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Conserved domains on  [gi|1062421413|gb|AOM03003|]
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molybdopterin molybdenumtransferase [Cobetia marina]

Protein Classification

molybdopterin molybdotransferase MoeA( domain architecture ID 11416749)

molybdopterin molybdotransferase MoeA mediates molybdenum ligation to molybdopterin

EC:  2.10.1.1
Gene Ontology:  GO:0046872|GO:0006777|GO:0061599

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
1-407 3.23e-151

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: 433.75  E-value: 3.23e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413   1 MAPLSSALSALRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDG--AWLPISQRIAAGQ- 77
Cdd:COG0303     1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAnpVTLRVVGEIAAGSp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  78 PTSALASASCARLFTGAEIPEGADVVVMQEEVTLRENEngtteAWLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAM 157
Cdd:COG0303    81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDR-----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPAD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 158 LGLLCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALAT 237
Cdd:COG0303   156 LGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGI-VPDDPEALRAALRE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 238 AAEQADLIVTCGGVSVGEEDHVRPAIEALG-SLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLR 316
Cdd:COG0303   235 ALAEADLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRL-----GGKPVFGLPGNPVSALVTFELFVR 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 317 PMLGEMLECDAlRALRSLRVRSAFS-ANTAIRQDHLRVTLTPaDDGQLEAHAFPDQNSAVLSSCVGAEALAVIPPHAQ-I 394
Cdd:COG0303   310 PALRKLAGLPP-PPPPRVRARLAEDlPKKPGRTEFLRVRLER-DDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEgV 387
                         410
                  ....*....|...
gi 1062421413 395 SPGDSVECLWLES 407
Cdd:COG0303   388 EAGEEVEVLLLDG 400
 
Name Accession Description Interval E-value
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
1-407 3.23e-151

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: 433.75  E-value: 3.23e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413   1 MAPLSSALSALRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDG--AWLPISQRIAAGQ- 77
Cdd:COG0303     1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAnpVTLRVVGEIAAGSp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  78 PTSALASASCARLFTGAEIPEGADVVVMQEEVTLRENEngtteAWLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAM 157
Cdd:COG0303    81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDR-----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPAD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 158 LGLLCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALAT 237
Cdd:COG0303   156 LGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGI-VPDDPEALRAALRE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 238 AAEQADLIVTCGGVSVGEEDHVRPAIEALG-SLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLR 316
Cdd:COG0303   235 ALAEADLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRL-----GGKPVFGLPGNPVSALVTFELFVR 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 317 PMLGEMLECDAlRALRSLRVRSAFS-ANTAIRQDHLRVTLTPaDDGQLEAHAFPDQNSAVLSSCVGAEALAVIPPHAQ-I 394
Cdd:COG0303   310 PALRKLAGLPP-PPPPRVRARLAEDlPKKPGRTEFLRVRLER-DDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEgV 387
                         410
                  ....*....|...
gi 1062421413 395 SPGDSVECLWLES 407
Cdd:COG0303   388 EAGEEVEVLLLDG 400
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
7-405 1.07e-144

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: 416.89  E-value: 1.07e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413   7 ALSALRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDGAW-LPISQRIAAGQ-PTSALAS 84
Cdd:cd00887     4 ARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtLRVVGEIPAGEpPDGPLGP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  85 ASCARLFTGAEIPEGADVVVMQEEVTLRENEngtteAWLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGLLCGQ 164
Cdd:cd00887    84 GEAVRIMTGAPLPEGADAVVMVEDTEEEGGR-----VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 165 GLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALATAAEQADL 244
Cdd:cd00887   159 GIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGI-VPDDPEALREALEEALEEADV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 245 IVTCGGVSVGEEDHVRPAIEAL-GSLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLRPMLGEML 323
Cdd:cd00887   238 VITSGGVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRL-----GGKPVFGLPGNPVSALVTFELFVRPALRKLQ 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 324 eCDALRALRSLRVRSAFS-ANTAIRQDHLRVTLTPaDDGQLEAHAFPDQNSAVLSSCVGAEALAVIPPHAQ-ISPGDSVE 401
Cdd:cd00887   313 -GAPEPEPPRVKARLAEDlKSKPGRREFLRVRLER-DEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEgLEAGEEVE 390

