|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
1-406 |
2.85e-142 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 411.49 E-value: 2.85e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 1 MICEIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREA 80
Cdd:PRK00549 1 MKAEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLGPTKDDLTKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 81 LAEALQLELVQDEKALEVVRRFFDRRGIPLTLNNLKQALVPAGGRAIDNPIGTAPGIIVEQAGKTYILVPGPPSEFNMMV 160
Cdd:PRK00549 81 VAKFLGRELVLDEEALAKIEDYFAKRGREMTENNRKQALIPEGATVLPNPVGTAPGMIIEVDGKTYIVLPGPPSELKPMF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 161 KEQVIPYLIGRLASQvGVIKSRVLKFCGIGESLLDEKLSDL-LKSTNPTIAPTAKFSEIHLRLTAKARQSDMAEEMIDAM 239
Cdd:PRK00549 161 EEYVVPYLSSAKGTG-EVLYSRVLRFFGIGESQLATTLRDLiDNQTNPTIAPYAKDGEVTLRLTAKARSEEEAEKLIDPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 240 ESRVRERLGAFIFGVDDETLPGAVTLVLREQGKTIAVAENFTGGQLSYQLSSAAGAESTFTAGLVArdYrQLQEKAclQL 319
Cdd:PRK00549 240 EEEIRDRVGDYFYGYDEDSLEEVVAKLLKEKGLTIATAESCTGGLLAARLTDFPGSSSYFKGGVVT--Y-SNEAKA--KL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 320 GDIPTRAMERAG--------HMASMVRKQFGTDIGAAVavqrSG--GDDAAVAEYNL---YIAADCNGRLMMKKVLW-SG 385
Cdd:PRK00549 315 LGVPPETLEEHGavseetaeEMAEGARKLLGADIGISI----TGvaGPDGGTEEKPVgtvYIGLATPGGETVVKELIlGG 390
|
410 420
....*....|....*....|.
gi 493567638 386 ERDEMAKRASTVALVLLWRYL 406
Cdd:PRK00549 391 SRSDIRERAVTYALDLLRRAL 411
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
4-251 |
1.35e-109 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 322.06 E-value: 1.35e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 4 EIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREALAE 83
Cdd:COG1058 3 EIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAVAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 84 ALQLELVQDEKALEVVRRFFDRRGIPLTLNNLKQALVPAGGRAIDNPIGTAPGIIVEQAGKTYILVPGPPSEFNMMVKEQ 163
Cdd:COG1058 83 ALGVPLVLDPEALALIEERFAKRGREMTENNLKQALLPEGAELLPNPVGTAPGFSIENNGKVVIFLPGVPSEMKPMFEEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 164 VIPYLIGRLASQvgVIKSRVLKFCGIGESLLDEKLSDLLKS-TNPTIAPTAKFSEIHLRLTAKARQSDMAEEMIDAMESR 242
Cdd:COG1058 163 VLPRLKKLFSGE--PIVSRTLRTFGIGESDLAELLEDLEARfPNVTIGSYPSDGEVRLRLTARGTDEEEAEAALEALEEE 240
|
....*....
gi 493567638 243 VRERLGAFI 251
Cdd:COG1058 241 LRERLGDYI 249
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
1-406 |
2.12e-99 |
|
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: 302.21 E-value: 2.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 1 MICEIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREA 80
Cdd:TIGR00200 1 LKAEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSDDLTAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 81 LAEALQLELVQDEKALEVVRRFFDRRGIPLTLNNLKQALVPAGGRAIDNPIGTAPGIIVEQAGKTYIL-VPGPPSEFNMM 159
Cdd:TIGR00200 81 IATAKGEPLVLNEAWLKEIERYFHETGRVMAPNNRKQALLPAGAEFLANPVGTAPGMFAVQLNRCLMLfTPGVPSEFRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 160 VKEQVIPYLIGRLASQVGVIkSRVLKFCGIGESLLDEKLSDLLKS-TNPTIAPTAKFSEIHLRLTAKARQSDMAEEMIDA 238
Cdd:TIGR00200 161 VEHEALPRLRERFSLPQPIV-SLVLRFFGIGESQLEADLADSLDTlTNPTGAPMAYRGEVPLRELKLTGPESEQQRAMEK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 239 MESRVRERLGAFIFGVDDETLPGAVTLVLREQGKTIAVAENFTGGQLSYQLSSAAGAESTFTAGLV--ARDYRQLQEKAC 316
Cdd:TIGR00200 240 LWLDIKRVAGQSVIGEDTEGLPAQISRELQERGFTLTLAESFTGGLLALQLTDHSGASKLFAGGVPlyANEVKPSQLGVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 317 LQLGD-IPTRAMERAGHMASMVRKQFGTDIGAAVAVQRSGGDDAAVAEYNLYIAADCNGRLMMKKVLWSGERDEMAKRAS 395
Cdd:TIGR00200 320 AETAHwIGAVSANHAAGLALGVSGFEGEDLGIALTGPAGPDFAERVRFGTVRYGLAIRQEVAMHALNMLGRRLGIRDIAA 399
|
410
....*....|.
