|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
1-262 |
2.91e-129 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 377.21 E-value: 2.91e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 1 MSIAIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHT 80
Cdd:PRK00549 1 MKAEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLGPTKDDLTKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 81 VAQIVGKDLVIDEPSLKYIESYFEEQGQEMTPNNKQQALVIEGSTVLANHHGMAPGMMVNFENKQIILLPGPPKEMQPMV 160
Cdd:PRK00549 81 VAKFLGRELVLDEEALAKIEDYFAKRGREMTENNRKQALIPEGATVLPNPVGTAPGMIIEVDGKTYIVLPGPPSELKPMF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 161 KNEL---LSHFINHNRIIHSELLRFAGIGESKVETVLIDLIDKQTNPTIAPLAGSHEVYIRLTANADSKEQAQSLIQPVK 237
Cdd:PRK00549 161 EEYVvpyLSSAKGTGEVLYSRVLRFFGIGESQLATTLRDLIDNQTNPTIAPYAKDGEVTLRLTAKARSEEEAEKLIDPLE 240
|
250 260
....*....|....*....|....*
gi 616461727 238 QEILDRIGEYYYGSDDTLIEQAVIK 262
Cdd:PRK00549 241 EEIRDRVGDYFYGYDEDSLEEVVAK 265
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
3-248 |
1.75e-108 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 318.21 E-value: 1.75e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 3 IAIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHTVA 82
Cdd:COG1058 2 AEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 83 QIVGKDLVIDEPSLKYIESYFEEQGQEMTPNNKQQALVIEGSTVLANHHGMAPGMMVNFENKQIILLPGPPKEMQPMVKN 162
Cdd:COG1058 82 EALGVPLVLDPEALALIEERFAKRGREMTENNLKQALLPEGAELLPNPVGTAPGFSIENNGKVVIFLPGVPSEMKPMFEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 163 ELLSHF--INHNRIIHSELLRFAGIGESKVETVLIDLIDKQTNPTIAPLAGSHEVYIRLTANADSKEQAQSLIQPVKQEI 240
Cdd:COG1058 162 EVLPRLkkLFSGEPIVSRTLRTFGIGESDLAELLEDLEARFPNVTIGSYPSDGEVRLRLTARGTDEEEAEAALEALEEEL 241
|
....*...
gi 616461727 241 LDRIGEYY 248
Cdd:COG1058 242 RERLGDYI 249
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
1-256 |
9.66e-87 |
|
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: 268.70 E-value: 9.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 1 MSIAIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHT 80
Cdd:TIGR00200 1 LKAEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSDDLTAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 81 VAQIVGKDLVIDEPSLKYIESYFEEQGQEMTPNNKQQALVIEGSTVLANHHGMAPGMMVNFENKQIIL-LPGPPKEMQPM 159
Cdd:TIGR00200 81 IATAKGEPLVLNEAWLKEIERYFHETGRVMAPNNRKQALLPAGAEFLANPVGTAPGMFAVQLNRCLMLfTPGVPSEFRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 160 VKNELLSHFINH---NRIIHSELLRFAGIGESKVETVLIDLIDKQTNPTIAPLAGSHEVYIRLTANADSKEQAQSLIQPV 236
Cdd:TIGR00200 161 VEHEALPRLRERfslPQPIVSLVLRFFGIGESQLEADLADSLDTLTNPTGAPMAYRGEVPLRELKLTGPESEQQRAMEKL 240
|
250 260
....*....|....*....|
gi 616461727 237 KQEILDRIGEYYYGSDDTLI 256
Cdd:TIGR00200 241 WLDIKRVAGQSVIGEDTEGL 260
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
2-168 |
8.17e-79 |
|
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: 239.69 E-value: 8.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 2 SIAIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHTV 81
Cdd:cd00885 1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 82 AQIVGKDLVIDEPSLKYIESYFEEQGQEMTPNNKQQALVIEGSTVLANHHGMAPGMMVNFENKQIILLPGPPKEMQPMVK 161
Cdd:cd00885 81 AKAFGRPLVLDEEALERIEARFARRGREMTEANLKQAMLPEGATLLPNPVGTAPGFSVEHNGKNVFLLPGVPSEMKPMLE 160
|
....*..
