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Conserved domains on  [gi|530413549|ref|XP_005256438|]
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pyrroline-5-carboxylate reductase 1, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

pyrroline-5-carboxylate reductase family protein( domain architecture ID 11417420)

pyrroline-5-carboxylate reductase family protein similar to pyrroline-5-carboxylate reductase that catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline

CATH:  1.10.3730.10|3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0004735|GO:0055129

Graphical summary

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List of domain hits

 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 530413549   1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvsAL-RKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345    3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALaERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  80 DEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:COG0345   80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAP---VVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549 160 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATI 239
Cdd:COG0345  157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTI 236

                        250       260
                 ....*....|....*....|....*....
gi 530413549 240 HALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:COG0345  237 AGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
 
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 530413549   1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvsAL-RKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345    3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALaERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  80 DEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:COG0345   80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAP---VVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549 160 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATI 239
Cdd:COG0345  157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTI 236

                        250       260
                 ....*....|....*....|....*....
gi 530413549 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 530413549   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASsPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PLN02688   1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  81 EIGADIEDRHIVVSCAAGVTISSIEKKLsafrPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PLN02688  80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH 240
Cdd:PLN02688 156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235

                        250       260
                 ....*....|....*....|....*...
gi 530413549 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 530413549   47 KMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRpapRVIRCMTNTPV 126
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  127 VVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLG 206
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530413549  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 530413549  164 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALH 243
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 530413549  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 530413549   1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvsAL-RKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345    3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALaERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  80 DEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:COG0345   80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAP---VVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549 160 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATI 239
Cdd:COG0345  157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTI 236

                        250       260
                 ....*....|....*....|....*....
gi 530413549 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 530413549   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASsPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PLN02688   1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  81 EIGADIEDRHIVVSCAAGVTISSIEKKLsafrPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PLN02688  80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH 240
Cdd:PLN02688 156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235

                        250       260
                 ....*....|....*....|....*...
gi 530413549 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 530413549   1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK11880   3 KKIGFIGGGNMASAIIGGLLASGV-PAKDIIVSDPSPEKRA-ALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  81 EIGADIEDrhIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PRK11880  81 ELKGQLDK--LVVSIAAGVTLARLERLLGADLP---VVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549 161 EVE-EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATI 239
Cdd:PRK11880 156 WVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTI 235

                        250       260
                 ....*....|....*....|....*....
gi 530413549 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 530413549   47 KMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRpapRVIRCMTNTPV 126
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  127 VVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLG 206
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530413549  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 530413549   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK07679   4 QNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQELHQKYGVKGTHNKKELLTDANILFLAMKPKDVAEALI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  81 EIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PRK07679  84 PFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVP---IIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH 240
Cdd:PRK07679 161 VVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEA 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 530413549 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 530413549   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKmgvkltphNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PTZ00431   4 IRVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPSKKNTPFVYLQS--------NEELAKTCDIIVLAVKPDLAGKVLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  81 EIgADIEDRHIVVSCAAGVTISSIEKKLSAfrpAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PTZ00431  76 EI-KPYLGSKLLISICGGLNLKTLEEMVGV---EAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH 240
Cdd:PTZ00431 152 EIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGITIV 231

                        250       260
                 ....*....|....*....|....*...
gi 530413549 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 530413549  164 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALH 243
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 530413549  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 530413549   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK07680   1 MNIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  81 EIGADIEDRHIVVSCAAGVTISSIEKKLSAfrPAPRVIRCMTNTpvvVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PRK07680  81 KLAPHLTDEHCLVSITSPISVEQLETLVPC--QVARIIPSITNR---ALSGASLFTFGSRCSEEDQQKLERLFSNISTPL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKM-GLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATI 239
Cdd:PRK07680 156 VIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLASEMLIGMGKLLEKGLYTLPTLQEKVCVKGGITG 235

                        250
                 ....*....|....*...
gi 530413549 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 530413549    4 GFIGAGQLAFALAKGFTAAGvlaAHKIM-ASSPDMDLATVSAlRKMGVKLTP-HNKETVQHSDVLFLAVKPHIIPFILDE 81
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAG---PHEVVvANSRNPEKAEELA-EEYGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSE 76

                          90
                  ....*....|....*..
gi 530413549   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 530413549   3 VGFIGAGQLAFALAKGFTAAGVLAAHKIM--ASSPDMDLATVSAlRKMGVKLTPHNKETVQHSDVLFLAVKP-HIIPFIL 79
Cdd:PRK06928   4 IGFIGYGSMADMIATKLLETEVATPEEIIlySSSKNEHFNQLYD-KYPTVELADNEAEIFTKCDHSFICVPPlAVLPLLK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  80 DEIGADIEDRHIVvSCAAGVTISSIeKKLSAFRPAPRVIRCMTNtpvVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:PRK06928  83 DCAPVLTPDRHVV-SIAAGVSLDDL-LEITPGLQVSRLIPSLTS---AVGVGTSLVAHAETVNEANKSRLEETLSHFSHV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549 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 530413549   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHkIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK06476   1 MKIGFIGTGAITEAMVTGLLTSPADVSE-IIVSPRNAQIAARLAERFPKVRIAKDNQAVVDRSDVVFLAVRPQIAEEVLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549  81 EIGADieDRHIVVSCAAGVTISSIEKklsAFRPAPRVIRCMTNTPVVVREGAT-VYAtgTHAQVEDgrLMEQLLSSVGFC 159
Cdd:PRK06476  80 ALRFR--PGQTVISVIAATDRAALLE---WIGHDVKLVRAIPLPFVAERKGVTaIYP--PDPFVAA--LFDALGTAVECD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413549 160 TEVEEDLIDAVTGLSGSgpaYaFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHP-GQLKDNVSSPGGAT 238
Cdd:PRK06476 151 SEEEYDLLAAASALMAT---Y-FGILETATGWLEEQGLKRQKARAYLAPLFASLAQDAVRSTKTDfSALSREFSTKGGLN 226

                        250       260
                 ....*....|....*....|....*...
gi 530413549 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 530413549   3 VGFIGAGQLAFALAKGFTAAGvlaaHKIMASSPDMDLATvSALRKMGVKLTP-HNKETVQHSDVLFLAVKPHIIPFILDE 81
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAAG----HEVVIGSRDPEKAA-ALAAELGPGARAgTNAEAAAAADVVVLAVPYEAVPDVLES 75

                         90
                 ....*....|....*
gi 530413549  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 530413549   1 MSVGFIGAGQLAFALAKGFTAAG--VLAAHkimASSPDmdlATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFI 78
Cdd:COG5495    4 MKIGIIGAGRVGTALAAALRAAGheVVGVY---SRSPA---SAERAAALLGAVPALDLEELAAEADLVLLAVPDDAIAEV 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 530413549  79 LDEI---GADIEDrHIVVSCAAGVTISSIEKKLSA 110
Cdd:COG5495   78 AAGLaaaGALRPG-QLVVHTSGALGSDVLAPAARA 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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