|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
3-404 |
1.35e-156 |
|
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: 447.23 E-value: 1.35e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 3 LLPVDEALARILKSAEPRGIEEVELSNAGGRVVATPVLAHLLQPPFDGSAMDGYALIAPD-NISYPVQFDIIGESAAGNR 81
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADlAGANPVTLRVVGEIAAGSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 82 FEGELGIGQAVRIFTGAPLPKGTDAIVIQEHTERSSNRLTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELDAAALSLAA 161
Cdd:COG0303 81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 162 ASGNAKIDVFKKPKVAIIATGDELVLPGEIPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQsDI 241
Cdd:COG0303 161 SLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALA-EA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 242 DILVTIGGASVGDRDFVHGALRKLGVELDFWKIAMRPGKPLMYGRveVNGKivHVIGLPGNPVSSLVCSLVFLRPLVARL 321
Cdd:COG0303 240 DLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGR--LGGK--PVFGLPGNPVSALVTFELFVRPALRKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 322 AG-TNSEADIRPAKLGIALPANDHRRDYIRATVEsRTDGTLVASPFPVQDSSMLSALVRSRALLIREENAPAAAIGDDCR 400
Cdd:COG0303 316 AGlPPPPPPRVRARLAEDLPKKPGRTEFLRVRLE-RDDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVE 394
|
....
gi 2296351947 401 ILML 404
Cdd:COG0303 395 VLLL 398
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
6-404 |
3.33e-150 |
|
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: 430.76 E-value: 3.33e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 6 VDEALARILKSAEPRGIEEVELSNAGGRVVATPVLAHLLQPPFDGSAMDGYALIAPDNISYPVQFDIIGESAAGNRFEGE 85
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLRVVGEIPAGEPPDGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 86 LGIGQAVRIFTGAPLPKGTDAIVIQEHTERSSNRLTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELDAAALSLAAASGN 165
Cdd:cd00887 81 LGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 166 AKIDVFKKPKVAIIATGDELVLPGEIPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQSdIDILV 245
Cdd:cd00887 161 AEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEE-ADVVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 246 TIGGASVGDRDFVHGALRKLGVELDFWKIAMRPGKPLMYGRveVNGKIvhVIGLPGNPVSSLVCSLVFLRPLVARLAG-T 324
Cdd:cd00887 240 TSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGR--LGGKP--VFGLPGNPVSALVTFELFVRPALRKLQGaP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 325 NSEADIRPAKLGIALPANDHRRDYIRATVEsRTDGTLVASPFPVQDSSMLSALVRSRALLIREENAPAAAIGDDCRILML 404
Cdd:cd00887 316 EPEPPRVKARLAEDLKSKPGRREFLRVRLE-RDEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
4-402 |
1.88e-85 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 271.49 E-value: 1.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 4 LPVDEALARILKSAEP-RGIEEVELSNAGGRVVATPVLAHLLQPPFDGSAMDGYALI--APDNISYpvqfDIIGESAAGN 80
Cdd:PRK14491 199 LSVSQGLDKILSLVTPvTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRsdDLEPESY----TLVGEVLAGH 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 81 RFEGELGIGQAVRIFTGAPLPKGTDAIVIQEHTERSSNRLTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELDAAALSLA 160
Cdd:PRK14491 275 QYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 161 AASGNAKIDVFKKPKVAIIATGDELVLPGEIPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQsD 240
Cdd:PRK14491 355 ASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAA-Q 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 241 IDILVTIGGASVGDRDFVHGALRKLGvELDFWKIAMRPGKPLMYGrvEVNGKIvhVIGLPGNPVSSLVCSLVFLRPLVAR 320
Cdd:PRK14491 434 ADVVISSGGVSVGDADYIKTALAKLG-QIDFWRINMRPGRPLAFG--QIGDSP--FFGLPGNPVAVMVSFLQFVEPALRK 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 321 LAG-TNSEADIRPAKLGIALPANDHRRDYIRATVESRTDGTLVASPFPVQDSSMLSALVRSRALLIREENAPAAAIGDDC 399
Cdd:PRK14491 509 LAGeQNWQPLLFPAIADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGETV 588
|
...
