|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
11-413 |
8.36e-110 |
|
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: 328.97 E-value: 8.36e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 11 SPEEAIDALARRIVTTGVQRVEIGESHDalrslhrRVLATPILADRDSPAADVSAMDGYAIRESDLLREGPIE--VTGES 88
Cdd:COG0303 3 SVEEALALILAAVRPLGTETVPLAEALG-------RVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTlrVVGEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 89 VPGSPPPSASDTG-VIRIFTGAIVPVGCDRVIQREHTDETApasasdsdslGQIQWTdqaKSIPAGANIRRQGENLSAGS 167
Cdd:COG0303 76 AAGSPPPGPLGPGeAVRIMTGAPLPEGADAVVMQEDTEREG----------DRVTIR---KPVAPGENIRRAGEDIAAGD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 168 IAVEAGLELTSPRLAALTNFGVQQVDLHKPVRVAVLTTGDELasgTAPDQsPLPPWKIRNSNASALLGLLTNQPwidCAP 247
Cdd:COG0303 143 VLLPAGTRLTPADLGLLASLGIAEVPVYRRPRVAILSTGDEL---VEPGE-PLGPGQIYDSNSYMLAALLREAG---AEV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 248 PMHAI--DEPAALLTAVEHAIEHHDVVLMTGGVSMGDYDYVPRILRESGAEIVFHKLPLRPGKPILGAVHQsdskSTLIL 325
Cdd:COG0303 216 VDLGIvpDDPEALRAALREALAEADLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLG----GKPVF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 326 GLPGNPVSATMGARRFAMPLIRKLAGMTNWEefPPLVTL---EEVSEKTLPLHWLRGVRLTQPG--LAALVIGKGSGDVA 400
Cdd:COG0303 292 GLPGNPVSALVTFELFVRPALRKLAGLPPPP--PPRVRArlaEDLPKKPGRTEFLRVRLERDDGelVVEPLGGQGSGLLS 369
|
410
....*....|...
gi 494547779 401 TLAGTDGFIEMPP 413
Cdd:COG0303 370 SLAEADGLIVLPE 382
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
13-413 |
2.97e-104 |
|
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: 314.43 E-value: 2.97e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 13 EEAIDALARRIVTTGVQRVEIGESHDalrslhrRVLATPILADRDSPAADVSAMDGYAIRESDLLREG-PIEVTGESVPG 91
Cdd:cd00887 2 EAARELLLALAPPLGTETVPLLEALG-------RVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASvTLRVVGEIPAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 92 SPPPSASDTG-VIRIFTGAIVPVGCDRVIQREHTDETApasasdsdslGQIQWTDQAKsipAGANIRRQGENLSAGSIAV 170
Cdd:cd00887 75 EPPDGPLGPGeAVRIMTGAPLPEGADAVVMVEDTEEEG----------GRVTITKPVK---PGQNIRRAGEDIKAGDVLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 171 EAGLELTSPRLAALTNFGVQQVDLHKPVRVAVLTTGDELASgtaPDQsPLPPWKIRNSNASALLGLLtNQPWIDCAPPMH 250
Cdd:cd00887 142 PAGTRLTPADIGLLASLGIAEVPVYRRPRVAIISTGDELVE---PGE-PLAPGQIYDSNSYMLAALL-RELGAEVVDLGI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 251 AIDEPAALLTAVEHAIEHHDVVLMTGGVSMGDYDYVPRILRESGAEIVFHKLPLRPGKPILGAVhqsdSKSTLILGLPGN 330
Cdd:cd00887 217 VPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGR----LGGKPVFGLPGN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 331 PVSATMGARRFAMPLIRKLAGMTNWEEFP-PLVTLEEVSEKTLPLHWLRgVRLTQ---PGLAALVIGKGSGDVATLAGTD 406
Cdd:cd00887 293 PVSALVTFELFVRPALRKLQGAPEPEPPRvKARLAEDLKSKPGRREFLR-VRLERdegGLVVAPPGGQGSGLLSSLARAD 371
|
....*..
