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Conserved domains on  [gi|15230853|ref|NP_189184|]
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Adenosylmethionine decarboxylase family protein [Arabidopsis thaliana]

Protein Classification

PLN02524 family protein( domain architecture ID 10010817)

PLN02524 family protein

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PLN02524 PLN02524
S-adenosylmethionine decarboxylase
1-346 0e+00

S-adenosylmethionine decarboxylase


:

Pssm-ID: 215287  Cd Length: 355  Bit Score: 612.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853    1 MAVSATGFEGFEKRLEISFFETTDFLDPQGKSLRSLTKSQLDEILTPAECTIVSSLTNSFVDSYVLSESSLFVYPYKIII 80
Cdd:PLN02524   1 MPVSAIGFEGFEKRLEITFFEPPVFADPNGRGLRALTRSQLDEILRPAECTIVSSLSNDQFDSYVLSESSLFVYPYKIII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853   81 KTCGTTKLLLSIPHILRLADSLCLTVKSVRYTRGSFIFPGAQSYPHRSFSEEVALLDDYFGKLNAGSKAFVMGGSDnNPQ 160
Cdd:PLN02524  81 KTCGTTKLLLSIPPLLELAARLSLSVRSVKYTRGSFIFPGAQPFPHRSFSEEVSVLDGHFGKLGLGGKAYVMGDPD-KGQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853  161 RWHVYSASSTEESaVCDKPVYTLEMCMTGLDNIKASVFFKTNS-VSASEMTISSGIRNILPGSEICDFNFEPCGYSMNSI 239
Cdd:PLN02524 160 KWHVYSASAHNSS-NSNEPVYTLEMCMTGLDREKASVFFKDSSlSSAEEMTKASGIRKILPESEICDFAFDPCGYSMNGI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853  240 EGDAVSTIHVTPEDGFSYASFETVGYDLKALNFKELVDRVLVCFGPEEFSVAVHANLGTEVLASDCVADVNGYFSQEREL 319
Cdd:PLN02524 239 EGDAISTIHVTPEDGFSYASFEAMGYDPGDLDLSQLVERVLACFKPKEFSVAVHANVGGEAGSWGCSLDPDGYSCKGRSC 318
                        330       340
                 ....*....|....*....|....*..
gi 15230853  320 EELGLGGSVLYQRFVKTVECCSPKSTL 346
Cdd:PLN02524 319 QELPGGGSVVYQTFTATGGCGSPRSTL 345
 
Name Accession Description Interval E-value
PLN02524 PLN02524
S-adenosylmethionine decarboxylase
1-346 0e+00

S-adenosylmethionine decarboxylase


Pssm-ID: 215287  Cd Length: 355  Bit Score: 612.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853    1 MAVSATGFEGFEKRLEISFFETTDFLDPQGKSLRSLTKSQLDEILTPAECTIVSSLTNSFVDSYVLSESSLFVYPYKIII 80
Cdd:PLN02524   1 MPVSAIGFEGFEKRLEITFFEPPVFADPNGRGLRALTRSQLDEILRPAECTIVSSLSNDQFDSYVLSESSLFVYPYKIII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853   81 KTCGTTKLLLSIPHILRLADSLCLTVKSVRYTRGSFIFPGAQSYPHRSFSEEVALLDDYFGKLNAGSKAFVMGGSDnNPQ 160
Cdd:PLN02524  81 KTCGTTKLLLSIPPLLELAARLSLSVRSVKYTRGSFIFPGAQPFPHRSFSEEVSVLDGHFGKLGLGGKAYVMGDPD-KGQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853  161 RWHVYSASSTEESaVCDKPVYTLEMCMTGLDNIKASVFFKTNS-VSASEMTISSGIRNILPGSEICDFNFEPCGYSMNSI 239
Cdd:PLN02524 160 KWHVYSASAHNSS-NSNEPVYTLEMCMTGLDREKASVFFKDSSlSSAEEMTKASGIRKILPESEICDFAFDPCGYSMNGI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853  240 EGDAVSTIHVTPEDGFSYASFETVGYDLKALNFKELVDRVLVCFGPEEFSVAVHANLGTEVLASDCVADVNGYFSQEREL 319
Cdd:PLN02524 239 EGDAISTIHVTPEDGFSYASFEAMGYDPGDLDLSQLVERVLACFKPKEFSVAVHANVGGEAGSWGCSLDPDGYSCKGRSC 318
                        330       340
                 ....*....|....*....|....*..
gi 15230853  320 EELGLGGSVLYQRFVKTVECCSPKSTL 346
Cdd:PLN02524 319 QELPGGGSVVYQTFTATGGCGSPRSTL 345
SAM_decarbox pfam01536
Adenosylmethionine decarboxylase; This is a family of S-adenosylmethionine decarboxylase ...
5-333 4.22e-169

