NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|530425819|ref|XP_005260820|]
View 

adipocyte plasma membrane-associated protein isoform X1 [Homo sapiens]

Protein Classification

strictosidine synthase family protein( domain architecture ID 11465301)

strictosidine synthase family protein with similarity to strictosidine synthase that catalyzes the stereospecific condensation of tryptamine with secologanin to form strictosidine, the key intermediate of indole alkaloid biosynthesis

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Str_synth super family cl22863
Strictosidine synthase; Strictosidine synthase (E.C. 4.3.3.2) is a key enzyme in alkaloid ...
 201-287 1.16e-28

Strictosidine synthase; Strictosidine synthase (E.C. 4.3.3.2) is a key enzyme in alkaloid biosynthesis. It catalyzes the condensation of tryptamine with secologanin to form strictosidine.


The actual alignment was detected with superfamily member pfam03088:

Pssm-ID: 354965 [Multi-domain]  Cd Length: 89  Bit Score: 105.21  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819  201 NDLTVTQDGRKIYFTDSSSKWQRRDYLLLVMEGTDDGRLLEYDTVTREVKVLLDQLRFPNGVQLSPAEDFVLVAETTMAR 280
Cdd:pfam03088   1 NALDVDPETGVLYFTDSSSRYDRRQVIAAFLEGDATGRLMKYDPTTKVTKVLLDDLYFPNGIALSPDGSFVLFCETPMAR 80


                  ....*..
gi 530425819  281 IRSSLVK 287
Cdd:pfam03088  81 ISRYWIK 87
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
 93-283 1.33e-19

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


:

Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 85.71  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819  93 RLFENQLVGPESIA--HIGDVMFTGTADGRVVKL--ENGEIETIARfgsgpcktrddepVCGRPLGIRAGPNGTLFVADA 168
Cdd:COG3386    1 KLADAGFRLGEGPVwdPDGRLYWVDIPGGRIHRYdpDGGAVEVFAE-------------PSGRPNGLAFDPDGRLLVADH 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819 169 YKGLFEVNPWKREVKLLLSSEtpieGKNMSFVNDLTVTQDGRkIYFTDSSskwqrrdylllvmEGTDDGRLLEYDTvTRE 248
Cdd:COG3386   68 GRGLVRFDPADGEVTVLADEY----GKPLNRPNDGVVDPDGR-LYFTDMG-------------EYLPTGALYRVDP-DGS 128

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530425819 249 VKVLLDQLRFPNGVQLSPAEDFVLVAETTMARIRS 283
Cdd:COG3386  129 LRVLADGLTFPNGIAFSPDGRTLYVADTGAGRIYR 163
 
Name Accession Description Interval E-value
Str_synth pfam03088
Strictosidine synthase; Strictosidine synthase (E.C. 4.3.3.2) is a key enzyme in alkaloid ...
 201-287 1.16e-28

Strictosidine synthase; Strictosidine synthase (E.C. 4.3.3.2) is a key enzyme in alkaloid biosynthesis. It catalyzes the condensation of tryptamine with secologanin to form strictosidine.


Pssm-ID: 281131 [Multi-domain]  Cd Length: 89  Bit Score: 105.21  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819  201 NDLTVTQDGRKIYFTDSSSKWQRRDYLLLVMEGTDDGRLLEYDTVTREVKVLLDQLRFPNGVQLSPAEDFVLVAETTMAR 280
Cdd:pfam03088   1 NALDVDPETGVLYFTDSSSRYDRRQVIAAFLEGDATGRLMKYDPTTKVTKVLLDDLYFPNGIALSPDGSFVLFCETPMAR 80


                  ....*..
gi 530425819  281 IRSSLVK 287
Cdd:pfam03088  81 ISRYWIK 87
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
 93-283 1.33e-19