gi 616461727 162 NELLSHF 168
Cdd:cd00885 161 EEVLPRL 167
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
4-165 |
5.87e-39 |
|
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: 136.22 E-value: 5.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 4 AIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHTVAQ 83
Cdd:pfam00994 1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 84 IVGKDLVIDEPSLKYIESYFeeqgqemtpnnkqqalviegstvlANHHGMAPGMMVNFENKQIILLPGPPKEMQPMVKNE 163
Cdd:pfam00994 81 LGGRELPGFEELFRGVSLKP------------------------GKPVGTAPGAILSRAGKTVFGLPGSPVAAKVMFELL 136
|
..
gi 616461727 164 LL 165
Cdd:pfam00994 137 LL 138
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
4-163 |
5.36e-29 |
|
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: 109.60 E-value: 5.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 4 AIIAVGSELLLG-QIANTNGQFLSKVFNEIGQNVLEHKVIG--DNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHT 80
Cdd:smart00852 1 AIISTGDELLSGgQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 81 VAQIVGKDLVIdepslkyiesyfeeQGQEMTPNNKQqalviegsTVLANHHGMAPGMMVnfeNKQIILLPGPPKEMQPMV 160
Cdd:smart00852 81 LAELGGRELLG--------------HGVAMRPGGPP--------GPLANLSGTAPGVRG---KKPVFGLPGNPVAALVMF 135
|
...
gi 616461727 161 KNE 163
Cdd:smart00852 136 EEL 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
1-262 |
2.91e-129 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 377.21 E-value: 2.91e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 1 MSIAIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHT 80
Cdd:PRK00549 1 MKAEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLGPTKDDLTKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 81 VAQIVGKDLVIDEPSLKYIESYFEEQGQEMTPNNKQQALVIEGSTVLANHHGMAPGMMVNFENKQIILLPGPPKEMQPMV 160
Cdd:PRK00549 81 VAKFLGRELVLDEEALAKIEDYFAKRGREMTENNRKQALIPEGATVLPNPVGTAPGMIIEVDGKTYIVLPGPPSELKPMF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 161 KNEL---LSHFINHNRIIHSELLRFAGIGESKVETVLIDLIDKQTNPTIAPLAGSHEVYIRLTANADSKEQAQSLIQPVK 237
Cdd:PRK00549 161 EEYVvpyLSSAKGTGEVLYSRVLRFFGIGESQLATTLRDLIDNQTNPTIAPYAKDGEVTLRLTAKARSEEEAEKLIDPLE 240
|
250 260
....*....|....*....|....*
gi 616461727 238 QEILDRIGEYYYGSDDTLIEQAVIK 262
Cdd:PRK00549 241 EEIRDRVGDYFYGYDEDSLEEVVAK 265
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
3-248 |
1.75e-108 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 318.21 E-value: 1.75e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 3 IAIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHTVA 82
Cdd:COG1058 2 AEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 83 QIVGKDLVIDEPSLKYIESYFEEQGQEMTPNNKQQALVIEGSTVLANHHGMAPGMMVNFENKQIILLPGPPKEMQPMVKN 162
Cdd:COG1058 82 EALGVPLVLDPEALALIEERFAKRGREMTENNLKQALLPEGAELLPNPVGTAPGFSIENNGKVVIFLPGVPSEMKPMFEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 163 ELLSHF--INHNRIIHSELLRFAGIGESKVETVLIDLIDKQTNPTIAPLAGSHEVYIRLTANADSKEQAQSLIQPVKQEI 240
Cdd:COG1058 162 EVLPRLkkLFSGEPIVSRTLRTFGIGESDLAELLEDLEARFPNVTIGSYPSDGEVRLRLTARGTDEEEAEAALEALEEEL 241
|
....*...