Adenosylmethionine decarboxylase; This is a family of S-adenosylmethionine decarboxylase (SAMDC) proenzymes. In the biosynthesis of polyamines SAMDC produces decarboxylated S-adenosylmethionine, which serves as the aminopropyl moiety necessary for spermidine and spermine biosynthesis from putrescine. The Pfam alignment contains both the alpha and beta chains that are cleaved to form the active enzyme.


Pssm-ID: 460243  Cd Length: 331  Bit Score: 473.94  E-value: 4.22e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853     5 ATGFEGFEKRLEISFFETTDFL-DPQGKSLRSLTKSQLDEILTPAECTIVSSLTNSFVDSYVLSESSLFVYPYKIIIKTC 83
Cdd:pfam01536   1 TIAFEGPEKLLEIWFSPSSGFIpSGDEGGLRSIPREKWEEILDLVKCEILSVKSNDKVDAYVLSESSLFVYPHKIILKTC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853    84 GTTKLLLSIPHILRLADSLC--LTVKSVRYTRGSFIFPGAQSYPHRSFSEEVALLDDYFGKlnagSKAFVMGgsDNNPQR 161
Cdd:pfam01536  81 GTTTLLLCLPPLLELAKEELgfLEVYKVFYSRKNFMFPEKQPSPHRSFSEEVAYLDKFFPN----GKAYVVG--RMNSDH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853   162 WHVYSASSTEESAVCDkPVYTLEMCMTGLDNIKASVFFKTNSVSASEMTISSGIRNILPGSEICDFNFEPCGYSMNSIEG 241
Cdd:pfam01536 155 WHLYTASDPESLSSPE-PDQTLEILMTGLDPEKAKQFYKDGHVSGAEMTKASGIDDILPGSIIDDFAFDPCGYSMNGIEG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853   242 D-AVSTIHVTPEDGFSYASFETVGYDLKALNFKELVDRVLVCFGPEEFSVAVHANLGTEVLASDCVADV------NGYFS 314
Cdd:pfam01536 234 DgAYSTIHVTPEDGFSYASFETNVPYDPEVDYSDLIRKVLKVFKPGKFSVTLFANSSSPSWAKCLKLDVsklqklGGYKR 313
                         330
                  ....*....|....*....
gi 15230853   315 QERELEELGlGGSVLYQRF 333
Cdd:pfam01536 314 LDRIVYELD-GYSLVYQSF 331
SAM_DCase TIGR00535
S-adenosylmethionine decarboxylase proenzyme, eukaryotic form; This enzyme is a key regulatory ...
8-336 2.74e-143

