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Conserved domains on  [gi|2531271090|gb|WJY74975|]
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Molybdopterin molybdenumtransferase [Corynebacterium canis]

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]; ...
9-404 2.09e-120

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: 355.17  E-value: 2.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090   9 LRSLSEHLDAVLSLATaPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPGPWTFPVIGDIPAGT 88
Cdd:COG0303     1 MISVEEALALILAAVR-PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  89 DVRTP-RRGAALRIMTGAPVPEepGL-AVVPVEHTNIPRGpqslpsSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRI 166
Cdd:COG0303    80 PPPGPlGPGEAVRIMTGAPLPE--GAdAVVMQEDTEREGD------RVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 167 DAATIAALVSTGNATVPVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA 238
Cdd:COG0303   152 TPADLGLLASLGIAEVPVYRRPRVAILSTGDELvepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 239 -LEAAKGSNLILTTGGISAGAFDIVRELLSP---DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPL 314
Cdd:COG0303   232 lREALAEADLVITSGGVSVGDYDLVKEALEElgaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 315 MRALSGQVPQgldERPQLMASAACEFHADSKRDRFIPVRIKYGTTPQAISSHRSGlGSHFVASLAGVTGLAYLPHGTGTT 394
Cdd:COG0303   312 LRKLAGLPPP---PPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQ-GSGLLSSLAEADGLIVLPEGVEGV 387
                         410
                  ....*....|
gi 2531271090 395 AIGQPVRVLL 404
Cdd:COG0303   388 EAGEEVEVLL 397
 
Name Accession Description Interval E-value
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
9-404 2.09e-120

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: 355.17  E-value: 2.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090   9 LRSLSEHLDAVLSLATaPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPGPWTFPVIGDIPAGT 88
Cdd:COG0303     1 MISVEEALALILAAVR-PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  89 DVRTP-RRGAALRIMTGAPVPEepGL-AVVPVEHTNIPRGpqslpsSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRI 166
Cdd:COG0303    80 PPPGPlGPGEAVRIMTGAPLPE--GAdAVVMQEDTEREGD------RVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 167 DAATIAALVSTGNATVPVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA 238
Cdd:COG0303   152 TPADLGLLASLGIAEVPVYRRPRVAILSTGDELvepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 239 -LEAAKGSNLILTTGGISAGAFDIVRELLSP---DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPL 314
Cdd:COG0303   232 lREALAEADLVITSGGVSVGDYDLVKEALEElgaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 315 MRALSGQVPQgldERPQLMASAACEFHADSKRDRFIPVRIKYGTTPQAISSHRSGlGSHFVASLAGVTGLAYLPHGTGTT 394
Cdd:COG0303   312 LRKLAGLPPP---PPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQ-GSGLLSSLAEADGLIVLPEGVEGV 387
                         410
                  ....*....|
gi 2531271090 395 AIGQPVRVLL 404
Cdd:COG0303   388 EAGEEVEVLL 397
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
14-404 1.26e-115

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: 342.55  E-value: 1.26e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  14 EHLDAVLSLATAPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGpGPWTFPVIGDIPAGTD-VRT 92
Cdd:cd00887     2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAG-ASVTLRVVGEIPAGEPpDGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  93 PRRGAALRIMTGAPVPEepGL-AVVPVEHTNIPRGpqslpsSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRIDAATI 171
Cdd:cd00887    81 LGPGEAVRIMTGAPLPE--GAdAVVMVEDTEEEGG------RVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 172 AALVSTGNATVPVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA-LEAA 242
Cdd:cd00887   153 GLLASLGIAEVPVYRRPRVAIISTGDELvepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREAlEEAL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 243 KGSNLILTTGGISAGAFDIVRELLS---PDVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPLMRALS 319
Cdd:cd00887   233 EEADVVITSGGVSVGDYDFVKEVLEelgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQ 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 320 GQVPqglDERPQLMASAACEFHADSKRDRFIPVRIKYGTTPQAISSHRSGlGSHFVASLAGVTGLAYLPHGTGTTAIGQP 399
Cdd:cd00887   313 GAPE---PEPPRVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQ-GSGLLSSLARADGLIVIPEGVEGLEAGEE 388

                  ....*
gi 2531271090 400 VRVLL 404
Cdd:cd00887   389 VEVLL 393
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
1-404 2.34e-67

