|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-268 |
4.79e-99 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 292.35 E-value: 4.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvsAL-RKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345 3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALaERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 80 DEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:COG0345 80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAP---VVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 160 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATI 239
Cdd:COG0345 157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTI 236
|
250 260
....*....|....*....|....*....
gi 767997438 240 HALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:COG0345 237 AGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
1-268 |
1.78e-94 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 280.69 E-value: 1.78e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASsPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 81 EIGADIEDRHIVVSCAAGVTISSIEKKLsafrPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PLN02688 80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH 240
Cdd:PLN02688 156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235
|
250 260
....*....|....*....|....*...
gi 767997438 241 ALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:PLN02688 236 GVHELEKGGFRAALMNAVVAAAKRSREL 263
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
47-267 |
4.37e-82 |
|
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 272911 [Multi-domain] Cd Length: 245 Bit Score: 248.71 E-value: 4.37e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 47 KMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRpapRVIRCMTNTPV 126
Cdd:TIGR00112 28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 127 VVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLG 206
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767997438 207 AQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTRE 267
Cdd:TIGR00112 185 AQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
164-267 |
1.06e-47 |
|
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.
Pssm-ID: 464294 [Multi-domain] Cd Length: 104 Bit Score: 155.63 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 164 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALH 243
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 767997438 244 VLESGGFRSLLINAVEASCIRTRE 267
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-268 |
4.79e-99 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 292.35 E-value: 4.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvsAL-RKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345 3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALaERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 80 DEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:COG0345 80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAP---VVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 160 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATI 239
Cdd:COG0345 157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTI 236
|
250 260
....*....|....*....|....*....
gi 767997438 240 HALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:COG0345 237 AGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
1-268 |
1.78e-94 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 280.69 E-value: 1.78e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASsPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 81 EIGADIEDRHIVVSCAAGVTISSIEKKLsafrPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PLN02688 80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH 240
Cdd:PLN02688 156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235
|
250 260
....*....|....*....|....*...
gi 767997438 241 ALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:PLN02688 236 GVHELEKGGFRAALMNAVVAAAKRSREL 263
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-268 |
4.62e-85 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 257.00 E-value: 4.62e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK11880 3 KKIGFIGGGNMASAIIGGLLASGV-PAKDIIVSDPSPEKRA-ALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 81 EIGADIEDrhIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PRK11880 81 ELKGQLDK--LVVSIAAGVTLARLERLLGADLP---VVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 161 EVE-EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATI 239
Cdd:PRK11880 156 WVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTI 235
|
250 260
....*....|....*....|....*....
gi 767997438 240 HALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:PRK11880 236 AALRVLEEKGLRAAVIEAVQAAAKRSKEL 264
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
47-267 |
4.37e-82 |
|
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 272911 [Multi-domain] Cd Length: 245 Bit Score: 248.71 E-value: 4.37e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 47 KMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRpapRVIRCMTNTPV 126
Cdd:TIGR00112 28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 127 VVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLG 206
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767997438 207 AQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTRE 267
Cdd:TIGR00112 185 AQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
|
|
| PRK07679 |
PRK07679 |
pyrroline-5-carboxylate reductase; Reviewed |
1-274 |
2.72e-49 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 181079 [Multi-domain] Cd Length: 279 Bit Score: 165.71 E-value: 2.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK07679 4 QNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQELHQKYGVKGTHNKKELLTDANILFLAMKPKDVAEALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 81 EIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PRK07679 84 PFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVP---IIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH 240
Cdd:PRK07679 161 VVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEA 240
|
250 260 270
....*....|....*....|....*....|....
gi 767997438 241 ALHVLESGGFRSLLINAVEASCIRTRELQSMADQ 274
Cdd:PRK07679 241 GIEVLQEHRFQQALISCITQATQRSHNLGKTLEQ 274
|
|
| PTZ00431 |
PTZ00431 |
pyrroline carboxylate reductase; Provisional |
1-268 |
1.26e-48 |
|
pyrroline carboxylate reductase; Provisional
Pssm-ID: 173621 [Multi-domain] Cd Length: 260 Bit Score: 163.20 E-value: 1.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKmgvkltphNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PTZ00431 4 IRVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPSKKNTPFVYLQS--------NEELAKTCDIIVLAVKPDLAGKVLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 81 EIgADIEDRHIVVSCAAGVTISSIEKKLSAfrpAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PTZ00431 76 EI-KPYLGSKLLISICGGLNLKTLEEMVGV---EAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH 240
Cdd:PTZ00431 152 EIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGITIV 231
|
250 260
....*....|....*....|....*...
gi 767997438 241 ALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:PTZ00431 232 GLYTLEKHAFKYTVMDAVESACQKSKSM 259
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
164-267 |
1.06e-47 |
|
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.
