|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
22-395 |
6.61e-174 |
|
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: 490.76 E-value: 6.61e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 22 PLPQERVALGDADSRILAAPLIADLDLPPWDNSAMDGYALRLDDWQGE---PLRVSQRIFAGQAP-APLEPGTCARIFTG 97
Cdd:COG0303 17 PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAnpvTLRVVGEIAAGSPPpGPLGPGEAVRIMTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 98 APVPAGADCVEMQENAEVlDDGRVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLGPVELGVAASLGRAQLEVHRRLKV 177
Cdd:COG0303 97 APLPEGADAVVMQEDTER-EGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 178 AVLSTGDELVAPGQPLGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRL--GSLQADLILSTGGVSVGEADY 255
Cdd:COG0303 176 AILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALreALAEADLVITSGGVSVGDYDL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 256 LGQALREEG-ELTLWKLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARPYLLRRAGKIDVAPLSVEVPAGFDWP 334
Cdd:COG0303 256 VKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLPPPPPPRVRARLAEDLP 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 975031383 335 RAGARREYQRARLENG----RAVPHRNQGSNVLQTAAWAHGLVELREDRT-FAEGDPVRFIPLAEL 395
Cdd:COG0303 336 KKPGRTEFLRVRLERDdgelVVEPLGGQGSGLLSSLAEADGLIVLPEGVEgVEAGEEVEVLLLDGL 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
22-392 |
3.43e-165 |
|
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: 468.51 E-value: 3.43e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 22 PLPQERVALGDADSRILAAPLIADLDLPPWDNSAMDGYALRLDDWQGEP--LRVSQRIFAGQAPA-PLEPGTCARIFTGA 98
Cdd:cd00887 14 PLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASvtLRVVGEIPAGEPPDgPLGPGEAVRIMTGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 99 PVPAGADCVEMQENAEVlDDGRVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLGPVELGVAASLGRAQLEVHRRLKVA 178
Cdd:cd00887 94 PLPEGADAVVMVEDTEE-EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 179 VLSTGDELVAPGQPLGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRLGSL--QADLILSTGGVSVGEADYL 256
Cdd:cd00887 173 IISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEAleEADVVITSGGVSVGDYDFV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 257 GQALREE-GELTLWKLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARPYLLRRAGKIDVAPLSVEVPAGFDWPR 335
Cdd:cd00887 253 KEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRVKARLAEDLKS 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 975031383 336 AGARREYQRARLEN----GRAVPHRNQGSNVLQTAAWAHGLVELREDRT-FAEGDPVRFIPL 392
Cdd:cd00887 333 KPGRREFLRVRLERdeggLVVAPPGGQGSGLLSSLARADGLIVIPEGVEgLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
25-396 |
5.33e-113 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 342.36 E-value: 5.33e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 25 QERVALGDADSRILAAPLIADLDLPPWDNSAMDGYALRLDDWQGEPLRVSQRIFAGQA-PAPLEPGTCARIFTGAPVPAG 103
Cdd:PRK14491 218 TEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESYTLVGEVLAGHQyDGTLQAGEAVRIMTGAPVPAG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 104 ADCVEMQENAEvLDDGRVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLGPVELGVAASLGRAQLEVHRRLKVAVLSTG 183
Cdd:PRK14491 298 ADTVVMRELAT-QDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 184 DELVAPGQPLGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRL--GSLQADLILSTGGVSVGEADYLGQALR 261
Cdd:PRK14491 377 DEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLeqAAAQADVVISSGGVSVGDADYIKTALA 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 262 EEGELTLWKLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARPYLLRRAGKIDVAPLSVEVPAGFDWPRAGARRE 341
Cdd:PRK14491 457 KLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKLAGEQNWQPLLFPAIADETLRSRQGRTE 536
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 975031383 342 YQRA--RL-ENGRA--VPHRNQGSNVLQTAAWAHGLVEL-REDRTFAEGDPVRFIPLAELL 396
Cdd:PRK14491 537 FSRGiyHLgADGRLhvRTTGKQGSGILSSMSEANCLIEIgPAAETVNAGETVTIQPLAGLL 597
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
22-165 |
5.51e-50 |
|
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: 165.43 E-value: 5.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 22 PLPQERVALGDADS--RILAAPLIADLDLPPWDNSAMDGYALRLDDwqGEPLRVSQRIFAGQAPAP-LEPGTCARIFTGA 98