gi 494547779 407 GFIEMPP 413
Cdd:cd00887 372 GLIVIPE 378
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
8-413 |
2.47e-59 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 203.69 E-value: 2.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 8 AFDSPEEAIDALARRIvtTGVQRVEigesHDALRSLHRRVLATPILADRDSPAADVSAMDGYAIRESDLLREGpIEVTGE 87
Cdd:PRK14491 197 AFLSVSQGLDKILSLV--TPVTETE----DVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPES-YTLVGE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 88 SVPGSPPPSASDTG-VIRIFTGAIVPVGCDRVIQREHTDEtapasasDSDSLgqiqwTDQAKsIPAGANIRRQGENLSAG 166
Cdd:PRK14491 270 VLAGHQYDGTLQAGeAVRIMTGAPVPAGADTVVMRELATQ-------DGDKV-----SFDGG-IKAGQNVRLAGEDLAQG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 167 SIAVEAGLELTSPRLAALTNFGVQQVDLHKPVRVAVLTTGDELAsgtAPDQsPLPPWKIRNSNASALLGLLTNqpwIDCA 246
Cdd:PRK14491 337 QVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQ---APGE-TLKPNCIYDSNRFTIKAMAKK---LGCE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 247 PPMHAI--DEPAALLTAVEHAIEHHDVVLMTGGVSMGDYDYVPRILRESGaEIVFHKLPLRPGKPIlgAVHQSDskSTLI 324
Cdd:PRK14491 410 VIDLGIieDSEAALEATLEQAAAQADVVISSGGVSVGDADYIKTALAKLG-QIDFWRINMRPGRPL--AFGQIG--DSPF 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 325 LGLPGNPVSATMGARRFAMPLIRKLAGMTNWE-EFPPLVTLEEVSEKTLPLHWLRGV-RLTQPG-LAALVIGK-GSGDVA 400
Cdd:PRK14491 485 FGLPGNPVAVMVSFLQFVEPALRKLAGEQNWQpLLFPAIADETLRSRQGRTEFSRGIyHLGADGrLHVRTTGKqGSGILS 564
|
410
....*....|...
gi 494547779 401 TLAGTDGFIEMPP 413
Cdd:PRK14491 565 SMSEANCLIEIGP 577
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
201-348 |
8.46e-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 trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 112.73 E-value: 8.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 201 AVLTTGDELASGtapdqsplppwKIRNSNASALLGLLTNQPwIDCAPPMHAIDEPAALLTAVEHAIEHHDVVLMTGGVSM 280
Cdd:pfam00994 1 AIITTGDELLPG-----------QIRDTNGPLLAALLREAG-AEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGP 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494547779 281 GDYDYVPRILRESGA------EIVFHKLPLRPGKPILGAVHQSDSK-STLILGLPGNPVSATMGARRFAMPLIRK 348
Cdd:pfam00994 69 GPDDVTPEALAELGGrelpgfEELFRGVSLKPGKPVGTAPGAILSRaGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
198-344 |
5.95e-27 |
|
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: 105.09 E-value: 5.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 198 VRVAVLTTGDELASGTapdqSPLPPWKIRNSNASALLGLLTNQpwidCAPPMHAI---DEPAALLTAVEHAIEHHDVVLM 274
Cdd:TIGR00177 1 PRVAVISVGDELVEGG----QPLEPGQIYDSNGPLLAALLQEA----GFNVVRLGivpDDPEEIREILRKAVDEADVVLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 275 TGGVSMGDYDYVPRILRE------SGAEIVFHKLPL----RPGKPILGAVHqsdsKSTLILGLPGNPVSATMGARRFAMP 344
Cdd:TIGR00177 73 TGGTGVGPRDVTPEALEElgekeiPGFGEFRMLSSLpvlsRPGKPATAGVR----GGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
201-341 |
8.25e-26 |
|
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: 101.51 E-value: 8.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 201 AVLTTGDELasgtapdqspLPPWKIRNSNASALLGLLTNQPWIDCAPPMHAI-DEPAALLTAVEHAIEHHDVVLMTGGVS 279
