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Conserved domains on  [gi|1060099122|ref|NP_001317452|]
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pyrroline-5-carboxylate reductase 1, mitochondrial isoform 6 [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]; ...
 1-214 1.48e-69

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: 213.39  E-value: 1.48e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvsALRKM-GVKLTPHNKETVQHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALAERyGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  80 DEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:COG0345    80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAP---VVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1060099122 160 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAA 214
Cdd:COG0345   157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAA 211
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-214 1.48e-69

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: 213.39  E-value: 1.48e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvsALRKM-GVKLTPHNKETVQHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALAERyGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  80 DEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:COG0345    80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAP---VVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1060099122 160 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAA 214
Cdd:COG0345   157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAA 211
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 1-214 2.31e-68

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 210.20  E-value: 2.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASsPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PLN02688    1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  81 EIGADIEDRHIVVSCAAGVTISSIEKKLsafrPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PLN02688   80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1060099122 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAA 214
Cdd:PLN02688  156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAA 209
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 47-214 4.25e-54

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: 173.21  E-value: 4.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  47 KMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRpapRVIRCMTNTPV 126
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122 127 VVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLG 206
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184


                  ....*...
gi 1060099122 207 AQALLGAA 214
Cdd:TIGR00112 185 AQTVKGAA 192
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 164-214 1.25e-19

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: 80.13  E-value: 1.25e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1060099122 164 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAA 214
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAA 51
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-214 1.48e-69

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: 213.39  E-value: 1.48e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvsALRKM-GVKLTPHNKETVQHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALAERyGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  80 DEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:COG0345    80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAP---VVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1060099122 160 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAA 214
Cdd:COG0345   157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAA 211
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 1-214 2.31e-68

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 210.20  E-value: 2.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASsPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PLN02688    1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  81 EIGADIEDRHIVVSCAAGVTISSIEKKLsafrPAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PLN02688   80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1060099122 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAA 214
Cdd:PLN02688  156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAA 209
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-214 1.83e-55

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 177.26  E-value: 1.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDLATvSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK11880    3 KKIGFIGGGNMASAIIGGLLASGV-PAKDIIVSDPSPEKRA-ALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  81 EIGADIEDrhIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PRK11880   81 ELKGQLDK--LVVSIAAGVTLARLERLLGADLP---VVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVV 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1060099122 161 EVE-EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAA 214
Cdd:PRK11880  156 WVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAA 210
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 47-214 4.25e-54

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: 173.21  E-value: 4.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  47 KMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRpapRVIRCMTNTPV 126
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122 127 VVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLG 206
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184


                  ....*...
gi 1060099122 207 AQALLGAA 214
Cdd:TIGR00112 185 AQTVKGAA 192
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 1-214 6.60e-36

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 127.58  E-value: 6.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK07679    4 QNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQELHQKYGVKGTHNKKELLTDANILFLAMKPKDVAEALI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  81 EIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPaprVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PRK07679   84 PFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVP---IIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1060099122 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAA 214
Cdd:PRK07679  161 VVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAA 214
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 1-216 1.12e-31

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 115.82  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKmgvkltphNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PTZ00431    4 IRVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPSKKNTPFVYLQS--------NEELAKTCDIIVLAVKPDLAGKVLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  81 EIgADIEDRHIVVSCAAGVTISSIEKKLSAfrpAPRVIRCMTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PTZ00431   76 EI-KPYLGSKLLISICGGLNLKTLEEMVGV---EAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQ 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1060099122 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGaAVH 216
Cdd:PTZ00431  152 EIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILG-SVH 206
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 164-214 1.25e-19

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: 80.13  E-value: 1.25e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1060099122 164 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAA 214
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAA 51
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
4-98 4.86e-19

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 78.43  E-value: 4.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   4 GFIGAGQLAFALAKGFTAAGvlaAHKIM-ASSPDMDLATVSAlRKMGVKLTP-HNKETVQHSDVLFLAVKPHIIPFILDE 81
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAG---PHEVVvANSRNPEKAEELA-EEYGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSE 76