gi 616461727 241 LDRIGEYY 248
Cdd:COG1058 242 RERLGDYI 249
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
1-256 |
9.66e-87 |
|
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: 268.70 E-value: 9.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 1 MSIAIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHT 80
Cdd:TIGR00200 1 LKAEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSDDLTAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 81 VAQIVGKDLVIDEPSLKYIESYFEEQGQEMTPNNKQQALVIEGSTVLANHHGMAPGMMVNFENKQIIL-LPGPPKEMQPM 159
Cdd:TIGR00200 81 IATAKGEPLVLNEAWLKEIERYFHETGRVMAPNNRKQALLPAGAEFLANPVGTAPGMFAVQLNRCLMLfTPGVPSEFRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 160 VKNELLSHFINH---NRIIHSELLRFAGIGESKVETVLIDLIDKQTNPTIAPLAGSHEVYIRLTANADSKEQAQSLIQPV 236
Cdd:TIGR00200 161 VEHEALPRLRERfslPQPIVSLVLRFFGIGESQLEADLADSLDTLTNPTGAPMAYRGEVPLRELKLTGPESEQQRAMEKL 240
|
250 260
....*....|....*....|
gi 616461727 237 KQEILDRIGEYYYGSDDTLI 256
Cdd:TIGR00200 241 WLDIKRVAGQSVIGEDTEGL 260
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
2-168 |
8.17e-79 |
|
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: 239.69 E-value: 8.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 2 SIAIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHTV 81
Cdd:cd00885 1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 82 AQIVGKDLVIDEPSLKYIESYFEEQGQEMTPNNKQQALVIEGSTVLANHHGMAPGMMVNFENKQIILLPGPPKEMQPMVK 161
Cdd:cd00885 81 AKAFGRPLVLDEEALERIEARFARRGREMTEANLKQAMLPEGATLLPNPVGTAPGFSVEHNGKNVFLLPGVPSEMKPMLE 160
|
....*..
gi 616461727 162 NELLSHF 168
Cdd:cd00885 161 EEVLPRL 167
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
4-165 |
5.87e-39 |
|
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: 136.22 E-value: 5.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 4 AIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHTVAQ 83
Cdd:pfam00994 1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 84 IVGKDLVIDEPSLKYIESYFeeqgqemtpnnkqqalviegstvlANHHGMAPGMMVNFENKQIILLPGPPKEMQPMVKNE 163
Cdd:pfam00994 81 LGGRELPGFEELFRGVSLKP------------------------GKPVGTAPGAILSRAGKTVFGLPGSPVAAKVMFELL 136
|
..
gi 616461727 164 LL 165
Cdd:pfam00994 137 LL 138
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
5-244 |
1.81e-38 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 138.61 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 5 IIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHTVAQI 84
Cdd:PRK01215 8 IITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGFAKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 85 VGKDLVIDEPSLKYIESYFEEQGQEMTPNNKQQALVIEGSTVLANHHGMAPGMMVNFENKQIILLPGPPKEMQPMVKNEL 164
Cdd:PRK01215 88 LGVELELNEDALRMILEKYEKRGIPLTPERKKMAMMPPGAVPLENPVGTAPGILIEHGGKDIVALPGVPREMEAIFENFV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 165 LSHFINHNRIIHSE-LLRFAGIGESKVETVLIDLIDKQTNPTIAPLAGSHEV-----YIRLTANADSKEQAQSLIQPVKQ 238
Cdd:PRK01215 168 EPLLKNRPPLKYYEdSILVEGVMESDLAPYVKELVKKYDRVYVKSHPKGYEVskpilEIQIAGSGEREEEAKVKVEKVLE 247
|
....*.
