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Conserved domains on  [gi|2462519269|ref|XP_054221877|]
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enolase 4 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DD_ENO4 cd22974
dimerization/docking (D/D) domain found in enolase 4 and similar proteins; Enolase (EC 4.2.1. ...
14-78 5.10e-36

dimerization/docking (D/D) domain found in enolase 4 and similar proteins; Enolase (EC 4.2.1.11), also known as phosphopyruvate hydratase, is a metalloenzyme responsible for the catalyzing the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), the ninth and penultimate step of glycolysis. ENO4, also called 2-phospho-D-glycerate hydro-lyase, may be required for sperm motility and function. It contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


:

Pssm-ID: 438543  Cd Length: 65  Bit Score: 126.51  E-value: 5.10e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462519269  14 RELQKLKQQAMEYYRENDVPRRLEELLNSTFYLQPADVYGHLANCFSKLAKPPTICKIVGKDVLD 78
Cdd:cd22974     1 RELYELKQKAAEYYRENGVPQKIEEALNSMFYDQPDDVYGYLANYFSKLSKPPTISRIRGREVLD 65
enolase_like super family cl40480
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ...
70-404 2.34e-10

Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.


The actual alignment was detected with superfamily member cd03313:

Pssm-ID: 477366 [Multi-domain]  Cd Length: 408  Bit Score: 61.73  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269  70 KIVGKDVLDGLGLPTLQVDIFCTIQNFPKNVCSVVISTHfeVHEnALpELAKAEEA-ERASAVSTAVQWVNSTITHELQG 148
Cdd:cd03313     1 KIKAREILDSRGNPTVEVEVTTEDGGVGRAAVPSGASTG--EHE-AV-ELRDGDKSrYLGKGVLKAVKNVNEIIAPALIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 149 MAPSDQAEVDHLLRiffaskvqedkgrkELEKSleystvptplppvppppppppptKKKGQkpgrkdtitekpiapaepv 228
Cdd:cd03313    77 MDVTDQRAIDKLLI--------------ELDGT-----------------------PNKSK------------------- 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 229 epvLsGSMAIGAVSLAVAKACAMLLNKPLYLNIAllkhnqeQPTTLSMPLLMVSLVSCGKSSSGKLNlMKEVICIPHPEL 308
Cdd:cd03313   101 ---L-GANAILGVSLAVAKAAAAALGLPLYRYLG-------GLAAYVLPVPMFNVINGGAHAGNKLD-FQEFMIVPVGAP 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 309 TTKQGVEMLMEMQKHINKIIempsppkaetkkghdgSKRGQQQITGKMSHlGCLTINCDSIEQPLLLIQEICANLGLELG 388
Cdd:cd03313   169 SFSEALRMGAEVYHTLKKVL----------------KKKGGLLATNVGDE-GGFAPNLSSNEEALDLLVEAIEKAGYEPG 231
                         330
                  ....*....|....*.
gi 2462519269 389 TNLHLAINCAGHELMD 404
Cdd:cd03313   232 KKIAIALDVAASEFYD 247
 
Name Accession Description Interval E-value
DD_ENO4 cd22974
dimerization/docking (D/D) domain found in enolase 4 and similar proteins; Enolase (EC 4.2.1. ...
14-78 5.10e-36

dimerization/docking (D/D) domain found in enolase 4 and similar proteins; Enolase (EC 4.2.1.11), also known as phosphopyruvate hydratase, is a metalloenzyme responsible for the catalyzing the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), the ninth and penultimate step of glycolysis. ENO4, also called 2-phospho-D-glycerate hydro-lyase, may be required for sperm motility and function. It contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438543  Cd Length: 65  Bit Score: 126.51  E-value: 5.10e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462519269  14 RELQKLKQQAMEYYRENDVPRRLEELLNSTFYLQPADVYGHLANCFSKLAKPPTICKIVGKDVLD 78
Cdd:cd22974     1 RELYELKQKAAEYYRENGVPQKIEEALNSMFYDQPDDVYGYLANYFSKLSKPPTISRIRGREVLD 65
enolase cd03313
Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of ...
70-404 2.34e-10

Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways. The reaction is facilitated by the presence of metal ions.