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


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 225.09  E-value: 2.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090   1 MTESELLVLRSLSEHLDAVLS-LATAPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPG---PW 76
Cdd:PRK14498    1 MKRKIFLTLVSLEEAREILESlLSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASeanPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  77 TFPVIGDIPAGTDVRTP-RRGAALRIMTGAPVPEEPGlAVVPVEHTnIPRGPqslpSSVTIFTAPKPSAHIRMRGEDTAI 155
Cdd:PRK14498   81 RLKLGGEVHAGEAPDVEvEPGEAVEIATGAPIPRGAD-AVVMVEDT-EEVDD----DTVEIYRPVAPGENVRPAGEDIVA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 156 GELTVAQGTRIDAATIAALVSTGNATVPVHQPIRVSILATGDELDR--------QIPNSNSPMLAALCQSQGAQTHVLPA 227
Cdd:PRK14498  155 GELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEpgeplkpgKIYDVNSYTLAAAVEEAGGEPVRYGI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 228 TGDTPAA-LRAALEAAKGSNLILTTGGISAGAFDIVRELLSP--DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAF 304
Cdd:PRK14498  235 VPDDEEElEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEElgEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSAL 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 305 VSFHLFVAPLMRALSGQVPqglDERPQLMASAACEFHADSKRDRFIPVRI-----KYGTTPQAISShrsglGShfVASLA 379
Cdd:PRK14498  315 TIFEEFVAPLLRKLAGLPP---PERATVKARLARRVRSELGREEFVPVSLgrvgdGYVAYPLSRGS-----GA--ITSLV 384
                         410       420
                  ....*....|....*....|....*
gi 2531271090 380 GVTGLAYLPHGTGTTAIGQPVRVLL 404
Cdd:PRK14498  385 RADGFIEIPANTEGLEAGEEVEVEL 409
MoeA_N pfam03453
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ...
35-178 3.88e-33

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: 121.13  E-value: 3.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  35 SDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPGPWTFPVIGDIPAgtdvRTPRRGAALRIMTGAPVPEepGL- 113
Cdd:pfam03453  14 LDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIAAGEPPG----PLLPGGEAVRIMTGAPLPE--GAd 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2531271090 114 AVVPVEHTNIPRGPQslpssVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRIDAATIAALVSTG 178
Cdd:pfam03453  88 AVVMVEDTEEGGGRT-----VEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
188-313 2.51e-25

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: 100.47  E-value: 2.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 188 IRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA-LEAAKGSNLILTTGGISAGA 258
Cdd:TIGR00177   1 PRVAVISVGDELveggqplePGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREIlRKAVDEADVVLTTGGTGVGP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2531271090 259 FDIVRELLSP--DVWF-----------GQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAP 313
Cdd:TIGR00177  81 RDVTPEALEElgEKEIpgfgefrmlssLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
192-310 6.62e-21

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: 88.03  E-value: 6.62e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  192 ILATGDEL--DRQIPNSNSPMLAALCQSQGAQT--HVLPATGDTPAA-LRAALEAAKGSNLILTTGGISAGAFDIVRELL 266
Cdd:smart00852   2 IISTGDELlsGGQIRDSNGPMLAALLRELGIEVvrVVVVGGPDDPEAiREALREALAEADVVITTGGTGPGPDDLTPEAL 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2531271090  267 SP----DVWFGQVALQPGKPQG---------AGTFDGIPILCLPGNPVSAFVSFHLF 310
Cdd:smart00852  82 AElggrELLGHGVAMRPGGPPGplanlsgtaPGVRGKKPVFGLPGNPVAALVMFEEL 138
 
Name Accession Description Interval E-value
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
9-404 2.09e-120

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: 355.17  E-value: 2.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090   9 LRSLSEHLDAVLSLATaPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPGPWTFPVIGDIPAGT 88
Cdd:COG0303     1 MISVEEALALILAAVR-PLGTETVPLAEALGRVLAEDVVAPRDVPPFDNSAMDGYAVRAADLAGANPVTLRVVGEIAAGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  89 DVRTP-RRGAALRIMTGAPVPEepGL-AVVPVEHTNIPRGpqslpsSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRI 166
Cdd:COG0303    80 PPPGPlGPGEAVRIMTGAPLPE--GAdAVVMQEDTEREGD------RVTIRKPVAPGENIRRAGEDIAAGDVLLPAGTRL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 167 DAATIAALVSTGNATVPVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA 238
Cdd:COG0303   152 TPADLGLLASLGIAEVPVYRRPRVAILSTGDELvepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 239 -LEAAKGSNLILTTGGISAGAFDIVRELLSP---DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPL 314
Cdd:COG0303   232 lREALAEADLVITSGGVSVGDYDLVKEALEElgaEVLFHKVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 315 MRALSGQVPQgldERPQLMASAACEFHADSKRDRFIPVRIKYGTTPQAISSHRSGlGSHFVASLAGVTGLAYLPHGTGTT 394
Cdd:COG0303   312 LRKLAGLPPP---PPPRVRARLAEDLPKKPGRTEFLRVRLERDDGELVVEPLGGQ-GSGLLSSLAEADGLIVLPEGVEGV 387
                         410
                  ....*....|
gi 2531271090 395 AIGQPVRVLL 404
Cdd:COG0303   388 EAGEEVEVLL 397
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
14-404 1.26e-115

