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Conserved domains on  [gi|23171562|gb|AAN13746|]
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Pyrroline-5-carboxylate reductase-like 2, isoform B [Drosophila melanogaster]

Protein Classification

pyrroline-5-carboxylate reductase (domain architecture ID 11485643)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
2-172 1.50e-70

pyrroline-5-carboxylate reductase; Reviewed


:

Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 213.85  E-value: 1.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    2 GITLSTIESSLSPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVD-ESQLDVVTALSGSGPA 80
Cdd:PRK11880  96 GVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWVDdEKQMDAVTAVSGSGPA 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562   81 YVFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALRQLELSGFRAAVSGAVE 160
Cdd:PRK11880 176 YVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAALRVLEEKGLRAAVIEAVQ 255
                        170
                 ....*....|..
gi 23171562  161 QATLRCRQISGK 172
Cdd:PRK11880 256 AAAKRSKELGKE 267
 
Name Accession Description Interval E-value
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
2-172 1.50e-70

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 213.85  E-value: 1.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    2 GITLSTIESSLSPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVD-ESQLDVVTALSGSGPA 80
Cdd:PRK11880  96 GVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWVDdEKQMDAVTAVSGSGPA 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562   81 YVFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALRQLELSGFRAAVSGAVE 160
Cdd:PRK11880 176 YVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAALRVLEEKGLRAAVIEAVQ 255
                        170
                 ....*....|..
gi 23171562  161 QATLRCRQISGK 172
Cdd:PRK11880 256 AAAKRSKELGKE 267
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
2-168 2.26e-65

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: 200.18  E-value: 2.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562     2 GITLSTIESSLSPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVDESQLDVVTALSGSGPAY 81
Cdd:TIGR00112  79 GVTLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAY 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    82 VFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALRQLELSGFRAAVSGAVEQ 161
Cdd:TIGR00112 159 VFLFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEA 238

                  ....*..
gi 23171562   162 ATLRCRQ 168
Cdd:TIGR00112 239 AVRRSRE 245
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism];
2-172 1.71e-64

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism];


Pssm-ID: 223422 [Multi-domain]  Cd Length: 266  Bit Score: 198.57  E-value: 1.71e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562   2 GITLSTIESSLsPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVDESQLDVVTALSGSGPAY 81
Cdd:COG0345  97 GVSIETLERLL-GGLRVVRVMPNTPALVGAGVTAISANANVSEEDKAFVEALLSAVGKVVEVEESLMDAVTALSGSGPAY 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562  82 VFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALRQLELSGFRAAVSGAVEQ 161
Cdd:COG0345 176 VFLFIEALADAGVRLGLPREEARELAAQTVAGAAKLLLESGEHPAELRDQVTSPGGTTIAGLRVLEEDGFRGAVIEAVEA 255
                       170
                ....*....|.
gi 23171562 162 ATLRCRQISGK 172
Cdd:COG0345 256 AYKRSEELGKQ 266
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
65-169 2.71e-50

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: 339361  Cd Length: 105  Bit Score: 156.77  E-value: 2.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    65 ESQLDVVTALSGSGPAYVFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALR 144
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVALGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLK 80
                          90       100
                  ....*....|....*....|....*
gi 23171562   145 QLELSGFRAAVSGAVEQATLRCRQI 169
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKEL 105
 
Name Accession Description Interval E-value
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
2-172 1.50e-70

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 213.85  E-value: 1.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    2 GITLSTIESSLSPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVD-ESQLDVVTALSGSGPA 80
Cdd:PRK11880  96 GVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWVDdEKQMDAVTAVSGSGPA 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562   81 YVFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALRQLELSGFRAAVSGAVE 160
Cdd:PRK11880 176 YVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAALRVLEEKGLRAAVIEAVQ 255
                        170
                 ....*....|..
gi 23171562  161 QATLRCRQISGK 172
Cdd:PRK11880 256 AAAKRSKELGKE 267
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
2-171 7.32e-69

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 209.81  E-value: 7.32e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    2 GITLSTIESSlSPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVDESQLDVVTALSGSGPAY 81
Cdd:PLN02688  97 GITLADLQEW-AGGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEKLLDAVTGLSGSGPAY 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562   82 VFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALRQLELSGFRAAVSGAVEQ 161
Cdd:PLN02688 176 IFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHELEKGGFRAALMNAVVA 255
                        170
                 ....*....|
gi 23171562  162 ATLRCRQISG 171
Cdd:PLN02688 256 AAKRSRELSK 265
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
2-168 2.26e-65

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: 200.18  E-value: 2.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562     2 GITLSTIESSLSPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVDESQLDVVTALSGSGPAY 81
Cdd:TIGR00112  79 GVTLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAY 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    82 VFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALRQLELSGFRAAVSGAVEQ 161
Cdd:TIGR00112 159 VFLFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEA 238

                  ....*..
gi 23171562   162 ATLRCRQ 168
Cdd:TIGR00112 239 AVRRSRE 245
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism];
2-172 1.71e-64

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism];