Pssm-ID: 239429 [Multi-domain]  Cd Length: 408  Bit Score: 61.73  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269  70 KIVGKDVLDGLGLPTLQVDIFCTIQNFPKNVCSVVISTHfeVHEnALpELAKAEEA-ERASAVSTAVQWVNSTITHELQG 148
Cdd:cd03313     1 KIKAREILDSRGNPTVEVEVTTEDGGVGRAAVPSGASTG--EHE-AV-ELRDGDKSrYLGKGVLKAVKNVNEIIAPALIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 149 MAPSDQAEVDHLLRiffaskvqedkgrkELEKSleystvptplppvppppppppptKKKGQkpgrkdtitekpiapaepv 228
Cdd:cd03313    77 MDVTDQRAIDKLLI--------------ELDGT-----------------------PNKSK------------------- 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 229 epvLsGSMAIGAVSLAVAKACAMLLNKPLYLNIAllkhnqeQPTTLSMPLLMVSLVSCGKSSSGKLNlMKEVICIPHPEL 308
Cdd:cd03313   101 ---L-GANAILGVSLAVAKAAAAALGLPLYRYLG-------GLAAYVLPVPMFNVINGGAHAGNKLD-FQEFMIVPVGAP 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 309 TTKQGVEMLMEMQKHINKIIempsppkaetkkghdgSKRGQQQITGKMSHlGCLTINCDSIEQPLLLIQEICANLGLELG 388
Cdd:cd03313   169 SFSEALRMGAEVYHTLKKVL----------------KKKGGLLATNVGDE-GGFAPNLSSNEEALDLLVEAIEKAGYEPG 231
                         330
                  ....*....|....*.
gi 2462519269 389 TNLHLAINCAGHELMD 404
Cdd:cd03313   232 KKIAIALDVAASEFYD 247
PTZ00081 PTZ00081
enolase; Provisional
65-410 3.72e-09

enolase; Provisional


Pssm-ID: 240259 [Multi-domain]  Cd Length: 439  Bit Score: 58.14  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269  65 PPTICKIVGKDVLDGLGLPTLQVDIFCTIQNFPKNVCSVViSTHfeVHEnALpELAKAEEAE-RASAVSTAVQWVNSTIT 143
Cdd:PTZ00081    1 MSTIKSIKAREILDSRGNPTVEVDLTTEKGVFRAAVPSGA-STG--IYE-AL-ELRDGDKSRyLGKGVLKAVENVNEIIA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 144 HELQGMAPSDQAEVDHLLriffaskVQEDKGRKElekslEYSTVptplppvppppppppptKKKgqkpgrkdtitekpia 223
Cdd:PTZ00081   76 PALIGKDVTDQKKLDKLM-------VEQLDGTKN-----EWGWC-----------------KSK---------------- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 224 paepvepvlSGSMAIGAVSLAVAKACAMLLNKPLYLNIALLKHNQEQPTTLSMPLLMVslVSCGKSSSGKLNlMKEVICI 303
Cdd:PTZ00081  111 ---------LGANAILAVSMAVARAAAAAKGVPLYKYLAQLAGKPTDKFVLPVPCFNV--INGGKHAGNKLA-FQEFMIA 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 304 PHPELTTKQGVEMLMEMQKHINKIIempsppkaETKKGHDGSKRGQQqitgkmshlGCLTINCDSIEQPLLLIQEicanl 383
Cdd:PTZ00081  179 PVGAPSFKEALRMGAEVYHSLKSVI--------KKKYGLDATNVGDE---------GGFAPNIKDPEEALDLLVE----- 236
                         330       340       350
                  ....*....|....*....|....*....|..
gi 2462519269 384 glelgtnlhlAINCAGHE-----LMDYeAASE 410
Cdd:PTZ00081  237 ----------AIKKAGYEgkvkiCMDV-AASE 257
Enolase_N pfam03952
Enolase, N-terminal domain;
68-258 1.59e-05

