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Conserved domains on  [gi|500046586|ref|WP_011727304|]
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pyrroline-5-carboxylate reductase [Mycolicibacterium smegmatis]

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]; ...
 1-282 1.27e-97

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: 287.34  E-value: 1.27e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   1 MSRIAIIGGGSMGEALLSGLLRAGRQVKDMVVAEKFPERAKYLADKYSVRVT-SVADAAENAHYVVVAVKPADVEKVIGE 79
Cdd:COG0345    2 SMKIGFIGAGNMGSAIIKGLLKSGVPPEDIIVSDRSPERLEALAERYGVRVTtDNAEAAAQADVVVLAVKPQDLAEVLEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  80 IAEAAanaetdTAEQVFVTIAAGVGTAYYEAKLPAGSPVIRVMPNAPVIVGGGVSALAPGRFATPEQLKEVSTLFDAVGG 159
Cdd:COG0345   82 LAPLL------DPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586 160 VITVSESQLDAVTALSGSGPAYFFLMAEAMVDAGVAVGLSRAVATDLVAQTMAGSAAMLLDRldqvnaaggaalDTTPAQ 239
Cdd:COG0345  156 VVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLES------------GEHPAE 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 500046586 240 LRATVTSPAGTTAAGLRELERGGLRAAVANAVEAAKTRSEQLG 282
Cdd:COG0345  224 LRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKELG 266
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-282 1.27e-97

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: 287.34  E-value: 1.27e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   1 MSRIAIIGGGSMGEALLSGLLRAGRQVKDMVVAEKFPERAKYLADKYSVRVT-SVADAAENAHYVVVAVKPADVEKVIGE 79
Cdd:COG0345    2 SMKIGFIGAGNMGSAIIKGLLKSGVPPEDIIVSDRSPERLEALAERYGVRVTtDNAEAAAQADVVVLAVKPQDLAEVLEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  80 IAEAAanaetdTAEQVFVTIAAGVGTAYYEAKLPAGSPVIRVMPNAPVIVGGGVSALAPGRFATPEQLKEVSTLFDAVGG 159
Cdd:COG0345   82 LAPLL------DPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586 160 VITVSESQLDAVTALSGSGPAYFFLMAEAMVDAGVAVGLSRAVATDLVAQTMAGSAAMLLDRldqvnaaggaalDTTPAQ 239
Cdd:COG0345  156 VVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLES------------GEHPAE 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 500046586 240 LRATVTSPAGTTAAGLRELERGGLRAAVANAVEAAKTRSEQLG 282
Cdd:COG0345  224 LRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKELG 266
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-282 1.15e-96

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 285.12  E-value: 1.15e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   1 MSRIAIIGGGSMGEALLSGLLRAGRQVKDMVVAEKFPERAKYLADKYSVRVT-SVADAAENAHYVVVAVKPADVEKVIge 79
Cdd:PRK11880   2 MKKIGFIGGGNMASAIIGGLLASGVPAKDIIVSDPSPEKRAALAEEYGVRAAtDNQEAAQEADVVVLAVKPQVMEEVL-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  80 iaeaaaNAETDTAEQVFVTIAAGVGTAYYEAKLPAGSPVIRVMPNAPVIVGGGVSALAPGRFATPEQLKEVSTLFDAVGG 159
Cdd:PRK11880  80 ------SELKGQLDKLVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586 160 VITV-SESQLDAVTALSGSGPAYFFLMAEAMVDAGVAVGLSRAVATDLVAQTMAGSAAMLLDRldqvnaaggaalDTTPA 238
Cdd:PRK11880 154 VVWVdDEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLES------------GEHPA 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 500046586 239 QLRATVTSPAGTTAAGLRELERGGLRAAVANAVEAAKTRSEQLG 282
Cdd:PRK11880 222 ELRDNVTSPGGTTIAALRVLEEKGLRAAVIEAVQAAAKRSKELG 265
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 20-264 6.17e-71

