|
Name |
Accession |
Description |
Interval |
E-value |
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
10-264 |
9.95e-89 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 263.51 E-value: 9.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALGVPL 89
Cdd:COG1058 9 DELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAVAEALGVPL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 90 ALHPEAKELISERIREthtdpatpvdFESPENQHRFNMGVFPAGATIIPNGYNRIPGFSVGD----LHFVPGFPVMAWPM 165
Cdd:COG1058 89 VLDPEALALIEERFAK----------RGREMTENNLKQALLPEGAELLPNPVGTAPGFSIENngkvVIFLPGVPSEMKPM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 166 IEWVLDTKYAHLHHATPHAERSLYVFELPESTLTPLMEKIERDFPGVRVFSLPSVGdaerggiyaRRHIDLGVKGE-PEA 244
Cdd:COG1058 159 FEEEVLPRLKKLFSGEPIVSRTLRTFGIGESDLAELLEDLEARFPNVTIGSYPSDG---------EVRLRLTARGTdEEE 229
|
250 260
....*....|....*....|
gi 493528495 245 VAAAFVKLREGVHLLGGDVV 264
Cdd:COG1058 230 AEAALEALEEELRERLGDYI 249
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
10-175 |
1.53e-55 |
|
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: 176.52 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALGVPL 89
Cdd:cd00885 9 DELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAVAKAFGRPL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 90 ALHPEAKELISERIRETHTdpatpvdfESPENQHRfnMGVFPAGATIIPNGYNRIPGFSVG----DLHFVPGFPVMAWPM 165
Cdd:cd00885 89 VLDEEALERIEARFARRGR--------EMTEANLK--QAMLPEGATLLPNPVGTAPGFSVEhngkNVFLLPGVPSEMKPM 158
|
170
....*....|
gi 493528495 166 IEWVLDTKYA 175
Cdd:cd00885 159 LEEEVLPRLR 168
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
11-265 |
2.81e-26 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 103.55 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 11 EILSGRRQD---KHLAKVIELLG---ARGLAldwaeyVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAA 84
Cdd:PRK01215 14 ELLIGRTVNtnaSWIARRLTYLGytvRRITV------VMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGFAKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 85 LGVPLALHPEAKELISERIrETHTDPATPvdfespenqHRFNMGVFPAGATIIPNGYNRIPGF--SVGDLHFV--PGFPV 160
Cdd:PRK01215 88 LGVELELNEDALRMILEKY-EKRGIPLTP---------ERKKMAMMPPGAVPLENPVGTAPGIliEHGGKDIValPGVPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 161 MAWPMIEWVLDtKYAHLHHATPHAERSLYVFELPESTLTPLMEKIERDFPGVRVFSLPSVGDAERGG----IYARRHIDL 236
Cdd:PRK01215 158 EMEAIFENFVE-PLLKNRPPLKYYEDSILVEGVMESDLAPYVKELVKKYDRVYVKSHPKGYEVSKPIleiqIAGSGEREE 236
|
250 260
....*....|....*....|....*....
gi 493528495 237 GVKGEPEAVAAafvKLREGVHLLGGDVVE 265
Cdd:PRK01215 237 EAKVKVEKVLE---ELKELIKKLGGIIRE 262
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
10-169 |
2.56e-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 trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 94.96 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQDKHLAKVI-ELLGARGLALDWAEYVG--DDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALG 86
Cdd:smart00852 7 DELLSGGQIRDSNGPMLaALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEALAELGG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 87 VPLALHPEAkeliserirethtdpatpvdfespenqhrfnmgVFPAGA-TIIPNGYNRIPGFSVGDLHFV-PGFPVMAWP 164
Cdd:smart00852 87 RELLGHGVA---------------------------------MRPGGPpGPLANLSGTAPGVRGKKPVFGlPGNPVAALV 133
|
....*
gi 493528495 165 MIEWV 169
Cdd:smart00852 134 MFEEL 138
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
10-170 |
3.76e-23 |
|
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: 91.93 E-value: 3.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALGVPL 89
Cdd:pfam00994 7 DELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAELGGREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 90 ALHPEAKELISERirethtdPATPVDFespenqhrfnmgvfpaGATIIPNGYNRIpgfsvgdLHFVPGFPVMAWPMIEWV 169
Cdd:pfam00994 87 PGFEELFRGVSLK-------PGKPVGT----------------APGAILSRAGKT-------VFGLPGSPVAAKVMFELL 136
|
.
gi 493528495 170 L 170
Cdd:pfam00994 137 L 137
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
10-167 |
8.16e-12 |
|
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 161761 [Multi-domain] Cd Length: 413 Bit Score: 64.54 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALGVPL 89
Cdd:TIGR00200 10 DELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSDDLTAETIATAKGEPL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 90 ALHPEAKELISERIRETHTDPAtpvdfesPENQHRfnmGVFPAGATIIPNGYNRIPGFSVGDLH-----FVPGFPVMAWP 164
Cdd:TIGR00200 90 VLNEAWLKEIERYFHETGRVMA-------PNNRKQ---ALLPAGAEFLANPVGTAPGMFAVQLNrclmlFTPGVPSEFRV 159
|
...