Enolase, N-terminal domain;


Pssm-ID: 461105 [Multi-domain]  Cd Length: 131  Bit Score: 44.29  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269  68 ICKIVGKDVLDGLGLPTLQVDIFCTIQNFPKNVCSVVIST-HFEVHEnaLPELAKAEEAERAsaVSTAVQWVNSTITHEL 146
Cdd:pfam03952   1 ITKVKAREILDSRGNPTVEVEVTLEDGTFGRAAVPSGASTgEHEAVE--LRDGDKSRYGGKG--VLKAVENVNEIIAPAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 147 QGMAPSDQAEVDHLLRiffaskvqedkgrkELEKSLEYSTVptplppvppppppppptkkkgqkpgrkdtitekpiapae 226
Cdd:pfam03952  77 IGMDATDQRAIDRALI--------------ELDGTENKSKL--------------------------------------- 103
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462519269 227 pvepvlsGSMAIGAVSLAVAKACAMLLNKPLY 258
Cdd:pfam03952 104 -------GANAILGVSLAVAKAAAAALGLPLY 128
Eno COG0148
Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: ...
131-258 1.23e-04

Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439918 [Multi-domain]  Cd Length: 426  Bit Score: 43.86  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 131 VSTAVQWVNSTITHELQGMAPSDQAEVDHLLriffaskVQ----EDKGRkeleksleystvptplppvppppppppptkk 206
Cdd:COG0148    64 VLKAVENVNEEIAPALIGMDATDQRAIDRAM-------IEldgtPNKSR------------------------------- 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462519269 207 kgqkpgrkdtitekpiapaepvepvLsGSMAIGAVSLAVAKACAMLLNKPLY 258
Cdd:COG0148   106 -------------------------L-GANAILGVSLAVAKAAAAALGLPLY 131
 
Name Accession Description Interval E-value
DD_ENO4 cd22974
dimerization/docking (D/D) domain found in enolase 4 and similar proteins; Enolase (EC 4.2.1. ...
14-78 5.10e-36

dimerization/docking (D/D) domain found in enolase 4 and similar proteins; Enolase (EC 4.2.1.11), also known as phosphopyruvate hydratase, is a metalloenzyme responsible for the catalyzing the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), the ninth and penultimate step of glycolysis. ENO4, also called 2-phospho-D-glycerate hydro-lyase, may be required for sperm motility and function. It contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438543  Cd Length: 65  Bit Score: 126.51  E-value: 5.10e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462519269  14 RELQKLKQQAMEYYRENDVPRRLEELLNSTFYLQPADVYGHLANCFSKLAKPPTICKIVGKDVLD 78
Cdd:cd22974     1 RELYELKQKAAEYYRENGVPQKIEEALNSMFYDQPDDVYGYLANYFSKLSKPPTISRIRGREVLD 65
enolase cd03313
Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of ...
70-404 2.34e-10

Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways. The reaction is facilitated by the presence of metal ions.