Cdd:smart00852 1 AIISTGDEL----------LSGGQIRDSNGPMLAALLRELGIEVVRVVVVGGpDDPEAIREALREALAEADVVITTGGTG 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494547779 280 MGDYDYVPRILRES-GAEIVFHKLPLRPGKPILGAVHQS-----DSKSTLILGLPGNPVSATMGARRF 341
Cdd:smart00852 71 PGPDDLTPEALAELgGRELLGHGVAMRPGGPPGPLANLSgtapgVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
11-413 |
8.36e-110 |
|
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: 328.97 E-value: 8.36e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 11 SPEEAIDALARRIVTTGVQRVEIGESHDalrslhrRVLATPILADRDSPAADVSAMDGYAIRESDLLREGPIE--VTGES 88
Cdd:COG0303 3 SVEEALALILAAVRPLGTETVPLAEALG-------RVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTlrVVGEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 89 VPGSPPPSASDTG-VIRIFTGAIVPVGCDRVIQREHTDETApasasdsdslGQIQWTdqaKSIPAGANIRRQGENLSAGS 167
Cdd:COG0303 76 AAGSPPPGPLGPGeAVRIMTGAPLPEGADAVVMQEDTEREG----------DRVTIR---KPVAPGENIRRAGEDIAAGD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 168 IAVEAGLELTSPRLAALTNFGVQQVDLHKPVRVAVLTTGDELasgTAPDQsPLPPWKIRNSNASALLGLLTNQPwidCAP 247
Cdd:COG0303 143 VLLPAGTRLTPADLGLLASLGIAEVPVYRRPRVAILSTGDEL---VEPGE-PLGPGQIYDSNSYMLAALLREAG---AEV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 248 PMHAI--DEPAALLTAVEHAIEHHDVVLMTGGVSMGDYDYVPRILRESGAEIVFHKLPLRPGKPILGAVHQsdskSTLIL 325
Cdd:COG0303 216 VDLGIvpDDPEALRAALREALAEADLVITSGGVSVGDYDLVKEALEELGAEVLFHKVAMKPGKPLAFGRLG----GKPVF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 326 GLPGNPVSATMGARRFAMPLIRKLAGMTNWEefPPLVTL---EEVSEKTLPLHWLRGVRLTQPG--LAALVIGKGSGDVA 400
Cdd:COG0303 292 GLPGNPVSALVTFELFVRPALRKLAGLPPPP--PPRVRArlaEDLPKKPGRTEFLRVRLERDDGelVVEPLGGQGSGLLS 369
|
410
....*....|...
gi 494547779 401 TLAGTDGFIEMPP 413
Cdd:COG0303 370 SLAEADGLIVLPE 382
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
13-413 |
2.97e-104 |
|
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: 314.43 E-value: 2.97e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 13 EEAIDALARRIVTTGVQRVEIGESHDalrslhrRVLATPILADRDSPAADVSAMDGYAIRESDLLREG-PIEVTGESVPG 91
Cdd:cd00887 2 EAARELLLALAPPLGTETVPLLEALG-------RVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASvTLRVVGEIPAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 92 SPPPSASDTG-VIRIFTGAIVPVGCDRVIQREHTDETApasasdsdslGQIQWTDQAKsipAGANIRRQGENLSAGSIAV 170
Cdd:cd00887 75 EPPDGPLGPGeAVRIMTGAPLPEGADAVVMVEDTEEEG----------GRVTITKPVK---PGQNIRRAGEDIKAGDVLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 171 EAGLELTSPRLAALTNFGVQQVDLHKPVRVAVLTTGDELASgtaPDQsPLPPWKIRNSNASALLGLLtNQPWIDCAPPMH 250
Cdd:cd00887 142 PAGTRLTPADIGLLASLGIAEVPVYRRPRVAIISTGDELVE---PGE-PLAPGQIYDSNSYMLAALL-RELGAEVVDLGI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 251 AIDEPAALLTAVEHAIEHHDVVLMTGGVSMGDYDYVPRILRESGAEIVFHKLPLRPGKPILGAVhqsdSKSTLILGLPGN 330
Cdd:cd00887 217 VPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKEVLEELGGEVLFHGVAMKPGKPLAFGR----LGGKPVFGLPGN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 331 PVSATMGARRFAMPLIRKLAGMTNWEEFP-PLVTLEEVSEKTLPLHWLRgVRLTQ---PGLAALVIGKGSGDVATLAGTD 406
Cdd:cd00887 293 PVSALVTFELFVRPALRKLQGAPEPEPPRvKARLAEDLKSKPGRREFLR-VRLERdegGLVVAPPGGQGSGLLSSLARAD 371
|
....*..
