|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
21-408 |
0e+00 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 575.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 21 NQFETIALHEAANRVLAEDVFSPINVPNFDNSAMDGYAISLQNFVENQPLAVIGKAFAGNPFSGKIQSGQCVRIMTGAKI 100
Cdd:PRK10680 25 TATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKAFAGQPFHGEWPAGTCIRIMTGAPV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 101 PENTDAVVMQEDTIIRDDGtMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLGIAEVKVFPKVKVAIL 180
Cdd:PRK10680 105 PEGCEAVVMQEQTEQTDDG-VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVRVALF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 181 STGDELVSVGEPLNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGEADFTKT 260
Cdd:PRK10680 184 STGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEADYTKT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 261 VIEKLGKIDFWKIAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQLAQPALMKLAGFSAEKIanfSPKLTACAAVSMK 340
Cdd:PRK10680 264 ILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNTASGL---PPRQRVRTASRLK 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575454316 341 KAVGRQDFQRGFFYADENGQLVVKTVGTQGSHIFSAFNESNCFIVLEQERGNVEVGERVVIQPFNLLL 408
Cdd:PRK10680 341 KTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEVGEWVEVEPFNALF 408
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
20-407 |
0e+00 |
|
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440072 [Multi-domain] Cd Length: 401 Bit Score: 531.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 20 PNQFETIALHEAANRVLAEDVFSPINVPNFDNSAMDGYAISLQNFVENQP--LAVIGKAFAGNPFSGKIQSGQCVRIMTG 97
Cdd:COG0303 17 PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtLRVVGEIAAGSPPPGPLGPGEAVRIMTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 98 AKIPENTDAVVMQEDTIiRDDGTMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLGIAEVKVFPKVKV 177
Cdd:COG0303 97 APLPEGADAVVMQEDTE-REGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 178 AILSTGDELVSVGEPLNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGEADF 257
Cdd:COG0303 176 AILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGVSVGDYDL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 258 TKTVIEKLG-KIDFWKIAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQLAQPALMKLAGFSAEKIanfsPKLTACAA 336
Cdd:COG0303 256 VKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLPPPPP----PRVRARLA 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575454316 337 VSMKKAVGRQDFQRGFFYADEnGQLVVKTVGTQGSHIFSAFNESNCFIVLEQERGNVEVGERVVIQPFNLL 407
Cdd:COG0303 332 EDLPKKPGRTEFLRVRLERDD-GELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLLLDGL 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
20-404 |
3.99e-180 |
|
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: 506.65 E-value: 3.99e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 20 PNQFETIALHEAANRVLAEDVFSPINVPNFDNSAMDGYAI-SLQNFVENQPLAVIGKAFAGNPFSGKIQSGQCVRIMTGA 98
Cdd:cd00887 14 PLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVrAADTAGASVTLRVVGEIPAGEPPDGPLGPGEAVRIMTGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 99 KIPENTDAVVMQEDTIiRDDGTMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLGIAEVKVFPKVKVA 178
Cdd:cd00887 94 PLPEGADAVVMVEDTE-EEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 179 ILSTGDELVSVGEPLNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGEADFT 258
Cdd:cd00887 173 IISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 259 KTVIEKL-GKIDFWKIAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQLAQPALMKLAGFSAEKIanfsPKLTACAAV 337
Cdd:cd00887 253 KEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEP----PRVKARLAE 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575454316 338 SMKKAVGRQDFQRGFFYADEnGQLVVKTVGTQGSHIFSAFNESNCFIVLEQERGNVEVGERVVIQPF 404
Cdd:cd00887 329 DLKSKPGRREFLRVRLERDE-GGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
24-165 |
5.22e-55 |
|
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: 178.53 E-value: 5.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 24 ETIALH--EAANRVLAEDVFSPINVPNFDNSAMDGYAI---SLQNFVENQPLAvigkafAGNPFSGKIQSGQCVRIMTGA 98
Cdd:pfam03453 7 ETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVraaDGFGASEVNPIA------AGEPPGPLLPGGEAVRIMTGA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575454316 99 KIPENTDAVVMQEDTIIRDDGTMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLG 165
Cdd:pfam03453 81 PLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
175-311 |
6.46e-42 |
|