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 85.71  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819  93 RLFENQLVGPESIA--HIGDVMFTGTADGRVVKL--ENGEIETIARfgsgpcktrddepVCGRPLGIRAGPNGTLFVADA 168
Cdd:COG3386    1 KLADAGFRLGEGPVwdPDGRLYWVDIPGGRIHRYdpDGGAVEVFAE-------------PSGRPNGLAFDPDGRLLVADH 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819 169 YKGLFEVNPWKREVKLLLSSEtpieGKNMSFVNDLTVTQDGRkIYFTDSSskwqrrdylllvmEGTDDGRLLEYDTvTRE 248
Cdd:COG3386   68 GRGLVRFDPADGEVTVLADEY----GKPLNRPNDGVVDPDGR-LYFTDMG-------------EYLPTGALYRVDP-DGS 128

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530425819 249 VKVLLDQLRFPNGVQLSPAEDFVLVAETTMARIRS 283
Cdd:COG3386  129 LRVLADGLTFPNGIAFSPDGRTLYVADTGAGRIYR 163
SSL_N pfam20067
Strictosidine synthase-like, N-terminal; This domain is found at the N-terminal of ...
 80-124 8.03e-06

Strictosidine synthase-like, N-terminal; This domain is found at the N-terminal of strictosidine synthase-like (SSL) proteins including Adipocyte plasma membrane- associated proteins (APMAPs) from animals, Protein STRICTOSIDINE SYNTHASE-LIKE (SSLs) from Arabidopsis and SGL proteins, being also present in bacterial sequences. It is about 50 amino acids in length. It contains residues involved in metal coordination in the active site. This domain is also found in Gluconolactonase and Sugar lactone lactonase. These proteins share a six-bladed beta-propeller fold structure and have similar structural and mechanistic features to SS (strictosidine synthase) that involve nucleophilic attack on an electrophilic substrate, although they do not catalyze the SS reaction as they lack the catalytic glutamate required for SS activity; they catalyze hydrolytic reactions instead. APMAPs shows similarity with paraoxonases (PON) and has a strong arylesterase activity with beta-naphthyl acetate and phenyl acetate. They are involved in adipocyte differentiation.


Pssm-ID: 437899 [Multi-domain]  Cd Length: 46  Bit Score: 42.09  E-value: 8.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 530425819   80 GVLHPNTKLRQAERLFENQLVGPESIAHIGD-VMFTGTADGRVVKL 124
Cdd:pfam20067   1 GPFAPNDRLAGAELIALGGEHGPEDIAVDPDgRLYTGLHDGRIVRM 46
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
 96-282 7.39e-04

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 40.38  E-value: 7.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819  96 ENQLVGPESIA--HIGDVMFTGTADGRVVKL--ENGEIETIARFGSGPCKTRddepvcgRPLGIRAGPNGTLFVADAYKG 171
Cdd:cd05819    4 PGELNNPQGIAvdSSGNIYVADTGNNRIQVFdpDGNFITSFGSFGSGDGQFN-------EPAGVAVDSDGNLYVADTGNH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819 172 lfEVNPWKREVKLLLSSETPIEGKNMSF-VNDLTVTQDGRkIYFTDSSSKwqrrdylllvmegtddgRLLEYDTVTREVK 250
Cdd:cd05819   77 --RIQKFDPDGNFLASFGGSGDGDGEFNgPRGIAVDSSGN-IYVADTGNH-----------------RIQKFDPDGEFLT 136

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530425819 251 VL------LDQLRFPNGVQLSPAEDfVLVAETTMARIR 282
Cdd:cd05819  137 TFgsggsgPGQFNGPTGVAVDSDGN-IYVADTGNHRIQ 173
 
Name Accession Description Interval E-value
Str_synth pfam03088
Strictosidine synthase; Strictosidine synthase (E.C. 4.3.3.2) is a key enzyme in alkaloid ...
 201-287 1.16e-28

Strictosidine synthase; Strictosidine synthase (E.C. 4.3.3.2) is a key enzyme in alkaloid biosynthesis. It catalyzes the condensation of tryptamine with secologanin to form strictosidine.


