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Conserved domains on  [gi|4505289|ref|NP_002452|]
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diphosphomevalonate decarboxylase [Homo sapiens]

Protein Classification

diphosphomevalonate/mevalonate 3,5-bisphosphate decarboxylase family protein( domain architecture ID 706585)

diphosphomevalonate/mevalonate 3,5-bisphosphate decarboxylase family protein similar to diphosphomevalonate decarboxylase (DMD) that catalyzes the decarboxylation of mevalonate 5-diphosphate (MVAPP) to isopentenyl diphosphate (IPP), and mevalonate 3,5-bisphosphate decarboxylase (MBD) that catalyzes the ATP-independent decarboxylation of (R)-mevalonate 3,5-bisphosphate to isopentenyl phosphate

EC:  4.1.1.-
Gene Ontology:  GO:0016831|GO:0008299

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MDD_C super family cl28577
Mevalonate 5-diphosphate decarboxylase C-terminal domain; Mevalonate diphosphate decarboxylase ...
10-337 1.09e-156

Mevalonate 5-diphosphate decarboxylase C-terminal domain; Mevalonate diphosphate decarboxylase (EC:4.1.1.33) catalyzes the ATP dependent decarboxylation of mevalonate 5-diphosphate (MVAPP) to form isopentenyl 5-diphosphate. The reaction is required for production of polyisoprenoids and sterols from acetyl-CoA. This entry represents the C-terminal domain of the mevalonate 5-diphosphate decarboxylase enzyme which is a member of the GHMP kinase superfamily.


The actual alignment was detected with superfamily member PLN02407:

Pssm-ID: 475042  Cd Length: 343  Bit Score: 445.01  E-value: 1.09e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    10 VTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLHQDQLKTTTTAVISKDFTEDRIWLNGREEDVGQPRLQACLREIRCL 89
Cdd:PLN02407   4 VTAQAPTNIAVIKYWGKRDEKLILPINSSISVTLDPDHLCATTTVAVSPSFDQDRLWLNGKEISLSGGRYQNCLREIRAR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    90 ARKRRNSRDGDPLPSSL--SCKVHVASVNNFPTAAGLASSAAGYACLAYTLARVYGV----ESDLSEVARRGSGSACRSL 163
Cdd:PLN02407  84 ATDVEDEEKGIKITKKDweKLHVHIASYNNFPTAAGLASSAAGFACLVFALAKLMNVkedfPGELSAIARQGSGSACRSL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289   164 YGGFVEWQMGEQADGKDSIARQVAPESHWPELRVLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPARMAEMARC 243
Cdd:PLN02407 164 YGGFVKWNMGKKEDGSDSIAVQLADEKHWDDLVIIIAVVSSRQKETSSTSGMRESVETSPLLQHRAKEVVPKRILQMEEA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289   244 IRERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNAHHGDTKVAYTFDAGPNAVIFTLDDTVAEFV 323
Cdd:PLN02407 244 IKNRDFASFAKLTCADSNQFHATCLDTSPPIFYMNDTSRRIISLVEKWNRSEGTPQVAYTFDAGPNAVLIALNRKVAAQL 323
                        330
                 ....*....|....*
gi 4505289   324 -AAVWHGFPPGSNGD 337
Cdd:PLN02407 324 lQRLLYYFPPSSDTD 338
 
Name Accession Description Interval E-value
PLN02407 PLN02407
diphosphomevalonate decarboxylase
10-337 1.09e-156

diphosphomevalonate decarboxylase


Pssm-ID: 178029  Cd Length: 343  Bit Score: 445.01  E-value: 1.09e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    10 VTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLHQDQLKTTTTAVISKDFTEDRIWLNGREEDVGQPRLQACLREIRCL 89
Cdd:PLN02407   4 VTAQAPTNIAVIKYWGKRDEKLILPINSSISVTLDPDHLCATTTVAVSPSFDQDRLWLNGKEISLSGGRYQNCLREIRAR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    90 ARKRRNSRDGDPLPSSL--SCKVHVASVNNFPTAAGLASSAAGYACLAYTLARVYGV----ESDLSEVARRGSGSACRSL 163
Cdd:PLN02407  84 ATDVEDEEKGIKITKKDweKLHVHIASYNNFPTAAGLASSAAGFACLVFALAKLMNVkedfPGELSAIARQGSGSACRSL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289   164 YGGFVEWQMGEQADGKDSIARQVAPESHWPELRVLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPARMAEMARC 243
Cdd:PLN02407 164 YGGFVKWNMGKKEDGSDSIAVQLADEKHWDDLVIIIAVVSSRQKETSSTSGMRESVETSPLLQHRAKEVVPKRILQMEEA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289   244 IRERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNAHHGDTKVAYTFDAGPNAVIFTLDDTVAEFV 323
Cdd:PLN02407 244 IKNRDFASFAKLTCADSNQFHATCLDTSPPIFYMNDTSRRIISLVEKWNRSEGTPQVAYTFDAGPNAVLIALNRKVAAQL 323
                        330
                 ....*....|....*
gi 4505289   324 -AAVWHGFPPGSNGD 337
Cdd:PLN02407 324 lQRLLYYFPPSSDTD 338
MDD_C pfam18376
Mevalonate 5-diphosphate decarboxylase C-terminal domain; Mevalonate diphosphate decarboxylase ...
197-382 3.70e-117

