|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
5-391 |
9.51e-138 |
|
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: 399.18 E-value: 9.51e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 5 VQTAVDIISNLTLSLNFEIIPIENATSRICAQDVFATSFLPKFNNSAMDGYAIIYED---KNSELEIIDIIFAGDNNDKL 81
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADtagASVTLRVVGEIPAGEPPDGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 82 LEKNSCIKIMTGAKIPENSTAIIPKEDIEELnDNKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIALLASQG 161
Cdd:cd00887 81 LGPGEAVRIMTGAPLPEGADAVVMVEDTEEE-GGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 162 ISHIKVYKKPKVTIFTSGEELKLHYEKIESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSLD-ADLII 240
Cdd:cd00887 160 IAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEeADVVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 241 TSGGVSVGDADFTKEAFYELGFETLFDGINVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMFGKILIQKFLGSKNIHQ 320
Cdd:cd00887 240 TSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEP 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847327014 321 NFILGKIKDTFCTKKGKTTIIPGFFDGE----FFEVSQKRSPGMVSILSSCNSMIIIDDEVETLKKDNLIKILPI 391
Cdd:cd00887 320 PRVKARLAEDLKSKPGRREFLRVRLERDegglVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
3-393 |
5.12e-131 |
|
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: 382.13 E-value: 5.12e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 3 INVQTAVDIISNLTLSLNFEIIPIENATSRICAQDVFATSFLPKFNNSAMDGYAIIYED----KNSELEIIDIIFAGDNN 78
Cdd:COG0303 2 ISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADlagaNPVTLRVVGEIAAGSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 79 DKLLEKNSCIKIMTGAKIPENSTAIIPKEDIEElNDNKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIALLA 158
Cdd:COG0303 82 PGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER-EGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 159 SQGISHIKVYKKPKVTIFTSGEELKLHYEKIESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSL-DAD 237
Cdd:COG0303 161 SLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALaEAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 238 LIITSGGVSVGDADFTKEAFYELGFETLFDGINVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMFGKILIQKFLGSKN 317
Cdd:COG0303 241 LVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLPP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 318 IHQNFILGKIKDTFCTKKGKTTIIPGFF---DGEFF-EVSQKRSPGMVSILSSCNSMIIIDDEVETLKKDNLIKILPINW 393
Cdd:COG0303 321 PPPPRVRARLAEDLPKKPGRTEFLRVRLerdDGELVvEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLLLDG 400
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
8-380 |
2.80e-77 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 251.29 E-value: 2.80e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 8 AVDIISNL--TLSLNFEIIPIENATSRICAQDVFATSFLPKFNNSAMDGYAI----IY---EDKNSELEIIDIIFAGDNN 78
Cdd:PRK14498 15 AREILESLlsELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVraadTFgasEANPVRLKLGGEVHAGEAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 79 DKLLEKNSCIKIMTGAKIPENSTAIIPKEDIEELNDNKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIALLA 158
Cdd:PRK14498 95 DVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 159 SQGISHIKVYKKPKVTIFTSGEELKLHYEKIESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSLD-AD 237
Cdd:PRK14498 175 AGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKeCD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 238 LIITSGGVSVGDADFTKEAFYELGfETLFDGINVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMFGKILIQKFLGSKN 317
Cdd:PRK14498 255 LVLLSGGTSAGAGDVTYRVIEELG-EVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLRKLAGLPP 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847327014 318 IHQNFILGKIKDTFCTKKGKTTIIP---GFFDGEFFEVSQKRSPGMVSILSSCNSMIIIDDEVETL 380
Cdd:PRK14498 334 PERATVKARLARRVRSELGREEFVPvslGRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTEGL 399
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
22-161 |
9.82e-43 |
|
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: 146.56 E-value: 9.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 22 EIIPIENATS--RICAQDVFATSFLPKFNNSAMDGYAIIYEDKNSELEIIdIIFAGDNNDKLLEKNSCIKIMTGAKIPEN 99
Cdd:pfam03453 7 ETVPLEALDAlgRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVN-PIAAGEPPGPLLPGGEAVRIMTGAPLPEG 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847327014 100 STAIIPKEDIEELNDNKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIALLASQG 161
Cdd:pfam03453 86 ADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
171-304 |
2.93e-32 |
|
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.