S-adenosylmethionine decarboxylase proenzyme, eukaryotic form; This enzyme is a key regulatory enzyme of the polyamine synthetic pathway. This protein is a pyruvoyl-dependent enzyme. The proenzyme is cleaved at a Ser residue that becomes a pyruvoyl group active site. [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 273124  Cd Length: 334  Bit Score: 408.47  E-value: 2.74e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853     8 FEGFEKRLEISFFETTDFLDpQGKSLRSLTKSQLDEILTPAECTIVSSLTNSFVDSYVLSESSLFVYPYKIIIKTCGTTK 87
Cdd:TIGR00535   1 FEGPEKLLEIWFFEHKKFID-EGKGLRAIGRAQIDEILDLARCTILSSKKNKSLDSYVLSESSLFIYDHKIIIKTCGTTK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853    88 LLLSIPHILRLADSL--CLTVKSVRYTRGSFIFPGAQSYPHRSFSEEVALLDDYFGKLnagsKAFVMGGSDnNPQRWHVY 165
Cdd:TIGR00535  80 LLFALPKILQLAEQLssWYKVFSVFYSRGCFLFPCAQPAIHRNFSEEVAYLNKFFGNG----KAYVVGDPA-KPQKWHLY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853   166 SASSTEESAVCDKPVYTLEMCMTGLDNIKASVFFKTNSVS----ASEMTISSGIRNILP-GSEICDFNFEPCGYSMNSIE 240
Cdd:TIGR00535 155 VAETERETPKIEDPDETLEMLMTGLDKEKASKFFKGPAASthnlGYQMTKNSGIDKIIPnSAQICDFDFEPCGYSMNAIL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853   241 G-DAVSTIHVTPEDGFSYASFETVGYDLKALNFKELVDRVLVCFGPEEFSVAVHANLGT-EVLASDCVADVNGYFSQERE 318
Cdd:TIGR00535 235 GeKAYSTIHVTPEKGFSYASFESNGIDQGKQDYLDLVLRVLNCFQPSEFSMTVFAKNYQnQSFQKLLSINESLPDYIKLD 314
                         330
                  ....*....|....*....
gi 15230853   319 LEELGLG-GSVLYQRFVKT 336
Cdd:TIGR00535 315 KQELDLGdYHLFYQKFQKK 333
 
Name Accession Description Interval E-value
PLN02524 PLN02524
S-adenosylmethionine decarboxylase
1-346 0e+00

S-adenosylmethionine decarboxylase


Pssm-ID: 215287  Cd Length: 355  Bit Score: 612.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853    1 MAVSATGFEGFEKRLEISFFETTDFLDPQGKSLRSLTKSQLDEILTPAECTIVSSLTNSFVDSYVLSESSLFVYPYKIII 80
Cdd:PLN02524   1 MPVSAIGFEGFEKRLEITFFEPPVFADPNGRGLRALTRSQLDEILRPAECTIVSSLSNDQFDSYVLSESSLFVYPYKIII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853   81 KTCGTTKLLLSIPHILRLADSLCLTVKSVRYTRGSFIFPGAQSYPHRSFSEEVALLDDYFGKLNAGSKAFVMGGSDnNPQ 160
Cdd:PLN02524  81 KTCGTTKLLLSIPPLLELAARLSLSVRSVKYTRGSFIFPGAQPFPHRSFSEEVSVLDGHFGKLGLGGKAYVMGDPD-KGQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853  161 RWHVYSASSTEESaVCDKPVYTLEMCMTGLDNIKASVFFKTNS-VSASEMTISSGIRNILPGSEICDFNFEPCGYSMNSI 239
Cdd:PLN02524 160 KWHVYSASAHNSS-NSNEPVYTLEMCMTGLDREKASVFFKDSSlSSAEEMTKASGIRKILPESEICDFAFDPCGYSMNGI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853  240 EGDAVSTIHVTPEDGFSYASFETVGYDLKALNFKELVDRVLVCFGPEEFSVAVHANLGTEVLASDCVADVNGYFSQEREL 319
Cdd:PLN02524 239 EGDAISTIHVTPEDGFSYASFEAMGYDPGDLDLSQLVERVLACFKPKEFSVAVHANVGGEAGSWGCSLDPDGYSCKGRSC 318
                        330       340
                 ....*....|....*....|....*..
gi 15230853  320 EELGLGGSVLYQRFVKTVECCSPKSTL 346
Cdd:PLN02524 319 QELPGGGSVVYQTFTATGGCGSPRSTL 345
SAM_decarbox pfam01536
Adenosylmethionine decarboxylase; This is a family of S-adenosylmethionine decarboxylase ...
5-333 4.22e-169

Adenosylmethionine decarboxylase; This is a family of S-adenosylmethionine decarboxylase (SAMDC) proenzymes. In the biosynthesis of polyamines SAMDC produces decarboxylated S-adenosylmethionine, which serves as the aminopropyl moiety necessary for spermidine and spermine biosynthesis from putrescine. The Pfam alignment contains both the alpha and beta chains that are cleaved to form the active enzyme.