Pssm-ID: 464294 [Multi-domain] Cd Length: 104 Bit Score: 155.63 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 164 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALH 243
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 767997438 244 VLESGGFRSLLINAVEASCIRTRE 267
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
| PRK07680 |
PRK07680 |
late competence protein ComER; Validated |
1-254 |
8.92e-22 |
|
late competence protein ComER; Validated
Pssm-ID: 181080 [Multi-domain] Cd Length: 273 Bit Score: 92.73 E-value: 8.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK07680 1 MNIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 81 EIGADIEDRHIVVSCAAGVTISSIEKKLSAfrPAPRVIRCMTNTpvvVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PRK07680 81 KLAPHLTDEHCLVSITSPISVEQLETLVPC--QVARIIPSITNR---ALSGASLFTFGSRCSEEDQQKLERLFSNISTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKM-GLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATI 239
Cdd:PRK07680 156 VIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLASEMLIGMGKLLEKGLYTLPTLQEKVCVKGGITG 235
|
250
....*....|....*...
gi 767997438 240 HALHVLES---GGFRSLL 254
Cdd:PRK07680 236 EGIKVLEEevgDMFHRLF 253
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
4-98 |
3.98e-19 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 80.35 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 4 GFIGAGQLAFALAKGFTAAGvlaAHKIM-ASSPDMDLATVSAlRKMGVKLTP-HNKETVQHSDVLFLAVKPHIIPFILDE 81
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAG---PHEVVvANSRNPEKAEELA-EEYGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSE 76
|
90
....*....|....*..
gi 767997438 82 IgADIEDRHIVVSCAAG 98
Cdd:pfam03807 77 L-SDLLKGKIVISIAAG 92
|
|
| PRK06928 |
PRK06928 |
pyrroline-5-carboxylate reductase; Reviewed |
3-238 |
9.66e-13 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235888 [Multi-domain] Cd Length: 277 Bit Score: 67.10 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 3 VGFIGAGQLAFALAKGFTAAGVLAAHKIM--ASSPDMDLATVSAlRKMGVKLTPHNKETVQHSDVLFLAVKP-HIIPFIL 79
Cdd:PRK06928 4 IGFIGYGSMADMIATKLLETEVATPEEIIlySSSKNEHFNQLYD-KYPTVELADNEAEIFTKCDHSFICVPPlAVLPLLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 80 DEIGADIEDRHIVvSCAAGVTISSIeKKLSAFRPAPRVIRCMTNtpvVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:PRK06928 83 DCAPVLTPDRHVV-SIAAGVSLDDL-LEITPGLQVSRLIPSLTS---AVGVGTSLVAHAETVNEANKSRLEETLSHFSHV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 160 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMG-LPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGAT 238
Cdd:PRK06928 158 MTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRNSsLSDEEAFQFLNFALAGTGKLLVEEDYTFSGTIERVATKGGIT 237
|
|
| PRK06476 |
PRK06476 |
pyrroline-5-carboxylate reductase; Reviewed |
1-266 |
1.47e-11 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235812 [Multi-domain] Cd Length: 258 Bit Score: 63.50 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 1 MSVGFIGAGQLAFALAKGFTAAGVLAAHkIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK06476 1 MKIGFIGTGAITEAMVTGLLTSPADVSE-IIVSPRNAQIAARLAERFPKVRIAKDNQAVVDRSDVVFLAVRPQIAEEVLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 81 EIGADieDRHIVVSCAAGVTISSIEKklsAFRPAPRVIRCMTNTPVVVREGAT-VYAtgTHAQVEDgrLMEQLLSSVGFC 159
Cdd:PRK06476 80 ALRFR--PGQTVISVIAATDRAALLE---WIGHDVKLVRAIPLPFVAERKGVTaIYP--PDPFVAA--LFDALGTAVECD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 160 TEVEEDLIDAVTGLSGSgpaYaFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHP-GQLKDNVSSPGGAT 238
Cdd:PRK06476 151 SEEEYDLLAAASALMAT---Y-FGILETATGWLEEQGLKRQKARAYLAPLFASLAQDAVRSTKTDfSALSREFSTKGGLN 226
|
250 260
....*....|....*....|....*...
gi 767997438 239 IHALHVLESGGFRSLLINAVEASCIRTR 266
Cdd:PRK06476 227 EQVLNDFSRQGGYAALTDALDRVLRRIN 254
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
3-96 |
2.78e-06 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 47.09 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 3 VGFIGAGQLAFALAKGFTAAGvlaaHKIMASSPDMDLATvSALRKMGVKLTP-HNKETVQHSDVLFLAVKPHIIPFILDE 81
Cdd:COG2085 1 IGIIGTGNIGSALARRLAAAG----HEVVIGSRDPEKAA-ALAAELGPGARAgTNAEAAAAADVVVLAVPYEAVPDVLES 75
|
90
....*....|....*
gi 767997438 82 IGADIEDRhIVVSCA 96
Cdd:COG2085 76 LGDALAGK-IVIDAT 89
|
|
| COG5495 |
COG5495 |
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
1-110 |
2.78e-04 |
|
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];
Pssm-ID: 444246 [Multi-domain] Cd Length: 286 Bit Score: 41.72 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997438 1 MSVGFIGAGQLAFALAKGFTAAG--VLAAHkimASSPDmdlATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFI 78
Cdd:COG5495 4 MKIGIIGAGRVGTALAAALRAAGheVVGVY---SRSPA---SAERAAALLGAVPALDLEELAAEADLVLLAVPDDAIAEV 77
|
90 100 110
....*....|....*....|....*....|....*
gi 767997438 79 LDEI---GADIEDrHIVVSCAAGVTISSIEKKLSA 110
Cdd:COG5495 78 AAGLaaaGALRPG-QLVVHTSGALGSDVLAPAARA 111
|
|
| |