gi 2296351947 400 RIL 402
Cdd:PRK14491 589 TIQ 591
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
19-153 |
1.43e-33 |
|
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: 122.29 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 19 PRGIEEVEL--SNAGGRVVATPVLAHLLQPPFDGSAMDGYALIAPDnisyPVQFDIIGESAAGNRFEGELGIGQAVRIFT 96
Cdd:pfam03453 3 LGTEETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAAD----GFGASEVNPIAAGEPPGPLLPGGEAVRIMT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2296351947 97 GAPLPKGTDAIVIQEHTERSSNR-LTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELD 153
Cdd:pfam03453 79 GAPLPEGADAVVMVEDTEEGGGRtVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLT 136
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
177-309 |
4.79e-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: 4.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 177 AIIATGDELVLPGeipgkdQIVASNSVGIAEIVRRAGGTPQDKGII--PDDPAKIEQAIEDSLqSDIDILVTIGGASVGD 254
Cdd:smart00852 1 AIISTGDELLSGG------QIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREAL-AEADVVITTGGTGPGP 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2296351947 255 RDFVHGALRK-LGVELDFWKIAMRPGKP-----LMYGRVEVNGKIVHVIGLPGNPVSSLVC 309
Cdd:smart00852 74 DDLTPEALAElGGRELLGHGVAMRPGGPpgplaNLSGTAPGVRGKKPVFGLPGNPVAALVM 134
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
174-316 |
5.16e-31 |
|
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: 115.88 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 174 PKVAIIATGDELVLPGEIPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQsDIDILVTIGGASVG 253
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVD-EADVVLTTGGTGVG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2296351947 254 DRDFVHGALRKLG----------VELDFWKIAMRPGKPLMYGRveVNGKIvhVIGLPGNPVSSLVCSLVFLRP 316
Cdd:TIGR00177 80 PRDVTPEALEELGekeipgfgefRMLSSLPVLSRPGKPATAGV--RGGTL--IFNLPGNPVSALVTFEVLILP 148
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
3-404 |
1.35e-156 |
|
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: 447.23 E-value: 1.35e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 3 LLPVDEALARILKSAEPRGIEEVELSNAGGRVVATPVLAHLLQPPFDGSAMDGYALIAPD-NISYPVQFDIIGESAAGNR 81
Cdd:COG0303 1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADlAGANPVTLRVVGEIAAGSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 82 FEGELGIGQAVRIFTGAPLPKGTDAIVIQEHTERSSNRLTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELDAAALSLAA 161
Cdd:COG0303 81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 162 ASGNAKIDVFKKPKVAIIATGDELVLPGEIPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQsDI 241
Cdd:COG0303 161 SLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALA-EA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 242 DILVTIGGASVGDRDFVHGALRKLGVELDFWKIAMRPGKPLMYGRveVNGKivHVIGLPGNPVSSLVCSLVFLRPLVARL 321
Cdd:COG0303 240 DLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGR--LGGK--PVFGLPGNPVSALVTFELFVRPALRKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 322 AG-TNSEADIRPAKLGIALPANDHRRDYIRATVEsRTDGTLVASPFPVQDSSMLSALVRSRALLIREENAPAAAIGDDCR 400
Cdd:COG0303 316 AGlPPPPPPRVRARLAEDLPKKPGRTEFLRVRLE-RDDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVE 394
|
....