Pssm-ID: 281131 [Multi-domain]  Cd Length: 89  Bit Score: 105.21  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819  201 NDLTVTQDGRKIYFTDSSSKWQRRDYLLLVMEGTDDGRLLEYDTVTREVKVLLDQLRFPNGVQLSPAEDFVLVAETTMAR 280
Cdd:pfam03088   1 NALDVDPETGVLYFTDSSSRYDRRQVIAAFLEGDATGRLMKYDPTTKVTKVLLDDLYFPNGIALSPDGSFVLFCETPMAR 80


                  ....*..
gi 530425819  281 IRSSLVK 287
Cdd:pfam03088  81 ISRYWIK 87
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
 93-283 1.33e-19

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 85.71  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819  93 RLFENQLVGPESIA--HIGDVMFTGTADGRVVKL--ENGEIETIARfgsgpcktrddepVCGRPLGIRAGPNGTLFVADA 168
Cdd:COG3386    1 KLADAGFRLGEGPVwdPDGRLYWVDIPGGRIHRYdpDGGAVEVFAE-------------PSGRPNGLAFDPDGRLLVADH 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819 169 YKGLFEVNPWKREVKLLLSSEtpieGKNMSFVNDLTVTQDGRkIYFTDSSskwqrrdylllvmEGTDDGRLLEYDTvTRE 248
Cdd:COG3386   68 GRGLVRFDPADGEVTVLADEY----GKPLNRPNDGVVDPDGR-LYFTDMG-------------EYLPTGALYRVDP-DGS 128

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530425819 249 VKVLLDQLRFPNGVQLSPAEDFVLVAETTMARIRS 283
Cdd:COG3386  129 LRVLADGLTFPNGIAFSPDGRTLYVADTGAGRIYR 163
SSL_N pfam20067
Strictosidine synthase-like, N-terminal; This domain is found at the N-terminal of ...
 80-124 8.03e-06

Strictosidine synthase-like, N-terminal; This domain is found at the N-terminal of strictosidine synthase-like (SSL) proteins including Adipocyte plasma membrane- associated proteins (APMAPs) from animals, Protein STRICTOSIDINE SYNTHASE-LIKE (SSLs) from Arabidopsis and SGL proteins, being also present in bacterial sequences. It is about 50 amino acids in length. It contains residues involved in metal coordination in the active site. This domain is also found in Gluconolactonase and Sugar lactone lactonase. These proteins share a six-bladed beta-propeller fold structure and have similar structural and mechanistic features to SS (strictosidine synthase) that involve nucleophilic attack on an electrophilic substrate, although they do not catalyze the SS reaction as they lack the catalytic glutamate required for SS activity; they catalyze hydrolytic reactions instead. APMAPs shows similarity with paraoxonases (PON) and has a strong arylesterase activity with beta-naphthyl acetate and phenyl acetate. They are involved in adipocyte differentiation.


Pssm-ID: 437899 [Multi-domain]  Cd Length: 46  Bit Score: 42.09  E-value: 8.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 530425819   80 GVLHPNTKLRQAERLFENQLVGPESIAHIGD-VMFTGTADGRVVKL 124
Cdd:pfam20067   1 GPFAPNDRLAGAELIALGGEHGPEDIAVDPDgRLYTGLHDGRIVRM 46
SGL pfam08450
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
 158-282 1.62e-05

SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE.


Pssm-ID: 462480 [Multi-domain]  Cd Length: 246  Bit Score: 45.33  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819  158 GPNGTLFVADAYkGLFEVNPWKREVKLLLSSETPiEGKNMSFvNDLTVTQDGRkIYFTDsssKWQRRDylllvmEGTDDG 237
Cdd:pfam08450  49 RDDGGLIVALKD-GVALLDLATGELTPLADPEDD-DWPLNRF-NDGKVDPDGR-FWFGT---MGDDEA------PGGDPG 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 530425819  238 RLLEYDTVTrEVKVLLDQLRFPNGVQLSPAEDFVLVAETTMARIR 282
Cdd:pfam08450 116 ALYRLDPDG-KLTRVLDGLTISNGLAWSPDGRTLYFADSPARKIW 159
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
113-276 3.48e-05