                  ....
gi 1062421413 402 CLWL 405
Cdd:cd00887   391 VLLL 394
PRK10680 PRK10680
molybdopterin biosynthesis protein MoeA; Provisional
3-378 2.37e-92

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 182643 [Multi-domain]  Cd Length: 411  Bit Score: 283.91  E-value: 2.37e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413   3 PLSSALSA-LRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDGAWLPISQRIAAGQP-TS 80
Cdd:PRK10680    9 SLETALTEmLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKAFAGQPfHG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  81 ALASASCARLFTGAEIPEGADVVVMQEEVtlRENENGTTeawLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGL 160
Cdd:PRK10680   89 EWPAGTCIRIMTGAPVPEGCEAVVMQEQT--EQTDDGVR---FTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 161 LCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALATAAE 240
Cdd:PRK10680  164 LASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGI-IRDDPHALRAAFIEADS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 241 QADLIVTCGGVSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRILNTQgdsvrVVGLPGNPVSSWVGGWLFLRPMLG 320
Cdd:PRK10680  243 QADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSW-----FCGLPGNPVSAALTFYQLVQPLLA 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1062421413 321 EMLECDALRALRSLRVRSA-FSANTAIRQDHLRVTLTPADDGQLEAHAFPDQNSAVLSS 378
Cdd:PRK10680  318 KLSGNTASGLPPRQRVRTAsRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSS 376
MoeA_N pfam03453
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ...
16-165 1.59e-39

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: 138.08  E-value: 1.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  16 PVMPVEQVPV--SKAAGRVLAEDIYAELDVPPADNSQMDGYCARVAdigDGAWLPISQRIAAGQPTSA-LASASCARLFT 92
Cdd:pfam03453   2 LLGTEETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAA---DGFGASEVNPIAAGEPPGPlLPGGEAVRIMT 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062421413  93 GAEIPEGADVVVMQEEVTLRENENGTTEAwlpgPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGLLCGQG 165
Cdd:pfam03453  79 GAPLPEGADAVVMVEDTEEGGGRTVEIRA----PVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
178-310 5.07e-31

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.


Pssm-ID: 214856 [Multi-domain]  Cd Length: 138  Bit Score: 115.38  E-value: 5.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  178 ALFATGDELiepgqpLEPGQIYNSNRVMLSQMLSDFGADVVLAPLN-VADTFEATRDALATAAEQADLIVTCGGVSVGEE 256
Cdd:smart00852   1 AIISTGDEL------LSGGQIRDSNGPMLAALLRELGIEVVRVVVVgGPDDPEAIREALREALAEADVVITTGGTGPGPD 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062421413  257 DHVRPAIEALGSLDL--WRLAIKPGKP-----LALGRILNTQGDSVrVVGLPGNPVSSWVG 310
Cdd:smart00852  75 DLTPEALAELGGRELlgHGVAMRPGGPpgplaNLSGTAPGVRGKKP-VFGLPGNPVAALVM 134
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
175-317 6.16e-30

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: 112.80  E-value: 6.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 175 VRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVlAPLNVADTFEATRDALATAAEQADLIVTCGGVSVG 254
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVV-RLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVG 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062421413 255 EEDHVRPAIEALG-----------SLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLRP 317
Cdd:TIGR00177  80 PRDVTPEALEELGekeipgfgefrMLSSLPVLSRPGKPATAGVR-----GGTLIFNLPGNPVSALVTFEVLILP 148
 
Name Accession Description Interval E-value
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
1-407 3.23e-151