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: 144.77 E-value: 6.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 175 VKVAILSTGDELVSVGEPLNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGE 254
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575454316 255 ADFTKTVIEKLGKIDFWK-----------IAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQLAQP 311
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGfgefrmlsslpVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-305 |
7.02e-35 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 125.78 E-value: 7.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 178 AILSTGDELVSvgeplnEGQIYDTNRFTVRLMLEKLNCEILDFGTL--PDNPEIFERTFVQAQRQADVLITSGGVSVGEA 255
Cdd:smart00852 1 AIISTGDELLS------GGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575454316 256 DFTKTVIEKLG--KIDFWKIAMKPGKPFAF---------GKLEKAWFFGLPGNPVSALVTF 305
Cdd:smart00852 75 DLTPEALAELGgrELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMF 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
21-408 |
0e+00 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 575.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 21 NQFETIALHEAANRVLAEDVFSPINVPNFDNSAMDGYAISLQNFVENQPLAVIGKAFAGNPFSGKIQSGQCVRIMTGAKI 100
Cdd:PRK10680 25 TATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKAFAGQPFHGEWPAGTCIRIMTGAPV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 101 PENTDAVVMQEDTIIRDDGtMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLGIAEVKVFPKVKVAIL 180
Cdd:PRK10680 105 PEGCEAVVMQEQTEQTDDG-VRFTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVRVALF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 181 STGDELVSVGEPLNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGEADFTKT 260
Cdd:PRK10680 184 STGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEADYTKT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 261 VIEKLGKIDFWKIAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQLAQPALMKLAGFSAEKIanfSPKLTACAAVSMK 340
Cdd:PRK10680 264 ILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPLLAKLSGNTASGL---PPRQRVRTASRLK 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575454316 341 KAVGRQDFQRGFFYADENGQLVVKTVGTQGSHIFSAFNESNCFIVLEQERGNVEVGERVVIQPFNLLL 408
Cdd:PRK10680 341 KTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSSFSLGNCFIVLERERGNVEVGEWVEVEPFNALF 408
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
20-407 |
0e+00 |
|
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440072 [Multi-domain] Cd Length: 401 Bit Score: 531.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 20 PNQFETIALHEAANRVLAEDVFSPINVPNFDNSAMDGYAISLQNFVENQP--LAVIGKAFAGNPFSGKIQSGQCVRIMTG 97
Cdd:COG0303 17 PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPvtLRVVGEIAAGSPPPGPLGPGEAVRIMTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 98 AKIPENTDAVVMQEDTIiRDDGTMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLGIAEVKVFPKVKV 177
Cdd:COG0303 97 APLPEGADAVVMQEDTE-REGDRVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPADLGLLASLGIAEVPVYRRPRV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 178 AILSTGDELVSVGEPLNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGEADF 257
Cdd:COG0303 176 AILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGVSVGDYDL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 258 TKTVIEKLG-KIDFWKIAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQLAQPALMKLAGFSAEKIanfsPKLTACAA 336
Cdd:COG0303 256 VKEALEELGaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLAGLPPPPP----PRVRARLA 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575454316 337 VSMKKAVGRQDFQRGFFYADEnGQLVVKTVGTQGSHIFSAFNESNCFIVLEQERGNVEVGERVVIQPFNLL 407
Cdd:COG0303 332 EDLPKKPGRTEFLRVRLERDD-GELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEGVEAGEEVEVLLLDGL 401
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
20-404 |
3.99e-180 |
|
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: 506.65 E-value: 3.99e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 20 PNQFETIALHEAANRVLAEDVFSPINVPNFDNSAMDGYAI-SLQNFVENQPLAVIGKAFAGNPFSGKIQSGQCVRIMTGA 98
Cdd:cd00887 14 PLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVrAADTAGASVTLRVVGEIPAGEPPDGPLGPGEAVRIMTGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 99 KIPENTDAVVMQEDTIiRDDGTMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLGIAEVKVFPKVKVA 178
Cdd:cd00887 94 PLPEGADAVVMVEDTE-EEGGRVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASLGIAEVPVYRRPRVA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 179 ILSTGDELVSVGEPLNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGEADFT 258