Pssm-ID: 460243  Cd Length: 331  Bit Score: 473.94  E-value: 4.22e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853     5 ATGFEGFEKRLEISFFETTDFL-DPQGKSLRSLTKSQLDEILTPAECTIVSSLTNSFVDSYVLSESSLFVYPYKIIIKTC 83
Cdd:pfam01536   1 TIAFEGPEKLLEIWFSPSSGFIpSGDEGGLRSIPREKWEEILDLVKCEILSVKSNDKVDAYVLSESSLFVYPHKIILKTC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853    84 GTTKLLLSIPHILRLADSLC--LTVKSVRYTRGSFIFPGAQSYPHRSFSEEVALLDDYFGKlnagSKAFVMGgsDNNPQR 161
Cdd:pfam01536  81 GTTTLLLCLPPLLELAKEELgfLEVYKVFYSRKNFMFPEKQPSPHRSFSEEVAYLDKFFPN----GKAYVVG--RMNSDH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853   162 WHVYSASSTEESAVCDkPVYTLEMCMTGLDNIKASVFFKTNSVSASEMTISSGIRNILPGSEICDFNFEPCGYSMNSIEG 241
Cdd:pfam01536 155 WHLYTASDPESLSSPE-PDQTLEILMTGLDPEKAKQFYKDGHVSGAEMTKASGIDDILPGSIIDDFAFDPCGYSMNGIEG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853   242 D-AVSTIHVTPEDGFSYASFETVGYDLKALNFKELVDRVLVCFGPEEFSVAVHANLGTEVLASDCVADV------NGYFS 314
Cdd:pfam01536 234 DgAYSTIHVTPEDGFSYASFETNVPYDPEVDYSDLIRKVLKVFKPGKFSVTLFANSSSPSWAKCLKLDVsklqklGGYKR 313
                         330
                  ....*....|....*....
gi 15230853   315 QERELEELGlGGSVLYQRF 333
Cdd:pfam01536 314 LDRIVYELD-GYSLVYQSF 331
SAM_DCase TIGR00535
S-adenosylmethionine decarboxylase proenzyme, eukaryotic form; This enzyme is a key regulatory ...
8-336 2.74e-143

S-adenosylmethionine decarboxylase proenzyme, eukaryotic form; This enzyme is a key regulatory enzyme of the polyamine synthetic pathway. This protein is a pyruvoyl-dependent enzyme. The proenzyme is cleaved at a Ser residue that becomes a pyruvoyl group active site. [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 273124  Cd Length: 334  Bit Score: 408.47  E-value: 2.74e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853     8 FEGFEKRLEISFFETTDFLDpQGKSLRSLTKSQLDEILTPAECTIVSSLTNSFVDSYVLSESSLFVYPYKIIIKTCGTTK 87
Cdd:TIGR00535   1 FEGPEKLLEIWFFEHKKFID-EGKGLRAIGRAQIDEILDLARCTILSSKKNKSLDSYVLSESSLFIYDHKIIIKTCGTTK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853    88 LLLSIPHILRLADSL--CLTVKSVRYTRGSFIFPGAQSYPHRSFSEEVALLDDYFGKLnagsKAFVMGGSDnNPQRWHVY 165
Cdd:TIGR00535  80 LLFALPKILQLAEQLssWYKVFSVFYSRGCFLFPCAQPAIHRNFSEEVAYLNKFFGNG----KAYVVGDPA-KPQKWHLY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853   166 SASSTEESAVCDKPVYTLEMCMTGLDNIKASVFFKTNSVS----ASEMTISSGIRNILP-GSEICDFNFEPCGYSMNSIE 240
Cdd:TIGR00535 155 VAETERETPKIEDPDETLEMLMTGLDKEKASKFFKGPAASthnlGYQMTKNSGIDKIIPnSAQICDFDFEPCGYSMNAIL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230853   241 G-DAVSTIHVTPEDGFSYASFETVGYDLKALNFKELVDRVLVCFGPEEFSVAVHANLGT-EVLASDCVADVNGYFSQERE 318
Cdd:TIGR00535 235 GeKAYSTIHVTPEKGFSYASFESNGIDQGKQDYLDLVLRVLNCFQPSEFSMTVFAKNYQnQSFQKLLSINESLPDYIKLD 314
                         330
                  ....*....|....*....
gi 15230853   319 LEELGLG-GSVLYQRFVKT 336
Cdd:TIGR00535 315 KQELDLGdYHLFYQKFQKK 333
 
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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