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: 219.05  E-value: 6.17e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   20 LLRAGRQVKDMVVAEKFPERAKYLADKYSVRVTS-VADAAENAHYVVVAVKPADVEKVIGEIAEAaanaetDTAEQVFVT 98
Cdd:TIGR00112   2 LKAGALAPYDIYVINRSPEKLAALAKELGIVASSdAQEAVKEADVVFLAVKPQDLEEVLSELKSE------KGKDKLLIS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   99 IAAGVGTAYYEAKLPAGSPVIRVMPNAPVIVGGGVSALAPGRFATPEQLKEVSTLFDAVGGVITVSESQLDAVTALSGSG 178
Cdd:TIGR00112  76 IAAGVTLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  179 PAYFFLMAEAMVDAGVAVGLSRAVATDLVAQTMAGSAAMLLDRldqvnaaggaalDTTPAQLRATVTSPAGTTAAGLREL 258
Cdd:TIGR00112 156 PAYVFLFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEES------------GEHPALLKDQVTSPGGTTIAGLAVL 223


                  ....*.
gi 500046586  259 ERGGLR 264
Cdd:TIGR00112 224 EEKGVR 229
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 165-264 4.82e-37

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: 127.13  E-value: 4.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  165 ESQLDAVTALSGSGPAYFFLMAEAMVDAGVAVGLSRAVATDLVAQTMAGSAAMLLDRldqvnaaggaalDTTPAQLRATV 244
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTS------------GEHPAELRDKV 68

                          90       100
                  ....*....|....*....|
gi 500046586  245 TSPAGTTAAGLRELERGGLR 264
Cdd:pfam14748  69 TSPGGTTIAGLAVLEEGGFR 88
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 3-68 1.10e-04

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 43.02  E-value: 1.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500046586   3 RIAIIGGGSMGEALLSGLLRAGrqVKDMVVAEKFPERAKYLADKYSVRVTSVADAAENAHYVVVAV 68
Cdd:cd05213  180 KVLVIGAGEMGELAAKHLAAKG--VAEITIANRTYERAEELAKELGGNAVPLDELLELLNEADVVI 243
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-282 1.27e-97

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: 287.34  E-value: 1.27e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   1 MSRIAIIGGGSMGEALLSGLLRAGRQVKDMVVAEKFPERAKYLADKYSVRVT-SVADAAENAHYVVVAVKPADVEKVIGE 79
Cdd:COG0345    2 SMKIGFIGAGNMGSAIIKGLLKSGVPPEDIIVSDRSPERLEALAERYGVRVTtDNAEAAAQADVVVLAVKPQDLAEVLEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  80 IAEAAanaetdTAEQVFVTIAAGVGTAYYEAKLPAGSPVIRVMPNAPVIVGGGVSALAPGRFATPEQLKEVSTLFDAVGG 159
Cdd:COG0345   82 LAPLL------DPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586 160 VITVSESQLDAVTALSGSGPAYFFLMAEAMVDAGVAVGLSRAVATDLVAQTMAGSAAMLLDRldqvnaaggaalDTTPAQ 239
Cdd:COG0345  156 VVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLES------------GEHPAE 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 500046586 240 LRATVTSPAGTTAAGLRELERGGLRAAVANAVEAAKTRSEQLG 282
Cdd:COG0345  224 LRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKELG 266
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-282 1.15e-96

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 285.12  E-value: 1.15e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   1 MSRIAIIGGGSMGEALLSGLLRAGRQVKDMVVAEKFPERAKYLADKYSVRVT-SVADAAENAHYVVVAVKPADVEKVIge 79
Cdd:PRK11880   2 MKKIGFIGGGNMASAIIGGLLASGVPAKDIIVSDPSPEKRAALAEEYGVRAAtDNQEAAQEADVVVLAVKPQVMEEVL-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  80 iaeaaaNAETDTAEQVFVTIAAGVGTAYYEAKLPAGSPVIRVMPNAPVIVGGGVSALAPGRFATPEQLKEVSTLFDAVGG 159
Cdd:PRK11880  80 ------SELKGQLDKLVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586 160 VITV-SESQLDAVTALSGSGPAYFFLMAEAMVDAGVAVGLSRAVATDLVAQTMAGSAAMLLDRldqvnaaggaalDTTPA 238
Cdd:PRK11880 154 VVWVdDEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLES------------GEHPA 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 500046586 239 QLRATVTSPAGTTAAGLRELERGGLRAAVANAVEAAKTRSEQLG 282
Cdd:PRK11880 222 ELRDNVTSPGGTTIAALRVLEEKGLRAAVIEAVQAAAKRSKELG 265
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 20-264 6.17e-71