Cdd:cd00887 173 IISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 259 KTVIEKL-GKIDFWKIAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQLAQPALMKLAGFSAEKIanfsPKLTACAAV 337
Cdd:cd00887 253 KEVLEELgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQGAPEPEP----PRVKARLAE 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575454316 338 SMKKAVGRQDFQRGFFYADEnGQLVVKTVGTQGSHIFSAFNESNCFIVLEQERGNVEVGERVVIQPF 404
Cdd:cd00887 329 DLKSKPGRREFLRVRLERDE-GGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEGLEAGEEVEVLLL 394
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
24-408 |
1.36e-158 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 459.85 E-value: 1.36e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 24 ETIALHEAANRVLAEDVFSPINVPNFDNSAMDGYAISLQNfVENQPLAVIGKAFAGNPFSGKIQSGQCVRIMTGAKIPEN 103
Cdd:PRK14491 219 EDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDD-LEPESYTLVGEVLAGHQYDGTLQAGEAVRIMTGAPVPAG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 104 TDAVVMQEDTIiRDDGTMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLGIAEVKVFPKVKVAILSTG 183
Cdd:PRK14491 298 ADTVVMRELAT-QDGDKVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 184 DELVSVGEPLNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGEADFTKTVIE 263
Cdd:PRK14491 377 DEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATLEQAAAQADVVISSGGVSVGDADYIKTALA 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 264 KLGKIDFWKIAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQLAQPALMKLAGfsaekIANFSP-KLTACAAVSMKKA 342
Cdd:PRK14491 457 KLGQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKLAG-----EQNWQPlLFPAIADETLRSR 531
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575454316 343 VGRQDFQRGFFYADENGQLVVKTVGTQGSHIFSAFNESNCFIVLEQERGNVEVGERVVIQPFNLLL 408
Cdd:PRK14491 532 QGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGETVTIQPLAGLL 597
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
18-404 |
1.43e-108 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 332.56 E-value: 1.43e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 18 PMPNQFETIALHEAANRVLAEDVFSPINVPNFDNSAMDGYAISLQNFV---ENQP--LAVIGKAFAGNPFSGKIQSGQCV 92
Cdd:PRK14498 25 ELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFgasEANPvrLKLGGEVHAGEAPDVEVEPGEAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 93 RIMTGAKIPENTDAVVMQEDTIIRDDGTMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLGIAEVKVF 172
Cdd:PRK14498 105 EIATGAPIPRGADAVVMVEDTEEVDDDTVEIYRPVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGALAAGGVAEVPVY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 173 PKVKVAILSTGDELVSVGEPLNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSV 252
Cdd:PRK14498 185 KKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVLLSGGTSA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 253 GEADFTKTVIEKLGKIDFWKIAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQLAQPALMKLAGFSAEKianfSPKLT 332
Cdd:PRK14498 265 GAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSALTIFEEFVAPLLRKLAGLPPPE----RATVK 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575454316 333 ACAAVSMKKAVGRQDFQR---GffyadENGQLVVKTVGTQGSHIFSAFNESNCFIVLEQERGNVEVGERVVIQPF 404
Cdd:PRK14498 341 ARLARRVRSELGREEFVPvslG-----RVGDGYVAYPLSRGSGAITSLVRADGFIEIPANTEGLEAGEEVEVELF 410
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
24-350 |
4.17e-79 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 250.22 E-value: 4.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 24 ETIALHEAANRVLAEDVFSPINVPNFDNSAMDGYAISLQNFVENQPLAVI-GKAFAGNPFSGKIQSGQCVRIMTGAKIPE 102
Cdd:PRK14690 43 KELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQVLPLIeGRAAAGVPFSGRVPEGMALRILTGAALPE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 103 NTDAVVMQEDTIIrDDGTMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLGIAEVKVFPKVKVAILST 182
Cdd:PRK14690 123 GVDTVVLEEDVAG-DGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRVAVLST 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 183 GDELVSVGEPLNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGEADFTKTVI 262
Cdd:PRK14690 202 GDELVEPGALAEVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAEADVILTSGGASAGDEDHVSALL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 263 EKLGKIDFWKIAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQLAQPALMKLAGFSAEKIANFspklTACAAVSMKKA 342
Cdd:PRK14690 282 REAGAMQSWRIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEGWSEPQGF----TVPAAFEKRKK 357
|
....*...
