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Conserved domains on  [gi|2171360776|ref|NP_001385895|]
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adipocyte plasma membrane-associated protein isoform 2 [Rattus norvegicus]

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

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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 ...
200-280 6.72e-29

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: 105.60  E-value: 6.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 200 NDLTITRDGRKIYFTDSSSKWQRRDYLLLVMEGTDDGRLLEYDTVTKEVKVLLDQLQFPNGVQLSPEEDFVLVAETAMAR 279
Cdd:pfam03088   1 NALDVDPETGVLYFTDSSSRYDRRQVIAAFLEGDATGRLMKYDPTTKVTKVLLDDLYFPNGIALSPDGSFVLFCETPMAR 80

                  .
gi 2171360776 280 I 280
Cdd:pfam03088  81 I 81
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
92-285 6.53e-22

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: 92.26  E-value: 6.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776  92 RLFENQLNGPESIVNI--GDVLFTGTADGRVVKL--ENGEIETIARfgsgpcktrddepTCGRPLGIRVGPNGTLFVVDA 167
Cdd:COG3386     1 KLADAGFRLGEGPVWDpdGRLYWVDIPGGRIHRYdpDGGAVEVFAE-------------PSGRPNGLAFDPDGRLLVADH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 168 YKGLFEVNPQKRSVKLLLSSEtpieGKKMSFVNDLTITRDGRkIYFTDSSskwqrrdylllvmEGTDDGRLLEYDTvTKE 247
Cdd:COG3386    68 GRGLVRFDPADGEVTVLADEY----GKPLNRPNDGVVDPDGR-LYFTDMG-------------EYLPTGALYRVDP-DGS 128
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2171360776 248 VKVLLDQLQFPNGVQLSPEEDFVLVAETAMARIRSCSV 285
Cdd:COG3386   129 LRVLADGLTFPNGIAFSPDGRTLYVADTGAGRIYRFDL 166
 
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 ...
200-280 6.72e-29

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: 105.60  E-value: 6.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 200 NDLTITRDGRKIYFTDSSSKWQRRDYLLLVMEGTDDGRLLEYDTVTKEVKVLLDQLQFPNGVQLSPEEDFVLVAETAMAR 279
Cdd:pfam03088   1 NALDVDPETGVLYFTDSSSRYDRRQVIAAFLEGDATGRLMKYDPTTKVTKVLLDDLYFPNGIALSPDGSFVLFCETPMAR 80

                  .
gi 2171360776 280 I 280
Cdd:pfam03088  81 I 81
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
92-285 6.53e-22

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: 92.26  E-value: 6.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776  92 RLFENQLNGPESIVNI--GDVLFTGTADGRVVKL--ENGEIETIARfgsgpcktrddepTCGRPLGIRVGPNGTLFVVDA 167
Cdd:COG3386     1 KLADAGFRLGEGPVWDpdGRLYWVDIPGGRIHRYdpDGGAVEVFAE-------------PSGRPNGLAFDPDGRLLVADH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 168 YKGLFEVNPQKRSVKLLLSSEtpieGKKMSFVNDLTITRDGRkIYFTDSSskwqrrdylllvmEGTDDGRLLEYDTvTKE 247
Cdd:COG3386    68 GRGLVRFDPADGEVTVLADEY----GKPLNRPNDGVVDPDGR-LYFTDMG-------------EYLPTGALYRVDP-DGS 128
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2171360776 248 VKVLLDQLQFPNGVQLSPEEDFVLVAETAMARIRSCSV 285
Cdd:COG3386   129 LRVLADGLTFPNGIAFSPDGRTLYVADTGAGRIYRFDL 166
SSL_N pfam20067
Strictosidine synthase-like, N-terminal; This domain is found at the N-terminal of ...
79-123 9.42e-07

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: 44.79  E-value: 9.42e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2171360776  79 GVLQPNTKLRQAERLFENQLNGPESIVnIGD--VLFTGTADGRVVKL 123
Cdd:pfam20067   1 GPFAPNDRLAGAELIALGGEHGPEDIA-VDPdgRLYTGLHDGRIVRM 46
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
95-281 1.94e-05

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: 45.00  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776  95 ENQLNGPESIV--NIGDVLFTGTADGRVVKL--ENGEIETIARFGSGPCKTRddeptcgRPLGIRVGPNGTLFVVDAYKG 170
Cdd:cd05819     4 PGELNNPQGIAvdSSGNIYVADTGNNRIQVFdpDGNFITSFGSFGSGDGQFN-------EPAGVAVDSDGNLYVADTGNH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 171 -LFEVNPQKRSVKLLLSSETPIEGkkMSFVNDLTITRDGRkIYFTDSSSKWqrrdylllVMEGTDDGRLLeydTVTKEVK 249
Cdd:cd05819    77 rIQKFDPDGNFLASFGGSGDGDGE--FNGPRGIAVDSSGN-IYVADTGNHR--------IQKFDPDGEFL---TTFGSGG 142
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2171360776 250 VLLDQLQFPNGVQLSPEEDfVLVAETAMARIR 281
Cdd:cd05819   143 SGPGQFNGPTGVAVDSDGN-IYVADTGNHRIQ 173
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
148-281 8.47e-04