gi 2296351947 401 ILML 404
Cdd:COG0303 395 VLLL 398
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
6-404 |
3.33e-150 |
|
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: 430.76 E-value: 3.33e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 6 VDEALARILKSAEPRGIEEVELSNAGGRVVATPVLAHLLQPPFDGSAMDGYALIAPDNISYPVQFDIIGESAAGNRFEGE 85
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVTLRVVGEIPAGEPPDGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 86 LGIGQAVRIFTGAPLPKGTDAIVIQEHTERSSNRLTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELDAAALSLAAASGN 165
Cdd:cd00887 81 LGPGEAVRIMTGAPLPEGADAVVMVEDTEEEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 166 AKIDVFKKPKVAIIATGDELVLPGEIPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQSdIDILV 245
Cdd:cd00887 161 AEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEE-ADVVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 246 TIGGASVGDRDFVHGALRKLGVELDFWKIAMRPGKPLMYGRveVNGKIvhVIGLPGNPVSSLVCSLVFLRPLVARLAG-T 324
Cdd:cd00887 240 TSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGR--LGGKP--VFGLPGNPVSALVTFELFVRPALRKLQGaP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 325 NSEADIRPAKLGIALPANDHRRDYIRATVEsRTDGTLVASPFPVQDSSMLSALVRSRALLIREENAPAAAIGDDCRILML 404
Cdd:cd00887 316 EPEPPRVKARLAEDLKSKPGRREFLRVRLE-RDEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
4-402 |
1.88e-85 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 271.49 E-value: 1.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 4 LPVDEALARILKSAEP-RGIEEVELSNAGGRVVATPVLAHLLQPPFDGSAMDGYALI--APDNISYpvqfDIIGESAAGN 80
Cdd:PRK14491 199 LSVSQGLDKILSLVTPvTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRsdDLEPESY----TLVGEVLAGH 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 81 RFEGELGIGQAVRIFTGAPLPKGTDAIVIQEHTERSSNRLTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELDAAALSLA 160
Cdd:PRK14491 275 QYDGTLQAGEAVRIMTGAPVPAGADTVVMRELATQDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 161 AASGNAKIDVFKKPKVAIIATGDELVLPGEIPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQsD 240
Cdd:PRK14491 355 ASLGFAEVPVFRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAA-Q 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 241 IDILVTIGGASVGDRDFVHGALRKLGvELDFWKIAMRPGKPLMYGrvEVNGKIvhVIGLPGNPVSSLVCSLVFLRPLVAR 320
Cdd:PRK14491 434 ADVVISSGGVSVGDADYIKTALAKLG-QIDFWRINMRPGRPLAFG--QIGDSP--FFGLPGNPVAVMVSFLQFVEPALRK 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 321 LAG-TNSEADIRPAKLGIALPANDHRRDYIRATVESRTDGTLVASPFPVQDSSMLSALVRSRALLIREENAPAAAIGDDC 399
Cdd:PRK14491 509 LAGeQNWQPLLFPAIADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGETV 588
|
...
gi 2296351947 400 RIL 402
Cdd:PRK14491 589 TIQ 591
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
2-390 |
3.19e-84 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 269.39 E-value: 3.19e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 2 SLLPVDEALARILK--SAEPRGIEEVELSNAGGRVVATPVLAHLLQPPFDGSAMDGYALIAPDNI----SYPVQFDIIGE 75
Cdd:PRK14498 8 TLVSLEEAREILESllSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFgaseANPVRLKLGGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 76 SAAGNRFEGELGIGQAVRIFTGAPLPKGTDAIVIQEHTER-SSNRLTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELDA 154
Cdd:PRK14498 88 VHAGEAPDVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEvDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 155 AALSLAAASGNAKIDVFKKPKVAIIATGDELVLPGEIPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIE 234
Cdd:PRK14498 168 RDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 235 DSLqSDIDILVTIGGASVGDRDFVHGALRKLGvELDFWKIAMRPGKPLMYGrvEVNGKIvhVIGLPGNPVSSLVCSLVFL 314
Cdd:PRK14498 248 KAL-KECDLVLLSGGTSAGAGDVTYRVIEELG-EVLVHGVAIKPGKPTILG--VIGGKP--VVGLPGYPVSALTIFEEFV 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2296351947 315 RPLVARLAGTNSEADIR-PAKLGIALPANDHRRDYIRATVeSRTDGTLVASPFPvQDSSMLSALVRSRALLIREENA 390
Cdd:PRK14498 322 APLLRKLAGLPPPERATvKARLARRVRSELGREEFVPVSL-GRVGDGYVAYPLS-RGSGAITSLVRADGFIEIPANT 396
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