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: 342.55  E-value: 1.26e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  14 EHLDAVLSLATAPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGpGPWTFPVIGDIPAGTD-VRT 92
Cdd:cd00887     2 EAARELLLALAPPLGTETVPLLEALGRVLAEDVVAPIDLPPFDNSAMDGYAVRAADTAG-ASVTLRVVGEIPAGEPpDGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  93 PRRGAALRIMTGAPVPEepGL-AVVPVEHTNIPRGpqslpsSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRIDAATI 171
Cdd:cd00887    81 LGPGEAVRIMTGAPLPE--GAdAVVMVEDTEEEGG------RVTITKPVKPGQNIRRAGEDIKAGDVLLPAGTRLTPADI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 172 AALVSTGNATVPVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA-LEAA 242
Cdd:cd00887   153 GLLASLGIAEVPVYRRPRVAIISTGDELvepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREAlEEAL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 243 KGSNLILTTGGISAGAFDIVRELLS---PDVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPLMRALS 319
Cdd:cd00887   233 EEADVVITSGGVSVGDYDFVKEVLEelgGEVLFHGVAMKPGKPLAFGRLGGKPVFGLPGNPVSALVTFELFVRPALRKLQ 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 320 GQVPqglDERPQLMASAACEFHADSKRDRFIPVRIKYGTTPQAISSHRSGlGSHFVASLAGVTGLAYLPHGTGTTAIGQP 399
Cdd:cd00887   313 GAPE---PEPPRVKARLAEDLKSKPGRREFLRVRLERDEGGLVVAPPGGQ-GSGLLSSLARADGLIVIPEGVEGLEAGEE 388

                  ....*
gi 2531271090 400 VRVLL 404
Cdd:cd00887   389 VEVLL 393
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
1-404 2.34e-67

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


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 225.09  E-value: 2.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090   1 MTESELLVLRSLSEHLDAVLS-LATAPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPG---PW 76
Cdd:PRK14498    1 MKRKIFLTLVSLEEAREILESlLSELPLGTEEVPLEEALGRVLAEDVYAPIDVPPFDRSAMDGYAVRAADTFGASeanPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  77 TFPVIGDIPAGTDVRTP-RRGAALRIMTGAPVPEEPGlAVVPVEHTnIPRGPqslpSSVTIFTAPKPSAHIRMRGEDTAI 155
Cdd:PRK14498   81 RLKLGGEVHAGEAPDVEvEPGEAVEIATGAPIPRGAD-AVVMVEDT-EEVDD----DTVEIYRPVAPGENVRPAGEDIVA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 156 GELTVAQGTRIDAATIAALVSTGNATVPVHQPIRVSILATGDELDR--------QIPNSNSPMLAALCQSQGAQTHVLPA 227
Cdd:PRK14498  155 GELILPKGTRLTPRDIGALAAGGVAEVPVYKKPRVGIISTGDELVEpgeplkpgKIYDVNSYTLAAAVEEAGGEPVRYGI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 228 TGDTPAA-LRAALEAAKGSNLILTTGGISAGAFDIVRELLSP--DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAF 304
Cdd:PRK14498  235 VPDDEEElEAALRKALKECDLVLLSGGTSAGAGDVTYRVIEElgEVLVHGVAIKPGKPTILGVIGGKPVVGLPGYPVSAL 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 305 VSFHLFVAPLMRALSGQVPqglDERPQLMASAACEFHADSKRDRFIPVRI-----KYGTTPQAISShrsglGShfVASLA 379
Cdd:PRK14498  315 TIFEEFVAPLLRKLAGLPP---PERATVKARLARRVRSELGREEFVPVSLgrvgdGYVAYPLSRGS-----GA--ITSLV 384
                         410       420
                  ....*....|....*....|....*
gi 2531271090 380 GVTGLAYLPHGTGTTAIGQPVRVLL 404
Cdd:PRK14498  385 RADGFIEIPANTEGLEAGEEVEVEL 409
PRK14491 PRK14491
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ...
11-403 5.22e-48