Pssm-ID: 272944 [Multi-domain] Cd Length: 148 Bit Score: 118.96 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 171 PKVTIFTSGEELKLHYEKIESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSLD-ADLIITSGGVSVGD 249
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDeADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847327014 250 ADFTKEAFYELgFETLFDG-----------INVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMF 304
Cdd:TIGR00177 81 RDVTPEALEEL-GEKEIPGfgefrmlsslpVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVL 145
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
175-302 |
2.53e-28 |
|
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: 108.06 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 175 IFTSGEELklhyekIESFQIYNSNTPTFISRTQELGCDVTFIG--QAKDTIEAIKELVNNSLD-ADLIITSGGVSVGDAD 251
Cdd:smart00852 2 IISTGDEL------LSGGQIRDSNGPMLAALLRELGIEVVRVVvvGGPDDPEAIREALREALAeADVVITTGGTGPGPDD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1847327014 252 FTKEAFYE-LGFETLFDGINVKPGKPTVF---------GKIKDTYILNLPGNPLASALIFE 302
Cdd:smart00852 76 LTPEALAElGGRELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMFE 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
5-391 |
9.51e-138 |
|
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: 399.18 E-value: 9.51e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 5 VQTAVDIISNLTLSLNFEIIPIENATSRICAQDVFATSFLPKFNNSAMDGYAIIYED---KNSELEIIDIIFAGDNNDKL 81
Cdd:cd00887 1 VEAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADtagASVTLRVVGEIPAGEPPDGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 82 LEKNSCIKIMTGAKIPENSTAIIPKEDIEELnDNKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIALLASQG 161
Cdd:cd00887 81 LGPGEAVRIMTGAPLPEGADAVVMVEDTEEE-GGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 162 ISHIKVYKKPKVTIFTSGEELKLHYEKIESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSLD-ADLII 240
Cdd:cd00887 160 IAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEeADVVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 241 TSGGVSVGDADFTKEAFYELGFETLFDGINVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMFGKILIQKFLGSKNIHQ 320
Cdd:cd00887 240 TSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEP 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847327014 321 NFILGKIKDTFCTKKGKTTIIPGFFDGE----FFEVSQKRSPGMVSILSSCNSMIIIDDEVETLKKDNLIKILPI 391
Cdd:cd00887 320 PRVKARLAEDLKSKPGRREFLRVRLERDegglVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
3-393 |
5.12e-131 |
|
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: 382.13 E-value: 5.12e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 3 INVQTAVDIISNLTLSLNFEIIPIENATSRICAQDVFATSFLPKFNNSAMDGYAIIYED----KNSELEIIDIIFAGDNN 78
Cdd:COG0303 2 ISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADlagaNPVTLRVVGEIAAGSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 79 DKLLEKNSCIKIMTGAKIPENSTAIIPKEDIEElNDNKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIALLA 158
Cdd:COG0303 82 PGPLGPGEAVRIMTGAPLPEGADAVVMQEDTER-EGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 159 SQGISHIKVYKKPKVTIFTSGEELKLHYEKIESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSL-DAD 237
Cdd:COG0303 161 SLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALaEAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 238 LIITSGGVSVGDADFTKEAFYELGFETLFDGINVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMFGKILIQKFLGSKN 317
Cdd:COG0303 241 LVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLPP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 318 IHQNFILGKIKDTFCTKKGKTTIIPGFF---DGEFF-EVSQKRSPGMVSILSSCNSMIIIDDEVETLKKDNLIKILPINW 393
Cdd:COG0303 321 PPPPRVRARLAEDLPKKPGRTEFLRVRLerdDGELVvEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLLLDG 400
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
8-380 |