3-376 |
4.39e-73 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 234.22 E-value: 4.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 3 LLPVDEALARILKSAEP-RGIEEVELSNAGGRVVATPVLAHLLQPPFDGSAMDGYALIAPD---NISYPVQfdiiGESAA 78
Cdd:PRK10680 7 LMSLETALTEMLSRVTPlTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADlasGQPLPVA----GKAFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 79 GNRFEGELGIGQAVRIFTGAPLPKGTDAIVIQEHTERSSNRLTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELDAAALS 158
Cdd:PRK10680 83 GQPFHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 159 LAAASGNAKIDVFKKPKVAIIATGDELVLPGEIPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQ 238
Cdd:PRK10680 163 VLASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEADS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 239 SdIDILVTIGGASVGDRDFVHGALRKLGvELDFWKIAMRPGKPLMYGRVEvngkivH--VIGLPGNPVSSLVCSLVFLRP 316
Cdd:PRK10680 243 Q-ADVVISSGGVSVGEADYTKTILEELG-EIAFWKLAIKPGKPFAFGKLS------NswFCGLPGNPVSAALTFYQLVQP 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2296351947 317 LVARLAG-TNSEADIR-PAKLGIALPANDHRRDYIRATVESRTDGTLVASPFPVQDSSMLSA 376
Cdd:PRK10680 315 LLAKLSGnTASGLPPRqRVRTASRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSS 376
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
5-402 |
3.20e-65 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 214.01 E-value: 3.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 5 PVDEALARILKSAEP-RGIEEVELSNAGGRVVATPVLAHLLQPPFDGSAMDGYALIAPDNISYPVQFDIIGESAAGNRFE 83
Cdd:PRK14690 24 PVDTALDLLRARLGPvTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQVLPLIEGRAAAGVPFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 84 GELGIGQAVRIFTGAPLPKGTDAIVIQEHTERSSNRLTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELDAAALSLAAAS 163
Cdd:PRK14690 104 GRVPEGMALRILTGAALPEGVDTVVLEEDVAGDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 164 GNAKIDVFKKPKVAIIATGDELVLPGEIPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIeDSLQSDIDI 243
Cdd:PRK14690 184 GLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARL-DRAAAEADV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 244 LVTIGGASVGDRDFVHGALRKLGVeLDFWKIAMRPGKPLMYGRvevnGKIVHVIGLPGNPVSSLVCSLVFLRPLVARLAG 323
Cdd:PRK14690 263 ILTSGGASAGDEDHVSALLREAGA-MQSWRIALKPGRPLALGL----WQGVPVFGLPGNPVAALVCTLVFARPAMSLLAG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 324 TNSEADIrpaklGIALPA------NDHRRDYIRATVesrTDGTlvASPFPVQDSSMLSALVRSRALLIREENAPAAAIGD 397
Cdd:PRK14690 338 EGWSEPQ-----GFTVPAafekrkKPGRREYLRARL---RQGH--AEVFRSEGSGRISGLSWAEGLVELGDGARRIAPGD 407
|
....*
gi 2296351947 398 DCRIL 402
Cdd:PRK14690 408 PVRFI 412
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
2-384 |
4.69e-60 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 205.82 E-value: 4.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 2 SLLPVDEALARILKSAEPRGIEEVELSNAGGRVVATPVLAHLLQPPFDGSAMDGYALIAPDNisyPVQFDIIGESAAGNR 81
Cdd:PLN02699 6 EMISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDG---PGEYPVITESRAGND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 82 FEG-ELGIGQAVRIFTGAPLPKGTDAIVIQEHTER------SSNRLTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELDA 154
Cdd:PLN02699 83 GLGvTLTPGTVAYVTTGGPIPDGADAVVQVEDTEVvedpldGSKRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 155 AALSLAAASGNAKIDVFKKPKVAIIATGDELVLPGE-IPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAI 233
Cdd:PLN02699 163 SEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTgTLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERIL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 234 EDSLQSDIDILVTIGGASVGDRDFVHGALRKLGvELDFWKIAMRPGKPLMYGRVEV-----NGKIVHVIGLPGNPVSSLV 308
Cdd:PLN02699 243 DEAISSGVDILLTSGGVSMGDRDFVKPLLEKRG-TVYFSKVLMKPGKPLTFAEIDAksapsNSKKMLAFGLPGNPVSCLV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 309 CSLVFLRPLVARLAGTNSEADIR-PAKLGIALPANDHRRDYIRATVE-SRTDGT----LVASPFPVQDSSMLSALVRSRA 382
Cdd:PLN02699 322 CFNLFVVPAIRYLAGWSNPHLLRvQARLREPIKLDPVRPEFHRAIIRwKLNDGSgnpgFVAESTGHQMSSRLLSMKSANA 401
|
..