Pssm-ID: 223422 [Multi-domain]  Cd Length: 266  Bit Score: 198.57  E-value: 1.71e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562   2 GITLSTIESSLsPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVDESQLDVVTALSGSGPAY 81
Cdd:COG0345  97 GVSIETLERLL-GGLRVVRVMPNTPALVGAGVTAISANANVSEEDKAFVEALLSAVGKVVEVEESLMDAVTALSGSGPAY 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562  82 VFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALRQLELSGFRAAVSGAVEQ 161
Cdd:COG0345 176 VFLFIEALADAGVRLGLPREEARELAAQTVAGAAKLLLESGEHPAELRDQVTSPGGTTIAGLRVLEEDGFRGAVIEAVEA 255
                       170
                ....*....|.
gi 23171562 162 ATLRCRQISGK 172
Cdd:COG0345 256 AYKRSEELGKQ 266
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
65-169 2.71e-50

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: 339361  Cd Length: 105  Bit Score: 156.77  E-value: 2.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    65 ESQLDVVTALSGSGPAYVFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALR 144
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVALGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLK 80
                          90       100
                  ....*....|....*....|....*
gi 23171562   145 QLELSGFRAAVSGAVEQATLRCRQI 169
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKEL 105
PRK12491 PRK12491
pyrroline-5-carboxylate reductase; Reviewed
2-173 5.39e-41

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 105695 [Multi-domain]  Cd Length: 272  Bit Score: 138.67  E-value: 5.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    2 GITLSTIESSLSPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVDESQLDVVTALSGSGPAY 81
Cdd:PRK12491  99 GKSIKSTENEFDRKLKVIRVMPNTPVLVGEGMSALSFNEMVTEKDIKEVLNIFNIFGQTEVVNEKLMDVVTSISGSSPAY 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562   82 VFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALRQLELSGFRAAVSGAVEQ 161
Cdd:PRK12491 179 VYMFIEAMADAAVLDGMPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTIEAVATLEEKGLRTAIISAMKR 258
                        170
                 ....*....|..
gi 23171562  162 ATLRCRQISGKT 173
Cdd:PRK12491 259 CTKKSMEMSSLT 270
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
2-162 3.01e-40

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 136.62  E-value: 3.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    2 GITLSTIESSLSPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVDESQLDVVTALSGSGPAY 81
Cdd:PTZ00431  92 GLNLKTLEEMVGVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQEIKEKDMDIATAISGCGPAY 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562   82 VFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALRQLELSGFRAAVSGAVEQ 161
Cdd:PTZ00431 172 VFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGITIVGLYTLEKHAFKYTVMDAVES 251

                 .
gi 23171562  162 A 162
Cdd:PTZ00431 252 A 252
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
2-173 1.94e-37

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 129.50  E-value: 1.94e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    2 GITLSTIESSLSPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVDESQLDVVTALSGSGPAY 81
Cdd:PRK07679 101 GVSTHSIRNLLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVSVVEEEDMHAVTALSGSGPAY 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562   82 VFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALRQLELSGFRAAVSGAVEQ 161
Cdd:PRK07679 181 IYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEAGIEVLQEHRFQQALISCITQ 260
                        170
                 ....*....|..
gi 23171562  162 ATLRCRQIsGKT 173
Cdd:PRK07679 261 ATQRSHNL-GKT 271
PRK07634 PRK07634
pyrroline-5-carboxylate reductase; Reviewed
2-147 4.48e-20

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181063 [Multi-domain]  Cd Length: 245  Bit Score: 83.65  E-value: 4.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    2 GITLSTIESSLSPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVDESQLDVVTALSGSGPAY 81
Cdd:PRK07634 101 GIGPSYLEERLPKGTPVAWIMPNTAAEIGKSISLYTMGQSVNETHKETLQLILKGIGTSQLCTEEEVHQLTAVTGSAPAF 180
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23171562   82 VFVMIEALADGAVHMGMPRDLAYRLASQTVLGAGHMVrDSGMHPGQLKDGVTSPAGSTAAALRQLE 147
Cdd:PRK07634 181 LYYFAESLIEATKSYGVDEETAKHLVIQMISGSASML-EQTQDPANLREQVTTPGGSTAEGLKALY 245
PRK07680 PRK07680
late competence protein ComER; Validated
3-147 3.02e-10

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 56.90  E-value: 3.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    3 ITLSTIESSLSPQarVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVDESQLDVVTALSGSGPAYV 82
Cdd:PRK07680  99 ISVEQLETLVPCQ--VARIIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIEEDITRVSSDIVSCGPAFF 176
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23171562   83 FVMIEALADGAVHM-GMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTAAALRQLE 147
Cdd:PRK07680 177 SYLLQRFIDAAVEEtNISKEEATTLASEMLIGMGKLLEKGLYTLPTLQEKVCVKGGITGEGIKVLE 242
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
2-140 7.58e-09

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 53.23  E-value: 7.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562    2 GITLSTIeSSLSPQARVIRVMPNLPAVVCSGCSVFVRGSKATDADADITQKLLQSVGTCEPVDESQLDVVTALSGSGPAY 81
Cdd:PRK06928 100 GVSLDDL-LEITPGLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETLSHFSHVMTIREENMDIASNLTSSSPGF 178
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171562   82 VFVMIEALADGAV-HMGMPRDLAYRLASQTVLGAGHMVRDSGMHPGQLKDGVTSPAGSTA 140
Cdd:PRK06928 179 IAAIFEEFAEAAVrNSSLSDEEAFQFLNFALAGTGKLLVEEDYTFSGTIERVATKGGITA 238
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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