gi 616461727 239 EILDRI 244
Cdd:PRK01215 248 ELKELI 253
|
|
| PRK03670 |
PRK03670 |
competence damage-inducible protein A; Provisional |
1-200 |
2.98e-33 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 167581 Cd Length: 252 Bit Score: 124.53 E-value: 2.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 1 MSIAIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALE-KYDTVILTGGLGPTKDDLTKH 79
Cdd:PRK03670 1 MFAEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSrKPEVLVISGGLGPTHDDVTML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 80 TVAQIVGKDLVIDEPSLKYIESYFEEQGQE-------MTPNNKQQALVIEGSTVLANHHGMAPGMMVNFENKQIILLPGP 152
Cdd:PRK03670 81 AVAEALGRELVLCEDCLERIKEFYEELYKKgliddptLNEARKKMAYLPEGAEPLENTEGAAPGAYIEHKGTKIFVLPGM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 616461727 153 PKEMQPMVKNELLSHfINHNRIIHSELLrfAGI-GESKVETVLIDLIDK 200
Cdd:PRK03670 161 PREMKAMLEKEVLPR-LGERKFVQKKFL--AEItDESKLAPILEEALER 206
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
4-163 |
5.36e-29 |
|
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: 109.60 E-value: 5.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 4 AIIAVGSELLLG-QIANTNGQFLSKVFNEIGQNVLEHKVIG--DNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHT 80
Cdd:smart00852 1 AIISTGDELLSGgQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 81 VAQIVGKDLVIdepslkyiesyfeeQGQEMTPNNKQqalviegsTVLANHHGMAPGMMVnfeNKQIILLPGPPKEMQPMV 160
Cdd:smart00852 81 LAELGGRELLG--------------HGVAMRPGGPP--------GPLANLSGTAPGVRG---KKPVFGLPGNPVAALVMF 135
|
...
gi 616461727 161 KNE 163
Cdd:smart00852 136 EEL 138
|
|
| CinA_KH |
pfam18146 |
Damage-inducible protein CinA KH domain; This domain is found in competence-induced protein A ... |
177-250 |
6.02e-27 |
|
Damage-inducible protein CinA KH domain; This domain is found in competence-induced protein A (CinA) present in Thermus thermophiles. CinA is important in the horizontal transfer of genes via competence and may also participate in the pyridine nucleotide cycle, which recycles products formed by non-redox uses of NAD. This domain has a KH-type fold and contains the absolutely conserved Glu-187, which stabilizes the binding of Mg2+ and hence polarizes the P=O bond for hydrolysis. A major feature of the CinA in T. thermophiles structure is the asymmetry in the dimer, which is caused by contact between a KH-type domain on the opposite chain and the bound ADP-ribose. This has the effect of closing the active site, allowing additional recognition of ADP-ribose by residues from the KH-type domain.
Pssm-ID: 436307 [Multi-domain] Cd Length: 73 Bit Score: 101.79 E-value: 6.02e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616461727 177 SELLRFAGIGESKVETVLIDLIDkQTNPTIAPLAGSHEVYIRLTANADSKEQAQSLIQPVKQEILDRIGEYYYG 250
Cdd:pfam18146 1 SRTLKTFGIGESQLEERLGDLID-RENPTIAPYAKDGEVTLRITAKAADEEEAEALIAPVEEEIRERLGDYIYG 73
|
|
| PRK03673 |
PRK03673 |
nicotinamide mononucleotide deamidase-related protein YfaY; |
5-165 |
7.40e-23 |
|
nicotinamide mononucleotide deamidase-related protein YfaY;
Pssm-ID: 179629 [Multi-domain] Cd Length: 396 Bit Score: 99.00 E-value: 7.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 5 IIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHTVAQI 84
Cdd:PRK03673 6 MLSTGDEVLHGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGGLGPTSDDLSALAAATA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 85 VGKDLVIDEPSLKYIESYFEEQGQEMTPNNKQQALVIEGSTVLANHHGMAPGMMVNFENKQIILLPGPPKEMQPMVKNEL 164
Cdd:PRK03673 86 AGEGLVLHEEWLAEMERFFAERGRVMAPSNRKQAELPASAEMIDNPVGTACGFALQLNRCLMFFTPGVPSEFKVMVEQEI 165
|
.
