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Conserved domains on  [gi|19115618|ref|NP_594706|]
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delta-1-pyrroline-5-carboxylate reductase [Schizosaccharomyces pombe]

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]; ...
 5-282 1.97e-87

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: 261.54  E-value: 1.97e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   5 CVLGCGTMGKALLTGIFDSIAEngndvsdeiiiPNKFYACVKFPKEKEDVQKLFGDRVkvvmgAKENAEMAAISNVLLLS 84
Cdd:COG0345   6 GFIGAGNMGSAIIKGLLKSGVP-----------PEDIIVSDRSPERLEALAERYGVRV-----TTDNAEAAAQADVVVLA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618  85 CKPQAAEDVLnsPKMKEAL-KGKLILSILAGKTISSLQSMLDESTRVIRIMPNTASRIRESMSVICPGPNATEEDIKFAE 163
Cdd:COG0345  70 VKPQDLAEVL--EELAPLLdPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVE 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618 164 WVFNGIGRSMKLPEKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTGRMVLQ-GQHPAMIRND 242
Cdd:COG0345 148 ALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLEsGEHPAELRDR 227

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 19115618 243 VSTPAGCTISGLLALEDGKIRSTIARGIEQATKTASGLGK 282
Cdd:COG0345 228 VTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKELGK 267
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 5-282 1.97e-87

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: 261.54  E-value: 1.97e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   5 CVLGCGTMGKALLTGIFDSIAEngndvsdeiiiPNKFYACVKFPKEKEDVQKLFGDRVkvvmgAKENAEMAAISNVLLLS 84
Cdd:COG0345   6 GFIGAGNMGSAIIKGLLKSGVP-----------PEDIIVSDRSPERLEALAERYGVRV-----TTDNAEAAAQADVVVLA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618  85 CKPQAAEDVLnsPKMKEAL-KGKLILSILAGKTISSLQSMLDESTRVIRIMPNTASRIRESMSVICPGPNATEEDIKFAE 163
Cdd:COG0345  70 VKPQDLAEVL--EELAPLLdPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVE 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618 164 WVFNGIGRSMKLPEKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTGRMVLQ-GQHPAMIRND 242
Cdd:COG0345 148 ALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLEsGEHPAELRDR 227

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 19115618 243 VSTPAGCTISGLLALEDGKIRSTIARGIEQATKTASGLGK 282
Cdd:COG0345 228 VTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKELGK 267
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 68-278 1.02e-76

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: 233.31  E-value: 1.02e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618    68 AKENAEMAAISNVLLLSCKPQAAEDVLNSPKMkEALKGKLILSILAGKTISSLQSMLDESTRVIRIMPNTASRIRESMSV 147
Cdd:TIGR00112  34 SSDAQEAVKEADVVFLAVKPQDLEEVLSELKS-EKGKDKLLISIAAGVTLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   148 ICPGPNATEEDIKFAEWVFNGIGRSMKLPEKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTG 227
Cdd:TIGR00112 113 IAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELAAQTVKGAA 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19115618   228 RMVLQ-GQHPAMIRNDVSTPAGCTISGLLALEDGKIRSTIARGIEQATKTAS 278
Cdd:TIGR00112 193 KLLEEsGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSR 244
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-282 9.32e-76

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 231.57  E-value: 9.32e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618    1 MSGFCVLGCGTMGKALLTGIfdsiAENGNDVSDEIII-PNkfyacvkfPKEKEDVQKLFGDRVkvvmgAKENAEMAAISN 79
Cdd:PRK11880   2 MKKIGFIGGGNMASAIIGGL----LASGVPAKDIIVSdPS--------PEKRAALAEEYGVRA-----ATDNQEAAQEAD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   80 VLLLSCKPQAAEDVLnsPKMKEALKgKLILSILAGKTISSLQSMLDESTRVIRIMPNTASRIRESMSVICPGPNATEEDI 159
Cdd:PRK11880  65 VVVLAVKPQVMEEVL--SELKGQLD-KLVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618  160 KFAEWVFNGIGRSMKLP-EKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTGRMVLQ-GQHPA 237
Cdd:PRK11880 142 ELVENLLSAFGKVVWVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLEsGEHPA 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 19115618  238 MIRNDVSTPAGCTISGLLALEDGKIRSTIARGIEQATKTASGLGK 282
Cdd:PRK11880 222 ELRDNVTSPGGTTIAALRVLEEKGLRAAVIEAVQAAAKRSKELGK 266
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 177-275 2.35e-43