gi 493567638 396 TVALVLLWRYL 406
Cdd:TIGR00200 400 EHGWIEVVESL 410
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
4-171 |
1.14e-78 |
|
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: 240.46 E-value: 1.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 4 EIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREALAE 83
Cdd:cd00885 3 EIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAVAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 84 ALQLELVQDEKALEVVRRFFDRRGIPLTLNNLKQALVPAGGRAIDNPIGTAPGIIVEQAGKTYILVPGPPSEFNMMVKEQ 163
Cdd:cd00885 83 AFGRPLVLDEEALERIEARFARRGREMTEANLKQAMLPEGATLLPNPVGTAPGFSVEHNGKNVFLLPGVPSEMKPMLEEE 162
|
....*...
gi 493567638 164 VIPYLIGR 171
Cdd:cd00885 163 VLPRLRER 170
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
4-168 |
5.90e-36 |
|
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: 128.91 E-value: 5.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 4 EIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREALAE 83
Cdd:pfam00994 1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 84 ALQLELVQDEKALEVVRRFFDRrgipltlnnlkqalvpaggraidnPIGTAPGIIVEQAGKTYILVPGPPSEFNMMVKEQ 163
Cdd:pfam00994 81 LGGRELPGFEELFRGVSLKPGK------------------------PVGTAPGAILSRAGKTVFGLPGSPVAAKVMFELL 136
|
....*
gi 493567638 164 VIPYL 168
Cdd:pfam00994 137 LLPLL 141
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
4-163 |
1.05e-25 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 101.13 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 4 EIIFTGTELLLG-QILNTNAQVIERELSTLGIDLYYQVTVG--DNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREA 80
Cdd:smart00852 1 AIISTGDELLSGgQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 81 LAEALQLELVqdekalevvrrffdrrgipltlnNLKQALVPAGG-RAIDNPIGTAPGIIVeqaGKTYILVPGPPSEFNMM 159
Cdd:smart00852 81 LAELGGRELL-----------------------GHGVAMRPGGPpGPLANLSGTAPGVRG---KKPVFGLPGNPVAALVM 134
|
....
gi 493567638 160 VKEQ 163
Cdd:smart00852 135 FEEL 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
1-406 |
2.85e-142 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 411.49 E-value: 2.85e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 1 MICEIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREA 80
Cdd:PRK00549 1 MKAEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLGPTKDDLTKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 81 LAEALQLELVQDEKALEVVRRFFDRRGIPLTLNNLKQALVPAGGRAIDNPIGTAPGIIVEQAGKTYILVPGPPSEFNMMV 160
Cdd:PRK00549 81 VAKFLGRELVLDEEALAKIEDYFAKRGREMTENNRKQALIPEGATVLPNPVGTAPGMIIEVDGKTYIVLPGPPSELKPMF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 161 KEQVIPYLIGRLASQvGVIKSRVLKFCGIGESLLDEKLSDL-LKSTNPTIAPTAKFSEIHLRLTAKARQSDMAEEMIDAM 239
Cdd:PRK00549 161 EEYVVPYLSSAKGTG-EVLYSRVLRFFGIGESQLATTLRDLiDNQTNPTIAPYAKDGEVTLRLTAKARSEEEAEKLIDPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 240 ESRVRERLGAFIFGVDDETLPGAVTLVLREQGKTIAVAENFTGGQLSYQLSSAAGAESTFTAGLVArdYrQLQEKAclQL 319
Cdd:PRK00549 240 EEEIRDRVGDYFYGYDEDSLEEVVAKLLKEKGLTIATAESCTGGLLAARLTDFPGSSSYFKGGVVT--Y-SNEAKA--KL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 320 GDIPTRAMERAG--------HMASMVRKQFGTDIGAAVavqrSG--GDDAAVAEYNL---YIAADCNGRLMMKKVLW-SG 385
Cdd:PRK00549 315 LGVPPETLEEHGavseetaeEMAEGARKLLGADIGISI----TGvaGPDGGTEEKPVgtvYIGLATPGGETVVKELIlGG 390
|
410 420
....*....|....*....|.