gi 575454316 343 VGRQDFQR 350
Cdd:PRK14690 358 PGRREYLR 365
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
25-399 |
5.05e-75 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 245.88 E-value: 5.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 25 TIALHEAANRVLAEDVFSPINVPNFDNSAMDGYAISLQNFVENQPlaVIGKAFAGNPFSG-KIQSGQCVRIMTGAKIPEN 103
Cdd:PLN02699 28 IVPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYP--VITESRAGNDGLGvTLTPGTVAYVTTGGPIPDG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 104 TDAVVMQEDTIIRDDG-----TMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLGIAEVKVFPKVKVA 178
Cdd:PLN02699 106 ADAVVQVEDTEVVEDPldgskRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERLGASEIGLLATVGVTMVKVYPRPTVA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 179 ILSTGDELVsvgEP----LNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQA-QRQADVLITSGGVSVG 253
Cdd:PLN02699 186 ILSTGDELV---EPttgtLGRGQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELERILDEAiSSGVDILLTSGGVSMG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 254 EADFTKTVIEKLGKIDFWKIAMKPGKPFAFGKLE---------KAWFFGLPGNPVSALVTFYQLAQPALMKLAGFsaeki 324
Cdd:PLN02699 263 DRDFVKPLLEKRGTVYFSKVLMKPGKPLTFAEIDaksapsnskKMLAFGLPGNPVSCLVCFNLFVVPAIRYLAGW----- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 325 ANFSP-KLTACAAVSMKKAVGRQDFQRGFF-YADENGQ----LVVKTVGTQGSHIFSAFNESNCFIVLEQERGNVEVGER 398
Cdd:PLN02699 338 SNPHLlRVQARLREPIKLDPVRPEFHRAIIrWKLNDGSgnpgFVAESTGHQMSSRLLSMKSANALLELPATGNVLSAGTS 417
|
.
gi 575454316 399 V 399
Cdd:PLN02699 418 V 418
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
17-308 |
2.30e-67 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 223.15 E-value: 2.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 17 LPMPNQFETIALHEAANRVLAEDVFSPINVPNFDNSAMDGYAIslQNFVENQPLAVIGKAFAGNPFSGKIQSGQCVRIMT 96
Cdd:PRK14497 24 LNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYAL--KSSCTPGEFKVIDKIGIGEFKEIHIKECEAVEVDT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 97 GAKIPENTDAVVMQEDTIIRDDGTMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLGIAEVKVFPKVK 176
Cdd:PRK14497 102 GSMIPMGADAVIKVENTKVINGNFIKIDKKINFGQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 177 VAILSTGDELVSVGEPLNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGEAD 256
Cdd:PRK14497 182 IYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKD 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 575454316 257 FTKTVIEKLGKIDFWKIAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQL 308
Cdd:PRK14497 262 FVHQAIRELGNIIVHGLKIKPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMV 313
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
24-165 |
5.22e-55 |
|
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: 178.53 E-value: 5.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 24 ETIALH--EAANRVLAEDVFSPINVPNFDNSAMDGYAI---SLQNFVENQPLAvigkafAGNPFSGKIQSGQCVRIMTGA 98
Cdd:pfam03453 7 ETVPLEalDALGRVLAEDVVAPRDVPPFDRSAMDGYAVraaDGFGASEVNPIA------AGEPPGPLLPGGEAVRIMTGA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575454316 99 KIPENTDAVVMQEDTIIRDDGTMMITKPVKLGANIRRVGEDVAQGSLVLAKGSQLNVSSLPLLASLG 165
Cdd:pfam03453 81 PLPEGADAVVMVEDTEEGGGRTVEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
175-311 |
6.46e-42 |
|
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: 144.77 E-value: 6.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 175 VKVAILSTGDELVSVGEPLNEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGE 254
Cdd:TIGR00177 1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575454316 255 ADFTKTVIEKLGKIDFWK-----------IAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQLAQP 311
