: 170.83 E-value: 7.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 20 PQQDTEVVDLFA--ANGRILATPVTSPLDFPHWDNSAMDGYAVRYEDVHNASTEQPvnleiveeIPAGYQPKLTLQPGQA 97
Cdd:pfam03453 2 LLGTEETVPLEAldALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLPGGEA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 427365491 98 ARIFTGAVIPQGADTVVMQEMTHREDHR-VLILTTPQLGEFVRRKASYYQAGTQLLPAGIKLTAAEIAVLAA 168
Cdd:pfam03453 74 VRIMTGAPLPEGADAVVMVEDTEEGGGRtVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLAS 145
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
180-327 |
8.72e-45 |
|
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: 152.47 E-value: 8.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 180 PRVAIFSTGDELVTVNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTIKQAITNADIVISSGGVSVGD 259
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 427365491 260 YDYVDKILDGLGAK-IHIRA---------VAMRPGKPLTVATFSnfyspvpspqSPIYFGLPGNPAAVLVTFWRFVQP 327
Cdd:TIGR00177 81 RDVTPEALEELGEKeIPGFGefrmlsslpVLSRPGKPATAGVRG----------GTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
183-324 |
1.64e-34 |
|
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: 125.01 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 183 AIFSTGDELVtvnqplQPGQIVDSNQYALAALVQQNGAEAILLGIV--KDNPEALQQTIKQAITNADIVISSGGVSVGDY 260
Cdd:smart00852 1 AIISTGDELL------SGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 427365491 261 DYVDKILDGLGAKIHIR-AVAMRPGKPLTVATFSNFYSPVPSPQSPIyFGLPGNPAAVLVTFWRF 324
Cdd:smart00852 75 DLTPEALAELGGRELLGhGVAMRPGGPPGPLANLSGTAPGVRGKKPV-FGLPGNPVAALVMFEEL 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
1-416 |
0e+00 |
|
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: 526.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 1 MLSVRDAADIIFNLVQPLDpqqdTEVVDLFAANGRILATPVTSPLDFPHWDNSAMDGYAVRYEDVHNASteqPVNLEIVE 80
Cdd:COG0303 1 MISVEEALALILAAVRPLG----TETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAN---PVTLRVVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 81 EIPAGYQPKLTLQPGQAARIFTGAVIPQGADTVVMQEMTHREDHRVLILTTPQLGEFVRRKASYYQAGTQLLPAGIKLTA 160
Cdd:COG0303 74 EIAAGSPPPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 161 AEIAVLAASQCPQIRVYRRPRVAIFSTGDELVTVNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTIK 240
Cdd:COG0303 154 ADLGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 241 QAITNADIVISSGGVSVGDYDYVDKILDGLGAKIHIRAVAMRPGKPLTVATFSNfyspvpspqsPIYFGLPGNPAAVLVT 320
Cdd:COG0303 234 EALAEADLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLGG----------KPVFGLPGNPVSALVT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 321 FWRFVQPVIQKLGGIAEGGKPEFmKVRSRDELRSDGKRETYIWGRLHLIDGVYEFHKAGGsHSSGNLINLAQTNALAVLP 400
Cdd:COG0303 304 FELFVRPALRKLAGLPPPPPPRV-RARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGG-QGSGLLSSLAEADGLIVLP 381
|
410
....*....|....*.
gi 427365491 401 VDTTLIPPGEKVDILL 416
Cdd:COG0303 382 EGVEGVEAGEEVEVLL 397
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
6-416 |
1.47e-174 |
|
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: 493.16 E-value: 1.47e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 6 DAADIIFNLVQPLDPqqdTEVVDLFAANGRILATPVTSPLDFPHWDNSAMDGYAVRYEDVHNASTEqpvnLEIVEEIPAG 85
Cdd:cd00887 2 EAARELLLALAPPLG---TETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVT----LRVVGEIPAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 86 YQPKLTLQPGQAARIFTGAVIPQGADTVVMQEMTHREDHRVLILTTPQLGEFVRRKASYYQAGTQLLPAGIKLTAAEIAV 165
Cdd:cd00887 75 EPPDGPLGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 166 LAASQCPQIRVYRRPRVAIFSTGDELVTVNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTIKQAITN 245
Cdd:cd00887 155 LASLGIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 246 ADIVISSGGVSVGDYDYVDKILDGLGAKIHIRAVAMRPGKPLTVATFSNfySPVpspqspiyFGLPGNPAAVLVTFWRFV 325
Cdd:cd00887 235 ADVVITSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGRLGG--KPV--------FGLPGNPVSALVTFELFV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 326 QPVIQKLGGIAEgGKPEFMKVRSRDELRSDGKRETYIWGRLHLIDGVYEFHKAGGsHSSGNLINLAQTNALAVLPVDTTL 405
Cdd:cd00887 305 RPALRKLQGAPE-PEPPRVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGG-QGSGLLSSLARADGLIVIPEGVEG 382
|
410
....*....|.