gi 493567638 386 ERDEMAKRASTVALVLLWRYL 406
Cdd:PRK00549 391 SRSDIRERAVTYALDLLRRAL 411
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
4-251 |
1.35e-109 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 322.06 E-value: 1.35e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 4 EIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREALAE 83
Cdd:COG1058 3 EIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAVAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 84 ALQLELVQDEKALEVVRRFFDRRGIPLTLNNLKQALVPAGGRAIDNPIGTAPGIIVEQAGKTYILVPGPPSEFNMMVKEQ 163
Cdd:COG1058 83 ALGVPLVLDPEALALIEERFAKRGREMTENNLKQALLPEGAELLPNPVGTAPGFSIENNGKVVIFLPGVPSEMKPMFEEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 164 VIPYLIGRLASQvgVIKSRVLKFCGIGESLLDEKLSDLLKS-TNPTIAPTAKFSEIHLRLTAKARQSDMAEEMIDAMESR 242
Cdd:COG1058 163 VLPRLKKLFSGE--PIVSRTLRTFGIGESDLAELLEDLEARfPNVTIGSYPSDGEVRLRLTARGTDEEEAEAALEALEEE 240
|
....*....
gi 493567638 243 VRERLGAFI 251
Cdd:COG1058 241 LRERLGDYI 249
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
1-406 |
2.12e-99 |
|
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: 302.21 E-value: 2.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 1 MICEIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREA 80
Cdd:TIGR00200 1 LKAEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSDDLTAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 81 LAEALQLELVQDEKALEVVRRFFDRRGIPLTLNNLKQALVPAGGRAIDNPIGTAPGIIVEQAGKTYIL-VPGPPSEFNMM 159
Cdd:TIGR00200 81 IATAKGEPLVLNEAWLKEIERYFHETGRVMAPNNRKQALLPAGAEFLANPVGTAPGMFAVQLNRCLMLfTPGVPSEFRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 160 VKEQVIPYLIGRLASQVGVIkSRVLKFCGIGESLLDEKLSDLLKS-TNPTIAPTAKFSEIHLRLTAKARQSDMAEEMIDA 238
Cdd:TIGR00200 161 VEHEALPRLRERFSLPQPIV-SLVLRFFGIGESQLEADLADSLDTlTNPTGAPMAYRGEVPLRELKLTGPESEQQRAMEK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 239 MESRVRERLGAFIFGVDDETLPGAVTLVLREQGKTIAVAENFTGGQLSYQLSSAAGAESTFTAGLV--ARDYRQLQEKAC 316
Cdd:TIGR00200 240 LWLDIKRVAGQSVIGEDTEGLPAQISRELQERGFTLTLAESFTGGLLALQLTDHSGASKLFAGGVPlyANEVKPSQLGVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 317 LQLGD-IPTRAMERAGHMASMVRKQFGTDIGAAVAVQRSGGDDAAVAEYNLYIAADCNGRLMMKKVLWSGERDEMAKRAS 395
Cdd:TIGR00200 320 AETAHwIGAVSANHAAGLALGVSGFEGEDLGIALTGPAGPDFAERVRFGTVRYGLAIRQEVAMHALNMLGRRLGIRDIAA 399
|
410
....*....|.
gi 493567638 396 TVALVLLWRYL 406
Cdd:TIGR00200 400 EHGWIEVVESL 410
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
4-171 |
1.14e-78 |
|
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: 240.46 E-value: 1.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 4 EIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREALAE 83
Cdd:cd00885 3 EIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAVAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 84 ALQLELVQDEKALEVVRRFFDRRGIPLTLNNLKQALVPAGGRAIDNPIGTAPGIIVEQAGKTYILVPGPPSEFNMMVKEQ 163
Cdd:cd00885 83 AFGRPLVLDEEALERIEARFARRGREMTEANLKQAMLPEGATLLPNPVGTAPGFSVEHNGKNVFLLPGVPSEMKPMLEEE 162
|
....*...