Cdd:TIGR00177 81 RDVTPEALEELGEKEIPGfgefrmlsslpVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
176-313 |
1.42e-38 |
|
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: 135.16 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 176 KVAILSTGDELVSvgeplneGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGEA 255
Cdd:cd00758 1 RVAIVTVSDELSQ-------GQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRR 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 256 DFTKTVIEKLGKIDFW--KIAMKPGKPFAFGKLEKAWFFGLPGNPVSALVTFYQLAQPAL 313
Cdd:cd00758 74 DVTPEALAELGEREAHgkGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPAL 133
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-315 |
4.04e-35 |
|
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: 126.59 E-value: 4.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 178 AILSTGDELVSvgeplneGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGEADF 257
Cdd:pfam00994 1 AIITTGDELLP-------GQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 258 TKTVIEKLG-------KIDFWKIAMKPGKPFAFGK---LEKAW--FFGLPGNPVSALVTFYQLAQPALMK 315
Cdd:pfam00994 74 TPEALAELGgrelpgfEELFRGVSLKPGKPVGTAPgaiLSRAGktVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
178-305 |
7.02e-35 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 125.78 E-value: 7.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 178 AILSTGDELVSvgeplnEGQIYDTNRFTVRLMLEKLNCEILDFGTL--PDNPEIFERTFVQAQRQADVLITSGGVSVGEA 255
Cdd:smart00852 1 AIISTGDELLS------GGQIRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575454316 256 DFTKTVIEKLG--KIDFWKIAMKPGKPFAF---------GKLEKAWFFGLPGNPVSALVTF 305
Cdd:smart00852 75 DLTPEALAELGgrELLGHGVAMRPGGPPGPlanlsgtapGVRGKKPVFGLPGNPVAALVMF 135
|
|
| MoeA_C |
pfam03454 |
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ... |
332-404 |
1.37e-14 |
|
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: 68.02 E-value: 1.37e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575454316 332 TACAAVSMKKAVGRQDFQRGFfYADENGQLVVKTVGTQGSHIFSAFNESNCFIVLEQERGNVEVGERVVIQPF 404
Cdd:pfam03454 1 KARLARDLKSDPGRREFVRVR-LHEEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGTEGLEAGEEVEVILL 72
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
176-249 |
8.69e-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: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 176 KVAILSTGDELVSvgeplneGQIYDTNRFTVRLMLEKLnceildfG-------TLPDNPEIFERTFVQAQRQADVLITSG 248
Cdd:cd00885 1 TAEIIAIGDELLS-------GQIVDTNAAFLAKELAEL-------GievyrvtVVGDDEDRIAEALRRASERADLVITTG 66
|
.
gi 575454316 249 G 249
Cdd:cd00885 67 G 67
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
176-262 |
6.71e-05 |
|
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: 44.90 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 176 KVAILSTGDELVsvgeplnEGQIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQRQADVLITSGGVSVGEA 255
Cdd:TIGR00200 2 KAEIISVGDELL-------LGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSD 74
|
....*..
gi 575454316 256 DFTKTVI 262
Cdd:TIGR00200 75 DLTAETI 81
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
160-296 |
6.26e-04 |
|
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: 41.38 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575454316 160 LLASLGIAEVKVFPKVKVAILSTGDElVSVGEplnegqIYDTNRFTVRLMLEKLNCEILDFGTLPDNPEIFERTFVQAQR 239
Cdd:cd03522 145 LARDGPLLRVAPFRPLRVGLIVTGSE-VYGGR------IEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAAAIAEALE 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 575454316 240 Q-ADVLITSGGVSVGEADFTKTVIEKLG-KIDFWKIAMKPGKPFAFGKLEKAWFFGLPG 296
Cdd:cd03522 218 AgAELLILTGGASVDPDDVTPAAIRAAGgEVIRYGMPVDPGNLLLLGYLGGVPVIGLPG 276
|
|
| |