gi 2296351947 383 LL 384
Cdd:PLN02699 402 LL 403
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
2-374 |
8.45e-51 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 178.85 E-value: 8.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 2 SLLPVDEALARILKSAEP-RGIEEVELSNAGGRVVATPVLAHLLQPPFDGSAMDGYALIAPdniSYPVQFDIIGESAAGN 80
Cdd:PRK14497 9 SLYSIDEAIKVFLSSLNFkPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSS---CTPGEFKVIDKIGIGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 81 RFEGELGIGQAVRIFTGAPLPKGTDAIVIQEHTERSS-NRLTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELDAAALSL 159
Cdd:PRK14497 86 FKEIHIKECEAVEVDTGSMIPMGADAVIKVENTKVINgNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 160 AAASGNAKIDVFKKPKVAIIATGDELVLPGEIPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLqS 239
Cdd:PRK14497 166 LASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAI-S 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 240 DIDILVTIGGASVGDRDFVHGALRKLGvELDFWKIAMRPGKPLMYGrvEVNGKivHVIGLPGNPVSSLVCSLVFLRPLVA 319
Cdd:PRK14497 245 VADVLILTGGTSAGEKDFVHQAIRELG-NIIVHGLKIKPGKPTILG--IVDGK--PVIGLPGNIVSTMVVLNMVILEYLK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2296351947 320 RLAGTNSE-ADIRPAKLGIALP--ANDHRRDYIRATVeSRTDGTLVASPFPVqDSSML 374
Cdd:PRK14497 320 SLYPSRKEiLGLGKIKARLALRvkADEHRNTLIPVYL-FKSDNSYYALPVPF-DSYMV 375
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
19-153 |
1.43e-33 |
|
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: 122.29 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 19 PRGIEEVEL--SNAGGRVVATPVLAHLLQPPFDGSAMDGYALIAPDnisyPVQFDIIGESAAGNRFEGELGIGQAVRIFT 96
Cdd:pfam03453 3 LGTEETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAAD----GFGASEVNPIAAGEPPGPLLPGGEAVRIMT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2296351947 97 GAPLPKGTDAIVIQEHTERSSNR-LTVHEGIEPGRHIRRAGLDFSPGDIVIPTGRELD 153
Cdd:pfam03453 79 GAPLPEGADAVVMVEDTEEGGGRtVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLT 136
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
177-309 |
4.79e-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: 4.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 177 AIIATGDELVLPGeipgkdQIVASNSVGIAEIVRRAGGTPQDKGII--PDDPAKIEQAIEDSLqSDIDILVTIGGASVGD 254
Cdd:smart00852 1 AIISTGDELLSGG------QIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREAL-AEADVVITTGGTGPGP 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2296351947 255 RDFVHGALRK-LGVELDFWKIAMRPGKP-----LMYGRVEVNGKIVHVIGLPGNPVSSLVC 309
Cdd:smart00852 74 DDLTPEALAElGGRELLGHGVAMRPGGPpgplaNLSGTAPGVRGKKPVFGLPGNPVAALVM 134
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
174-316 |
5.16e-31 |
|
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: 115.88 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 174 PKVAIIATGDELVLPGEIPGKDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQsDIDILVTIGGASVG 253
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVD-EADVVLTTGGTGVG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2296351947 254 DRDFVHGALRKLG----------VELDFWKIAMRPGKPLMYGRveVNGKIvhVIGLPGNPVSSLVCSLVFLRP 316
Cdd:TIGR00177 80 PRDVTPEALEELGekeipgfgefRMLSSLPVLSRPGKPATAGV--RGGTL--IFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
177-320 |
4.89e-29 |
|
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: 110.03 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 177 AIIATGDELVLpgeipgkDQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQSDiDILVTIGGASVGDRD 256
Cdd:pfam00994 1 AIITTGDELLP-------GQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEA-DVVITTGGTGPGPDD 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2296351947 257 FVHGALRKLG------VELDFWKIAMRPGKPLMYGRV-EVNGKIVHVIGLPGNPVSSLVCSLVFLRPLVAR 320
Cdd:pfam00994 73 VTPEALAELGgrelpgFEELFRGVSLKPGKPVGTAPGaILSRAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
175-318 |
1.06e-19 |
|
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. The domain is presumed to bind molybdopterin.