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: 433.75  E-value: 3.23e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413   1 MAPLSSALSALRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDG--AWLPISQRIAAGQ- 77
Cdd:COG0303     1 MISVEEALALILAAVRPLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGAnpVTLRVVGEIAAGSp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  78 PTSALASASCARLFTGAEIPEGADVVVMQEEVTLRENEngtteAWLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAM 157
Cdd:COG0303    81 PPGPLGPGEAVRIMTGAPLPEGADAVVMQEDTEREGDR-----VTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRLTPAD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 158 LGLLCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALAT 237
Cdd:COG0303   156 LGLLASLGIAEVPVYRRPRVAILSTGDELVEPGEPLGPGQIYDSNSYMLAALLREAGAEVVDLGI-VPDDPEALRAALRE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 238 AAEQADLIVTCGGVSVGEEDHVRPAIEALG-SLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLR 316
Cdd:COG0303   235 ALAEADLVITSGGVSVGDYDLVKEALEELGaEVLFHKVAMKPGKPLAFGRL-----GGKPVFGLPGNPVSALVTFELFVR 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 317 PMLGEMLECDAlRALRSLRVRSAFS-ANTAIRQDHLRVTLTPaDDGQLEAHAFPDQNSAVLSSCVGAEALAVIPPHAQ-I 394
Cdd:COG0303   310 PALRKLAGLPP-PPPPRVRARLAEDlPKKPGRTEFLRVRLER-DDGELVVEPLGGQGSGLLSSLAEADGLIVLPEGVEgV 387
                         410
                  ....*....|...
gi 1062421413 395 SPGDSVECLWLES 407
Cdd:COG0303   388 EAGEEVEVLLLDG 400
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
7-405 1.07e-144

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: 416.89  E-value: 1.07e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413   7 ALSALRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDGAW-LPISQRIAAGQ-PTSALAS 84
Cdd:cd00887     4 ARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAGASVtLRVVGEIPAGEpPDGPLGP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  85 ASCARLFTGAEIPEGADVVVMQEEVTLRENEngtteAWLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGLLCGQ 164
Cdd:cd00887    84 GEAVRIMTGAPLPEGADAVVMVEDTEEEGGR-----VTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADIGLLASL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 165 GLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALATAAEQADL 244
Cdd:cd00887   159 GIAEVPVYRRPRVAIISTGDELVEPGEPLAPGQIYDSNSYMLAALLRELGAEVVDLGI-VPDDPEALREALEEALEEADV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 245 IVTCGGVSVGEEDHVRPAIEAL-GSLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLRPMLGEML 323
Cdd:cd00887   238 VITSGGVSVGDYDFVKEVLEELgGEVLFHGVAMKPGKPLAFGRL-----GGKPVFGLPGNPVSALVTFELFVRPALRKLQ 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 324 eCDALRALRSLRVRSAFS-ANTAIRQDHLRVTLTPaDDGQLEAHAFPDQNSAVLSSCVGAEALAVIPPHAQ-ISPGDSVE 401
Cdd:cd00887   313 -GAPEPEPPRVKARLAEDlKSKPGRREFLRVRLER-DEGGLVVAPPGGQGSGLLSSLARADGLIVIPEGVEgLEAGEEVE 390

                  ....
gi 1062421413 402 CLWL 405
Cdd:cd00887   391 VLLL 394
PRK10680 PRK10680
molybdopterin biosynthesis protein MoeA; Provisional
3-378 2.37e-92

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 182643 [Multi-domain]  Cd Length: 411  Bit Score: 283.91  E-value: 2.37e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413   3 PLSSALSA-LRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDGAWLPISQRIAAGQP-TS 80
Cdd:PRK10680    9 SLETALTEmLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQPLPVAGKAFAGQPfHG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  81 ALASASCARLFTGAEIPEGADVVVMQEEVtlRENENGTTeawLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGL 160
Cdd:PRK10680   89 EWPAGTCIRIMTGAPVPEGCEAVVMQEQT--EQTDDGVR---FTAEVRSGQNIRRRGEDISQGAVVFPAGTRLTTAELPV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 161 LCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALATAAE 240
Cdd:PRK10680  164 LASLGIAEVPVVRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGI-IRDDPHALRAAFIEADS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 241 QADLIVTCGGVSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRILNTQgdsvrVVGLPGNPVSSWVGGWLFLRPMLG 320
Cdd:PRK10680  243 QADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSW-----FCGLPGNPVSAALTFYQLVQPLLA 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1062421413 321 EMLECDALRALRSLRVRSA-FSANTAIRQDHLRVTLTPADDGQLEAHAFPDQNSAVLSS 378
Cdd:PRK10680  318 KLSGNTASGLPPRQRVRTAsRLKKTPGRLDFQRGILQRNADGELEVTTTGHQGSHIFSS 376
PRK14491 PRK14491
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ...
16-400 4.98e-86