gi 493567638 164 VIPYLIGR 171
Cdd:cd00885 163 VLPRLRER 170
|
|
| PRK03673 |
PRK03673 |
nicotinamide mononucleotide deamidase-related protein YfaY; |
4-337 |
9.15e-51 |
|
nicotinamide mononucleotide deamidase-related protein YfaY;
Pssm-ID: 179629 [Multi-domain] Cd Length: 396 Bit Score: 175.66 E-value: 9.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 4 EIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREALAE 83
Cdd:PRK03673 5 EMLSTGDEVLHGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGGLGPTSDDLSALAAAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 84 ALQLELVQDEKALEVVRRFFDRRGIPLTLNNLKQALVPAGGRAIDNPIGTAPGIIVEQAGKTYILVPGPPSEFNMMVKEQ 163
Cdd:PRK03673 85 AAGEGLVLHEEWLAEMERFFAERGRVMAPSNRKQAELPASAEMIDNPVGTACGFALQLNRCLMFFTPGVPSEFKVMVEQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 164 VIPYLIGRLASQVGVIKSRVLKFcGIGESLLDEKLSDLLKSTNPTIAPTAKFSEIHLRLTAKARQSdmaeemiDAMES-- 241
Cdd:PRK03673 165 ILPRLRERFSLPEPPLCLRLTTF-GRSESDLAQSLDPLPLPPGVVMGYRSSMPIIELKLTGPASQR-------QAMEQlw 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 242 -RVRERLG-AFIF-GVddETLPGAVTLVLREQGKTIAVAENFTGGQLSYQLSSAAgaestftAGLVARDYRQLQEKAclq 318
Cdd:PRK03673 237 qQVRRVAGqSVIFeGT--EGLPAQIARRLQERQLSLTLSEQFTAGLLALQLSRAG-------APLLAGEVLPSQEET--- 304
|
330 340
....*....|....*....|
gi 493567638 319 LGDIPTRAMERAG-HMASMV 337
Cdd:PRK03673 305 LAQTAHWATERRAnHFAGLA 324
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
4-171 |
7.33e-50 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 169.42 E-value: 7.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 4 EIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREALAE 83
Cdd:PRK01215 7 WIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGFAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 84 ALQLELVQDEKALEVVRRFFDRRGIPLTLNNLKQALVPAGGRAIDNPIGTAPGIIVEQAGKTYILVPGPPSEFNMMVKEQ 163
Cdd:PRK01215 87 ALGVELELNEDALRMILEKYEKRGIPLTPERKKMAMMPPGAVPLENPVGTAPGILIEHGGKDIVALPGVPREMEAIFENF 166
|
....*...
gi 493567638 164 VIPYLIGR 171
Cdd:PRK01215 167 VEPLLKNR 174
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
4-168 |
5.90e-36 |
|
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: 128.91 E-value: 5.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 4 EIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREALAE 83
Cdd:pfam00994 1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 84 ALQLELVQDEKALEVVRRFFDRrgipltlnnlkqalvpaggraidnPIGTAPGIIVEQAGKTYILVPGPPSEFNMMVKEQ 163
Cdd:pfam00994 81 LGGRELPGFEELFRGVSLKPGK------------------------PVGTAPGAILSRAGKTVFGLPGSPVAAKVMFELL 136
|
....*
gi 493567638 164 VIPYL 168
Cdd:pfam00994 137 LLPLL 141
|
|
| PRK03670 |
PRK03670 |
competence damage-inducible protein A; Provisional |
1-242 |
2.57e-29 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 167581 Cd Length: 252 Bit Score: 114.51 E-value: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 1 MICEIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRA-DLIIVGGGLGPTEDDISRE 79
Cdd:PRK03670 1 MFAEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKpEVLVISGGLGPTHDDVTML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 80 ALAEALQLELVQDEKALEVVRRFFDR---RGI---PlTLNNL--KQALVPAGGRAIDNPIGTAPGIIVEQAGKTYILVPG 151
Cdd:PRK03670 81 AVAEALGRELVLCEDCLERIKEFYEElykKGLiddP-TLNEArkKMAYLPEGAEPLENTEGAAPGAYIEHKGTKIFVLPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 152 PPSEFNMMVKEQVIPyligRLASQVGVIKsrvlKFCG--IGESLLDEKLSDLLKSTNPTIAPTAKFSEIHLRLTAKARQS 229
Cdd:PRK03670 160 MPREMKAMLEKEVLP----RLGERKFVQK----KFLAeiTDESKLAPILEEALERFNVKIHSSPKGFGKYIGIIIFAEDE 231
|
250
....*....|...