gi 427365491 406 IPPGEKVDILL 416
Cdd:cd00887 383 LEAGEEVEVLL 393
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
1-416 |
4.36e-112 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 342.19 E-value: 4.36e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 1 MLSVRDAADIIFNLVQPldPQQDTEVVDLFAANGRILATPVTSPLDFPHWDNSAMDGYAVRYEDVHNASTEQPVNLEIVE 80
Cdd:PRK14498 9 LVSLEEAREILESLLSE--LPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASEANPVRLKLGG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 81 EIPAGYQPKLTLQPGQAARIFTGAVIPQGADTVVMQEMTHREDHR-VLILT--TPqlGEFVRRKASYYQAGTQLLPAGIK 157
Cdd:PRK14498 87 EVHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDtVEIYRpvAP--GENVRPAGEDIVAGELILPKGTR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 158 LTAAEIAVLAASQCPQIRVYRRPRVAIFSTGDELVTVNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQ 237
Cdd:PRK14498 165 LTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 238 TIKQAITNADIVISSGGVSVGDYDYVDKILDGLGaKIHIRAVAMRPGKPLTVATFSNfySPVpspqspiyFGLPGNPAAV 317
Cdd:PRK14498 245 ALRKALKECDLVLLSGGTSAGAGDVTYRVIEELG-EVLVHGVAIKPGKPTILGVIGG--KPV--------VGLPGYPVSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 318 LVTFWRFVQPVIQKLGGIAEgGKPEFMKVRSRDELRSDGKRETYIwgRLHLIDG-----VYEFHKaggshSSGNLINLAQ 392
Cdd:PRK14498 314 LTIFEEFVAPLLRKLAGLPP-PERATVKARLARRVRSELGREEFV--PVSLGRVgdgyvAYPLSR-----GSGAITSLVR 385
|
410 420
....*....|....*....|....
gi 427365491 393 TNALAVLPVDTTLIPPGEKVDILL 416
Cdd:PRK14498 386 ADGFIEIPANTEGLEAGEEVEVEL 409
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
1-415 |
1.80e-106 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 326.57 E-value: 1.80e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 1 MLSVRDAADIIFNLVQPLdpqQDTEVVDLFAANGRILATPVTSPLDFPHWDNSAMDGYAVRYEDVHNASteqpvnLEIVE 80
Cdd:PRK14491 198 FLSVSQGLDKILSLVTPV---TETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPES------YTLVG 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 81 EIPAGYQPKLTLQPGQAARIFTGAVIPQGADTVVMQEMTHREDHRVLILTTPQLGEFVRrkasyyQAGTQL------LPA 154
Cdd:PRK14491 269 EVLAGHQYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQNVR------LAGEDLaqgqvaLAA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 155 GIKLTAAEIAVLAASQCPQIRVYRRPRVAIFSTGDELVTVNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEA 234
Cdd:PRK14491 343 GTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAA 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 235 LQQTIKQAITNADIVISSGGVSVGDYDYVDKILDGLGaKIHIRAVAMRPGKPLTVATFSNfySPvpspqspiYFGLPGNP 314
Cdd:PRK14491 423 LEATLEQAAAQADVVISSGGVSVGDADYIKTALAKLG-QIDFWRINMRPGRPLAFGQIGD--SP--------FFGLPGNP 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 315 AAVLVTFWRFVQPVIQKLGGIaEGGKPEFMKVRSRDELRSDGKRETYIWGRLHL-IDGVYEFhKAGGSHSSGNLINLAQT 393
Cdd:PRK14491 492 VAVMVSFLQFVEPALRKLAGE-QNWQPLLFPAIADETLRSRQGRTEFSRGIYHLgADGRLHV-RTTGKQGSGILSSMSEA 569
|
410 420
....*....|....*....|..