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: 219.05  E-value: 6.17e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   20 LLRAGRQVKDMVVAEKFPERAKYLADKYSVRVTS-VADAAENAHYVVVAVKPADVEKVIGEIAEAaanaetDTAEQVFVT 98
Cdd:TIGR00112   2 LKAGALAPYDIYVINRSPEKLAALAKELGIVASSdAQEAVKEADVVFLAVKPQDLEEVLSELKSE------KGKDKLLIS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   99 IAAGVGTAYYEAKLPAGSPVIRVMPNAPVIVGGGVSALAPGRFATPEQLKEVSTLFDAVGGVITVSESQLDAVTALSGSG 178
Cdd:TIGR00112  76 IAAGVTLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  179 PAYFFLMAEAMVDAGVAVGLSRAVATDLVAQTMAGSAAMLLDRldqvnaaggaalDTTPAQLRATVTSPAGTTAAGLREL 258
Cdd:TIGR00112 156 PAYVFLFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEES------------GEHPALLKDQVTSPGGTTIAGLAVL 223


                  ....*.
gi 500046586  259 ERGGLR 264
Cdd:TIGR00112 224 EEKGVR 229
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 2-282 2.82e-64

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 202.49  E-value: 2.82e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   2 SRIAIIGGGSMGEALLSGLLRAGRQV-KDMVVAEKFPERAKYLADKYSVRVT-SVADAAENAHYVVVAVKPADVEKVIGE 79
Cdd:PLN02688   1 FRVGFIGAGKMAEAIARGLVASGVVPpSRISTADDSNPARRDVFQSLGVKTAaSNTEVVKSSDVIILAVKPQVVKDVLTE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  80 IAEAAanaetdTAEQVFVTIAAGVGTAYYEAKLPaGSPVIRVMPNAPVIVGGGVSALAPGRFATPEQLKEVSTLFDAVGG 159
Cdd:PLN02688  81 LRPLL------SKDKLLVSVAAGITLADLQEWAG-GRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586 160 VITVSESQLDAVTALSGSGPAYFFLMAEAMVDAGVAVGLSRAVATDLVAQTMAGSAAMLLDRldqvnaaggaalDTTPAQ 239
Cdd:PLN02688 154 IWVVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLET------------GKHPGQ 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 500046586 240 LRATVTSPAGTTAAGLRELERGGLRAAVANAVEAAKTRSEQLG 282
Cdd:PLN02688 222 LKDMVTSPGGTTIAGVHELEKGGFRAALMNAVVAAAKRSRELS 264
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 4-284 7.73e-53

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 173.80  E-value: 7.73e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   4 IAIIGGGSMGEALLSGLLRAGR-QVKDMVVAEKFPE-RAKYLADKYSVRVT-SVADAAENAHYVVVAVKPADVEKVIgei 80
Cdd:PRK07679   6 ISFLGAGSIAEAIIGGLLHANVvKGEQITVSNRSNEtRLQELHQKYGVKGThNKKELLTDANILFLAMKPKDVAEAL--- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  81 aeaAANAETDTAEQVFVTIAAGVGTAYYEAKLPAGSPVIRVMPNAPVIVGGGVSALAPGRFATPEQLKEVSTLFDAVGGV 160
Cdd:PRK07679  83 ---IPFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586 161 ITVSESQLDAVTALSGSGPAYFFLMAEAMVDAGVAVGLSRAVATDLVAQTMAGSAAMLldrldqvnaaggAALDTTPAQL 240
Cdd:PRK07679 160 SVVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEML------------KASEKHPSIL 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 500046586 241 RATVTSPAGTTAAGLRELERGGLRAAVANAVEAAKTRSEQLGIT 284
Cdd:PRK07679 228 RKEITSPGGTTEAGIEVLQEHRFQQALISCITQATQRSHNLGKT 271
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 165-264 4.82e-37