gi 493528495 165 MIE 167
Cdd:TIGR00200 160 MVE 162
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
10-264 |
9.95e-89 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 263.51 E-value: 9.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALGVPL 89
Cdd:COG1058 9 DELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAVAEALGVPL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 90 ALHPEAKELISERIREthtdpatpvdFESPENQHRFNMGVFPAGATIIPNGYNRIPGFSVGD----LHFVPGFPVMAWPM 165
Cdd:COG1058 89 VLDPEALALIEERFAK----------RGREMTENNLKQALLPEGAELLPNPVGTAPGFSIENngkvVIFLPGVPSEMKPM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 166 IEWVLDTKYAHLHHATPHAERSLYVFELPESTLTPLMEKIERDFPGVRVFSLPSVGdaerggiyaRRHIDLGVKGE-PEA 244
Cdd:COG1058 159 FEEEVLPRLKKLFSGEPIVSRTLRTFGIGESDLAELLEDLEARFPNVTIGSYPSDG---------EVRLRLTARGTdEEE 229
|
250 260
....*....|....*....|
gi 493528495 245 VAAAFVKLREGVHLLGGDVV 264
Cdd:COG1058 230 AEAALEALEEELRERLGDYI 249
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
10-175 |
1.53e-55 |
|
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: 176.52 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALGVPL 89
Cdd:cd00885 9 DELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAVAKAFGRPL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 90 ALHPEAKELISERIRETHTdpatpvdfESPENQHRfnMGVFPAGATIIPNGYNRIPGFSVG----DLHFVPGFPVMAWPM 165
Cdd:cd00885 89 VLDEEALERIEARFARRGR--------EMTEANLK--QAMLPEGATLLPNPVGTAPGFSVEhngkNVFLLPGVPSEMKPM 158
|
170
....*....|
gi 493528495 166 IEWVLDTKYA 175
Cdd:cd00885 159 LEEEVLPRLR 168
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
11-265 |
2.81e-26 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 103.55 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 11 EILSGRRQD---KHLAKVIELLG---ARGLAldwaeyVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAA 84
Cdd:PRK01215 14 ELLIGRTVNtnaSWIARRLTYLGytvRRITV------VMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGFAKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 85 LGVPLALHPEAKELISERIrETHTDPATPvdfespenqHRFNMGVFPAGATIIPNGYNRIPGF--SVGDLHFV--PGFPV 160
Cdd:PRK01215 88 LGVELELNEDALRMILEKY-EKRGIPLTP---------ERKKMAMMPPGAVPLENPVGTAPGIliEHGGKDIValPGVPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 161 MAWPMIEWVLDtKYAHLHHATPHAERSLYVFELPESTLTPLMEKIERDFPGVRVFSLPSVGDAERGG----IYARRHIDL 236
Cdd:PRK01215 158 EMEAIFENFVE-PLLKNRPPLKYYEDSILVEGVMESDLAPYVKELVKKYDRVYVKSHPKGYEVSKPIleiqIAGSGEREE 236
|
250 260
....*....|....*....|....*....
gi 493528495 237 GVKGEPEAVAAafvKLREGVHLLGGDVVE 265
Cdd:PRK01215 237 EAKVKVEKVLE---ELKELIKKLGGIIRE 262
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
10-169 |
2.56e-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 trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 94.96 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQDKHLAKVI-ELLGARGLALDWAEYVG--DDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALG 86
Cdd:smart00852 7 DELLSGGQIRDSNGPMLaALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEALAELGG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 87 VPLALHPEAkeliserirethtdpatpvdfespenqhrfnmgVFPAGA-TIIPNGYNRIPGFSVGDLHFV-PGFPVMAWP 164
Cdd:smart00852 87 RELLGHGVA---------------------------------MRPGGPpGPLANLSGTAPGVRGKKPVFGlPGNPVAALV 133
|
....*
gi 493528495 165 MIEWV 169
Cdd:smart00852 134 MFEEL 138
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
10-170 |
3.76e-23 |
|
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: 91.93 E-value: 3.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALGVPL 89
Cdd:pfam00994 7 DELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAELGGREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 90 ALHPEAKELISERirethtdPATPVDFespenqhrfnmgvfpaGATIIPNGYNRIpgfsvgdLHFVPGFPVMAWPMIEWV 169
Cdd:pfam00994 87 PGFEELFRGVSLK-------PGKPVGT----------------APGAILSRAGKT-------VFGLPGSPVAAKVMFELL 136
|
.
gi 493528495 170 L 170
Cdd:pfam00994 137 L 137
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
42-139 |
3.02e-15 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 74.83 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 42 VGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALGVPLALHPEAKELISERIREThtdpatpvDFESPEN 121
Cdd:PRK00549 42 VGDNPERLLSALEIAEERSDLIITTGGLGPTKDDLTKETVAKFLGRELVLDEEALAKIEDYFAKR--------GREMTEN 113
|
90
....*....|....*...