gi 494547779 407 GFIEMPP 413
Cdd:cd00887 372 GLIVIPE 378
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
8-413 |
2.47e-59 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 203.69 E-value: 2.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 8 AFDSPEEAIDALARRIvtTGVQRVEigesHDALRSLHRRVLATPILADRDSPAADVSAMDGYAIRESDLLREGpIEVTGE 87
Cdd:PRK14491 197 AFLSVSQGLDKILSLV--TPVTETE----DVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPES-YTLVGE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 88 SVPGSPPPSASDTG-VIRIFTGAIVPVGCDRVIQREHTDEtapasasDSDSLgqiqwTDQAKsIPAGANIRRQGENLSAG 166
Cdd:PRK14491 270 VLAGHQYDGTLQAGeAVRIMTGAPVPAGADTVVMRELATQ-------DGDKV-----SFDGG-IKAGQNVRLAGEDLAQG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 167 SIAVEAGLELTSPRLAALTNFGVQQVDLHKPVRVAVLTTGDELAsgtAPDQsPLPPWKIRNSNASALLGLLTNqpwIDCA 246
Cdd:PRK14491 337 QVALAAGTRLSAPEQGLLASLGFAEVPVFRRPKVAVFSTGDEVQ---APGE-TLKPNCIYDSNRFTIKAMAKK---LGCE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 247 PPMHAI--DEPAALLTAVEHAIEHHDVVLMTGGVSMGDYDYVPRILRESGaEIVFHKLPLRPGKPIlgAVHQSDskSTLI 324
Cdd:PRK14491 410 VIDLGIieDSEAALEATLEQAAAQADVVISSGGVSVGDADYIKTALAKLG-QIDFWRINMRPGRPL--AFGQIG--DSPF 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 325 LGLPGNPVSATMGARRFAMPLIRKLAGMTNWE-EFPPLVTLEEVSEKTLPLHWLRGV-RLTQPG-LAALVIGK-GSGDVA 400
Cdd:PRK14491 485 FGLPGNPVAVMVSFLQFVEPALRKLAGEQNWQpLLFPAIADETLRSRQGRTEFSRGIyHLGADGrLHVRTTGKqGSGILS 564
|
410
....*....|...
gi 494547779 401 TLAGTDGFIEMPP 413
Cdd:PRK14491 565 SMSEANCLIEIGP 577
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
11-415 |
1.23e-58 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 202.37 E-value: 1.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 11 SPEEAIDALARRIVTTGVQRVEIGeSHDALRslhrRVLATPILADRDSPAADVSAMDGYAIRESDLL--REG-PIE--VT 85
Cdd:PRK14498 11 SLEEAREILESLLSELPLGTEEVP-LEEALG----RVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFgaSEAnPVRlkLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 86 GESVPGSPPPSASDTGV-IRIFTGAIVPVGCDRVIQREHTDETapasasDSDSLgQIQwtdqaKSIPAGANIRRQGENLS 164
Cdd:PRK14498 86 GEVHAGEAPDVEVEPGEaVEIATGAPIPRGADAVVMVEDTEEV------DDDTV-EIY-----RPVAPGENVRPAGEDIV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 165 AGSIAVEAGLELTSPRLAALTNFGVQQVDLHKPVRVAVLTTGDELASgtaPDQsPLPPWKIRNSNASALLGLLTNQPWID 244
Cdd:PRK14498 154 AGELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVE---PGE-PLKPGKIYDVNSYTLAAAVEEAGGEP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 245 CAPPmHAIDEPAALLTAVEHAIEHHDVVLMTGGVSMGDYDYVPRILRESGaEIVFHKLPLRPGKP-ILGAVhqsdsKSTL 323
Cdd:PRK14498 230 VRYG-IVPDDEEELEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEELG-EVLVHGVAIKPGKPtILGVI-----GGKP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 324 ILGLPGNPVSATMGARRFAMPLIRKLAGMTnwEEFPPLVT----LEEVSEktLPLHWLRGVRLTQ--PGLAALVIGKGSG 397
Cdd:PRK14498 303 VVGLPGYPVSALTIFEEFVAPLLRKLAGLP--PPERATVKarlaRRVRSE--LGREEFVPVSLGRvgDGYVAYPLSRGSG 378
|
410
....*....|....*...