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: 127.13  E-value: 4.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  165 ESQLDAVTALSGSGPAYFFLMAEAMVDAGVAVGLSRAVATDLVAQTMAGSAAMLLDRldqvnaaggaalDTTPAQLRATV 244
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTS------------GEHPAELRDKV 68

                          90       100
                  ....*....|....*....|
gi 500046586  245 TSPAGTTAAGLRELERGGLR 264
Cdd:pfam14748  69 TSPGGTTIAGLAVLEEGGFR 88
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 3-264 2.26e-32

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 120.06  E-value: 2.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   3 RIAIIGGGSMGEALLSGLLRAgrqvkDMVVAEKFPERAKYLADKYSVRVTSVADAAENAHYVVVAVKPADVEKVIGEIAE 82
Cdd:PTZ00431   5 RVGFIGLGKMGSALAYGIENS-----NIIGKENIYYHTPSKKNTPFVYLQSNEELAKTCDIIVLAVKPDLAGKVLLEIKP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  83 AAanaetdtAEQVFVTIAAGVGTAYYEAKLPAGSPVIRVMPNAPVIVGGGVSALAPGRFATPEQLKEVSTLFDAVGGVIT 162
Cdd:PTZ00431  80 YL-------GSKLLISICGGLNLKTLEEMVGVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586 163 VSESQLDAVTALSGSGPAYFFLMAEAMVDAGVAVGLSRAVATDLVAQTMAGSAAMLldrldqvnaaggAALDTTPAQLRA 242
Cdd:PTZ00431 153 IKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMV------------KASDQPVQQLKD 220

                        250       260
                 ....*....|....*....|..
gi 500046586 243 TVTSPAGTTAAGLRELERGGLR 264
Cdd:PTZ00431 221 DVCSPGGITIVGLYTLEKHAFK 242
PRK07680 PRK07680
late competence protein ComER; Validated
 3-261 8.93e-22

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 91.96  E-value: 8.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   3 RIAIIGGGSMGEALLSGLLRAGR-QVKDMVVAEKFPERAKYLADKY-SVRVT-SVADAAENAHYVVVAVKPADVEKVIGE 79
Cdd:PRK07680   2 NIGFIGTGNMGTILIEAFLESGAvKPSQLTITNRTPAKAYHIKERYpGIHVAkTIEEVISQSDLIFICVKPLDIYPLLQK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  80 IAEAAanaetdTAEQVFVTIAAGVGTAYYEAKLPagSPVIRVMPNAPVIVGGGVSALAPGRFATPEQLKEVSTLFDAVGG 159
Cdd:PRK07680  82 LAPHL------TDEHCLVSITSPISVEQLETLVP--CQVARIIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNIST 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586 160 VITVSESQLDAVTALSGSGPAYFFLMAEAMVDAGVA-VGLSRAVATDLVAQTMAGSAAMLLDRLdqvnaaggaaldTTPA 238
Cdd:PRK07680 154 PLVIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEeTNISKEEATTLASEMLIGMGKLLEKGL------------YTLP 221

                        250       260
                 ....*....|....*....|...
gi 500046586 239 QLRATVTSPAGTTAAGLRELERG 261
Cdd:PRK07680 222 TLQEKVCVKGGITGEGIKVLEEE 244
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
5-102 9.65e-14

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 65.33  E-value: 9.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586    5 AIIGGGSMGEALLSGLLRAGRQvKDMVVAEKFPERAKYLADKYSVRVT--SVADAAENAHYVVVAVKPADVEKVIGEIAE 82
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPH-EVVVANSRNPEKAEELAEEYGVGATavDNEEAAEEADVVFLAVKPEDAPDVLSELSD 79