Cdd:pfam03453 3 LGTEETVPLEALDAlgRVLAEDVVAPRDVPPFDRSAMDGYAVRAAD--GFGASEVNPIAAGEPPGPlLPGGEAVRIMTGA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 975031383 99 PVPAGADCVEMQENAEVLDDGRVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLGPVELGVAASLG 165
Cdd:pfam03453 81 PLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
175-309 |
3.25e-40 |
|
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: 139.76 E-value: 3.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 175 LKVAVLSTGDELVAPGQPLGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRL--GSLQADLILSTGGVSVGE 252
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILrkAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 975031383 253 ADYLGQALREEGE-----------LTLWKLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARP 309
Cdd:TIGR00177 81 RDVTPEALEELGEkeipgfgefrmLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-306 |
1.34e-30 |
|
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: 114.22 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 178 AVLSTGDELVAPGQplgpgqIYNSNRALLISWLRRLGCEVSDQGIL--PDDLAETRKRLGSL--QADLILSTGGVSVGEA 253
Cdd:smart00852 1 AIISTGDELLSGGQ------IRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREAlaEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 975031383 254 DYLGQALREEGELTL--WKLALKPGKPLT---------CGRFRGIPLIGLPGNPASTLVTFGLL 306
Cdd:smart00852 75 DLTPEALAELGGRELlgHGVAMRPGGPPGplanlsgtaPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
22-395 |
6.61e-174 |
|
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: 490.76 E-value: 6.61e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 22 PLPQERVALGDADSRILAAPLIADLDLPPWDNSAMDGYALRLDDWQGE---PLRVSQRIFAGQAP-APLEPGTCARIFTG 97
Cdd:COG0303 17 PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAnpvTLRVVGEIAAGSPPpGPLGPGEAVRIMTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 98 APVPAGADCVEMQENAEVlDDGRVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLGPVELGVAASLGRAQLEVHRRLKV 177
Cdd:COG0303 97 APLPEGADAVVMQEDTER-EGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 178 AVLSTGDELVAPGQPLGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRL--GSLQADLILSTGGVSVGEADY 255
Cdd:COG0303 176 AILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALreALAEADLVITSGGVSVGDYDL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 256 LGQALREEG-ELTLWKLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARPYLLRRAGKIDVAPLSVEVPAGFDWP 334
Cdd:COG0303 256 VKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLPPPPPPRVRARLAEDLP 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 975031383 335 RAGARREYQRARLENG----RAVPHRNQGSNVLQTAAWAHGLVELREDRT-FAEGDPVRFIPLAEL 395
Cdd:COG0303 336 KKPGRTEFLRVRLERDdgelVVEPLGGQGSGLLSSLAEADGLIVLPEGVEgVEAGEEVEVLLLDGL 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
22-392 |
3.43e-165 |
|
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: 468.51 E-value: 3.43e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 22 PLPQERVALGDADSRILAAPLIADLDLPPWDNSAMDGYALRLDDWQGEP--LRVSQRIFAGQAPA-PLEPGTCARIFTGA 98
Cdd:cd00887 14 PLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASvtLRVVGEIPAGEPPDgPLGPGEAVRIMTGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 99 PVPAGADCVEMQENAEVlDDGRVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLGPVELGVAASLGRAQLEVHRRLKVA 178
Cdd:cd00887 94 PLPEGADAVVMVEDTEE-EGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 179 VLSTGDELVAPGQPLGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRLGSL--QADLILSTGGVSVGEADYL 256
Cdd:cd00887 173 IISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEAleEADVVITSGGVSVGDYDFV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 257 GQALREE-GELTLWKLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARPYLLRRAGKIDVAPLSVEVPAGFDWPR 335
Cdd:cd00887 253 KEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEPPRVKARLAEDLKS 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 975031383 336 AGARREYQRARLEN----GRAVPHRNQGSNVLQTAAWAHGLVELREDRT-FAEGDPVRFIPL 392
Cdd:cd00887 333 KPGRREFLRVRLERdeggLVVAPPGGQGSGLLSSLARADGLIVIPEGVEgLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
25-396 |
5.33e-113 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 342.36 E-value: 5.33e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 25 QERVALGDADSRILAAPLIADLDLPPWDNSAMDGYALRLDDWQGEPLRVSQRIFAGQA-PAPLEPGTCARIFTGAPVPAG 103