gi 494547779 398 DVATLAGTDGFIEMPPLA 415
Cdd:PRK14498 379 AITSLVRADGFIEIPANT 396
|
|
| PRK10680 |
PRK10680 |
molybdopterin biosynthesis protein MoeA; Provisional |
46-355 |
5.30e-55 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 182643 [Multi-domain] Cd Length: 411 Bit Score: 187.61 E-value: 5.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 46 RVLATPILADRDSPAADVSAMDGYAIRESDLLREGPIEVTGESVPGSPPPSASDTGV-IRIFTGAIVPVGCDRVIQREHT 124
Cdd:PRK10680 38 RITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKAFAGQPFHGEWPAGTcIRIMTGAPVPEGCEAVVMQEQT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 125 DETAPAsasdsdslgqIQWTDQAKsipAGANIRRQGENLSAGSIAVEAGLELTSPRLAALTNFGVQQVDLHKPVRVAVLT 204
Cdd:PRK10680 118 EQTDDG----------VRFTAEVR---SGQNIRRRGEDISQGAVVFPAGTRLTTAELPVLASLGIAEVPVVRKVRVALFS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 205 TGDELasgTAPDQsPLPPWKIRNSNASALLGLLTNqpwIDCAPPMHAI--DEPAALLTAVEHAIEHHDVVLMTGGVSMGD 282
Cdd:PRK10680 185 TGDEL---QLPGQ-PLGDGQIYDTNRLAVHLMLEQ---LGCEVINLGIirDDPHALRAAFIEADSQADVVISSGGVSVGE 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494547779 283 YDYVPRILRESGaEIVFHKLPLRPGKPI-LGAVHQSdskstLILGLPGNPVSATMGARRFAMPLIRKLAGMTNW 355
Cdd:PRK10680 258 ADYTKTILEELG-EIAFWKLAIKPGKPFaFGKLSNS-----WFCGLPGNPVSAALTFYQLVQPLLAKLSGNTAS 325
|
|
| PRK14690 |
PRK14690 |
molybdopterin biosynthesis protein MoeA; Provisional |
46-420 |
4.60e-39 |
|
molybdopterin biosynthesis protein MoeA; Provisional
Pssm-ID: 237789 [Multi-domain] Cd Length: 419 Bit Score: 145.45 E-value: 4.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 46 RVLATPILADRDSPAADVSAMDGYAIreSDLLREG----PIEvTGESVPGSPPPSASDTG-VIRIFTGAIVPVGCDRVIQ 120
Cdd:PRK14690 53 HVLAHDAVALRSNPPQANSAVDGYGF--AGAAPEGaqvlPLI-EGRAAAGVPFSGRVPEGmALRILTGAALPEGVDTVVL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 121 REHTdetapasASDSdslGQIQWTDQAKSipaGANIRRQGENLSAGSIAVEAGLELTSPRLAALTNFGVQQVDLHKPVRV 200
Cdd:PRK14690 130 EEDV-------AGDG---HRIAFHGPLKM---GANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRVSVRRPLRV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 201 AVLTTGDELasgTAPDQSpLPPWKIRNSNASALLGLLtnQPWIDCAPPM-HAIDEPAALLTAVEHAIEHHDVVLMTGGVS 279
Cdd:PRK14690 197 AVLSTGDEL---VEPGAL-AEVGQIYDANRPMLLALA--RRWGHAPVDLgRVGDDRAALAARLDRAAAEADVILTSGGAS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 280 MGDYDYVPRILRESGAEIVFhKLPLRPGKPILGAVHQsdskSTLILGLPGNPVSATMGARRFAMPLIRKLAGmTNWEEfP 359
Cdd:PRK14690 271 AGDEDHVSALLREAGAMQSW-RIALKPGRPLALGLWQ----GVPVFGLPGNPVAALVCTLVFARPAMSLLAG-EGWSE-P 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494547779 360 PLVTLEEVSEKTLP---LHWLRGvRLTQpGLAALVIGKGSGDVATLAGTDGFIEMPPLANHAGP 420
Cdd:PRK14690 344 QGFTVPAAFEKRKKpgrREYLRA-RLRQ-GHAEVFRSEGSGRISGLSWAEGLVELGDGARRIAP 405
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
11-417 |
4.68e-34 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 133.40 E-value: 4.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 11 SPEEAIDALARRI-VTTGVQRVEIGESHDalrslhrRVLATPILADRDSPAADVSAMDGYAIRESdlLREGPIEVTGESV 89
Cdd:PRK14497 12 SIDEAIKVFLSSLnFKPKIVKVEVKDSFG-------YVSAEDLMSPIDYPPFSRSTVDGYALKSS--CTPGEFKVIDKIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 90 PGSPPPSASDTGV-IRIFTGAIVPVGCDRVIQREHTDetapasasdsdsLGQIQWTDQAKSIPAGANIRRQGENLSAGSI 168
Cdd:PRK14497 83 IGEFKEIHIKECEaVEVDTGSMIPMGADAVIKVENTK------------VINGNFIKIDKKINFGQNIGWIGSDIPKGSI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 169 AVEAGLELTSPRLAALTNFGVQQVDLHKPVRVAVLTTGDELASgtaPDQsPLPPWKIRNSNASALLGLLTNQPWiDCAPP 248
Cdd:PRK14497 151 ILRKGEVISHEKIGLLASLGISSVKVYEKPKIYLIATGDELVE---PGN-SLSPGKIYESNLHYLYSKLKSEGY-KIVGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 249 MHAIDEPAALLTAVEHAIEHHDVVLMTGGVSMGDYDYVPRILRESGaEIVFHKLPLRPGKP-ILGAVhqsdsKSTLILGL 327
Cdd:PRK14497 226 SLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKDFVHQAIRELG-NIIVHGLKIKPGKPtILGIV-----DGKPVIGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 328 PGNPVSATMGARRFAMPLIRKLAG----MTNWEEFPPLVTLEEVSEKT----LPLHWLRGvrltQPGLAALVIGKGSGDV 399
Cdd:PRK14497 300 PGNIVSTMVVLNMVILEYLKSLYPsrkeILGLGKIKARLALRVKADEHrntlIPVYLFKS----DNSYYALPVPFDSYMV 375
|
410
....*....|....*...