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 40.00  E-value: 8.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 148 CGRPLGIRVGPNGTLFVVDAYKG-LFEVNPQKRSVklllsseTPIEGKKMSFVNDLTITRDGRkIYFTDSSskwqrrdyl 226
Cdd:COG4257    16 GSGPRDVAVDPDGAVWFTDQGGGrIGRLDPATGEF-------TEYPLGGGSGPHGIAVDPDGN-LWFTDNG--------- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2171360776 227 llvmegtdDGRLLEYDTVTKEVKVLL--DQLQFPNGVQLSPEEDfVLVAETAMARIR 281
Cdd:COG4257    79 --------NNRIGRIDPKTGEITTFAlpGGGSNPHGIAFDPDGN-LWFTDQGGNRIG 126
 
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 ...
200-280 6.72e-29

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: 105.60  E-value: 6.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 200 NDLTITRDGRKIYFTDSSSKWQRRDYLLLVMEGTDDGRLLEYDTVTKEVKVLLDQLQFPNGVQLSPEEDFVLVAETAMAR 279
Cdd:pfam03088   1 NALDVDPETGVLYFTDSSSRYDRRQVIAAFLEGDATGRLMKYDPTTKVTKVLLDDLYFPNGIALSPDGSFVLFCETPMAR 80

                  .
gi 2171360776 280 I 280
Cdd:pfam03088  81 I 81
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
92-285 6.53e-22

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: 92.26  E-value: 6.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776  92 RLFENQLNGPESIVNI--GDVLFTGTADGRVVKL--ENGEIETIARfgsgpcktrddepTCGRPLGIRVGPNGTLFVVDA 167
Cdd:COG3386     1 KLADAGFRLGEGPVWDpdGRLYWVDIPGGRIHRYdpDGGAVEVFAE-------------PSGRPNGLAFDPDGRLLVADH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 168 YKGLFEVNPQKRSVKLLLSSEtpieGKKMSFVNDLTITRDGRkIYFTDSSskwqrrdylllvmEGTDDGRLLEYDTvTKE 247
Cdd:COG3386    68 GRGLVRFDPADGEVTVLADEY----GKPLNRPNDGVVDPDGR-LYFTDMG-------------EYLPTGALYRVDP-DGS 128
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2171360776 248 VKVLLDQLQFPNGVQLSPEEDFVLVAETAMARIRSCSV 285
Cdd:COG3386   129 LRVLADGLTFPNGIAFSPDGRTLYVADTGAGRIYRFDL 166
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
79-281 1.84e-08

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 54.26  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776  79 GVLQPNTKlrQAERLFENQLNGPESIV--NIGDVLFTGTADGRVVKL--ENGEIETIArfgsGPCKTRDdeptcgrPLGI 154
Cdd:COG4257    41 GRLDPATG--EFTEYPLGGGSGPHGIAvdPDGNLWFTDNGNNRIGRIdpKTGEITTFA----LPGGGSN-------PHGI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 155 RVGPNGTLFVVDAYKG-LFEVNPQKRSVKLLLSsetpieGKKMSFVNDLTITRDGRkIYFTDSSSkwqrrdylllvmegt 233
Cdd:COG4257   108 AFDPDGNLWFTDQGGNrIGRLDPATGEVTEFPL------PTGGAGPYGIAVDPDGN-LWVTDFGA--------------- 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2171360776 234 ddGRLLEYDTVTKEVKV--LLDQLQFPNGVQLSPeEDFVLVAETAMARIR 281
Cdd:COG4257   166 --NAIGRIDPDTGTLTEyaLPTPGAGPRGLAVDP-DGNLWVADTGSGRIG 212
SGL pfam08450
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
143-285 6.45e-07

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: 49.18  E-value: 6.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 143 DDEPTCGRPlgirvGPNGTLFVVDAYkGLFEVNPQKRSVKLLLSSETPiEGKKMSFvNDLTITRDGRkIYFTDsssKWQR 222
Cdd:pfam08450  40 PGPVGAIAP-----RDDGGLIVALKD-GVALLDLATGELTPLADPEDD-DWPLNRF-NDGKVDPDGR-FWFGT---MGDD 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2171360776 223 RDylllvmEGTDDGRLLEYDTVTKeVKVLLDQLQFPNGVQLSPEEDFVLVAETAMARIRSCSV 285
Cdd:pfam08450 108 EA------PGGDPGALYRLDPDGK-LTRVLDGLTISNGLAWSPDGRTLYFADSPARKIWAYDY 163
SSL_N pfam20067
Strictosidine synthase-like, N-terminal; This domain is found at the N-terminal of ...
79-123 9.42e-07

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: 44.79  E-value: 9.42e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2171360776  79 GVLQPNTKLRQAERLFENQLNGPESIVnIGD--VLFTGTADGRVVKL 123
Cdd:pfam20067   1 GPFAPNDRLAGAELIALGGEHGPEDIA-VDPdgRLYTGLHDGRIVRM 46
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
108-275 4.98e-06