2.80e-77 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 251.29 E-value: 2.80e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 8 AVDIISNL--TLSLNFEIIPIENATSRICAQDVFATSFLPKFNNSAMDGYAI----IY---EDKNSELEIIDIIFAGDNN 78
Cdd:PRK14498 15 AREILESLlsELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVraadTFgasEANPVRLKLGGEVHAGEAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 79 DKLLEKNSCIKIMTGAKIPENSTAIIPKEDIEELNDNKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIALLA 158
Cdd:PRK14498 95 DVEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 159 SQGISHIKVYKKPKVTIFTSGEELKLHYEKIESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSLD-AD 237
Cdd:PRK14498 175 AGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKeCD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 238 LIITSGGVSVGDADFTKEAFYELGfETLFDGINVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMFGKILIQKFLGSKN 317
Cdd:PRK14498 255 LVLLSGGTSAGAGDVTYRVIEELG-EVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLRKLAGLPP 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847327014 318 IHQNFILGKIKDTFCTKKGKTTIIP---GFFDGEFFEVSQKRSPGMVSILSSCNSMIIIDDEVETL 380
Cdd:PRK14498 334 PERATVKARLARRVRSELGREEFVPvslGRVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTEGL 399
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
11-390 |
1.51e-74 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 242.98 E-value: 1.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 11 IISNLTLSLNFEIIPIENATSRICAQDVFATSFLPKFNNSAMDGYAIIYEDKNSE-LEIIDIIFAGDNNDKLLEKNSCIK 89
Cdd:PRK14491 208 ILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPEsYTLVGEVLAGHQYDGTLQAGEAVR 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 90 IMTGAKIPENSTAIIPKEDIEElNDNKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIALLASQGISHIKVYK 169
Cdd:PRK14491 288 IMTGAPVPAGADTVVMRELATQ-DGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFR 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 170 KPKVTIFTSGEELKLHYEKIESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKE-LVNNSLDADLIITSGGVSVG 248
Cdd:PRK14491 367 RPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEAtLEQAAAQADVVISSGGVSVG 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 249 DADFTKEAFYELGfETLFDGINVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMFGKILIQKFLGSKNIHQNFILGKIK 328
Cdd:PRK14491 447 DADYIKTALAKLG-QIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKLAGEQNWQPLLFPAIAD 525
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1847327014 329 DTFCTKKGKTTIIPGFF----DGEfFEV--SQKRSPGMVSILSSCNSMIIIDDEVETLKKDNLIKILP 390
Cdd:PRK14491 526 ETLRSRQGRTEFSRGIYhlgaDGR-LHVrtTGKQGSGILSSMSEANCLIEIGPAAETVNAGETVTIQP 592
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
3-320 |
1.21e-67 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 219.96 E-value: 1.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 3 INVQTAV-DIISNLTLSLNFEIIPIENATSRICAQDVFATSFLPKFNNSAMDGYAIIYEDKNSE--LEIIDIIFAGDNND 79
Cdd:PRK10680 8 MSLETALtEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGqpLPVAGKAFAGQPFH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 80 KLLEKNSCIKIMTGAKIPENSTAIIPKEDiEELNDNKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIALLAS 159
Cdd:PRK10680 88 GEWPAGTCIRIMTGAPVPEGCEAVVMQEQ-TEQTDDGVRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLAS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 160 QGISHIKVYKKPKVTIFTSGEELKLHYEKIESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKE-LVNNSLDADL 238
Cdd:PRK10680 167 LGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAaFIEADSQADV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 239 IITSGGVSVGDADFTKEAFYELGfETLFDGINVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMFGKILIQKFLGSKNI 318
Cdd:PRK10680 247 VISSGGVSVGEADYTKTILEELG-EIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNTAS 325
|
..