Pssm-ID: 239429 [Multi-domain]  Cd Length: 408  Bit Score: 61.73  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269  70 KIVGKDVLDGLGLPTLQVDIFCTIQNFPKNVCSVVISTHfeVHEnALpELAKAEEA-ERASAVSTAVQWVNSTITHELQG 148
Cdd:cd03313     1 KIKAREILDSRGNPTVEVEVTTEDGGVGRAAVPSGASTG--EHE-AV-ELRDGDKSrYLGKGVLKAVKNVNEIIAPALIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 149 MAPSDQAEVDHLLRiffaskvqedkgrkELEKSleystvptplppvppppppppptKKKGQkpgrkdtitekpiapaepv 228
Cdd:cd03313    77 MDVTDQRAIDKLLI--------------ELDGT-----------------------PNKSK------------------- 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 229 epvLsGSMAIGAVSLAVAKACAMLLNKPLYLNIAllkhnqeQPTTLSMPLLMVSLVSCGKSSSGKLNlMKEVICIPHPEL 308
Cdd:cd03313   101 ---L-GANAILGVSLAVAKAAAAALGLPLYRYLG-------GLAAYVLPVPMFNVINGGAHAGNKLD-FQEFMIVPVGAP 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 309 TTKQGVEMLMEMQKHINKIIempsppkaetkkghdgSKRGQQQITGKMSHlGCLTINCDSIEQPLLLIQEICANLGLELG 388
Cdd:cd03313   169 SFSEALRMGAEVYHTLKKVL----------------KKKGGLLATNVGDE-GGFAPNLSSNEEALDLLVEAIEKAGYEPG 231
                         330
                  ....*....|....*.
gi 2462519269 389 TNLHLAINCAGHELMD 404
Cdd:cd03313   232 KKIAIALDVAASEFYD 247
PTZ00081 PTZ00081
enolase; Provisional
65-410 3.72e-09

enolase; Provisional


Pssm-ID: 240259 [Multi-domain]  Cd Length: 439  Bit Score: 58.14  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269  65 PPTICKIVGKDVLDGLGLPTLQVDIFCTIQNFPKNVCSVViSTHfeVHEnALpELAKAEEAE-RASAVSTAVQWVNSTIT 143
Cdd:PTZ00081    1 MSTIKSIKAREILDSRGNPTVEVDLTTEKGVFRAAVPSGA-STG--IYE-AL-ELRDGDKSRyLGKGVLKAVENVNEIIA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 144 HELQGMAPSDQAEVDHLLriffaskVQEDKGRKElekslEYSTVptplppvppppppppptKKKgqkpgrkdtitekpia 223
Cdd:PTZ00081   76 PALIGKDVTDQKKLDKLM-------VEQLDGTKN-----EWGWC-----------------KSK---------------- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 224 paepvepvlSGSMAIGAVSLAVAKACAMLLNKPLYLNIALLKHNQEQPTTLSMPLLMVslVSCGKSSSGKLNlMKEVICI 303
Cdd:PTZ00081  111 ---------LGANAILAVSMAVARAAAAAKGVPLYKYLAQLAGKPTDKFVLPVPCFNV--INGGKHAGNKLA-FQEFMIA 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 304 PHPELTTKQGVEMLMEMQKHINKIIempsppkaETKKGHDGSKRGQQqitgkmshlGCLTINCDSIEQPLLLIQEicanl 383
Cdd:PTZ00081  179 PVGAPSFKEALRMGAEVYHSLKSVI--------KKKYGLDATNVGDE---------GGFAPNIKDPEEALDLLVE----- 236
                         330       340       350
                  ....*....|....*....|....*....|..
gi 2462519269 384 glelgtnlhlAINCAGHE-----LMDYeAASE 410
Cdd:PTZ00081  237 ----------AIKKAGYEgkvkiCMDV-AASE 257
Enolase_N pfam03952
Enolase, N-terminal domain;
68-258 1.59e-05

Enolase, N-terminal domain;


Pssm-ID: 461105 [Multi-domain]  Cd Length: 131  Bit Score: 44.29  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269  68 ICKIVGKDVLDGLGLPTLQVDIFCTIQNFPKNVCSVVIST-HFEVHEnaLPELAKAEEAERAsaVSTAVQWVNSTITHEL 146
Cdd:pfam03952   1 ITKVKAREILDSRGNPTVEVEVTLEDGTFGRAAVPSGASTgEHEAVE--LRDGDKSRYGGKG--VLKAVENVNEIIAPAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 147 QGMAPSDQAEVDHLLRiffaskvqedkgrkELEKSLEYSTVptplppvppppppppptkkkgqkpgrkdtitekpiapae 226
Cdd:pfam03952  77 IGMDATDQRAIDRALI--------------ELDGTENKSKL--------------------------------------- 103
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462519269 227 pvepvlsGSMAIGAVSLAVAKACAMLLNKPLY 258
Cdd:pfam03952 104 -------GANAILGVSLAVAKAAAAALGLPLY 128
Eno COG0148
Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: ...
131-258 1.23e-04

Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439918 [Multi-domain]  Cd Length: 426  Bit Score: 43.86  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 131 VSTAVQWVNSTITHELQGMAPSDQAEVDHLLriffaskVQ----EDKGRkeleksleystvptplppvppppppppptkk 206
Cdd:COG0148    64 VLKAVENVNEEIAPALIGMDATDQRAIDRAM-------IEldgtPNKSR------------------------------- 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462519269 207 kgqkpgrkdtitekpiapaepvepvLsGSMAIGAVSLAVAKACAMLLNKPLY 258
Cdd:COG0148   106 -------------------------L-GANAILGVSLAVAKAAAAALGLPLY 131
DD_RII_PKA-like cd12084
dimerization/docking (D/D) domain of the type II Regulatory subunit of cAMP-dependent protein ...
29-62 1.32e-04

dimerization/docking (D/D) domain of the type II Regulatory subunit of cAMP-dependent protein kinase and similar domains; cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence (IS), and two c-AMP binding domains. RI and RII subunits are distinguished by their IS; RII subunits contain a phosphorylation site and are both substrates and inhibitors while RI subunits are pseudo-substrates. RI subunits require ATP and Mg ions to form a stable holoenzyme while RII subunits do not. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis.


Pssm-ID: 438517  Cd Length: 36  Bit Score: 38.94  E-value: 1.32e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462519269  29 ENDVPRRLEELLNSTFYLQPADVYGHLANCFSKL 62
Cdd:cd12084     2 PEGLRELLEDFTREVLREQPEDVYEFAADYFEKL 35
DD_AtENO3-like cd22962
dimerization/docking (D/D) domain found in Arabidopsis thaliana cytosolic enolase 3 (ENO3) and ...
21-65 1.64e-04

dimerization/docking (D/D) domain found in Arabidopsis thaliana cytosolic enolase 3 (ENO3) and similar proteins; Enolase (EC 4.2.1.11), also known as phosphopyruvate hydratase, is a metalloenzyme responsible for catalyzing the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), the ninth and penultimate step of glycolysis. The subfamily includes Arabidopsis thaliana ENO3, also called ENOC, 2-phospho-D-glycerate hydro-lyase 3, or 2-phosphoglycerate dehydratase 3. It contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438531  Cd Length: 45  Bit Score: 39.10  E-value: 1.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462519269  21 QQAMEYYRENDVPRRLEELLNSTFYLQPADVYGHLANCFSKLAKP 65
Cdd:cd22962     1 ASVQEYLEKHKLEEKLEEAVNAVVKEKPEDPFGFLAQLLRKRAPP 45
eno PRK00077
enolase; Provisional
131-258 6.38e-04

enolase; Provisional


Pssm-ID: 234617 [Multi-domain]  Cd Length: 425  Bit Score: 41.61  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462519269 131 VSTAVQWVNSTITHELQGMAPSDQAEVDHLLRiffaskvqedkgrkELE----KS-Leystvptplppvppppppppptk 205
Cdd:PRK00077   64 VLKAVENVNEEIAPALIGLDALDQRAIDKAMI--------------ELDgtpnKSkL----------------------- 106
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462519269 206 kkgqkpgrkdtitekpiapaepvepvlsGSMAIGAVSLAVAKACAMLLNKPLY 258
Cdd:PRK00077  107 ----------------------------GANAILGVSLAVAKAAADSLGLPLY 131
 
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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