gi 493567638 230 DMAEEMIDAMESR 242
Cdd:PRK03670 232 EEIEKAVEFMEER 244
|
|
| CinA_KH |
pfam18146 |
Damage-inducible protein CinA KH domain; This domain is found in competence-induced protein A ... |
181-253 |
3.79e-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: 102.95 E-value: 3.79e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493567638 181 SRVLKFCGIGESLLDEKLSDLLKSTNPTIAPTAKFSEIHLRLTAKARQSDMAEEMIDAMESRVRERLGAFIFG 253
Cdd:pfam18146 1 SRTLKTFGIGESQLEERLGDLIDRENPTIAPYAKDGEVTLRITAKAADEEEAEALIAPVEEEIRERLGDYIYG 73
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
4-163 |
1.05e-25 |
|
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.
Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 101.13 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 4 EIIFTGTELLLG-QILNTNAQVIERELSTLGIDLYYQVTVG--DNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREA 80
Cdd:smart00852 1 AIISTGDELLSGgQIRDSNGPMLAALLRELGIEVVRVVVVGgpDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 81 LAEALQLELVqdekalevvrrffdrrgipltlnNLKQALVPAGG-RAIDNPIGTAPGIIVeqaGKTYILVPGPPSEFNMM 159
Cdd:smart00852 81 LAELGGRELL-----------------------GHGVAMRPGGPpGPLANLSGTAPGVRG---KKPVFGLPGNPVAALVM 134
|
....
gi 493567638 160 VKEQ 163
Cdd:smart00852 135 FEEL 138
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
3-168 |
1.26e-14 |
|
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: 70.45 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 3 CEIIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDISREALA 82
Cdd:cd00758 2 VAIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 83 EALQLELVQDekalevvrrffdrrGIPLtlnnlkqalvpAGGRaidnpigtaPGIIVEQAGKTYILVPGPPSEFNMMVKE 162
Cdd:cd00758 82 ELGEREAHGK--------------GVAL-----------APGS---------RTAFGIIGKVLIINLPGSPKSALTTFEA 127
|
....*.
gi 493567638 163 QVIPYL 168
Cdd:cd00758 128 LVLPAL 133
|
|
| CinA |
pfam02464 |
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, ... |
256-406 |
1.38e-14 |
|
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 Pfam family consists of putative competence-damaged proteins from the cin operon. Some members of this family have nicotinamide mononucleotide (NMN) deamidase activity.
Pssm-ID: 460565 Cd Length: 155 Bit Score: 70.64 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 256 DETLPGAVTLVLREQGKTIAVAENFTGGQLSYQLSSAAGAESTFTAGLVArdYrQLQEKACLqLGdIPTRAMER------ 329
Cdd:pfam02464 1 LESLAEEVGKLLKARGLTLATAESCTGGLLAAALTSVPGASDVFLGGVVT--Y-SNEAKREL-LG-VPPETLEEhgavse 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 330 --AGHMASMVRKQFGTDIGAA---VAVQRSGGDDAAVAeyNLYIAADCNGRLMMKKVLWSGERDEMAKRASTVALVLLWR 404
Cdd:pfam02464 76 evAREMAEGARKRLGADIGVAitgIAGPSGGTEGKPVG--TVYIAIAGPGGTVTRRLNFGGDREAIREQAVVAALELLRR 153
|
..
gi 493567638 405 YL 406
Cdd:pfam02464 154 LL 155
|
|
| PncC |
COG1546 |
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ... |
256-405 |
1.26e-12 |
|
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; Nicotinamide mononucleotide (NMN) deamidase PncC is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 441155 Cd Length: 154 Bit Score: 65.06 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 256 DETLPGAVTLVLREQGKTIAVAENFTGGQLSYQLSSAAGAESTFTAGLVARDYRQLQEkaclQLGdIPTRAMER------ 329
Cdd:COG1546 1 LESLAEVVGELLRERGLTLATAESCTGGLIAAALTDVPGSSAVFDGGFVTYSNEAKEE----LLG-VPAETLEKhgavse 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 330 --AGHMASMVRKQFGTDIGAAVavqrSG-----GDDAAVAEYNLYIAADCNGRLMMKKVLWSGERDEMAKRASTVALVLL 402
Cdd:COG1546 76 evAREMAEGARRLSGADIAVAV----TGiagpgGGTPGKPVGTVYIALAGPGGVVVRRLHFGGDREAVREQAVRAALDLL 151
|
...