gi 1847327014 319 HQ 320
Cdd:PRK10680 326 GL 327
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
4-373 |
6.92e-61 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 205.81 E-value: 6.92e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 4 NVQTAVDIISNLTLSLNF----EIIPIENATSRICAQDVFATSFLPKFNNSAMDGYAIIYEDKNSELEIIDIIFAGDNND 79
Cdd:PRK14497 9 SLYSIDEAIKVFLSSLNFkpkiVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGEFKVIDKIGIGEFKE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 80 KLLEKNSCIKIMTGAKIPENSTAIIPKEDIEELNDNKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIALLAS 159
Cdd:PRK14497 89 IHIKECEAVEVDTGSMIPMGADAVIKVENTKVINGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLAS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 160 QGISHIKVYKKPKVTIFTSGEELKLHYEKIESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSLD-ADL 238
Cdd:PRK14497 169 LGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISvADV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 239 IITSGGVSVGDADFTKEAFYELGfETLFDGINVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMFGKILIQKFLGSKNi 318
Cdd:PRK14497 249 LILTGGTSAGEKDFVHQAIRELG-NIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPSRK- 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847327014 319 hQNFILGKIKDTFCTK----KGKTTIIPGFF---DGEFFEVSQKRSPGMVSILSSCNSMIII 373
Cdd:PRK14497 327 -EILGLGKIKARLALRvkadEHRNTLIPVYLfksDNSYYALPVPFDSYMVGTFSLTDGYIML 387
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
3-319 |
2.63e-53 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 187.71 E-value: 2.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 3 INVQTAVDIISNLTLSLNFEIIPIENATSRICAQDVFATSFLPKFNNSAMDGYAIIYEDKNSELEIIDIIFAG-DNNDKL 81
Cdd:PLN02699 8 ISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGnDGLGVT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 82 LEKNSCIKIMTGAKIPENSTAIIPKEDIEELND-----NKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIAL 156
Cdd:PLN02699 88 LTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDpldgsKRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASEIGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 157 LASQGISHIKVYKKPKVTIFTSGEELKLHYEK-IESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSL- 234
Cdd:PLN02699 168 LATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDEAIs 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 235 -DADLIITSGGVSVGDADFTKEAFYELGfETLFDGINVKPGKPTVFGKI---------KDTYILNLPGNPLASALIFEMF 304
Cdd:PLN02699 248 sGVDILLTSGGVSMGDRDFVKPLLEKRG-TVYFSKVLMKPGKPLTFAEIdaksapsnsKKMLAFGLPGNPVSCLVCFNLF 326
|
330
....*....|....*
gi 1847327014 305 GKILIQKFLGSKNIH 319
Cdd:PLN02699 327 VVPAIRYLAGWSNPH 341
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
22-161 |
9.82e-43 |
|
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: 146.56 E-value: 9.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 22 EIIPIENATS--RICAQDVFATSFLPKFNNSAMDGYAIIYEDKNSELEIIdIIFAGDNNDKLLEKNSCIKIMTGAKIPEN 99
Cdd:pfam03453 7 ETVPLEALDAlgRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVN-PIAAGEPPGPLLPGGEAVRIMTGAPLPEG 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847327014 100 STAIIPKEDIEELNDNKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIALLASQG 161
Cdd:pfam03453 86 ADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
171-304 |
2.93e-32 |
|
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.
Pssm-ID: 272944 [Multi-domain] Cd Length: 148 Bit Score: 118.96 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 171 PKVTIFTSGEELKLHYEKIESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSLD-ADLIITSGGVSVGD 249
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDeADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847327014 250 ADFTKEAFYELgFETLFDG-----------INVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMF 304
Cdd:TIGR00177 81 RDVTPEALEEL-GEKEIPGfgefrmlsslpVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVL 145
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
5-306 |
2.42e-30 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 120.79 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 5 VQTAVDII-SNLTLSLNFEIIPIENATSRICAQDVFATSFLPKFNNSAMDGYAIIYEdKNSELEIIDII----FAGDNND 79
Cdd:PRK14690 25 VDTALDLLrARLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGA-APEGAQVLPLIegraAAGVPFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 80 KLLEKNSCIKIMTGAKIPENSTAIIPKEDIEeLNDNKIKILKNVKEFQHIRYIGEDIKQNELLINIGDEINFSKIALLAS 159
Cdd:PRK14690 104 GRVPEGMALRILTGAALPEGVDTVVLEEDVA-GDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 160 QGISHIKVYKKPKVTIFTSGEELKLHYEKIESFQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNN-SLDADL 238