Pssm-ID: 238387 [Multi-domain] Cd Length: 133 Bit Score: 84.32 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 175 KVAIIATGDELVLpGEIPGKDQIVASnsvgiaEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLqSDIDILVTIGGASVGD 254
Cdd:cd00758 1 RVAIVTVSDELSQ-GQIEDTNGPALE------ALLEDLGCEVIYAGVVPDDADSIRAALIEAS-READLVLTTGGTGVGR 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2296351947 255 RDFVHGALRKLG-VELDFWKIAMRPGKPLMYGRVevngKIVHVIGLPGNPVSSLVCSLVFLRPLV 318
Cdd:cd00758 73 RDVTPEALAELGeREAHGKGVALAPGSRTAFGII----GKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
171-301 |
9.53e-09 |
|
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: 56.40 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 171 FKKPKVAIIATGDElVLPGEIPGKDQIVasnsvgIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQSDIDILVTIGGA 250
Cdd:cd03522 157 FRPLRVGLIVTGSE-VYGGRIEDKFGPV------LRARLAALGVELVEQVIVPHDEAAIAAAIAEALEAGAELLILTGGA 229
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2296351947 251 SVGDRDFVHGALRKLGVELDFWKIAMRPGKPLMYGRVEVngkiVHVIGLPG 301
Cdd:cd03522 230 SVDPDDVTPAAIRAAGGEVIRYGMPVDPGNLLLLGYLGG----VPVIGLPG 276
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
332-404 |
1.36e-08 |
|
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: 51.07 E-value: 1.36e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2296351947 332 PAKLGIALPANDHRRDYIRATVESrTDGTLVASPFPVQDSSMLSALVRSRALLIREENAPAAAIGDDCRILML 404
Cdd:pfam03454 1 KARLARDLKSDPGRREFVRVRLHE-EDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
175-249 |
8.55e-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: 45.55 E-value: 8.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2296351947 175 KVAIIATGDELvLPGeipgkdQIVASNSVGIAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQSDiDILVTIGG 249
Cdd:cd00885 1 TAEIIAIGDEL-LSG------QIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERA-DLVITTGG 67
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
205-256 |
6.71e-05 |
|
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440287 [Multi-domain] Cd Length: 169 Bit Score: 43.18 E-value: 6.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2296351947 205 IAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSL-QSDIDILVTIGGASVGDRD 256
Cdd:COG0521 34 LVELLEEAGHEVVARRIVPDDKDAIRAALRELIdDEGVDLVLTTGGTGLSPRD 86
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
197-265 |
8.37e-05 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 44.16 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296351947 197 IVASNSVG-----------IAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSLQSDIDILVTIGGASVGDRDFVHGALRKL 265
Cdd:PRK03604 161 LVLSDSIAagtkedrsgklIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAEGYALIITTGGTGLGPRDVTPEALAPL 240
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
205-256 |
2.30e-04 |
|
MogA_MoaB 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). MogA, together with MoeA, 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. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.
Pssm-ID: 238451 [Multi-domain] Cd Length: 152 Bit Score: 41.31 E-value: 2.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2296351947 205 IAEIVRRAGGTPQDKGIIPDDPAKIEQAIEDSL-QSDIDILVTIGGASVGDRD 256
Cdd:cd00886 25 LVELLEEAGHEVVAYEIVPDDKDEIREALIEWAdEDGVDLILTTGGTGLAPRD 77
|
|
| |