gi 493567638 403 WRY 405
Cdd:COG1546 152 REL 154
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
3-136 |
5.70e-12 |
|
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: 63.10 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 3 CEIIFTGTELLLG-------QILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDD 75
Cdd:TIGR00177 3 VAVISVGDELVEGgqplepgQIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRD 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493567638 76 ISREALAEALqlelvqdEKALEVVRRFFDRRGIPLtlnNLKQALVPAGGRAIDNPIGTAPG 136
Cdd:TIGR00177 83 VTPEALEELG-------EKEIPGFGEFRMLSSLPV---LSRPGKPATAGVRGGTLIFNLPG 133
|
|
| PncC_domain |
TIGR00199 |
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is ... |
267-403 |
4.77e-10 |
|
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species. Several bacterial species have a protein consisting largely of the C-terminal domain of CinA but lacking the N-terminal domain, including nicotinamide mononucleotide (NMN) deamidase (3.5.1.42) proteins PncC in Shewanella oneidensis and ygaD in E. coli. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129303 [Multi-domain] Cd Length: 146 Bit Score: 57.41 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 267 LREQGKTIAVAENFTGGQLSYQLSSAAGAESTFTAGLVArdyrqLQEKACLQLGDIPTRAMERAG--------HMASMVR 338
Cdd:TIGR00199 5 LKALGLTVATAESCTGGLLAHALTDISGASKYFGGGVVC-----YTNQVKINLLGVSQETLARFGavseecaaEMALGVK 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493567638 339 KQFGTDIGAAVA--VQRSGGDDAAVAEYNLYIAADCNGRLMMKKVLWSGERDEMAKRASTVALVLLW 403
Cdd:TIGR00199 80 ERFGADVGIAISgiAGPDGGEEEKPGGTVWFIWIIAKGQAYTAEMHFAGDRETIRALAVRYALHQLL 146
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
5-84 |
4.28e-08 |
|
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: 54.81 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 5 IIFTGTELL-------LGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDIS 77
Cdd:cd00887 173 IISTGDELVepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSVGDYDFV 252
|
....*..
gi 493567638 78 REALAEA 84
Cdd:cd00887 253 KEVLEEL 259
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
5-83 |
1.46e-07 |
|
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: 53.17 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 5 IIFTGTELL-------LGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGGLGPTEDDIS 77
Cdd:COG0303 177 ILSTGDELVepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGVSVGDYDLV 256
|
....*.
gi 493567638 78 REALAE 83
Cdd:COG0303 257 KEALEE 262
|
|
| MoeA_like |
cd03522 |
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ... |
5-84 |
5.72e-05 |
|
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: 44.84 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 5 IIFTGTELLLGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAG-RADLIIVGGGLGPTEDDISREALAE 83
Cdd:cd03522 164 LIVTGSEVYGGRIEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAAAIAEALEaGAELLILTGGASVDPDDVTPAAIRA 243
|
.
gi 493567638 84 A 84
Cdd:cd03522 244 A 244
|
|
| PRK14498 |
PRK14498 |
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
5-68 |
2.07e-03 |
|
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional
Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 40.20 E-value: 2.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493567638 5 IIFTGTELL-------LGQILNTNAQVIERELSTLGIDLYYQVTVGDNLQRCAAAIKQAAGRADLIIVGGG 68
Cdd:PRK14498 191 IISTGDELVepgeplkPGKIYDVNSYTLAAAVEEAGGEPVRYGIVPDDEEELEAALRKALKECDLVLLSGG 261
|
|
| PRK03657 |
PRK03657 |
2-oxo-tetronate isomerase; |
257-408 |
2.63e-03 |
|
2-oxo-tetronate isomerase;
Pssm-ID: 235149 Cd Length: 170 Bit Score: 38.34 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 257 ETLPGAVTLVLREQGKTIAVAENFTGGQLSYQLSSAAGAESTFTAGLVArdyrqLQEKACLQLGDIPTRAMER------- 329
Cdd:PRK03657 13 ENLTKALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVT-----FTDEAKMKILSVSQQSLERysavsea 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493567638 330 -AGHMASMVRKQFGTDIGAAVA--VQRSGGDDAAVAEyNLYIAADCNGRLMMKKVLWSGERDEMAKRASTVALVLLWRYL 406
Cdd:PRK03657 88 vVAEMATGAIERADADISIAISgyGGPEGGEDGTPAG-TVWFAWNIKGQTYTARMHFAGDCETVLAKAVRFALAQLLQLL 166
|
..
gi 493567638 407 KH 408
Cdd:PRK03657 167 LK 168
|
|
| |