Cdd:PRK14690 183 VGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRaAAEADV 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1847327014 239 IITSGGVSVGDADFTKEAFYELGFETLFDgINVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMFGK 306
Cdd:PRK14690 263 ILTSGGASAGDEDHVSALLREAGAMQSWR-IALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFAR 329
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
175-302 |
2.53e-28 |
|
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: 108.06 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 175 IFTSGEELklhyekIESFQIYNSNTPTFISRTQELGCDVTFIG--QAKDTIEAIKELVNNSLD-ADLIITSGGVSVGDAD 251
Cdd:smart00852 2 IISTGDEL------LSGGQIRDSNGPMLAALLRELGIEVVRVVvvGGPDDPEAIREALREALAeADVVITTGGTGPGPDD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1847327014 252 FTKEAFYE-LGFETLFDGINVKPGKPTVF---------GKIKDTYILNLPGNPLASALIFE 302
Cdd:smart00852 76 LTPEALAElGGRELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMFE 136
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
175-311 |
3.06e-27 |
|
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: 105.41 E-value: 3.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 175 IFTSGEELKLHyekiesfQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSLD-ADLIITSGGVSVGDADFT 253
Cdd:pfam00994 2 IITTGDELLPG-------QIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEeADVVITTGGTGPGPDDVT 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1847327014 254 KEAFYELG------FETLFDGINVKPGKPTVFGKI-----KDTYILNLPGNPLASALIFEMFGKILIQK 311
Cdd:pfam00994 75 PEALAELGgrelpgFEELFRGVSLKPGKPVGTAPGailsrAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
172-304 |
6.50e-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: 101.65 E-value: 6.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 172 KVTIFTSGEELKLHyekiesfQIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSLD-ADLIITSGGVSVGDA 250
Cdd:cd00758 1 RVAIVTVSDELSQG-------QIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASReADLVLTTGGTGVGRR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1847327014 251 DFTKEAFYELG-FETLFDGINVKPGKPTVFGKIKDTYILNLPGNPLASALIFEMF 304
Cdd:cd00758 74 DVTPEALAELGeREAHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEAL 128
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
155-292 |
2.45e-06 |
|
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: 49.08 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 155 ALLASQGISHIKVYKKPKVTIFTSGEE--LKLHYEKIEsfqiynsntPTFISRTQELGCDVTFIGQAKDTIEAIKELVNN 232
Cdd:cd03522 144 ALARDGPLLRVAPFRPLRVGLIVTGSEvyGGRIEDKFG---------PVLRARLAALGVELVEQVIVPHDEAAIAAAIAE 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847327014 233 SLD--ADLIITSGGVSVGDADFTKEAFYELGFETLFDGINVKPGKPTVFGKIKDTYILNLPG 292
Cdd:cd03522 215 ALEagAELLILTGGASVDPDDVTPAAIRAAGGEVIRYGMPVDPGNLLLLGYLGGVPVIGLPG 276
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
220-294 |
7.84e-06 |
|
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: 45.88 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 220 KDTIEAIKELVNNSLD---ADLIITSGGVSVGDADFTKEAFYEL------GFETLFDGINVKPGKPT------VFGKIKD 284
Cdd:COG0521 52 PDDKDAIRAALRELIDdegVDLVLTTGGTGLSPRDVTPEATRPLldkelpGFGELFRALSLEEIGPSailsraVAGIRGG 131
|
90
....*....|
gi 1847327014 285 TYILNLPGNP 294
Cdd:COG0521 132 TLIFNLPGSP 141
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
193-256 |
8.00e-04 |
|
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.
Pssm-ID: 238450 [Multi-domain] Cd Length: 170 Bit Score: 39.77 E-value: 8.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1847327014 193 QIYNSNTPTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSLD-ADLIITSGGvsVG---DaDFTKEA 256
Cdd:cd00885 15 QIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASErADLVITTGG--LGpthD-DLTREA 79
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
200-298 |
8.80e-04 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 41.08 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 200 PTFISRTQELGCDVTFIGQAKDTIEAIKELVNNSLDA--DLIITSGGVSVGDADFTKEAFYELgFETLFDGI-----NVK 272
Cdd:PRK03604 178 KLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAEgyALIITTGGTGLGPRDVTPEALAPL-LERRLPGIaealrSWG 256
|
90 100 110
....*....|....*....|....*....|...
gi 1847327014 273 PGK-PT------VFGKIKDTYILNLPGNPLASA 298
Cdd:PRK03604 257 QGRtPTamlsrlVAGMIGNSLVVALPGSPGGAS 289
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
220-308 |
1.96e-03 |
|
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: 38.61 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847327014 220 KDTIEAIKELVN---NSLDADLIITSGGVSVGDADFTKEAFYEL------GFETLFDGINVKPGKPTVF-----GKIKDT 285
Cdd:cd00886 43 PDDKDEIREALIewaDEDGVDLILTTGGTGLAPRDVTPEATRPLldkelpGFGEAFRALSLEETGTAMLsravaGIRGGT 122
|
90 100
....*....|....*....|....*..
gi 1847327014 286 YILNLPGNP----LASALIFEMFGKIL 308
Cdd:cd00886 123 LIFNLPGSPkavrEALEVILPELPHLL 149
|
|
| |