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: 143.31  E-value: 2.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   177 EKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTGRMVLQGQ-HPAMIRNDVSTPAGCTISGLL 255
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGeHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|
gi 19115618   256 ALEDGKIRSTIARGIEQATK 275
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATK 100
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 5-282 1.97e-87

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: 261.54  E-value: 1.97e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   5 CVLGCGTMGKALLTGIFDSIAEngndvsdeiiiPNKFYACVKFPKEKEDVQKLFGDRVkvvmgAKENAEMAAISNVLLLS 84
Cdd:COG0345   6 GFIGAGNMGSAIIKGLLKSGVP-----------PEDIIVSDRSPERLEALAERYGVRV-----TTDNAEAAAQADVVVLA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618  85 CKPQAAEDVLnsPKMKEAL-KGKLILSILAGKTISSLQSMLDESTRVIRIMPNTASRIRESMSVICPGPNATEEDIKFAE 163
Cdd:COG0345  70 VKPQDLAEVL--EELAPLLdPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVE 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618 164 WVFNGIGRSMKLPEKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTGRMVLQ-GQHPAMIRND 242
Cdd:COG0345 148 ALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLEsGEHPAELRDR 227

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 19115618 243 VSTPAGCTISGLLALEDGKIRSTIARGIEQATKTASGLGK 282
Cdd:COG0345 228 VTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKELGK 267
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 68-278 1.02e-76

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: 233.31  E-value: 1.02e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618    68 AKENAEMAAISNVLLLSCKPQAAEDVLNSPKMkEALKGKLILSILAGKTISSLQSMLDESTRVIRIMPNTASRIRESMSV 147
Cdd:TIGR00112  34 SSDAQEAVKEADVVFLAVKPQDLEEVLSELKS-EKGKDKLLISIAAGVTLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   148 ICPGPNATEEDIKFAEWVFNGIGRSMKLPEKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTG 227
Cdd:TIGR00112 113 IAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELAAQTVKGAA 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19115618   228 RMVLQ-GQHPAMIRNDVSTPAGCTISGLLALEDGKIRSTIARGIEQATKTAS 278
Cdd:TIGR00112 193 KLLEEsGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSR 244
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-282 9.32e-76

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 231.57  E-value: 9.32e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618    1 MSGFCVLGCGTMGKALLTGIfdsiAENGNDVSDEIII-PNkfyacvkfPKEKEDVQKLFGDRVkvvmgAKENAEMAAISN 79
Cdd:PRK11880   2 MKKIGFIGGGNMASAIIGGL----LASGVPAKDIIVSdPS--------PEKRAALAEEYGVRA-----ATDNQEAAQEAD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   80 VLLLSCKPQAAEDVLnsPKMKEALKgKLILSILAGKTISSLQSMLDESTRVIRIMPNTASRIRESMSVICPGPNATEEDI 159
Cdd:PRK11880  65 VVVLAVKPQVMEEVL--SELKGQLD-KLVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618  160 KFAEWVFNGIGRSMKLP-EKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTGRMVLQ-GQHPA 237
Cdd:PRK11880 142 ELVENLLSAFGKVVWVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLEsGEHPA 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 19115618  238 MIRNDVSTPAGCTISGLLALEDGKIRSTIARGIEQATKTASGLGK 282
Cdd:PRK11880 222 ELRDNVTSPGGTTIAALRVLEEKGLRAAVIEAVQAAAKRSKELGK 266
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 3-282 2.79e-67