Mevalonate 5-diphosphate decarboxylase C-terminal domain; Mevalonate diphosphate decarboxylase (EC:4.1.1.33) catalyzes the ATP dependent decarboxylation of mevalonate 5-diphosphate (MVAPP) to form isopentenyl 5-diphosphate. The reaction is required for production of polyisoprenoids and sterols from acetyl-CoA. This entry represents the C-terminal domain of the mevalonate 5-diphosphate decarboxylase enzyme which is a member of the GHMP kinase superfamily.


Pssm-ID: 465732  Cd Length: 186  Bit Score: 338.38  E-value: 3.70e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    197 VLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPARMAEMARCIRERDFPSFAQLTMKDSNQFHATCLDTFPPISY 276
Cdd:pfam18376   1 VLILVVSDEKKEVSSTSGMQRSVETSPLLKHRAEHVVPERMEAMEKAILAKDFETFAEITMKDSNQFHAVCLDTYPPIFY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    277 LNAISWRIIHLVHRFNAHHGDTKVAYTFDAGPNAVIFTLDDTVAEFVAAVWHGFPPGSNGDTFLKGLQVRPAPLSAELQA 356
Cdd:pfam18376  81 LNDTSRAIIQLVHAYNEFAGRIKVAYTFDAGPNAVLYLLEKDVPKVLSLLKHFFPPSTNGDQFFKGLPVLPSELSEELKA 160
                         170       180
                  ....*....|....*....|....*.
gi 4505289    357 ALAMEPTPGGVKYIIVTQVGPGPQIL 382
Cdd:pfam18376 161 SLAMKPIPGGVKYIIHTKVGDGPRVL 186
mevDPdecarb TIGR01240
diphosphomevalonate decarboxylase; This enzyme catalyzes the last step in the synthesis of ...
10-330 3.09e-88

diphosphomevalonate decarboxylase; This enzyme catalyzes the last step in the synthesis of isopentenyl diphosphate (IPP) in the mevalonate pathway. Alternate names: mevalonate diphosphate decarboxylase; pyrophosphomevalonate decarboxylase [Central intermediary metabolism, Other]


Pssm-ID: 130307  Cd Length: 305  Bit Score: 269.51  E-value: 3.09e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289     10 VTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLhqDQLKTTTTAVISKDFTEDRIWLNGREE-DVGQPRLQACLREIRc 88
Cdd:TIGR01240   1 ASVTAYVNIATIKYWGKRNTKLNLPTNSSISLTL--SQLRTLTSVAFADEFERDTFYLNGTLQhSIDNEKTSNCLDDFR- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289     89 larkrrnsrdgdpLPSSLSCKVHVASVNNFPTAAGLASSAAGYACLAYTLARVYGVESD---LSEVARRGSGSACRSLYG 165
Cdd:TIGR01240  78 -------------QLRKEQEKLHIVSQNNFPTAAGLASSASGLAALVSACAKLYQLPLDtseLSRIARKGSGSACRSLFG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    166 GFVEWQMGEqaDGKDSIARQVAPESHWPELRVLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPaRMAEMARCIR 245
Cdd:TIGR01240 145 GYVAWEKGK--DDHSSAAVQVADDSDWPQ*AMCVLVVNDIKKDVSSRQGMQLTVATSELFKEWIEHVVP-DFEV*RKAIK 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    246 ERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNahHGDTKVAYTFDAGPNAVIFTLDDTVAEFVAA 325
Cdd:TIGR01240 222 TKDFATFGKETEANSLSMHATTLDAFPPFFYLNDTSKRAMSAVHTLR--QGGTICYFTMDAGPNVKVLYLAENLSKLFEF 299

                  ....*
gi 4505289    326 VWHGF 330
Cdd:TIGR01240 300 IYKLF 304
MVD1 COG3407
Mevalonate pyrophosphate decarboxylase [Lipid transport and metabolism]; Mevalonate ...
9-381 4.83e-86