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 44.30  E-value: 3.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819 113 FTGTADGRVVKLENGEIETIARFGSGPCKTRDDEPVCGRPLGIRAGPNG-TLFVADAYKG-LFEVNPWKREVKlllsseT 190
Cdd:COG3391   73 ADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGgRLYVADSGNGrVSVIDTATGKVV------A 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819 191 PIEGKNMSfvNDLTVTQDGRKIYFTDSSSkwqrrDYLLLVmegtddgrLLEYDTVTREVKVLLDQLRFPNGVQLSPAEDF 270
Cdd:COG3391  147 TIPVGAGP--HGIAVDPDGKRLYVANSGS-----NTVSVI--------VSVIDTATGKVVATIPVGGGPVGVAVSPDGRR 211


                 ....*.
gi 530425819 271 VLVAET 276
Cdd:COG3391  212 LYVANR 217
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
 96-282 7.39e-04

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 40.38  E-value: 7.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819  96 ENQLVGPESIA--HIGDVMFTGTADGRVVKL--ENGEIETIARFGSGPCKTRddepvcgRPLGIRAGPNGTLFVADAYKG 171
Cdd:cd05819    4 PGELNNPQGIAvdSSGNIYVADTGNNRIQVFdpDGNFITSFGSFGSGDGQFN-------EPAGVAVDSDGNLYVADTGNH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819 172 lfEVNPWKREVKLLLSSETPIEGKNMSF-VNDLTVTQDGRkIYFTDSSSKwqrrdylllvmegtddgRLLEYDTVTREVK 250
Cdd:cd05819   77 --RIQKFDPDGNFLASFGGSGDGDGEFNgPRGIAVDSSGN-IYVADTGNH-----------------RIQKFDPDGEFLT 136

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530425819 251 VL------LDQLRFPNGVQLSPAEDfVLVAETTMARIR 282
Cdd:cd05819  137 TFgsggsgPGQFNGPTGVAVDSDGN-IYVADTGNHRIQ 173
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
109-282 1.68e-03

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 39.23  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819 109 GDVMFTGTADGRVVKL--ENGEIETIARFGSGpcktrddepvcGRPLGIRAGPNGTLFVADAYKG-LFEVNPWKREVKLL 185
Cdd:COG4257  113 GNLWFTDQGGNRIGRLdpATGEVTEFPLPTGG-----------AGPYGIAVDPDGNLWVTDFGANaIGRIDPDTGTLTEY 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819 186 lssETPIEGKNmsfVNDLTVTQDGRkIYFTDssskwqrrdylllvmegTDDGRLLEYDTVTREVK--VLLDQLRFPNGVQ 263
Cdd:COG4257  182 ---ALPTPGAG---PRGLAVDPDGN-LWVAD-----------------TGSGRIGRFDPKTGTVTeyPLPGGGARPYGVA 237

                        170
                 ....*....|....*....
gi 530425819 264 LSPAeDFVLVAETTMARIR 282
Cdd:COG4257  238 VDGD-GRVWFAESGANRIV 255
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
101-219 2.84e-03

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 38.46  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425819 101 GPESIA--HIGDVMFTGTADGRVVKL--ENGEIETIARFGSGpcktrddepvcGRPLGIRAGPNGTLFVADAYKG-LFEV 175
Cdd:COG4257  146 GPYGIAvdPDGNLWVTDFGANAIGRIdpDTGTLTEYALPTPG-----------AGPRGLAVDPDGNLWVADTGSGrIGRF 214

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 530425819 176 NPWKREVKLLLSSETPiegknmSFVNDLTVTQDGRkIYFTDSSS 219
Cdd:COG4257  215 DPKTGTVTEYPLPGGG------ARPYGVAVDGDGR-VWFAESGA 251
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH