|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
21-290 |
1.87e-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: 293.51 E-value: 1.87e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 21 QSMSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvsALRKM-GVKLTPHNKETVQHSDVLFLAVKPHIIPF 99
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALAERyGVRVTTDNAEAAAQADVVVLAVKPQDLAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 100 ILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVG 179
Cdd:COG0345 78 VLEELAPLLDPDKLVISIAAGVTLATLEEALGGGAP---VVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 180 FCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGA 259
Cdd:COG0345 155 KVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGT 234
|
250 260 270
....*....|....*....|....*....|.
gi 1159374919 260 TIHALHVLESGGFRSLLINAVEASCIRTREL 290
Cdd:COG0345 235 TIAGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
23-290 |
9.51e-95 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 281.85 E-value: 9.51e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 23 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASsPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 102
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 103 EIGADIEDRHIVVSCAAGVTISSIEKKLsafrPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 182
Cdd:PLN02688 80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 183 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH 262
Cdd:PLN02688 156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235
|
250 260
....*....|....*....|....*...
gi 1159374919 263 ALHVLESGGFRSLLINAVEASCIRTREL 290
Cdd:PLN02688 236 GVHELEKGGFRAALMNAVVAAAKRSREL 263
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
69-289 |
2.31e-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: 249.48 E-value: 2.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 69 KMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRpapRVIRCMTNTPV 148
Cdd:TIGR00112 28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 149 VVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLG 228
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159374919 229 AQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTRE 289
Cdd:TIGR00112 185 AQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
186-289 |
1.07e-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: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 186 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALH 265
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 1159374919 266 VLESGGFRSLLINAVEASCIRTRE 289
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
21-290 |
1.87e-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: 293.51 E-value: 1.87e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 21 QSMSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvsALRKM-GVKLTPHNKETVQHSDVLFLAVKPHIIPF 99
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALAERyGVRVTTDNAEAAAQADVVVLAVKPQDLAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 100 ILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVG 179
Cdd:COG0345 78 VLEELAPLLDPDKLVISIAAGVTLATLEEALGGGAP---VVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 180 FCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGA 259
Cdd:COG0345 155 KVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGT 234
|
250 260 270
....*....|....*....|....*....|.
gi 1159374919 260 TIHALHVLESGGFRSLLINAVEASCIRTREL 290
Cdd:COG0345 235 TIAGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
23-290 |
9.51e-95 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 281.85 E-value: 9.51e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 23 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASsPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 102
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 103 EIGADIEDRHIVVSCAAGVTISSIEKKLsafrPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 182
Cdd:PLN02688 80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 183 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH 262
Cdd:PLN02688 156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235
|
250 260
....*....|....*....|....*...
gi 1159374919 263 ALHVLESGGFRSLLINAVEASCIRTREL 290
Cdd:PLN02688 236 GVHELEKGGFRAALMNAVVAAAKRSREL 263
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
21-290 |
2.79e-85 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 257.38 E-value: 2.79e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 21 QSMSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFI 100
Cdd:PRK11880 1 MMKKIGFIGGGNMASAIIGGLLASGV-PAKDIIVSDPSPEKRA-ALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 101 LDEIGADIEDrhIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGF 180
Cdd:PRK11880 79 LSELKGQLDK--LVVSIAAGVTLARLERLLGADLP---VVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 181 CTEVE-EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGA 259
Cdd:PRK11880 154 VVWVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGT 233
|
250 260 270
....*....|....*....|....*....|.
gi 1159374919 260 TIHALHVLESGGFRSLLINAVEASCIRTREL 290
Cdd:PRK11880 234 TIAALRVLEEKGLRAAVIEAVQAAAKRSKEL 264
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
69-289 |
2.31e-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: 249.48 E-value: 2.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 69 KMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRpapRVIRCMTNTPV 148
Cdd:TIGR00112 28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 149 VVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLG 228
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159374919 229 AQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTRE 289
Cdd:TIGR00112 185 AQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
|
|
| PRK07679 |
PRK07679 |
pyrroline-5-carboxylate reductase; Reviewed |
23-296 |
1.70e-49 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 181079 [Multi-domain] Cd Length: 279 Bit Score: 166.10 E-value: 1.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 23 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 102
Cdd:PRK07679 4 QNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQELHQKYGVKGTHNKKELLTDANILFLAMKPKDVAEALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 103 EIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 182
Cdd:PRK07679 84 PFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVP---IIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 183 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH 262
Cdd:PRK07679 161 VVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1159374919 263 ALHVLESGGFRSLLINAVEASCIRTRELQSMADQ 296
Cdd:PRK07679 241 GIEVLQEHRFQQALISCITQATQRSHNLGKTLEQ 274
|
|
| PTZ00431 |
PTZ00431 |
pyrroline carboxylate reductase; Provisional |
21-290 |
9.12e-49 |
|
pyrroline carboxylate reductase; Provisional
Pssm-ID: 173621 [Multi-domain] Cd Length: 260 Bit Score: 163.97 E-value: 9.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 21 QSMSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKmgvkltphNKETVQHSDVLFLAVKPHIIPFI 100
Cdd:PTZ00431 2 ENIRVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPSKKNTPFVYLQS--------NEELAKTCDIIVLAVKPDLAGKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 101 LDEIgADIEDRHIVVSCAAGVTISSIEKKLSAfrpAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGF 180
Cdd:PTZ00431 74 LLEI-KPYLGSKLLISICGGLNLKTLEEMVGV---EAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 181 CTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGAT 260
Cdd:PTZ00431 150 IQEIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGIT 229
|
250 260 270
....*....|....*....|....*....|
gi 1159374919 261 IHALHVLESGGFRSLLINAVEASCIRTREL 290
Cdd:PTZ00431 230 IVGLYTLEKHAFKYTVMDAVESACQKSKSM 259
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
186-289 |
1.07e-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: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 186 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALH 265
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 1159374919 266 VLESGGFRSLLINAVEASCIRTRE 289
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
| PRK07680 |
PRK07680 |
late competence protein ComER; Validated |
23-276 |
1.01e-21 |
|
late competence protein ComER; Validated
Pssm-ID: 181080 [Multi-domain] Cd Length: 273 Bit Score: 92.34 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 23 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 102
Cdd:PRK07680 1 MNIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 103 EIGADIEDRHIVVSCAAGVTISSIEKKLSAfrPAPRVIRCMTNTpvvVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 182
Cdd:PRK07680 81 KLAPHLTDEHCLVSITSPISVEQLETLVPC--QVARIIPSITNR---ALSGASLFTFGSRCSEEDQQKLERLFSNISTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 183 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKM-GLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATI 261
Cdd:PRK07680 156 VIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLASEMLIGMGKLLEKGLYTLPTLQEKVCVKGGITG 235
|
250
....*....|....*...
gi 1159374919 262 HALHVLES---GGFRSLL 276
Cdd:PRK07680 236 EGIKVLEEevgDMFHRLF 253
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
26-120 |
2.92e-19 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 81.12 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 26 GFIGAGQLAFALAKGFTAAGvlaAHKIM-ASSPDMDLATvSALRKMGVKLTP-HNKETVQHSDVLFLAVKPHIIPFILDE 103
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAG---PHEVVvANSRNPEKAE-ELAEEYGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSE 76
|
90
....*....|....*..
gi 1159374919 104 IgADIEDRHIVVSCAAG 120
Cdd:pfam03807 77 L-SDLLKGKIVISIAAG 92
|
|
| PRK06928 |
PRK06928 |
pyrroline-5-carboxylate reductase; Reviewed |
25-260 |
1.25e-12 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235888 [Multi-domain] Cd Length: 277 Bit Score: 67.10 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 25 VGFIGAGQLAFALAKGFTAAGVLAAHKIM--ASSPDMDLATVSAlRKMGVKLTPHNKETVQHSDVLFLAVKP-HIIPFIL 101
Cdd:PRK06928 4 IGFIGYGSMADMIATKLLETEVATPEEIIlySSSKNEHFNQLYD-KYPTVELADNEAEIFTKCDHSFICVPPlAVLPLLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 102 DEIGADIEDRHiVVSCAAGVTISSIeKKLSAFRPAPRVIRCMTNtpvVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 181
Cdd:PRK06928 83 DCAPVLTPDRH-VVSIAAGVSLDDL-LEITPGLQVSRLIPSLTS---AVGVGTSLVAHAETVNEANKSRLEETLSHFSHV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 182 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMG-LPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGAT 260
Cdd:PRK06928 158 MTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRNSsLSDEEAFQFLNFALAGTGKLLVEEDYTFSGTIERVATKGGIT 237
|
|
| PRK06476 |
PRK06476 |
pyrroline-5-carboxylate reductase; Reviewed |
23-288 |
1.59e-11 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235812 [Multi-domain] Cd Length: 258 Bit Score: 63.50 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 23 MSVGFIGAGQLAFALAKGFTAAGVLAAHkIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 102
Cdd:PRK06476 1 MKIGFIGTGAITEAMVTGLLTSPADVSE-IIVSPRNAQIAARLAERFPKVRIAKDNQAVVDRSDVVFLAVRPQIAEEVLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 103 EIgaDIEDRHIVVSCAAGVTISSIEKklsAFRPAPRVIRCMTNTPVVVREGAT-VYAtgTHAQVEDgrLMEQLLSSVGFC 181
Cdd:PRK06476 80 AL--RFRPGQTVISVIAATDRAALLE---WIGHDVKLVRAIPLPFVAERKGVTaIYP--PDPFVAA--LFDALGTAVECD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 182 TEVEEDLIDAVTGLSGSgpaYaFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHP-GQLKDNVSSPGGAT 260
Cdd:PRK06476 151 SEEEYDLLAAASALMAT---Y-FGILETATGWLEEQGLKRQKARAYLAPLFASLAQDAVRSTKTDfSALSREFSTKGGLN 226
|
250 260
....*....|....*....|....*...
gi 1159374919 261 IHALHVLESGGFRSLLINAVEASCIRTR 288
Cdd:PRK06476 227 EQVLNDFSRQGGYAALTDALDRVLRRIN 254
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
25-118 |
2.13e-06 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 47.47 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 25 VGFIGAGQLAFALAKGFTAAGvlaaHKIMASSPDMDLATvSALRKMGVKLTP-HNKETVQHSDVLFLAVKPHIIPFILDE 103
Cdd:COG2085 1 IGIIGTGNIGSALARRLAAAG----HEVVIGSRDPEKAA-ALAAELGPGARAgTNAEAAAAADVVVLAVPYEAVPDVLES 75
|
90
....*....|....*
gi 1159374919 104 IGADIEDRhIVVSCA 118
Cdd:COG2085 76 LGDALAGK-IVIDAT 89
|
|
| COG5495 |
COG5495 |
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
23-132 |
2.12e-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: 42.11 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159374919 23 MSVGFIGAGQLAFALAKGFTAAG--VLAAHkimASSPDmdlATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFI 100
Cdd:COG5495 4 MKIGIIGAGRVGTALAAALRAAGheVVGVY---SRSPA---SAERAAALLGAVPALDLEELAAEADLVLLAVPDDAIAEV 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1159374919 101 LDEI---GADIEDrHIVVSCAAGVTISSIEKKLSA 132
Cdd:COG5495 78 AAGLaaaGALRPG-QLVVHTSGALGSDVLAPAARA 111
|
|
|