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 210.20  E-value: 2.79e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618    3 GFcvLGCGTMGKALLTGIfdsiaengndVSDEIIIPNKFYACVKFPKEKEDVQKLFGdrVKVvmgAKENAEMAAISNVLL 82
Cdd:PLN02688   4 GF--IGAGKMAEAIARGL----------VASGVVPPSRISTADDSNPARRDVFQSLG--VKT---AASNTEVVKSSDVII 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   83 LSCKPQAAEDVLNSPKMKEaLKGKLILSILAGKTISSLQSMLDEStRVIRIMPNTASRIRESMSVICPGPNATEEDIKFA 162
Cdd:PLN02688  67 LAVKPQVVKDVLTELRPLL-SKDKLLVSVAAGITLADLQEWAGGR-RVVRVMPNTPCLVGEAASVMSLGPAATADDRDLV 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618  163 EWVFNGIGRSMKLPEKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTGRMVLQ-GQHPAMIRN 241
Cdd:PLN02688 145 ATLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLEtGKHPGQLKD 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 19115618  242 DVSTPAGCTISGLLALEDGKIRSTIARGIEQATKTASGLGK 282
Cdd:PLN02688 225 MVTSPGGTTIAGVHELEKGGFRAALMNAVVAAAKRSRELSK 265
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 177-275 2.35e-43

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: 143.31  E-value: 2.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   177 EKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTGRMVLQGQ-HPAMIRNDVSTPAGCTISGLL 255
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGeHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|
gi 19115618   256 ALEDGKIRSTIARGIEQATK 275
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATK 100
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 7-282 7.27e-39

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 137.21  E-value: 7.27e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618    7 LGCGTMGKALLTGIFDSIAENGNdvsdEIIIPNKfyacvKFPKEKEDVQKLFGdrvkvVMGAKENAEMAAISNVLLLSCK 86
Cdd:PRK07679   9 LGAGSIAEAIIGGLLHANVVKGE----QITVSNR-----SNETRLQELHQKYG-----VKGTHNKKELLTDANILFLAMK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   87 PQAAEDVLNSpkMKEALKG-KLILSILAGKTISSLQSMLDESTRVIRIMPNTASRIRESMSVICPGPNATEEDIKFAEWV 165
Cdd:PRK07679  75 PKDVAEALIP--FKEYIHNnQLIISLLAGVSTHSIRNLLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQTAKAL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618  166 FNGIGRSMKLPEKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTGRMVLQG-QHPAMIRNDVS 244
Cdd:PRK07679 153 FETIGLVSVVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASeKHPSILRKEIT 232

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 19115618  245 TPAGCTISGLLALEDGKIRSTIARGIEQATKTASGLGK 282
Cdd:PRK07679 233 SPGGTTEAGIEVLQEHRFQQALISCITQATQRSHNLGK 270
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 3-281 8.56e-37

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 131.61  E-value: 8.56e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618    3 GFcvLGCGTMGKALLTGIfdsiaENGNDVSDEiiipNKFYacvkFPKEKEDVQKLFgdrvkvvmgAKENAEMAAISNVLL 82
Cdd:PTZ00431   7 GF--IGLGKMGSALAYGI-----ENSNIIGKE----NIYY----HTPSKKNTPFVY---------LQSNEELAKTCDIIV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   83 LSCKPQAAEDVLNspKMKEALKGKLILSILAGKTISSLQSMLDESTRVIRIMPNTASRIRESMSVICPGPNATEEDIKFA 162
Cdd:PTZ00431  63 LAVKPDLAGKVLL--EIKPYLGSKLLISICGGLNLKTLEEMVGVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKV 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618  163 EWVFNGIGRSMKLPEKLIDAATAVCGSGPAFVATMIEAMTDGGVMMGIPFPQAQELAAQTMVGTGRMVLQGQHPA-MIRN 241
Cdd:PTZ00431 141 IDIFSACGIIQEIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVqQLKD 220

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 19115618  242 DVSTPAGCTISGLLALEDGKIRSTIARGIEQATKTASGLG 281
Cdd:PTZ00431 221 DVCSPGGITIVGLYTLEKHAFKYTVMDAVESACQKSKSMH 260
PRK07680 PRK07680
late competence protein ComER; Validated
 6-260 1.53e-11