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional


Pssm-ID: 237729 [Multi-domain]  Cd Length: 597  Bit Score: 273.03  E-value: 4.98e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  16 PVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDGAWlPISQRIAAGQPTSALASASCA-RLFTGA 94
Cdd:PRK14491  214 PVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDDLEPESY-TLVGEVLAGHQYDGTLQAGEAvRIMTGA 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  95 EIPEGADVVVMQEEVTLRENE---NGTTEAwlpgpripGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGLLCGQGLSYVSV 171
Cdd:PRK14491  293 PVPAGADTVVMRELATQDGDKvsfDGGIKA--------GQNVRLAGEDLAQGQVALAAGTRLSAPEQGLLASLGFAEVPV 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 172 RHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVlaPLNVA-DTFEATRDALATAAEQADLIVTCGG 250
Cdd:PRK14491  365 FRRPKVAVFSTGDEVQAPGETLKPNCIYDSNRFTIKAMAKKLGCEVI--DLGIIeDSEAALEATLEQAAAQADVVISSGG 442
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 251 VSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRIlntqGDSVrVVGLPGNPVSSWVGGWLFLRPML----GE----- 321
Cdd:PRK14491  443 VSVGDADYIKTALAKLGQIDFWRINMRPGRPLAFGQI----GDSP-FFGLPGNPVAVMVSFLQFVEPALrklaGEqnwqp 517
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 322 -MLECDALRALRSLRVRSAFSantairqdhlRVTLTPADDGQLEAHAFPDQNSAVLSSCVGAEALAVI-PPHAQISPGDS 399
Cdd:PRK14491  518 lLFPAIADETLRSRQGRTEFS----------RGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIgPAAETVNAGET 587

                  .
gi 1062421413 400 V 400
Cdd:PRK14491  588 V 588
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
8-401 2.37e-83

putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 267.08  E-value: 2.37e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413   8 LSALREccPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADI-----GDGAWLPISQRIAAGQ-PTSA 81
Cdd:PRK14498   20 ESLLSE--LPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTfgaseANPVRLKLGGEVHAGEaPDVE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  82 LASASCARLFTGAEIPEGADVVVMQEEVTLRENENGTTEAwlpgPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGLL 161
Cdd:PRK14498   98 VEPGEAVEIATGAPIPRGADAVVMVEDTEEVDDDTVEIYR----PVAPGENVRPAGEDIVAGELILPKGTRLTPRDIGAL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 162 CGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALATAAEQ 241
Cdd:PRK14498  174 AAGGVAEVPVYKKPRVGIISTGDELVEPGEPLKPGKIYDVNSYTLAAAVEEAGGEPVRYGI-VPDDEEELEAALRKALKE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 242 ADLIVTCGGVSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLRPMLGE 321
Cdd:PRK14498  253 CDLVLLSGGTSAGAGDVTYRVIEELGEVLVHGVAIKPGKPTILGVI-----GGKPVVGLPGYPVSALTIFEEFVAPLLRK 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 322 ML-----ECDALRALRSLRVRSAFSantaiRQDHLRVTLTPADDGQLeahAFP-DQNSAVLSSCVGAEALAVIPPHAQ-I 394
Cdd:PRK14498  328 LAglpppERATVKARLARRVRSELG-----REEFVPVSLGRVGDGYV---AYPlSRGSGAITSLVRADGFIEIPANTEgL 399

                  ....*..
gi 1062421413 395 SPGDSVE 401
Cdd:PRK14498  400 EAGEEVE 406
PRK14690 PRK14690
molybdopterin biosynthesis protein MoeA; Provisional
3-400 7.67e-73