gi 616461727 165 L 165
Cdd:PRK03673 166 L 166
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
1-165 |
6.52e-22 |
|
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: 90.84 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 1 MSIAIIAVGSELLLG-------QIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTK 73
Cdd:TIGR00177 1 PRVAVISVGDELVEGgqplepgQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 74 DDLTKHTVAQIvgkdlvidepslkyIESYFEEQGQEMTpnnkqqalviEGSTVLANHHGMaPGMMVNFENKQIILLPGPP 153
Cdd:TIGR00177 81 RDVTPEALEEL--------------GEKEIPGFGEFRM----------LSSLPVLSRPGK-PATAGVRGGTLIFNLPGNP 135
|
170
....*....|..
gi 616461727 154 KEMQPMVKNELL 165
Cdd:TIGR00177 136 VSALVTFEVLIL 147
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
3-169 |
6.44e-18 |
|
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: 79.31 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 3 IAIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDDLTKHTVA 82
Cdd:cd00758 2 VAIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 83 QIVGKDLVIDepslkyiesyfeeqGQEMTPnnkqqalviegstvlanhhgMAPGMMVNFENKQIILLPGPPKEMQPMVkN 162
Cdd:cd00758 82 ELGEREAHGK--------------GVALAP--------------------GSRTAFGIIGKVLIINLPGSPKSALTTF-E 126
|
....*..
gi 616461727 163 ELLSHFI 169
Cdd:cd00758 127 ALVLPAL 133
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
3-87 |
2.87e-10 |
|
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: 61.36 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 3 IAIIAVGSELL-------LGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDD 75
Cdd:cd00887 171 VAIISTGDELVepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYD 250
|
90
....*....|..
gi 616461727 76 LTKHTVAQIVGK 87
Cdd:cd00887 251 FVKEVLEELGGE 262
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
3-84 |
2.92e-08 |
|
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: 55.10 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 3 IAIIAVGSELL-------LGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDD 75
Cdd:COG0303 175 VAILSTGDELVepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGVSVGDYD 254
|
....*....
gi 616461727 76 LTKHTVAQI 84
Cdd:COG0303 255 LVKEALEEL 263
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
1-77 |
9.62e-08 |
|
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: 50.94 E-value: 9.62e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616461727 1 MSIAIIAVGSELLLGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALE--KYDTVILTGGLGPTKDDLT 77
Cdd:cd00886 1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADedGVDLILTTGGTGLAPRDVT 79
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
3-68 |
2.26e-05 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 46.36 E-value: 2.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616461727 3 IAIIAVGSELL-------LGQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGG 68
Cdd:PRK14498 189 VGIISTGDELVepgeplkPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVLLSGG 261
|
|
| PRK14497 |
PRK14497 |
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional |
3-90 |
2.87e-04 |
|
putative molybdopterin biosynthesis protein MoeA/unknown domain fusion protein; Provisional
Pssm-ID: 172968 [Multi-domain] Cd Length: 546 Bit Score: 42.87 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616461727 3 IAIIAVGSELLL-------GQIANTNGQFLSKVFNEIGQNVLEHKVIGDNKKRLESSVRHALEKYDTVILTGGLGPTKDD 75
Cdd:PRK14497 182 IYLIATGDELVEpgnslspGKIYESNLHYLYSKLKSEGYKIVGLSLLSDDKESIKNEIKRAISVADVLILTGGTSAGEKD 261
|
90
....*....|....*
gi 616461727 76 LTkHTVAQIVGKDLV 90
Cdd:PRK14497 262 FV-HQAIRELGNIIV 275
|
|
| |