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 46.61  E-value: 4.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 108 GDVLF-TGTADGRVVKLENGEIETIARFGSGpcktrddeptcGRPLGIRVGPNG-TLFVVDAYKG-LFEVNPQKRSVKll 184
Cdd:COG3391    79 GRRLYvANSGSGRVSVIDLATGKVVATIPVG-----------GGPRGLAVDPDGgRLYVADSGNGrVSVIDTATGKVV-- 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 185 lsseTPIEGKKMSfvNDLTITRDGRKIYFTDSSSkwqrrDYLLLVmegtddgrLLEYDTVTKEVKVLLDQLQFPNGVQLS 264
Cdd:COG3391   146 ----ATIPVGAGP--HGIAVDPDGKRLYVANSGS-----NTVSVI--------VSVIDTATGKVVATIPVGGGPVGVAVS 206
                         170
                  ....*....|.
gi 2171360776 265 PEEDFVLVAET 275
Cdd:COG3391   207 PDGRRLYVANR 217
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
95-281 1.94e-05

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: 45.00  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776  95 ENQLNGPESIV--NIGDVLFTGTADGRVVKL--ENGEIETIARFGSGPCKTRddeptcgRPLGIRVGPNGTLFVVDAYKG 170
Cdd:cd05819     4 PGELNNPQGIAvdSSGNIYVADTGNNRIQVFdpDGNFITSFGSFGSGDGQFN-------EPAGVAVDSDGNLYVADTGNH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 171 -LFEVNPQKRSVKLLLSSETPIEGkkMSFVNDLTITRDGRkIYFTDSSSKWqrrdylllVMEGTDDGRLLeydTVTKEVK 249
Cdd:cd05819    77 rIQKFDPDGNFLASFGGSGDGDGE--FNGPRGIAVDSSGN-IYVADTGNHR--------IQKFDPDGEFL---TTFGSGG 142
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2171360776 250 VLLDQLQFPNGVQLSPEEDfVLVAETAMARIR 281
Cdd:cd05819   143 SGPGQFNGPTGVAVDSDGN-IYVADTGNHRIQ 173
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
108-281 2.87e-05

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 44.63  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 108 GDVLFTGTADGRVVKL--ENGEIETIARFGSGpcktrddeptcGRPLGIRVGPNGTLFVVDAYKG-LFEVNPQKRSVKLL 184
Cdd:COG4257   113 GNLWFTDQGGNRIGRLdpATGEVTEFPLPTGG-----------AGPYGIAVDPDGNLWVTDFGANaIGRIDPDTGTLTEY 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 185 lssETPIEGkkmSFVNDLTITRDGRkIYFTDssskwqrrdylllvmegTDDGRLLEYDTVTKEVK--VLLDQLQFPNGVQ 262
Cdd:COG4257   182 ---ALPTPG---AGPRGLAVDPDGN-LWVAD-----------------TGSGRIGRFDPKTGTVTeyPLPGGGARPYGVA 237
                         170
                  ....*....|....*....
gi 2171360776 263 LSPeEDFVLVAETAMARIR 281
Cdd:COG4257   238 VDG-DGRVWFAESGANRIV 255
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
94-280 7.39e-04

Uncharacterized NHL-repeat domain in bacterial 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.


Pssm-ID: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 40.35  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776  94 FENQLNGPESI-VNIGDVLFTGTADGRVV--KLENGEIETIARFGSGPCKTRddeptcgRPLGIRVGPNGTLFVVDAYKG 170
Cdd:cd14963     5 FGDPLNKPMGVaVSDGRIYVADTNNHRVQvfDYEGKFKKSFGGPGTGPGEFK-------YPYGIAVDSDGNIYVADLYNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 171 LFEV-NPQKRSVKLLLSSEtpiEGKKMSFVNDLTItrDGRKIYFTDSSskwqrrdylllvmegtdDGRLLEYDTVTKEVK 249
Cdd:cd14963    78 RIQVfDPDGKFLKYFPEKK---DRVKLISPAGLAI--DDGKLYVSDVK-----------------KHKVIVFDLEGKLLL 135
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2171360776 250 VL------LDQLQFPNGVQLSpEEDFVLVAETAMARI 280
Cdd:cd14963   136 EFgkpgsePGELSYPNGIAVD-EDGNIYVADSGNGRI 171
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
148-281 8.47e-04

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 40.00  E-value: 8.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360776 148 CGRPLGIRVGPNGTLFVVDAYKG-LFEVNPQKRSVklllsseTPIEGKKMSFVNDLTITRDGRkIYFTDSSskwqrrdyl 226
Cdd:COG4257    16 GSGPRDVAVDPDGAVWFTDQGGGrIGRLDPATGEF-------TEYPLGGGSGPHGIAVDPDGN-LWFTDNG--------- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2171360776 227 llvmegtdDGRLLEYDTVTKEVKVLL--DQLQFPNGVQLSPEEDfVLVAETAMARIR 281
Cdd:COG4257    79 --------NNRIGRIDPKTGEITTFAlpGGGSNPHGIAFDPDGN-LWFTDQGGNRIG 126
 
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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