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 237789 [Multi-domain]  Cd Length: 419  Bit Score: 234.04  E-value: 7.67e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413   3 PLSSALSALRE-CCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCARVADIGDGAWLPISQ-RIAAGQPTS 80
Cdd:PRK14690   24 PVDTALDLLRArLGPVTDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGAAPEGAQVLPLIEgRAAAGVPFS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  81 ALASASCA-RLFTGAEIPEGADVVVMQEEVTLrenenGTTEAWLPGPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLG 159
Cdd:PRK14690  104 GRVPEGMAlRILTGAALPEGVDTVVLEEDVAG-----DGHRIAFHGPLKMGANTRKAGEDVIAGDVALPAGRRLTPADLA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 160 LLCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFG-ADVVLAplNVADTFEATRDALATA 238
Cdd:PRK14690  179 LLSAVGLTRVSVRRPLRVAVLSTGDELVEPGALAEVGQIYDANRPMLLALARRWGhAPVDLG--RVGDDRAALAARLDRA 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 239 AEQADLIVTCGGVSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRilnTQGdsVRVVGLPGNPVSSWVGGWLFLRPM 318
Cdd:PRK14690  257 AAEADVILTSGGASAGDEDHVSALLREAGAMQSWRIALKPGRPLALGL---WQG--VPVFGLPGNPVAALVCTLVFARPA 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 319 LGeMLECDALRALRSLRVRSAFSANT-AIRQDHLRVTLTpadDGQLEahAFPDQNSAVLSSCVGAEALAVIPPHA-QISP 396
Cdd:PRK14690  332 MS-LLAGEGWSEPQGFTVPAAFEKRKkPGRREYLRARLR---QGHAE--VFRSEGSGRISGLSWAEGLVELGDGArRIAP 405

                  ....
gi 1062421413 397 GDSV 400
Cdd:PRK14690  406 GDPV 409
PRK14497 PRK14497
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
11-401 7.61e-53

putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional


Pssm-ID: 172968 [Multi-domain]  Cd Length: 546  Bit Score: 184.63  E-value: 7.61e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  11 LRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYCA---------RVAD-IGDGAWLPIsqRIAAGQpts 80
Cdd:PRK14497   21 LSSLNFKPKIVKVEVKDSFGYVSAEDLMSPIDYPPFSRSTVDGYALkssctpgefKVIDkIGIGEFKEI--HIKECE--- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  81 alasasCARLFTGAEIPEGADVVVMQEEVTLREnengtteawlpGPRIP-------GDNIRRQGRDVTRGTRLIAAGTRL 153
Cdd:PRK14497   96 ------AVEVDTGSMIPMGADAVIKVENTKVIN-----------GNFIKidkkinfGQNIGWIGSDIPKGSIILRKGEVI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 154 DAAMLGLLCGQGLSYVSVRHKVRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRD 233
Cdd:PRK14497  159 SHEKIGLLASLGISSVKVYEKPKIYLIATGDELVEPGNSLSPGKIYESNLHYLYSKLKSEGYKIVGLSL-LSDDKESIKN 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 234 ALATAAEQADLIVTCGGVSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWvggwl 313
Cdd:PRK14497  238 EIKRAISVADVLILTGGTSAGEKDFVHQAIRELGNIIVHGLKIKPGKPTILGIV-----DGKPVIGLPGNIVSTM----- 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 314 flrpMLGEMLECDALRALRSLRVR-------SAFSANtAIRQDHLRVTLTPA----DDGQLEAHAFPdQNSAVLSSCVGA 382
Cdd:PRK14497  308 ----VVLNMVILEYLKSLYPSRKEilglgkiKARLAL-RVKADEHRNTLIPVylfkSDNSYYALPVP-FDSYMVGTFSLT 381
                         410
                  ....*....|....*....
gi 1062421413 383 EALAVIPPHAQISPGDSVE 401
Cdd:PRK14497  382 DGYIMLGPNEEIEEGKEVE 400
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
1-403 3.10e-45