gi 427365491 394 NALAVLPVDTTLIPPGEKVDIL 415
Cdd:PRK14491 570 NCLIEIGPAAETVNAGETVTIQ 591
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
1-414 |
4.90e-99 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 301.63 E-value: 4.90e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 1 MLSVRDAADIIFNLVQPLdpqQDTEVVDLFAANGRILATPVTSPLDFPHWDNSAMDGYAVRYEDVhnaSTEQPvnLEIVE 80
Cdd:PRK10680 7 LMSLETALTEMLSRVTPL---TATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADL---ASGQP--LPVAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 81 EIPAGyQPKLTLQP-GQAARIFTGAVIPQGADTVVMQEMTHREDHRVLILTTPQLGEFVRRKASYYQAGTQLLPAGIKLT 159
Cdd:PRK10680 79 KAFAG-QPFHGEWPaGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 160 AAEIAVLAASQCPQIRVYRRPRVAIFSTGDELVTVNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTI 239
Cdd:PRK10680 158 TAELPVLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 240 KQAITNADIVISSGGVSVGDYDYVDKILDGLGaKIHIRAVAMRPGKPLTVATFSNFYspvpspqspiYFGLPGNPAAVLV 319
Cdd:PRK10680 238 IEADSQADVVISSGGVSVGEADYTKTILEELG-EIAFWKLAIKPGKPFAFGKLSNSW----------FCGLPGNPVSAAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 320 TFWRFVQPVIQKLGGIAEGGKPEFMKVRSRDELRSDGKRETYIWGRLHL-IDGVYEFHKAG--GSH--SSgnlinLAQTN 394
Cdd:PRK10680 307 TFYQLVQPLLAKLSGNTASGLPPRQRVRTASRLKKTPGRLDFQRGILQRnADGELEVTTTGhqGSHifSS-----FSLGN 381
|
410 420
....*....|....*....|
gi 427365491 395 ALAVLPVDTTLIPPGEKVDI 414
Cdd:PRK10680 382 CFIVLERERGNVEVGEWVEV 401
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
1-423 |
1.12e-67 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 227.00 E-value: 1.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 1 MLSVRDAADIIFNLVQPLDPQqdteVVDLFAANGRILATPVTSPLDFPHWDNSAMDGYAVryedvhnASTEQPVNLEIVE 80
Cdd:PLN02699 7 MISVEEALSIVLSVAARLSPV----IVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAV-------VASDGPGEYPVIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 81 EIPAG-YQPKLTLQPGQAARIFTGAVIPQGADTVVMQEMTHR------EDHRVLILTTPQLGEFVRRKASYYQAGTQLLP 153
Cdd:PLN02699 76 ESRAGnDGLGVTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVvedpldGSKRVRILSQASKGQDIRPVGCDIEKDAKVLK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 154 AGIKLTAAEIAVLAASQCPQIRVYRRPRVAIFSTGDELVT-VNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNP 232
Cdd:PLN02699 156 AGERLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEpTTGTLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 233 EALQQTIKQAIT-NADIVISSGGVSVGDYDYVDKILDGLGaKIHIRAVAMRPGKPLTVATFSNfySPVPSPQSPIY-FGL 310
Cdd:PLN02699 236 EELERILDEAISsGVDILLTSGGVSMGDRDFVKPLLEKRG-TVYFSKVLMKPGKPLTFAEIDA--KSAPSNSKKMLaFGL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 311 PGNPAAVLVTFWRFVQPVIQKLGGIAEggkPEFMKVRSR-------DELRSDGKRETYIWgrlHLIDGVYE---FHKAGG 380
Cdd:PLN02699 313 PGNPVSCLVCFNLFVVPAIRYLAGWSN---PHLLRVQARlrepiklDPVRPEFHRAIIRW---KLNDGSGNpgfVAESTG 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 427365491 381 SHSSGNLINLAQTNALAVLPVDTTLIPPGEKVD-ILLSQVMSHT 423
Cdd:PLN02699 387 HQMSSRLLSMKSANALLELPATGNVLSAGTSVSaIIISDISSKS 430
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
1-380 |
5.76e-58 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 198.88 E-value: 5.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 1 MLSVRDAADIIFNlvqPLDPQQDTEVVDLFAANGRILATPVTSPLDFPHWDNSAMDGYAVRyedvhnaSTEQPVNLEIVE 80
Cdd:PRK14497 10 LYSIDEAIKVFLS---SLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALK-------SSCTPGEFKVID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 81 EIPAGYQPKLTLQPGQAARIFTGAVIPQGADTVVMQEMTHR-EDHRVLILTTPQLGEFVRRKASYYQAGTQLLPAGIKLT 159