                          90
                  ....*....|....*..
gi 1060099122  82 IgADIEDRHIVVSCAAG 98
Cdd:pfam03807  77 L-SDLLKGKIVISIAAG 92
PRK07680 PRK07680
late competence protein ComER; Validated
 1-212 3.09e-17

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 77.70  E-value: 3.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK07680    1 MNIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  81 EIGADIEDRHIVVSCAAGVTISSIEKKLSAfrPAPRVIRCMTNTpvvVREGATVYATGTHAQVEDGRLMEQLLSSVGFCT 160
Cdd:PRK07680   81 KLAPHLTDEHCLVSITSPISVEQLETLVPC--QVARIIPSITNR---ALSGASLFTFGSRCSEEDQQKLERLFSNISTPL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1060099122 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKM-GLPRRLAVRLGAQALLG 212
Cdd:PRK07680  156 VIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLASEMLIG 208
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 3-180 4.70e-10

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 57.86  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   3 VGFIGAGQLAFALAKGFTAAGVLAAHKIM--ASSPDMDLATVSAlRKMGVKLTPHNKETVQHSDVLFLAVKP-HIIPFIL 79
Cdd:PRK06928    4 IGFIGYGSMADMIATKLLETEVATPEEIIlySSSKNEHFNQLYD-KYPTVELADNEAEIFTKCDHSFICVPPlAVLPLLK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  80 DEIGADIEDRHiVVSCAAGVTISSIeKKLSAFRPAPRVIRCMTNtpvVVREGATVYATGTHAQVEDGRLMEQLLSSVGFC 159
Cdd:PRK06928   83 DCAPVLTPDRH-VVSIAAGVSLDDL-LEITPGLQVSRLIPSLTS---AVGVGTSLVAHAETVNEANKSRLEETLSHFSHV 157

                         170       180
                  ....*....|....*....|.
gi 1060099122 160 TEVEEDLIDAVTGLSGSGPAY 180
Cdd:PRK06928  158 MTIREENMDIASNLTSSSPGF 178
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 1-202 5.45e-09

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 54.64  E-value: 5.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHkIMASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD 80
Cdd:PRK06476    1 MKIGFIGTGAITEAMVTGLLTSPADVSE-IIVSPRNAQIAARLAERFPKVRIAKDNQAVVDRSDVVFLAVRPQIAEEVLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122  81 EIGADieDRHIVVSCAAGVTISSIEKklsAFRPAPRVIRCMTNTPVVVREGAT-VYAtgTHAQVEDgrLMEQLLSSVGFC 159
Cdd:PRK06476   80 ALRFR--PGQTVISVIAATDRAALLE---WIGHDVKLVRAIPLPFVAERKGVTaIYP--PDPFVAA--LFDALGTAVECD 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1060099122 160 TEVEEDLIDAVTGLSGSgpaYaFTALDALADGGVKMGLPRRLA 202
Cdd:PRK06476  151 SEEEYDLLAAASALMAT---Y-FGILETATGWLEEQGLKRQKA 189
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
3-96 6.41e-06

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 45.16  E-value: 6.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   3 VGFIGAGQLAFALAKGFTAAGvlaaHKIMASSPDMDLATvSALRKMGVKLTP-HNKETVQHSDVLFLAVKPHIIPFILDE 81
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAG----HEVVIGSRDPEKAA-ALAAELGPGARAgTNAEAAAAADVVVLAVPYEAVPDVLES 75

                          90
                  ....*....|....*
gi 1060099122  82 IGADIEDRhIVVSCA 96
Cdd:COG2085    76 LGDALAGK-IVIDAT 89
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-110 2.26e-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: 40.95  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099122   1 MSVGFIGAGQLAFALAKGFTAAG--VLAAHkimASSPDmdlATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFI 78
Cdd:COG5495     4 MKIGIIGAGRVGTALAAALRAAGheVVGVY---SRSPA---SAERAAALLGAVPALDLEELAAEADLVLLAVPDDAIAEV 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1060099122  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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