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 165.76  E-value: 3.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413   1 MAPLSSALSALRECCPVMPVEQVPVSKAAGRVLAEDIYAELDVPPADNSQMDGYcARVADIGDGAWlPISQRIAAGQPTS 80
Cdd:PLN02699    7 MISVEEALSIVLSVAARLSPVIVPLHEALGKVLAEDIRAPDPLPPYPASVKDGY-AVVASDGPGEY-PVITESRAGNDGL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  81 A--LASASCARLFTGAEIPEGADVVVMQEEVTLRENENGTTEAwlpgPRI-----PGDNIRRQGRDVTRGTRLIAAGTRL 153
Cdd:PLN02699   85 GvtLTPGTVAYVTTGGPIPDGADAVVQVEDTEVVEDPLDGSKR----VRIlsqasKGQDIRPVGCDIEKDAKVLKAGERL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 154 DAAMLGLLCGQGLSYVSVRHKVRVALFATGDELIEPGQP-LEPGQIYNSNRVMLSQMLSDFGADVVlaPLNVA-DTFEAT 231
Cdd:PLN02699  161 GASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEPTTGtLGRGQIRDSNRAMLLAAAIQQQCKVV--DLGIArDDEEEL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 232 RDALATA-AEQADLIVTCGGVSVGEEDHVRPAIEALGSLDLWRLAIKPGKPLALGRILNTQGDS----VRVVGLPGNPVS 306
Cdd:PLN02699  239 ERILDEAiSSGVDILLTSGGVSMGDRDFVKPLLEKRGTVYFSKVLMKPGKPLTFAEIDAKSAPSnskkMLAFGLPGNPVS 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 307 SWVGGWLFLRPMLGEMLECDALRALR-SLRVRSAFSANtAIRQDHLRVTLT-PADDGQLE----AHAFPDQNSAVLSSCV 380
Cdd:PLN02699  319 CLVCFNLFVVPAIRYLAGWSNPHLLRvQARLREPIKLD-PVRPEFHRAIIRwKLNDGSGNpgfvAESTGHQMSSRLLSMK 397
                         410       420
                  ....*....|....*....|....
gi 1062421413 381 GAEALAVIPP-HAQISPGDSVECL 403
Cdd:PLN02699  398 SANALLELPAtGNVLSAGTSVSAI 421
MoeA_N pfam03453
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ...
16-165 1.59e-39

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: 138.08  E-value: 1.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  16 PVMPVEQVPV--SKAAGRVLAEDIYAELDVPPADNSQMDGYCARVAdigDGAWLPISQRIAAGQPTSA-LASASCARLFT 92
Cdd:pfam03453   2 LLGTEETVPLeaLDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAA---DGFGASEVNPIAAGEPPGPlLPGGEAVRIMT 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062421413  93 GAEIPEGADVVVMQEEVTLRENENGTTEAwlpgPRIPGDNIRRQGRDVTRGTRLIAAGTRLDAAMLGLLCGQG 165
Cdd:pfam03453  79 GAPLPEGADAVVMVEDTEEGGGRTVEIRA----PVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
178-310 5.07e-31

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.


Pssm-ID: 214856 [Multi-domain]  Cd Length: 138  Bit Score: 115.38  E-value: 5.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413  178 ALFATGDELiepgqpLEPGQIYNSNRVMLSQMLSDFGADVVLAPLN-VADTFEATRDALATAAEQADLIVTCGGVSVGEE 256
Cdd:smart00852   1 AIISTGDEL------LSGGQIRDSNGPMLAALLRELGIEVVRVVVVgGPDDPEAIREALREALAEADVVITTGGTGPGPD 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062421413  257 DHVRPAIEALGSLDL--WRLAIKPGKP-----LALGRILNTQGDSVrVVGLPGNPVSSWVG 310
Cdd:smart00852  75 DLTPEALAELGGRELlgHGVAMRPGGPpgplaNLSGTAPGVRGKKP-VFGLPGNPVAALVM 134
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
178-319 6.70e-31

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.