Cdd:PRK14497 80 KIGIGEFKEIHIKECEAVEVDTGSMIPMGADAVIKVENTKViNGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 160 AAEIAVLAASQCPQIRVYRRPRVAIFSTGDELVTVNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTI 239
Cdd:PRK14497 160 HEKIGLLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 240 KQAITNADIVISSGGVSVGDYDYVDKILDGLGaKIHIRAVAMRPGKPLTVATFSNfySPVpspqspiyFGLPGNPAAVLV 319
Cdd:PRK14497 240 KRAISVADVLILTGGTSAGEKDFVHQAIRELG-NIIVHGLKIKPGKPTILGIVDG--KPV--------IGLPGNIVSTMV 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 427365491 320 TFWRFVQPVIQKLGG----IAEGGKpefMKVRSRDELRSDGKRETYIwgrlhlidGVYEFHKAGG 380
Cdd:PRK14497 309 VLNMVILEYLKSLYPsrkeILGLGK---IKARLALRVKADEHRNTLI--------PVYLFKSDNS 362
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
18-415 |
2.45e-57 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 193.98 E-value: 2.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 18 LDPQQDTEVVDLFAANGRILATPVTSPLDFPHWDNSAMDGYAVRyedvhNASTEQPVNLEIVE-EIPAGYQPKLTLQPGQ 96
Cdd:PRK14690 36 LGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFA-----GAAPEGAQVLPLIEgRAAAGVPFSGRVPEGM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 97 AARIFTGAVIPQGADTVVMQEMTHREDHRVLILTTPQLGEFVRRKASYYQAGTQLLPAGIKLTAAEIAVLAASQCPQIRV 176
Cdd:PRK14690 111 ALRILTGAALPEGVDTVVLEEDVAGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 177 YRRPRVAIFSTGDELVTVNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTIKQAITNADIVISSGGVS 256
Cdd:PRK14690 191 RRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGAS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 257 VGDYDYVDKILDGLGAKIHIRaVAMRPGKPLTVATFSNfySPVpspqspiyFGLPGNPAAVLVTFWRFVQPVIQKLGGiA 336
Cdd:PRK14690 271 AGDEDHVSALLREAGAMQSWR-IALKPGRPLALGLWQG--VPV--------FGLPGNPVAALVCTLVFARPAMSLLAG-E 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 427365491 337 EGGKPEFMKVRSRDELRSDGKRETYIWGRLHliDGVYEFHKAGGshsSGNLINLAQTNALAVLPVDTTLIPPGEKVDIL 415
Cdd:PRK14690 339 GWSEPQGFTVPAAFEKRKKPGRREYLRARLR--QGHAEVFRSEG---SGRISGLSWAEGLVELGDGARRIAPGDPVRFI 412
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
20-168 |
7.96e-52 |
|
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: 170.83 E-value: 7.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 20 PQQDTEVVDLFA--ANGRILATPVTSPLDFPHWDNSAMDGYAVRYEDVHNASTEQPvnleiveeIPAGYQPKLTLQPGQA 97
Cdd:pfam03453 2 LLGTEETVPLEAldALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNP--------IAAGEPPGPLLPGGEA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 427365491 98 ARIFTGAVIPQGADTVVMQEMTHREDHR-VLILTTPQLGEFVRRKASYYQAGTQLLPAGIKLTAAEIAVLAA 168
Cdd:pfam03453 74 VRIMTGAPLPEGADAVVMVEDTEEGGGRtVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLAS 145
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
180-327 |
8.72e-45 |
|
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: 152.47 E-value: 8.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 180 PRVAIFSTGDELVTVNQPLQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTIKQAITNADIVISSGGVSVGD 259
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 427365491 260 YDYVDKILDGLGAK-IHIRA---------VAMRPGKPLTVATFSnfyspvpspqSPIYFGLPGNPAAVLVTFWRFVQP 327
Cdd:TIGR00177 81 RDVTPEALEELGEKeIPGFGefrmlsslpVLSRPGKPATAGVRG----------GTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
183-331 |
7.90e-36 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 128.52 E-value: 7.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 183 AIFSTGDELVtvnqplqPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTIKQAITNADIVISSGGVSVGDYDY 262
Cdd:pfam00994 1 AIITTGDELL-------PGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 427365491 263 VDKILDGLGAK------IHIRAVAMRPGKPLTVATFsnfysPVPSPQSPIYFGLPGNPAAVLVTFWRFVQPVIQK 331