gi 494547779 400 ATLAGTDGFIEMPPLANH 417
Cdd:PRK14497 376 GTFSLTDGYIMLGPNEEI 393
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
201-348 |
8.46e-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 trimerization.
Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 112.73 E-value: 8.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 201 AVLTTGDELASGtapdqsplppwKIRNSNASALLGLLTNQPwIDCAPPMHAIDEPAALLTAVEHAIEHHDVVLMTGGVSM 280
Cdd:pfam00994 1 AIITTGDELLPG-----------QIRDTNGPLLAALLREAG-AEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGP 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494547779 281 GDYDYVPRILRESGA------EIVFHKLPLRPGKPILGAVHQSDSK-STLILGLPGNPVSATMGARRFAMPLIRK 348
Cdd:pfam00994 69 GPDDVTPEALAELGGrelpgfEELFRGVSLKPGKPVGTAPGAILSRaGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
|
|
| MoeA_N |
pfam03453 |
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ... |
46-188 |
1.53e-29 |
|
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: 111.89 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 46 RVLATPILADRDSPAADVSAMDGYAIRESDLlrEGPIEVTGESVPGSPPPSASDTGVIRIFTGAIVPVGCDRVIQREHTD 125
Cdd:pfam03453 19 RVLAEDVVAPRDVPPFDRSAMDGYAVRAADG--FGASEVNPIAAGEPPGPLLPGGEAVRIMTGAPLPEGADAVVMVEDTE 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494547779 126 ETAPASasdsdslgqiqwTDQAKSIPAGANIRRQGENLSAGSIAVEAGLELTSPRLAALTNFG 188
Cdd:pfam03453 97 EGGGRT------------VEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
|
|
| PLN02699 |
PLN02699 |
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
20-354 |
2.47e-29 |
|
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 120.69 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 20 ARRIVTTGVQRVE--IGESHDALRslhrRVLATPILADRDSPAADVSAMDGYAIRESDllreGPIE--VTGESVPGSPPP 95
Cdd:PLN02699 13 ALSIVLSVAARLSpvIVPLHEALG----KVLAEDIRAPDPLPPYPASVKDGYAVVASD----GPGEypVITESRAGNDGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 96 SASDT--GVIRIFTGAIVPVGCDRVIQREHTDETapasasdSDSLGQIQWTDQAKSIPAGANIRRQGENLSAGSIAVEAG 173
Cdd:PLN02699 85 GVTLTpgTVAYVTTGGPIPDGADAVVQVEDTEVV-------EDPLDGSKRVRILSQASKGQDIRPVGCDIEKDAKVLKAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 174 LELTSPRLAALTNFGVQQVDLHKPVRVAVLTTGDELASgtaPDQSPLPPWKIRNSNASALLGLLTNQPwIDCAPPMHAID 253
Cdd:PLN02699 158 ERLGASEIGLLATVGVTMVKVYPRPTVAILSTGDELVE---PTTGTLGRGQIRDSNRAMLLAAAIQQQ-CKVVDLGIARD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 254 EPAALLTAVEHAIEHH-DVVLMTGGVSMGDYDYVPRILRESGaEIVFHKLPLRPGKPILGAV-----HQSDSKSTLILGL 327
Cdd:PLN02699 234 DEEELERILDEAISSGvDILLTSGGVSMGDRDFVKPLLEKRG-TVYFSKVLMKPGKPLTFAEidaksAPSNSKKMLAFGL 312
|
330 340
....*....|....*....|....*..