Pssm-ID: 425979 [Multi-domain]  Cd Length: 143  Bit Score: 115.42  E-value: 6.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 178 ALFATGDELIepgqplePGQIYNSNRVMLSQMLSDFGADVVlAPLNVADTFEATRDALATAAEQADLIVTCGGVSVGEED 257
Cdd:pfam00994   1 AIITTGDELL-------PGQIRDTNGPLLAALLREAGAEVI-RYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDD 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062421413 258 HVRPAIEALG-------SLDLWRLAIKPGKPLALGRILNTQGDSVRVVGLPGNPVSSWVGGWLFLRPML 319
Cdd:pfam00994  73 VTPEALAELGgrelpgfEELFRGVSLKPGKPVGTAPGAILSRAGKTVFGLPGSPVAAKVMFELLLLPLL 141
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
175-317 6.16e-30

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: 112.80  E-value: 6.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 175 VRVALFATGDELIEPGQPLEPGQIYNSNRVMLSQMLSDFGADVVlAPLNVADTFEATRDALATAAEQADLIVTCGGVSVG 254
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPLEPGQIYDSNGPLLAALLQEAGFNVV-RLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVG 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062421413 255 EEDHVRPAIEALG-----------SLDLWRLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLRP 317
Cdd:TIGR00177  80 PRDVTPEALEELGekeipgfgefrMLSSLPVLSRPGKPATAGVR-----GGTLIFNLPGNPVSALVTFEVLILP 148
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
176-319 3.13e-22

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: 91.64  E-value: 3.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 176 RVALFATGDELIepgqplePGQIYNSNRVMLSQMLSDFGADVVLAPLnVADTFEATRDALATAAEQADLIVTCGGVSVGE 255
Cdd:cd00758     1 RVAIVTVSDELS-------QGQIEDTNGPALEALLEDLGCEVIYAGV-VPDDADSIRAALIEASREADLVLTTGGTGVGR 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062421413 256 EDHVRPAIEALGSLDLW--RLAIKPGKPLALGRIlntqgDSVRVVGLPGNPVSSWVGGWLFLRPML 319
Cdd:cd00758    73 RDVTPEALAELGEREAHgkGVALAPGSRTAFGII-----GKVLIINLPGSPKSALTTFEALVLPAL 133
MoeA_C pfam03454
MoeA C-terminal region (domain IV); This domain is found in proteins involved in biosynthesis ...
347-401 2.53e-07

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: 47.61  E-value: 2.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1062421413 347 RQDHLRVTLTpADDGQLEAHAFPDQNSAVLSSCVGAEALAVIPPH-AQISPGDSVE 401
Cdd:pfam03454  14 RREFVRVRLH-EEDGRYYAEPIGKQGSGMLSSLAEANGLIVVPEGtEGLEAGEEVE 68
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
176-250 5.32e-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: 5.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1062421413 176 RVALFATGDELIepgqplePGQIYNSNRVMLSQMLSDFGADVVLApLNVADTFEATRDALATAAEQADLIVTCGG 250
Cdd:cd00885     1 TAEIIAIGDELL-------SGQIVDTNAAFLAKELAELGIEVYRV-TVVGDDEDRIAEALRRASERADLVITTGG 67
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
181-250 6.87e-04

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 41.70  E-value: 6.87e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 181 ATGDELIEpgqplepGQIYNSNRVMLSQMLSDFGADVVLApLNVADTFEATRDALATAAEQADLIVTCGG 250
Cdd:PRK00549    7 AVGTELLL-------GQIVNTNAQFLSEKLAELGIDVYHQ-TVVGDNPERLLSALEIAEERSDLIITTGG 68
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
210-302 1.09e-03

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: 40.61  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062421413 210 LSDFGADVVLAPLnVADTFEATRDALATAAEQADLIVTC-GGVSVGEEDHVRPAIEALG-SLDLWRLAIKPGKPLALGRI 287
Cdd:cd03522   188 LAALGVELVEQVI-VPHDEAAIAAAIAEALEAGAELLILtGGASVDPDDVTPAAIRAAGgEVIRYGMPVDPGNLLLLGYL 266
                          90
                  ....*....|....*
gi 1062421413 288 lntqgDSVRVVGLPG 302
Cdd:cd03522   267 -----GGVPVIGLPG 276
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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