Cdd:pfam00994 74 TPEALAELGGRelpgfeELFRGVSLKPGKPVGTAPG-----AILSRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
183-324 |
1.64e-34 |
|
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: 125.01 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 183 AIFSTGDELVtvnqplQPGQIVDSNQYALAALVQQNGAEAILLGIV--KDNPEALQQTIKQAITNADIVISSGGVSVGDY 260
Cdd:smart00852 1 AIISTGDELL------SGGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 427365491 261 DYVDKILDGLGAKIHIR-AVAMRPGKPLTVATFSNFYSPVPSPQSPIyFGLPGNPAAVLVTFWRF 324
Cdd:smart00852 75 DLTPEALAELGGRELLGhGVAMRPGGPPGPLANLSGTAPGVRGKKPV-FGLPGNPVAALVMFEEL 138
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
181-329 |
2.63e-26 |
|
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: 102.81 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 181 RVAIFSTGDELvtvnqplQPGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTIKQAITNADIVISSGGVSVGDY 260
Cdd:cd00758 1 RVAIVTVSDEL-------SQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 261 DYVDKILDGLGAK-IHIRAVAMRPGKPLTVATFsnfyspvpspQSPIYFGLPGNPAAVLVTFWRFVQPVI 329
Cdd:cd00758 74 DVTPEALAELGEReAHGKGVALAPGSRTAFGII----------GKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
345-416 |
2.58e-15 |
|
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: 70.33 E-value: 2.58e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 427365491 345 KVRSRDELRSDGKRETYIWGRLHLIDGVYEFHKAGgSHSSGNLINLAQTNALAVLPVDTTLIPPGEKVDILL 416
Cdd:pfam03454 1 KARLARDLKSDPGRREFVRVRLHEEDGRYYAEPIG-KQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVIL 71
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
181-254 |
6.01e-10 |
|
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: 57.88 E-value: 6.01e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 427365491 181 RVAIFSTGDELVTvnqplqpGQIVDSN-QYaLAALVQQNGAEAILLGIVKDNPEALQQTIKQAITNADIVISSGG 254
Cdd:cd00885 1 TAEIIAIGDELLS-------GQIVDTNaAF-LAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGG 67
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
184-254 |
3.51e-06 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 49.02 E-value: 3.51e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 427365491 184 IFSTGDELVTvnqplqpGQIVDSN-QY---ALAALvqqnGAEAILLGIVKDNPEALQQTIKQAITNADIVISSGG 254
Cdd:PRK00549 5 IIAVGTELLL-------GQIVNTNaQFlseKLAEL----GIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGG 68
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
181-337 |
9.09e-06 |
|
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 161761 [Multi-domain] Cd Length: 413 Bit Score: 47.59 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 181 RVAIFSTGDELVTvnqplqpGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTIKQAITNADIVISSGGVSVGDY 260
Cdd:TIGR00200 2 KAEIISVGDELLL-------GQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427365491 261 DYV---------------DKILDGLGAKIHIRAVAMRPGK------PLTVATFSNFYSPVPS----PQSPIY-FGLPGNP 314
Cdd:TIGR00200 75 DLTaetiatakgeplvlnEAWLKEIERYFHETGRVMAPNNrkqallPAGAEFLANPVGTAPGmfavQLNRCLmLFTPGVP 154
|
170 180
....*....|....*....|...
gi 427365491 315 AAVLVTFWRFVQPVIQKLGGIAE 337
Cdd:TIGR00200 155 SEFRVMVEHEALPRLRERFSLPQ 177
|
|
| PRK03673 |
PRK03673 |
nicotinamide mononucleotide deamidase-related protein YfaY; |
181-254 |
3.92e-04 |
|
nicotinamide mononucleotide deamidase-related protein YfaY;
Pssm-ID: 179629 [Multi-domain] Cd Length: 396 Bit Score: 42.38 E-value: 3.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 427365491 181 RVAIFSTGDELVTvnqplqpGQIVDSNQYALAALVQQNGAEAILLGIVKDNPEALQQTIKQAITNADIVISSGG 254
Cdd:PRK03673 3 RVEMLSTGDEVLH-------GQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGG 69
|
|
| |