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


Pssm-ID: 237729 [Multi-domain]  Cd Length: 597  Bit Score: 172.49  E-value: 5.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  11 SLSEHLDAVLSLATAPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADfngPGPWTFPVIGDIPAGTDV 90
Cdd:PRK14491  200 SVSQGLDKILSLVTPVTETEDVALDELDGRVLAQDVISPVNVPQHTNSAMDGYAFRSDD---LEPESYTLVGEVLAGHQY 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  91 RTP-RRGAALRIMTGAPVPEEpGLAVVPVEHTNIPRGpqslpsSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRIDAA 169
Cdd:PRK14491  277 DGTlQAGEAVRIMTGAPVPAG-ADTVVMRELATQDGD------KVSFDGGIKAGQNVRLAGEDLAQGQVALAAGTRLSAP 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 170 TIAALVSTGNATVPVHQPIRVSILATGDEL----DRQIPN----SNSPMLAALCQSQGAQTHVLPATGDTPAALRAA-LE 240
Cdd:PRK14491  350 EQGLLASLGFAEVPVFRRPKVAVFSTGDEVqapgETLKPNciydSNRFTIKAMAKKLGCEVIDLGIIEDSEAALEATlEQ 429
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 241 AAKGSNLILTTGGISAGAFDIVRELLSP--DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPLMRAL 318
Cdd:PRK14491  430 AAAQADVVISSGGVSVGDADYIKTALAKlgQIDFWRINMRPGRPLAFGQIGDSPFFGLPGNPVAVMVSFLQFVEPALRKL 509
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 319 SGQVPQgldERPQLMASAACEFHADSKRDRFIPVRIKYGTTPQAISSHRSGLGSHFVASLAGVTGLAYLPHGTGTTAIGQ 398
Cdd:PRK14491  510 AGEQNW---QPLLFPAIADETLRSRQGRTEFSRGIYHLGADGRLHVRTTGKQGSGILSSMSEANCLIEIGPAAETVNAGE 586

                  ....*
gi 2531271090 399 PVRVL 403
Cdd:PRK14491  587 TVTIQ 591
PRK10680 PRK10680
molybdopterin biosynthesis protein MoeA; Provisional
9-329 5.79e-45

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 182643 [Multi-domain]  Cd Length: 411  Bit Score: 160.26  E-value: 5.79e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090   9 LRSLSEHLDAVLSLATAPTPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPGPwtFPVIGDIPAGT 88
Cdd:PRK10680    7 LMSLETALTEMLSRVTPLTATETLPLVQCFGRITASDIVSPLDVPGFDNSAMDGYAVRLADLASGQP--LPVAGKAFAGQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  89 --DVRTPrRGAALRIMTGAPVPEEPGlAVVPVEHTniprgpqSLPSSVTIFTAP-KPSAHIRMRGEDTAIGELTVAQGTR 165
Cdd:PRK10680   85 pfHGEWP-AGTCIRIMTGAPVPEGCE-AVVMQEQT-------EQTDDGVRFTAEvRSGQNIRRRGEDISQGAVVFPAGTR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 166 IDAATIAALVSTGNATVPVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRA 237
Cdd:PRK10680  156 LTTAELPVLASLGIAEVPVVRKVRVALFSTGDELqlpgqplgDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 238 A-LEAAKGSNLILTTGGISAGAFDIVRELLSP--DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPL 314
Cdd:PRK10680  236 AfIEADSQADVVISSGGVSVGEADYTKTILEElgEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSAALTFYQLVQPL 315
                         330
                  ....*....|....*
gi 2531271090 315 MRALSGQVPQGLDER 329
Cdd:PRK10680  316 LAKLSGNTASGLPPR 330
PRK14690 PRK14690
molybdopterin biosynthesis protein MoeA; Provisional
27-403 1.64e-41