Cdd:PRK14491 218 TEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESYTLVGEVLAGHQyDGTLQAGEAVRIMTGAPVPAG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 104 ADCVEMQENAEvLDDGRVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLGPVELGVAASLGRAQLEVHRRLKVAVLSTG 183
Cdd:PRK14491 298 ADTVVMRELAT-QDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 184 DELVAPGQPLGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRL--GSLQADLILSTGGVSVGEADYLGQALR 261
Cdd:PRK14491 377 DEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLeqAAAQADVVISSGGVSVGDADYIKTALA 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 262 EEGELTLWKLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARPYLLRRAGKIDVAPLSVEVPAGFDWPRAGARRE 341
Cdd:PRK14491 457 KLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKLAGEQNWQPLLFPAIADETLRSRQGRTE 536
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 975031383 342 YQRA--RL-ENGRA--VPHRNQGSNVLQTAAWAHGLVEL-REDRTFAEGDPVRFIPLAELL 396
Cdd:PRK14491 537 FSRGiyHLgADGRLhvRTTGKQGSGILSSMSEANCLIEIgPAAETVNAGETVTIQPLAGLL 597
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
22-397 |
2.27e-107 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 322.04 E-value: 2.27e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 22 PLPQ-ERVALGDADSRILAAPLIADLDLPPWDNSAMDGYALRLDDWQ-GEPLRVSQRIFAGQA-----PAplepGTCARI 94
Cdd:PRK10680 23 PLTAtETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLAsGQPLPVAGKAFAGQPfhgewPA----GTCIRI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 95 FTGAPVPAGADCVEMQENAEVLDDGrVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLGPVELGVAASLGRAQLEVHRR 174
Cdd:PRK10680 99 MTGAPVPEGCEAVVMQEQTEQTDDG-VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 175 LKVAVLSTGDELVAPGQPLGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRL--GSLQADLILSTGGVSVGE 252
Cdd:PRK10680 178 VRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFieADSQADVVISSGGVSVGE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 253 ADYLGQALREEGELTLWKLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARPYLLRRAGKIDVA-PLSVEVPAGF 331
Cdd:PRK10680 258 ADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNTASGlPPRQRVRTAS 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 975031383 332 DWPRAGARREYQR---ARLENG----RAVPHrnQGSNVLQTAAWAHGLVELREDR-TFAEGDPVRFIPLAELLK 397
Cdd:PRK10680 338 RLKKTPGRLDFQRgilQRNADGelevTTTGH--QGSHIFSSFSLGNCFIVLERERgNVEVGEWVEVEPFNALFG 409
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
2-394 |
5.48e-87 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 276.32 E-value: 5.48e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 2 SLLSLEEALARLLAMAAEDgPLPQERVALGDADSRILAAPLIADLDLPPWDNSAMDGYALRLDDWQG----EP--LRVSQ 75
Cdd:PRK14498 8 TLVSLEEAREILESLLSEL-PLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGaseaNPvrLKLGG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 76 RIFAGQAPA-PLEPGTCARIFTGAPVPAGADCVEMQENAEVLDDGRVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLG 154
Cdd:PRK14498 87 EVHAGEAPDvEVEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 155 PVELGVAASLGRAQLEVHRRLKVAVLSTGDELVAPGQPLGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRL 234
Cdd:PRK14498 167 PRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 235 --GSLQADLILSTGGVSVGEADYLGQALREEGELTLWKLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARPYLL 312
Cdd:PRK14498 247 rkALKECDLVLLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 313 RRAGKIDVAPLSVEVPAGFDWPRAGARREYQRARL----ENGRAVPhRNQGSNVLQTAAWAHGLVELREDRTFAE-GDPV 387
Cdd:PRK14498 327 KLAGLPPPERATVKARLARRVRSELGREEFVPVSLgrvgDGYVAYP-LSRGSGAITSLVRADGFIEIPANTEGLEaGEEV 405
|
410
....*....|
gi 975031383 388 R---FIPLAE 394
Cdd:PRK14498 406 EvelFGPLVE 415
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
26-393 |
1.58e-85 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 266.40 E-value: 1.58e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 26 ERVALGDADSRILAAPLIADLDLPPWDNSAMDGYAL---RLDDWQGEPL---RVSQRI-FAGQAPAplepGTCARIFTGA 98
Cdd:PRK14690 43 KELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFagaAPEGAQVLPLiegRAAAGVpFSGRVPE----GMALRILTGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 99 PVPAGADCVEMQENAEvLDDGRVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLGPVELGVAASLGRAQLEVHRRLKVA 178
Cdd:PRK14690 119 ALPEGVDTVVLEEDVA-GDGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRVA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 179 VLSTGDELVAPGQPLGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRL--GSLQADLILSTGGVSVGEADYL 256