                          90       100
                  ....*....|....*....|
gi 500046586   83 aaanaetDTAEQVFVTIAAG 102
Cdd:pfam03807  80 -------LLKGKIVISIAAG 92
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 1-254 1.22e-13

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 69.41  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   1 MSRIAIIGGGSMGEALLSGLLRAGRQVKD--MVVAEKFPERAKYLADKYSVrvTSVADAAEN----AHYVVVAVKPADVE 74
Cdd:PRK06928   1 MEKIGFIGYGSMADMIATKLLETEVATPEeiILYSSSKNEHFNQLYDKYPT--VELADNEAEiftkCDHSFICVPPLAVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  75 KVIGEIAEAAanaetdTAEQVFVTIAAGVGTAYYeAKLPAGSPVIRVMPNAPVIVGGGVSALAPGRFATPEQLKEVSTLF 154
Cdd:PRK06928  79 PLLKDCAPVL------TPDRHVVSIAAGVSLDDL-LEITPGLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586 155 DAVGGVITVSESQLDAVTALSGSGPAYFFLMAEAMVDAGVA-VGLSRAVATDLVAQTMAGSAAMLLDRldqvnaaggaal 233
Cdd:PRK06928 152 SHFSHVMTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRnSSLSDEEAFQFLNFALAGTGKLLVEE------------ 219

                        250       260
                 ....*....|....*....|.
gi 500046586 234 DTTPAQLRATVTSPAGTTAAG 254
Cdd:PRK06928 220 DYTFSGTIERVATKGGITAEG 240
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 3-262 2.68e-10

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 59.65  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   3 RIAIIGGGSMGEALLSGLLRAGRQVKDMVVAEKFPERAKYLADKY-SVRVT----SVADAAEnahYVVVAVKPADVEKVI 77
Cdd:PRK06476   2 KIGFIGTGAITEAMVTGLLTSPADVSEIIVSPRNAQIAARLAERFpKVRIAkdnqAVVDRSD---VVFLAVRPQIAEEVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586  78 GEIaeaaanaeTDTAEQVFVTIAAGVGTAYYEAKLPAGSPVIRVMPNAPVIVGGGVSALAPGRfatpeqlKEVSTLFDAV 157
Cdd:PRK06476  79 RAL--------RFRPGQTVISVIAATDRAALLEWIGHDVKLVRAIPLPFVAERKGVTAIYPPD-------PFVAALFDAL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586 158 GGVITV-SESQLDAVTALSGSGPAYFFLMaEAMVDAGVAVGLSRAVATDLVaqtmagsaAMLLDRLDQVNAAGGAaldTT 236
Cdd:PRK06476 144 GTAVECdSEEEYDLLAAASALMATYFGIL-ETATGWLEEQGLKRQKARAYL--------APLFASLAQDAVRSTK---TD 211

                        250       260
                 ....*....|....*....|....*.
gi 500046586 237 PAQLRATVTSPAGTTAAGLRELERGG 262
Cdd:PRK06476 212 FSALSREFSTKGGLNEQVLNDFSRQG 237
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
4-77 1.50e-07

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 50.55  E-value: 1.50e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500046586   4 IAIIGGGSMGEALLSGLLRAGRQVkdmVVAEKFPERAKYLADKY--SVRVTSVADAAENAHYVVVAVKPADVEKVI 77
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAAGHEV---VIGSRDPEKAAALAAELgpGARAGTNAEAAAAADVVVLAVPYEAVPDVL 73
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 3-77 6.97e-05

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 43.63  E-value: 6.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   3 RIAIIGGGSMGEALLSGLLRAGrqVKDMVVAEKFPERAKYLADKYSVRVTSVADAAE---NAHYVVVA-------VKPAD 72
Cdd:PRK00045 184 KVLVIGAGEMGELVAKHLAEKG--VRKITVANRTLERAEELAEEFGGEAIPLDELPEalaEADIVISStgaphpiIGKGM 261


                 ....*
gi 500046586  73 VEKVI 77
Cdd:PRK00045 262 VERAL 266
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 3-68 1.10e-04