molybdopterin biosynthesis protein MoeA; Provisional


Pssm-ID: 237789 [Multi-domain]  Cd Length: 419  Bit Score: 151.22  E-value: 1.64e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  27 TPVTTMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHAdfNGPGPWTFPVI-GDIPAGT--DVRTPRrGAALRIMT 103
Cdd:PRK14690   40 TDIKELDLSDALGHVLAHDAVALRSNPPQANSAVDGYGFAGA--APEGAQVLPLIeGRAAAGVpfSGRVPE-GMALRILT 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 104 GAPVPEepGLAVVPVEHtNIPRGPQSLPssvtiFTAP-KPSAHIRMRGEDTAIGELTVAQGTRIDAATIAALVSTGNATV 182
Cdd:PRK14690  117 GAALPE--GVDTVVLEE-DVAGDGHRIA-----FHGPlKMGANTRKAGEDVIAGDVALPAGRRLTPADLALLSAVGLTRV 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 183 PVHQPIRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAALEAAKG-SNLILTTGG 253
Cdd:PRK14690  189 SVRRPLRVAVLSTGDELvepgalaeVGQIYDANRPMLLALARRWGHAPVDLGRVGDDRAALAARLDRAAAeADVILTSGG 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 254 ISAGAFDIVRELLSP----DVWfgQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPLMRALSGQ---VPQGL 326
Cdd:PRK14690  269 ASAGDEDHVSALLREagamQSW--RIALKPGRPLALGLWQGVPVFGLPGNPVAALVCTLVFARPAMSLLAGEgwsEPQGF 346
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2531271090 327 DerpqlmASAACEFHADSKRDRFIPVRIKYGTTPQAISShrsglGSHFVASLAGVTGLAYLPHGTGTTAIGQPVRVL 403
Cdd:PRK14690  347 T------VPAAFEKRKKPGRREYLRARLRQGHAEVFRSE-----GSGRISGLSWAEGLVELGDGARRIAPGDPVRFI 412
PLN02699 PLN02699
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase
11-322 9.60e-40

Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase


Pssm-ID: 215376 [Multi-domain]  Cd Length: 659  Bit Score: 150.35  E-value: 9.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  11 SLSEHLDAVLSLATAPTPVTtMAPSDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADfngpGPWTFPVIGDIPAGTD- 89
Cdd:PLN02699    9 SVEEALSIVLSVAARLSPVI-VPLHEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASD----GPGEYPVITESRAGNDg 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  90 ---VRTPrrGAALRIMTGAPVPEEPGlAVVPVEHTNIPRGPQSLPSSVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRI 166
Cdd:PLN02699   84 lgvTLTP--GTVAYVTTGGPIPDGAD-AVVQVEDTEVVEDPLDGSKRVRILSQASKGQDIRPVGCDIEKDAKVLKAGERL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 167 DAATIAALVSTGNATVPVHQPIRVSILATGDELDR---------QIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRA 237
Cdd:PLN02699  161 GASEIGLLATVGVTMVKVYPRPTVAILSTGDELVEpttgtlgrgQIRDSNRAMLLAAAIQQQCKVVDLGIARDDEEELER 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 238 A--LEAAKGSNLILTTGGISAGAFDIVRELLSP--DVWFGQVALQPGKPQGAGTFDGIP---------ILCLPGNPVSAF 304
Cdd:PLN02699  241 IldEAISSGVDILLTSGGVSMGDRDFVKPLLEKrgTVYFSKVLMKPGKPLTFAEIDAKSapsnskkmlAFGLPGNPVSCL 320
                         330
                  ....*....|....*...
gi 2531271090 305 VSFHLFVAPLMRALSGQV 322
Cdd:PLN02699  321 VCFNLFVVPAIRYLAGWS 338
MoeA_N pfam03453
MoeA N-terminal region (domain I and II); This family contains two structural domains. One of ...
35-178 3.88e-33

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: 121.13  E-value: 3.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  35 SDALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADFNGPGPWTFPVIGDIPAgtdvRTPRRGAALRIMTGAPVPEepGL- 113
Cdd:pfam03453  14 LDALGRVLAEDVVAPRDVPPFDRSAMDGYAVRAADGFGASEVNPIAAGEPPG----PLLPGGEAVRIMTGAPLPE--GAd 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2531271090 114 AVVPVEHTNIPRGPQslpssVTIFTAPKPSAHIRMRGEDTAIGELTVAQGTRIDAATIAALVSTG 178
Cdd:pfam03453  88 AVVMVEDTEEGGGRT-----VEIRAPVAPGENVRRAGEDIKAGEVVLPAGTRLTPAEIGLLASLG 147
PRK14497 PRK14497
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
36-354 2.20e-31