Mevalonate pyrophosphate decarboxylase [Lipid transport and metabolism]; Mevalonate pyrophosphate decarboxylase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 442633  Cd Length: 322  Bit Score: 264.36  E-value: 4.83e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    9 AVTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLhqDQLKTTTTAVISKDFTEDRIWLNGREED-VGQPRLQACLREIR 87
Cdd:COG3407   5 SATARAHSNIALIKYWGKRDEELNLPANPSLSLTL--DAFYTTTTVEFDKDLAEDEFILNGEPQKgKFLPKISKFLDRVR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289   88 CLARKRRnsrdgdplpsslscKVHVASVNNFPTAAGLASSAAGYACLAYTLARVYGVESD---LSEVARRGSGSACRSLY 164
Cdd:COG3407  83 ALAGKSY--------------HARIESENNFPTAAGLASSASGFAALALAANSAEGLDLDdrkLSRLARLGSGSACRSIF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289  165 GGFVEWQMGEqaDGKDSIARQVAPEsHWPeLRVLILVVSAEKKLTGSTVGMRaSVETSPLLRFRAESvVPARMAEMARCI 244
Cdd:COG3407 149 GGFVEWGKGE--DDEDSYAVPIPAE-DWD-LADIILVVDKGEKKVSSREGMK-TAETSPFYPAWVEQ-AEEDLEKLKEAI 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289  245 RERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNAhhGDTKVAYTFDAGPNAVIFTLDDTVAEFVA 324
Cdd:COG3407 223 KAGDFEALGEIAESNALRMHATMMTSNPPFIYWKPNTLEVINAVRELRE--EGLPVYFTLDAGPNVKVLCPEEDAEKVAA 300
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4505289  325 AvwhgfppgsngdtflkglqvrpapLSAELqaalameptpgGVKYIIVTQVGPGPQI 381
Cdd:COG3407 301 F------------------------LAAEL-----------VNGQVIVDKPGPGARL 322
 
Name Accession Description Interval E-value
PLN02407 PLN02407
diphosphomevalonate decarboxylase
10-337 1.09e-156

diphosphomevalonate decarboxylase


Pssm-ID: 178029  Cd Length: 343  Bit Score: 445.01  E-value: 1.09e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    10 VTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLHQDQLKTTTTAVISKDFTEDRIWLNGREEDVGQPRLQACLREIRCL 89
Cdd:PLN02407   4 VTAQAPTNIAVIKYWGKRDEKLILPINSSISVTLDPDHLCATTTVAVSPSFDQDRLWLNGKEISLSGGRYQNCLREIRAR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    90 ARKRRNSRDGDPLPSSL--SCKVHVASVNNFPTAAGLASSAAGYACLAYTLARVYGV----ESDLSEVARRGSGSACRSL 163
Cdd:PLN02407  84 ATDVEDEEKGIKITKKDweKLHVHIASYNNFPTAAGLASSAAGFACLVFALAKLMNVkedfPGELSAIARQGSGSACRSL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289   164 YGGFVEWQMGEQADGKDSIARQVAPESHWPELRVLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPARMAEMARC 243
Cdd:PLN02407 164 YGGFVKWNMGKKEDGSDSIAVQLADEKHWDDLVIIIAVVSSRQKETSSTSGMRESVETSPLLQHRAKEVVPKRILQMEEA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289   244 IRERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNAHHGDTKVAYTFDAGPNAVIFTLDDTVAEFV 323
Cdd:PLN02407 244 IKNRDFASFAKLTCADSNQFHATCLDTSPPIFYMNDTSRRIISLVEKWNRSEGTPQVAYTFDAGPNAVLIALNRKVAAQL 323
                        330
                 ....*....|....*
gi 4505289   324 -AAVWHGFPPGSNGD 337
Cdd:PLN02407 324 lQRLLYYFPPSSDTD 338
MDD_C pfam18376
Mevalonate 5-diphosphate decarboxylase C-terminal domain; Mevalonate diphosphate decarboxylase ...
197-382 3.70e-117

Mevalonate 5-diphosphate decarboxylase C-terminal domain; Mevalonate diphosphate decarboxylase (EC:4.1.1.33) catalyzes the ATP dependent decarboxylation of mevalonate 5-diphosphate (MVAPP) to form isopentenyl 5-diphosphate. The reaction is required for production of polyisoprenoids and sterols from acetyl-CoA. This entry represents the C-terminal domain of the mevalonate 5-diphosphate decarboxylase enzyme which is a member of the GHMP kinase superfamily.