Cdd:PRK14690 198 VLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLdrAAAEADVILTSGGASAGDEDHV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 257 GQALREEGELTLWKLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARPYLLRRAGKIDVAPLSVEVPAGFDWPRA 336
Cdd:PRK14690 278 SALLREAGAMQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEGWSEPQGFTVPAAFEKRKK 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 975031383 337 GARREYQRARLENGRAVPHRNQGSNVLQTAAWAHGLVELRED-RTFAEGDPVRFIPLA 393
Cdd:PRK14690 358 PGRREYLRARLRQGHAEVFRSEGSGRISGLSWAEGLVELGDGaRRIAPGDPVRFIPYG 415
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
19-311 |
1.62e-66 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 220.45 E-value: 1.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 19 EDGPLPQ-ERVALGDADSRILAAPLIADLDLPPWDNSAMDGYALRLDDWQGEpLRVSQRIFAGQ-APAPLEPGTCARIFT 96
Cdd:PRK14497 23 SLNFKPKiVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSCTPGE-FKVIDKIGIGEfKEIHIKECEAVEVDT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 97 GAPVPAGADCVEMQENAEVLDDGRVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLGPVELGVAASLGRAQLEVHRRLK 176
Cdd:PRK14497 102 GSMIPMGADAVIKVENTKVINGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 177 VAVLSTGDELVAPGQPLGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRL--GSLQADLILSTGGVSVGEAD 254
Cdd:PRK14497 182 IYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIkrAISVADVLILTGGTSAGEKD 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 975031383 255 YLGQALREEGELTLWKLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARPYL 311
Cdd:PRK14497 262 FVHQAIRELGNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYL 318
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
28-348 |
7.74e-60 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 205.05 E-value: 7.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 28 VALGDADSRILAAPLIADLDLPPWDNSAMDGYALRLDDWQGE-PLRVSQRIFAGQAPAPLEPGTCARIFTGAPVPAGADC 106
Cdd:PLN02699 29 VPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEyPVITESRAGNDGLGVTLTPGTVAYVTTGGPIPDGADA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 107 VEMQENAEVLDDG-----RVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLGPVELGVAASLGRAQLEVHRRLKVAVLS 181
Cdd:PLN02699 109 VVQVEDTEVVEDPldgskRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASEIGLLATVGVTMVKVYPRPTVAILS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 182 TGDELVAPGQP-LGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRLG---SLQADLILSTGGVSVGEADYLG 257
Cdd:PLN02699 189 TGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDeaiSSGVDILLTSGGVSMGDRDFVK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 258 QALREEGELTLWKLALKPGKPLTCGRFRGIP---------LIGLPGNPASTLVTFGLLARPYLLRRAGKIDVAPLSVEV- 327
Cdd:PLN02699 269 PLLEKRGTVYFSKVLMKPGKPLTFAEIDAKSapsnskkmlAFGLPGNPVSCLVCFNLFVVPAIRYLAGWSNPHLLRVQAr 348
|
330 340
....*....|....*....|....
gi 975031383 328 ---PAGFDwpraGARREYQRARLE 348
Cdd:PLN02699 349 lrePIKLD----PVRPEFHRAIIR 368
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
22-165 |
5.51e-50 |
|
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: 165.43 E-value: 5.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 22 PLPQERVALGDADS--RILAAPLIADLDLPPWDNSAMDGYALRLDDwqGEPLRVSQRIFAGQAPAP-LEPGTCARIFTGA 98
Cdd:pfam03453 3 LGTEETVPLEALDAlgRVLAEDVVAPRDVPPFDRSAMDGYAVRAAD--GFGASEVNPIAAGEPPGPlLPGGEAVRIMTGA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 975031383 99 PVPAGADCVEMQENAEVLDDGRVRFVEMLRPGRNIRRRGNEVKVGDEVLSAGTVLGPVELGVAASLG 165
Cdd:pfam03453 81 PLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
175-309 |
3.25e-40 |
|
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: 139.76 E-value: 3.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 175 LKVAVLSTGDELVAPGQPLGPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRL--GSLQADLILSTGGVSVGE 252
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILrkAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 975031383 253 ADYLGQALREEGE-----------LTLWKLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARP 309
Cdd:TIGR00177 81 RDVTPEALEELGEkeipgfgefrmLSSLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-313 |
4.10e-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 trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 123.51 E-value: 4.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 178 AVLSTGDELVapgqplgPGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRK--RLGSLQADLILSTGGVSVGEADY 255