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


Pssm-ID: 172968 [Multi-domain]  Cd Length: 546  Bit Score: 125.31  E-value: 2.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  36 DALGLTLAANIYAKLAVPPFHNSAMDGFLVHHADfngpGPWTFPVIGDIPAG--TDVRTpRRGAALRIMTGAPVPEEpGL 113
Cdd:PRK14497   37 DSFGYVSAEDLMSPIDYPPFSRSTVDGYALKSSC----TPGEFKVIDKIGIGefKEIHI-KECEAVEVDTGSMIPMG-AD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 114 AVVPVEHTNIPRGPQSLPSSVTIFtapkpSAHIRMRGEDTAIGELTVAQGTRIDAATIAALVSTGNATVPVHQPIRVSIL 193
Cdd:PRK14497  111 AVIKVENTKVINGNFIKIDKKINF-----GQNIGWIGSDIPKGSIILRKGEVISHEKIGLLASLGISSVKVYEKPKIYLI 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 194 ATGDELDR--------QIPNSNSPMLAALCQSQGAQ----THVlpaTGDTPAALRAALEAAKGSNLILTTGGISAGAFDI 261
Cdd:PRK14497  186 ATGDELVEpgnslspgKIYESNLHYLYSKLKSEGYKivglSLL---SDDKESIKNEIKRAISVADVLILTGGTSAGEKDF 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 262 VRELLSPdvwFGQVALQ-----PGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPLMRALSGQVPQGLDErPQLMASA 336
Cdd:PRK14497  263 VHQAIRE---LGNIIVHglkikPGKPTILGIVDGKPVIGLPGNIVSTMVVLNMVILEYLKSLYPSRKEILGL-GKIKARL 338
                         330
                  ....*....|....*...
gi 2531271090 337 ACEFHADSKRDRFIPVRI 354
Cdd:PRK14497  339 ALRVKADEHRNTLIPVYL 356
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
188-313 2.51e-25

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: 100.47  E-value: 2.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 188 IRVSILATGDEL--------DRQIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA-LEAAKGSNLILTTGGISAGA 258
Cdd:TIGR00177   1 PRVAVISVGDELveggqplePGQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREIlRKAVDEADVVLTTGGTGVGP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2531271090 259 FDIVRELLSP--DVWF-----------GQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAP 313
Cdd:TIGR00177  81 RDVTPEALEElgEKEIpgfgefrmlssLPVLSRPGKPATAGVRGGTLIFNLPGNPVSALVTFEVLILP 148
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
192-317 9.68e-24

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: 95.78  E-value: 9.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 192 ILATGDELDR-QIPNSNSPMLAALCQSQGAQTHVLPATGDTPAALRAA-LEAAKGSNLILTTGGISAGAFDIVRELLSP- 268
Cdd:pfam00994   2 IITTGDELLPgQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEAlRAAAEEADVVITTGGTGPGPDDVTPEALAEl 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2531271090 269 --------DVWFGQVALQPGKPQGAGTF-----DGIPILCLPGNPVSAFVSFHLFVAPLMRA 317
Cdd:pfam00994  82 ggrelpgfEELFRGVSLKPGKPVGTAPGailsrAGKTVFGLPGSPVAAKVMFELLLLPLLRH 143
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
192-310 6.62e-21

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: 88.03  E-value: 6.62e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090  192 ILATGDEL--DRQIPNSNSPMLAALCQSQGAQT--HVLPATGDTPAA-LRAALEAAKGSNLILTTGGISAGAFDIVRELL 266
Cdd:smart00852   2 IISTGDELlsGGQIRDSNGPMLAALLRELGIEVvrVVVVGGPDDPEAiREALREALAEADVVITTGGTGPGPDDLTPEAL 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2531271090  267 SP----DVWFGQVALQPGKPQG---------AGTFDGIPILCLPGNPVSAFVSFHLF 310
Cdd:smart00852  82 AElggrELLGHGVAMRPGGPPGplanlsgtaPGVRGKKPVFGLPGNPVAALVMFEEL 138
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
189-314 6.33e-19

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: 82.39  E-value: 6.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531271090 189 RVSILATGDELDR-QIPNSNSPMLAALCQSQGAQTHVLPATGDTPAA-LRAALEAAKGSNLILTTGGISAGAFDIVRELL 266
Cdd:cd00758     1 RVAIVTVSDELSQgQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSiRAALIEASREADLVLTTGGTGVGRRDVTPEAL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2531271090 267 SP----DVWFGQVALQPGKPQGAGTFDGIPILCLPGNPVSAFVSFHLFVAPL 314
Cdd:cd00758    81 AElgerEAHGKGVALAPGSRTAFGIIGKVLIINLPGSPKSALTTFEALVLPA 132
 
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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