gi 493528495 122 QHRfnMGVFPAGATIIPN 139
Cdd:PRK00549 114 NRK--QALIPEGATVLPN 129
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
10-167 |
8.16e-12 |
|
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 161761 [Multi-domain] Cd Length: 413 Bit Score: 64.54 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALGVPL 89
Cdd:TIGR00200 10 DELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSDDLTAETIATAKGEPL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 90 ALHPEAKELISERIRETHTDPAtpvdfesPENQHRfnmGVFPAGATIIPNGYNRIPGFSVGDLH-----FVPGFPVMAWP 164
Cdd:TIGR00200 90 VLNEAWLKEIERYFHETGRVMA-------PNNRKQ---ALLPAGAEFLANPVGTAPGMFAVQLNrclmlFTPGVPSEFRV 159
|
...
gi 493528495 165 MIE 167
Cdd:TIGR00200 160 MVE 162
|
|
| PRK03670 |
PRK03670 |
competence damage-inducible protein A; Provisional |
10-218 |
4.30e-09 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 167581 Cd Length: 252 Bit Score: 55.58 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIA-SGDIVFSTGGIGATPDDHTRQCAAAALGVP 88
Cdd:PRK03670 10 DELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSrKPEVLVISGGLGPTHDDVTMLAVAEALGRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 89 LALhpeaKELISERIRETHTDPATPVDFESPE-NQHRFNMGVFPAGATIIPNGYNRIPGFSV---GDLHFV-PGFPVMAW 163
Cdd:PRK03670 90 LVL----CEDCLERIKEFYEELYKKGLIDDPTlNEARKKMAYLPEGAEPLENTEGAAPGAYIehkGTKIFVlPGMPREMK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493528495 164 PMIEwvldtkyahlHHATPH-AERSL----YVFELP-ESTLTPLMEKIERDFpGVRVFSLP 218
Cdd:PRK03670 166 AMLE----------KEVLPRlGERKFvqkkFLAEITdESKLAPILEEALERF-NVKIHSSP 215
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
14-77 |
1.27e-07 |
|
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440287 [Multi-domain] Cd Length: 169 Bit Score: 50.12 E-value: 1.27e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493528495 14 SGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASG--DIVFSTGGIGATPDDHT 77
Cdd:COG0521 23 RGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEgvDLVLTTGGTGLSPRDVT 88
|
|
| PRK03673 |
PRK03673 |
nicotinamide mononucleotide deamidase-related protein YfaY; |
10-159 |
3.20e-07 |
|
nicotinamide mononucleotide deamidase-related protein YfaY;
Pssm-ID: 179629 [Multi-domain] Cd Length: 396 Bit Score: 50.85 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALGVPL 89
Cdd:PRK03673 11 DEVLHGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGGLGPTSDDLSALAAATAAGEGL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493528495 90 ALHPE----AKELISERIREThtdpatpvdfeSPENQHRFNMgvfPAGATIIPNGYNRIPGFSVG----DLHFVPGFP 159
Cdd:PRK03673 91 VLHEEwlaeMERFFAERGRVM-----------APSNRKQAEL---PASAEMIDNPVGTACGFALQlnrcLMFFTPGVP 154
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
9-87 |
3.23e-07 |
|
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: 48.49 E-value: 3.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493528495 9 GDEILSGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQCAAAALGV 87
Cdd:cd00758 8 SDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALAELGER 86
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
42-92 |
3.72e-06 |
|
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: 47.39 E-value: 3.72e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 493528495 42 VGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQcAAAALGVPLALH 92
Cdd:COG0303 221 VPDDPEALRAALREALAEADLVITSGGVSVGDYDLVKE-ALEELGAEVLFH 270
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
14-77 |
8.22e-06 |
|
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.
Pssm-ID: 238451 [Multi-domain] Cd Length: 152 Bit Score: 44.78 E-value: 8.22e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493528495 14 SGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASG--DIVFSTGGIGATPDDHT 77
Cdd:cd00886 14 AGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDgvDLILTTGGTGLAPRDVT 79
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
10-86 |
1.79e-05 |
|
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: 43.84 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493528495 10 DEILSGRRQ-------DKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQcAA 82
Cdd:TIGR00177 10 DELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRDVTPE-AL 88
|
....
gi 493528495 83 AALG 86
Cdd:TIGR00177 89 EELG 92
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
42-92 |
5.16e-04 |
|
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: 40.94 E-value: 5.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 493528495 42 VGDDPARITATLARAIASGDIVFSTGGIGATPDDHTRQcAAAALGVPLALH 92
Cdd:cd00887 217 VPDDPEALREALEEALEEADVVITSGGVSVGDYDFVKE-VLEELGGEVLFH 266
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
11-84 |
2.96e-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: 38.30 E-value: 2.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493528495 11 EILSGRRQDKHLAKVIELLGARGLALDWAEYVGDDPARITATLARAIASG-DIVFSTGGIGATPDDHTRQCAAAA 84
Cdd:cd03522 170 EVYGGRIEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAAAIAEALEAGaELLILTGGASVDPDDVTPAAIRAA 244
|
|
| |