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 63.07  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618    6 VLGCGTMGKALLtgifDSIAENGNDVSDEIIIPNKFYAcvkfpKEKEDVQKLFGDRVkvvmgAKENAEMAAISNVLLLSC 85
Cdd:PRK07680   5 FIGTGNMGTILI----EAFLESGAVKPSQLTITNRTPA-----KAYHIKERYPGIHV-----AKTIEEVISQSDLIFICV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   86 KPQAAEDVLNspKMKEAL-KGKLILSILAGKTISSLQSMLDesTRVIRIMPNTASRIRESMSVICPGPNATEEDIKFAEW 164
Cdd:PRK07680  71 KPLDIYPLLQ--KLAPHLtDEHCLVSITSPISVEQLETLVP--CQVARIIPSITNRALSGASLFTFGSRCSEEDQQKLER 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618  165 VFNGIGRSMKLPEKLIDAATAVCGSGPAFVATMIEAMTDGGV-MMGIPFPQAQELAAQTMVGTGRMVLQGQH-PAMIRND 242
Cdd:PRK07680 147 LFSNISTPLVIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVeETNISKEEATTLASEMLIGMGKLLEKGLYtLPTLQEK 226

                        250
                 ....*....|....*...
gi 19115618  243 VSTPAGCTISGLLALEDG 260
Cdd:PRK07680 227 VCVKGGITGEGIKVLEEE 244
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
5-114 2.59e-10

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 56.09  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618     5 CVLGCGTMGKALLTGIfdsiAENGndvSDEIIIpnkfyACVKFPKEKEDVQKLFGDRVKVVmgakENAEMAAISNVLLLS 84
Cdd:pfam03807   1 GFIGAGNMGEALARGL----VAAG---PHEVVV-----ANSRNPEKAEELAEEYGVGATAV----DNEEAAEEADVVFLA 64

                          90       100       110
                  ....*....|....*....|....*....|
gi 19115618    85 CKPQAAEDVLNSpkMKEALKGKLILSILAG 114
Cdd:pfam03807  65 VKPEDAPDVLSE--LSDLLKGKIVISIAAG 92
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 3-248 9.17e-10

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 57.72  E-value: 9.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618    3 GFcvLGCGTMGKALLTGIFDSiaenGNDVSdEIIIPnkfyacvkfPKEKEDVQKLFGDRVKVVMgAKENAEMAAISNVLL 82
Cdd:PRK06476   4 GF--IGTGAITEAMVTGLLTS----PADVS-EIIVS---------PRNAQIAARLAERFPKVRI-AKDNQAVVDRSDVVF 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   83 LSCKPQAAEDVLNSPKMKealKGKLILSILAGKTISSLQSMLDESTRVIRIMPNTASRIRESMSVICPgPNateediKFA 162
Cdd:PRK06476  67 LAVRPQIAEEVLRALRFR---PGQTVISVIAATDRAALLEWIGHDVKLVRAIPLPFVAERKGVTAIYP-PD------PFV 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618  163 EWVFNGIGRSMKLPEK----LIDAATAVCGSGPAFvatmIEAMTDGGVMMGIPFPQAQELAAQTMVG-TGRMVLQGQHP- 236
Cdd:PRK06476 137 AALFDALGTAVECDSEeeydLLAAASALMATYFGI----LETATGWLEEQGLKRQKARAYLAPLFASlAQDAVRSTKTDf 212

                        250
                 ....*....|..
gi 19115618  237 AMIRNDVSTPAG 248
Cdd:PRK06476 213 SALSREFSTKGG 224
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 1-206 3.43e-05

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 44.37  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618    1 MSGFCVLGCGTMGKALLTGIFdsiaENGNDVSDEIIIpnkfyacvkFPKEKEDVQKLFGDRVKVVMGAKENAEMAAISNV 80
Cdd:PRK06928   1 MEKIGFIGYGSMADMIATKLL----ETEVATPEEIIL---------YSSSKNEHFNQLYDKYPTVELADNEAEIFTKCDH 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115618   81 LLLsCKPQAAedVLnsPKMKE----ALKGKLILSILAGKTISSLqsmLDEST--RVIRIMPNTASRIRESMSVICPGPNA 154
Cdd:PRK06928  68 SFI-CVPPLA--VL--PLLKDcapvLTPDRHVVSIAAGVSLDDL---LEITPglQVSRLIPSLTSAVGVGTSLVAHAETV 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19115618  155 TEEDIKFAEWVFNGIGRSMKLPEKLIDAATAVCGSGPAFVATMIEAMTDGGV 206
Cdd:PRK06928 140 NEANKSRLEETLSHFSHVMTIREENMDIASNLTSSSPGFIAAIFEEFAEAAV 191
 
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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