Pssm-ID: 465732  Cd Length: 186  Bit Score: 338.38  E-value: 3.70e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    197 VLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPARMAEMARCIRERDFPSFAQLTMKDSNQFHATCLDTFPPISY 276
Cdd:pfam18376   1 VLILVVSDEKKEVSSTSGMQRSVETSPLLKHRAEHVVPERMEAMEKAILAKDFETFAEITMKDSNQFHAVCLDTYPPIFY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    277 LNAISWRIIHLVHRFNAHHGDTKVAYTFDAGPNAVIFTLDDTVAEFVAAVWHGFPPGSNGDTFLKGLQVRPAPLSAELQA 356
Cdd:pfam18376  81 LNDTSRAIIQLVHAYNEFAGRIKVAYTFDAGPNAVLYLLEKDVPKVLSLLKHFFPPSTNGDQFFKGLPVLPSELSEELKA 160
                         170       180
                  ....*....|....*....|....*.
gi 4505289    357 ALAMEPTPGGVKYIIVTQVGPGPQIL 382
Cdd:pfam18376 161 SLAMKPIPGGVKYIIHTKVGDGPRVL 186
mevDPdecarb TIGR01240
diphosphomevalonate decarboxylase; This enzyme catalyzes the last step in the synthesis of ...
10-330 3.09e-88

diphosphomevalonate decarboxylase; This enzyme catalyzes the last step in the synthesis of isopentenyl diphosphate (IPP) in the mevalonate pathway. Alternate names: mevalonate diphosphate decarboxylase; pyrophosphomevalonate decarboxylase [Central intermediary metabolism, Other]


Pssm-ID: 130307  Cd Length: 305  Bit Score: 269.51  E-value: 3.09e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289     10 VTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLhqDQLKTTTTAVISKDFTEDRIWLNGREE-DVGQPRLQACLREIRc 88
Cdd:TIGR01240   1 ASVTAYVNIATIKYWGKRNTKLNLPTNSSISLTL--SQLRTLTSVAFADEFERDTFYLNGTLQhSIDNEKTSNCLDDFR- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289     89 larkrrnsrdgdpLPSSLSCKVHVASVNNFPTAAGLASSAAGYACLAYTLARVYGVESD---LSEVARRGSGSACRSLYG 165
Cdd:TIGR01240  78 -------------QLRKEQEKLHIVSQNNFPTAAGLASSASGLAALVSACAKLYQLPLDtseLSRIARKGSGSACRSLFG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    166 GFVEWQMGEqaDGKDSIARQVAPESHWPELRVLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPaRMAEMARCIR 245
Cdd:TIGR01240 145 GYVAWEKGK--DDHSSAAVQVADDSDWPQ*AMCVLVVNDIKKDVSSRQGMQLTVATSELFKEWIEHVVP-DFEV*RKAIK 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    246 ERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNahHGDTKVAYTFDAGPNAVIFTLDDTVAEFVAA 325
Cdd:TIGR01240 222 TKDFATFGKETEANSLSMHATTLDAFPPFFYLNDTSKRAMSAVHTLR--QGGTICYFTMDAGPNVKVLYLAENLSKLFEF 299

                  ....*
gi 4505289    326 VWHGF 330
Cdd:TIGR01240 300 IYKLF 304
MVD1 COG3407
Mevalonate pyrophosphate decarboxylase [Lipid transport and metabolism]; Mevalonate ...
9-381 4.83e-86

Mevalonate pyrophosphate decarboxylase [Lipid transport and metabolism]; Mevalonate pyrophosphate decarboxylase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 442633  Cd Length: 322  Bit Score: 264.36  E-value: 4.83e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289    9 AVTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLhqDQLKTTTTAVISKDFTEDRIWLNGREED-VGQPRLQACLREIR 87
Cdd:COG3407   5 SATARAHSNIALIKYWGKRDEELNLPANPSLSLTL--DAFYTTTTVEFDKDLAEDEFILNGEPQKgKFLPKISKFLDRVR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289   88 CLARKRRnsrdgdplpsslscKVHVASVNNFPTAAGLASSAAGYACLAYTLARVYGVESD---LSEVARRGSGSACRSLY 164
Cdd:COG3407  83 ALAGKSY--------------HARIESENNFPTAAGLASSASGFAALALAANSAEGLDLDdrkLSRLARLGSGSACRSIF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289  165 GGFVEWQMGEqaDGKDSIARQVAPEsHWPeLRVLILVVSAEKKLTGSTVGMRaSVETSPLLRFRAESvVPARMAEMARCI 244
Cdd:COG3407 149 GGFVEWGKGE--DDEDSYAVPIPAE-DWD-LADIILVVDKGEKKVSSREGMK-TAETSPFYPAWVEQ-AEEDLEKLKEAI 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505289  245 RERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNAhhGDTKVAYTFDAGPNAVIFTLDDTVAEFVA 324
Cdd:COG3407 223 KAGDFEALGEIAESNALRMHATMMTSNPPFIYWKPNTLEVINAVRELRE--EGLPVYFTLDAGPNVKVLCPEEDAEKVAA 300
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4505289  325 AvwhgfppgsngdtflkglqvrpapLSAELqaalameptpgGVKYIIVTQVGPGPQI 381
Cdd:COG3407 301 F------------------------LAAEL-----------VNGQVIVDKPGPGARL 322
 
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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