Cdd:pfam00994 1 AIITTGDELL-------PGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEalRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 256 LGQALREEGELTL-------WKLALKPGKPLTCGRF-----RGIPLIGLPGNPASTLVTFGLLARPYLLR 313
Cdd:pfam00994 74 TPEALAELGGRELpgfeelfRGVSLKPGKPVGTAPGailsrAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-306 |
1.34e-30 |
|
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: 114.22 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 178 AVLSTGDELVAPGQplgpgqIYNSNRALLISWLRRLGCEVSDQGIL--PDDLAETRKRLGSL--QADLILSTGGVSVGEA 253
Cdd:smart00852 1 AIISTGDELLSGGQ------IRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREAlaEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 975031383 254 DYLGQALREEGELTL--WKLALKPGKPLT---------CGRFRGIPLIGLPGNPASTLVTFGLL 306
Cdd:smart00852 75 DLTPEALAELGGRELlgHGVAMRPGGPPGplanlsgtaPGVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
176-311 |
3.38e-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: 102.04 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 176 KVAVLSTGDELVApgqplgpGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRKRL--GSLQADLILSTGGVSVGEA 253
Cdd:cd00758 1 RVAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALieASREADLVLTTGGTGVGRR 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 254 DYLGQALREEGELTLW--KLALKPGKPLTCGRFRGIPLIGLPGNPASTLVTFGLLARPYL 311
Cdd:cd00758 74 DVTPEALAELGEREAHgkGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
327-392 |
1.04e-09 |
|
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: 54.54 E-value: 1.04e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 975031383 327 VPAGFDWPRAGARREYQRARLENGR----AVPHRNQGSNVLQTAAWAHGLVELREDRTF-AEGDPVRFIPL 392
Cdd:pfam03454 2 ARLARDLKSDPGRREFVRVRLHEEDgryyAEPIGKQGSGMLSSLAEANGLIVVPEGTEGlEAGEEVEVILL 72
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
161-294 |
3.74e-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: 57.56 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 975031383 161 AASLGRAQ--LEVH--RRLKVAVLSTGDELvapgqplGPGQIYNSNRALLISWLRRLGCEVSDQGILPDD---LAETRKR 233
Cdd:cd03522 142 AEALARDGplLRVApfRPLRVGLIVTGSEV-------YGGRIEDKFGPVLRARLAALGVELVEQVIVPHDeaaIAAAIAE 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 975031383 234 LGSLQADLILSTGGVSVGEADYLGQALREEG-ELTLWKLALKPGKPLTCGRFRGIPLIGLPG 294
Cdd:cd03522 215 ALEAGAELLILTGGASVDPDDVTPAAIRAAGgEVIRYGMPVDPGNLLLLGYLGGVPVIGLPG 276
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
176-247 |
8.30e-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: 8.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 975031383 176 KVAVLSTGDELVapgqplgPGQIYNSNRALLISWLRRLGCEVSDQGILPDD---LAETRKRLGSlQADLILSTGG 247
Cdd:cd00885 1 TAEIIAIGDELL-------SGQIVDTNAAFLAKELAELGIEVYRVTVVGDDedrIAEALRRASE-RADLVITTGG 67
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
204-268 |
2.85e-05 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 45.70 E-value: 2.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 975031383 204 ALLISWLRRLGCEVSDQGILPDDLAETRKRLGSLQA---DLILSTGGVSVGEADYLGQALREEGELTL 268
Cdd:PRK03604 178 KLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVAAWIAegyALIITTGGTGLGPRDVTPEALAPLLERRL 245
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
205-247 |
8.79e-04 |
|
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: 39.72 E-value: 8.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 975031383 205 LLISWLRRLGCEVSDQGILPDDLAETRKRLGSL----QADLILSTGG 247
Cdd:COG0521 33 ALVELLEEAGHEVVARRIVPDDKDAIRAALRELiddeGVDLVLTTGG 79
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
175-248 |
4.19e-03 |
|
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: 39.12 E-value: 4.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 975031383 175 LKVAVLSTGDELVApgqplgpGQIYNSNRALLISWLRRLGCEVSDQGILPDDLAETRK--RLGSLQADLILSTGGV 248
Cdd:TIGR00200 1 LKAEIISVGDELLL-------GQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTiiRIASERADVLIFNGGL 69
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
204-247 |
5.95e-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: 37.07 E-value: 5.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 975031383 204 ALLISWLRRLGCEVSDQGILPDDLAETRKRL----GSLQADLILSTGG 247
Cdd:cd00886 23 PALVELLEEAGHEVVAYEIVPDDKDEIREALiewaDEDGVDLILTTGG 70
|
|
| |