gi 494547779 328 PGNPVSATMGARRFAMPLIRKLAGMTN 354
Cdd:PLN02699 313 PGNPVSCLVCFNLFVVPAIRYLAGWSN 339
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
198-344 |
5.95e-27 |
|
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: 105.09 E-value: 5.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 198 VRVAVLTTGDELASGTapdqSPLPPWKIRNSNASALLGLLTNQpwidCAPPMHAI---DEPAALLTAVEHAIEHHDVVLM 274
Cdd:TIGR00177 1 PRVAVISVGDELVEGG----QPLEPGQIYDSNGPLLAALLQEA----GFNVVRLGivpDDPEEIREILRKAVDEADVVLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 275 TGGVSMGDYDYVPRILRE------SGAEIVFHKLPL----RPGKPILGAVHqsdsKSTLILGLPGNPVSATMGARRFAMP 344
Cdd:TIGR00177 73 TGGTGVGPRDVTPEALEElgekeiPGFGEFRMLSSLpvlsRPGKPATAGVR----GGTLIFNLPGNPVSALVTFEVLILP 148
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
201-341 |
8.25e-26 |
|
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: 101.51 E-value: 8.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 201 AVLTTGDELasgtapdqspLPPWKIRNSNASALLGLLTNQPWIDCAPPMHAI-DEPAALLTAVEHAIEHHDVVLMTGGVS 279
Cdd:smart00852 1 AIISTGDEL----------LSGGQIRDSNGPMLAALLRELGIEVVRVVVVGGpDDPEAIREALREALAEADVVITTGGTG 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494547779 280 MGDYDYVPRILRES-GAEIVFHKLPLRPGKPILGAVHQS-----DSKSTLILGLPGNPVSATMGARRF 341
Cdd:smart00852 71 PGPDDLTPEALAELgGRELLGHGVAMRPGGPPGPLANLSgtapgVRGKKPVFGLPGNPVAALVMFEEL 138
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
199-335 |
2.24e-16 |
|
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: 75.46 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 199 RVAVLTTGDELASGtapdqsplppwKIRNSNASALLGLLTNQPWidcaPPMHAI---DEPAALLTAVEHAIEHHDVVLMT 275
Cdd:cd00758 1 RVAIVTVSDELSQG-----------QIEDTNGPALEALLEDLGC----EVIYAGvvpDDADSIRAALIEASREADLVLTT 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494547779 276 GGVSMGDYDYVPRILRESGA-EIVFHKLPLRPGKPILGAVHqsdsKSTLILGLPGNPVSAT 335
Cdd:cd00758 66 GGTGVGRRDVTPEALAELGErEAHGKGVALAPGSRTAFGII----GKVLIINLPGSPKSAL 122
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
199-277 |
5.54e-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: 46.32 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 199 RVAVLTTGDELASGtapdqsplppwKIRNSNASALLGLLTNQPWidcapPMHAI----DEPAALLTAVEHAIEHHDVVLM 274
Cdd:cd00885 1 TAEIIAIGDELLSG-----------QIVDTNAAFLAKELAELGI-----EVYRVtvvgDDEDRIAEALRRASERADLVIT 64
|
...
gi 494547779 275 TGG 277
Cdd:cd00885 65 TGG 67
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
181-313 |
2.21e-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: 42.92 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494547779 181 LAALTNFGVQQVDLHKPVRVAVLTTGDELASGTAPDqsplppwKIRNSNAS--ALLGLLTNQPWIdCAppmhaiDEPAAL 258
Cdd:cd03522 143 EALARDGPLLRVAPFRPLRVGLIVTGSEVYGGRIED-------KFGPVLRArlAALGVELVEQVI-VP------HDEAAI 208
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494547779 259 LTAVEHAIEHHD-VVLMTGGVSMGDYDYVPRILRESGAEIVFHKLPLRPG----------KPILGA 313
Cdd:cd03522 209 AAAIAEALEAGAeLLILTGGASVDPDDVTPAAIRAAGGEVIRYGMPVDPGnllllgylggVPVIGL 274
|
|
| |