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 43.02  E-value: 1.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500046586   3 RIAIIGGGSMGEALLSGLLRAGrqVKDMVVAEKFPERAKYLADKYSVRVTSVADAAENAHYVVVAV 68
Cdd:cd05213  180 KVLVIGAGEMGELAAKHLAAKG--VAEITIANRTYERAEELAKELGGNAVPLDELLELLNEADVVI 243
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 1-67 2.38e-04

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 40.25  E-value: 2.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500046586    1 MSRIAIIGGGSMGEALLSGLLRAGrqVKDMVVAEKFPERAKYLADKYS----VRVTSVADAAENAHYVVVA 67
Cdd:pfam01488  12 DKKVLLIGAGEMGELVAKHLLAKG--AKEVTIANRTIERAQELAEKFGgveaLPLDDLKEYLAEADIVISA 80
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-77 4.92e-04

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 40.87  E-value: 4.92e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500046586   1 MSRIAIIGGGSMGEALLSGLLRAGRQVkdmVVAEKFPERAKYLADKYSVRVTSVADAAENAHYVVVAVK-PADVEKVI 77
Cdd:COG2084    1 MMKVGFIGLGAMGAPMARNLLKAGHEV---TVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPdDAAVEEVL 75
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 3-77 8.19e-04

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 38.99  E-value: 8.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500046586    3 RIAIIGGGSMGEALLSGLLRAGRQVkdmVVAEKFPERAKYLADKYSVRVTSVADAAENAHYVVVAVK-PADVEKVI 77
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTV---TVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPaGAAVDAVI 73
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 3-77 9.12e-04

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 40.23  E-value: 9.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   3 RIAIIGGGSMGEALLSGLLRAGRQVkdMVVAEkfPERAKYLADK-------------YSVRVTSVADAAENAHYVVVAVK 69
Cdd:COG1893    2 KIAILGAGAIGGLLGARLARAGHDV--TLVAR--GAHAEALRENglrlespdgdrttVPVPAVTDPEELGPADLVLVAVK 77


                 ....*...
gi 500046586  70 PADVEKVI 77
Cdd:COG1893   78 AYDLEAAA 85
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
1-73 1.59e-03

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 39.45  E-value: 1.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500046586   1 MSRIAIIGGGSMGEALLSGLLRAGRQVKdmvVAEKFPERAKYLADKYSVRVTSVADAAENAHYVVVAVKPADV 73
Cdd:PRK15461   1 MAAIAFIGLGQMGSPMASNLLKQGHQLQ---VFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDL 70
MviM COG0673
Predicted dehydrogenase [General function prediction only];
3-68 3.28e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 38.37  E-value: 3.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500046586   3 RIAIIGGGSMGEALLSGLLRAGRqVKDMVVAEKFPERAKYLADKYSVRV-TSVAD--AAENAHYVVVAV 68
Cdd:COG0673    5 RVGIIGAGGIGRAHAPALAALPG-VELVAVADRDPERAEAFAEEYGVRVyTDYEEllADPDIDAVVIAT 72
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 3-77 5.34e-03

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 37.78  E-value: 5.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046586   3 RIAIIGGGSMGEALLSGLLRAGrqVKDMVVAEKFPERAKYLADKYSVRVTSVADAAE---NAHYVVVA-------VKPAD 72
Cdd:COG0373  184 TVLVIGAGEMGELAARHLAAKG--VKRITVANRTLERAEELAEEFGGEAVPLEELPEalaEADIVISStgaphpvITKEM 261


                 ....*
gi 500046586  73 VEKVI 77
Cdd:COG0373  262 VERAL 266
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 3-68 9.41e-03

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 36.94  E-value: 9.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500046586   3 RIAIIGGGSMGEALLSGLLRAGRQVK----DMVVAEKFPER---AKYLADKY---SVRVTS-VADAAENAHYVVVAV 68
Cdd:COG0240    2 KIAVLGAGSWGTALAKVLARNGHEVTlwgrDPEVAEEINETrenPRYLPGVKlpeNLRATSdLEEALAGADLVLLAV 78
 
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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