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Conserved domains on  [gi|2171360870|ref|NP_001385894|]
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adipocyte plasma membrane-associated protein isoform 1 [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 ...
200-287 1.06e-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: 110.22  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 200 NDLTITRDGRKIYFTDSSSKWQRRDYLLLVMEGTDDGRLLEYDTVTKEVKVLLDQLQFPNGVQLSPEEDFVLVAETAMAR 279
Cdd:pfam03088   1 NALDVDPETGVLYFTDSSSRYDRRQVIAAFLEGDATGRLMKYDPTTKVTKVLLDDLYFPNGIALSPDGSFVLFCETPMAR 80

                  ....*...
gi 2171360870 280 IRRVYVSG 287
Cdd:pfam03088  81 ISRYWIKE 88
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
92-319 6.67e-26

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: 105.36  E-value: 6.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870  92 RLFENQLNGPESIVNI--GDVLFTGTADGRVVKL--ENGEIETIARfgsgpcktrddepTCGRPLGIRVGPNGTLFVVDA 167
Cdd:COG3386     1 KLADAGFRLGEGPVWDpdGRLYWVDIPGGRIHRYdpDGGAVEVFAE-------------PSGRPNGLAFDPDGRLLVADH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 168 YKGLFEVNPQKRSVKLLLSSEtpieGKKMSFVNDLTITRDGRkIYFTDSSskwqrrdylllvmEGTDDGRLLEYDTvTKE 247
Cdd:COG3386    68 GRGLVRFDPADGEVTVLADEY----GKPLNRPNDGVVDPDGR-LYFTDMG-------------EYLPTGALYRVDP-DGS 128
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2171360870 248 VKVLLDQLQFPNGVQLSPEEDFVLVAETAMARIRRV-YVSGLMKGGADMFVE--NMPGFPDNIRPSSSGGYWVAA 319
Cdd:COG3386   129 LRVLADGLTFPNGIAFSPDGRTLYVADTGAGRIYRFdLDADGTLGNRRVFADlpDGPGGPDGLAVDADGNLWVAL 203
 
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 ...
200-287 1.06e-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: 110.22  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 200 NDLTITRDGRKIYFTDSSSKWQRRDYLLLVMEGTDDGRLLEYDTVTKEVKVLLDQLQFPNGVQLSPEEDFVLVAETAMAR 279
Cdd:pfam03088   1 NALDVDPETGVLYFTDSSSRYDRRQVIAAFLEGDATGRLMKYDPTTKVTKVLLDDLYFPNGIALSPDGSFVLFCETPMAR 80

                  ....*...
gi 2171360870 280 IRRVYVSG 287
Cdd:pfam03088  81 ISRYWIKE 88
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
92-319 6.67e-26

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: 105.36  E-value: 6.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870  92 RLFENQLNGPESIVNI--GDVLFTGTADGRVVKL--ENGEIETIARfgsgpcktrddepTCGRPLGIRVGPNGTLFVVDA 167
Cdd:COG3386     1 KLADAGFRLGEGPVWDpdGRLYWVDIPGGRIHRYdpDGGAVEVFAE-------------PSGRPNGLAFDPDGRLLVADH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 168 YKGLFEVNPQKRSVKLLLSSEtpieGKKMSFVNDLTITRDGRkIYFTDSSskwqrrdylllvmEGTDDGRLLEYDTvTKE 247
Cdd:COG3386    68 GRGLVRFDPADGEVTVLADEY----GKPLNRPNDGVVDPDGR-LYFTDMG-------------EYLPTGALYRVDP-DGS 128
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2171360870 248 VKVLLDQLQFPNGVQLSPEEDFVLVAETAMARIRRV-YVSGLMKGGADMFVE--NMPGFPDNIRPSSSGGYWVAA 319
Cdd:COG3386   129 LRVLADGLTFPNGIAFSPDGRTLYVADTGAGRIYRFdLDADGTLGNRRVFADlpDGPGGPDGLAVDADGNLWVAL 203
SGL pfam08450
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
143-318 2.64e-10

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: 60.35  E-value: 2.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 143 DDEPTCGRPlgirvGPNGTLFVVDAYkGLFEVNPQKRSVKLLLSSETPiEGKKMSFvNDLTITRDGRkIYFTDsssKWQR 222
Cdd:pfam08450  40 PGPVGAIAP-----RDDGGLIVALKD-GVALLDLATGELTPLADPEDD-DWPLNRF-NDGKVDPDGR-FWFGT---MGDD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 223 RDylllvmEGTDDGRLLEYDTVTKeVKVLLDQLQFPNGVQLSPEEDFVLVAETAMARIRR--VYVSGLMKGGADMFV--E 298
Cdd:pfam08450 108 EA------PGGDPGALYRLDPDGK-LTRVLDGLTISNGLAWSPDGRTLYFADSPARKIWAydYDLDGGLISNRRVFAdfK 180
                         170       180
                  ....*....|....*....|
gi 2171360870 299 NMPGFPDNIRPSSSGGYWVA 318
Cdd:pfam08450 181 PGLGRPDGMAVDAEGNVWVA 200
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
95-283 4.49e-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: 44.62  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870  95 ENQLNGPESIV--NIGDVLFTGTADGRVVKL--ENGEIETIARFGSGPCKTRddeptcgRPLGIRVGPNGTLFVVDAYKG 170
Cdd:cd05819     4 PGELNNPQGIAvdSSGNIYVADTGNNRIQVFdpDGNFITSFGSFGSGDGQFN-------EPAGVAVDSDGNLYVADTGNH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 171 -LFEVNPQKRSVKLLLSSETPIEGkkMSFVNDLTITRDGRkIYFTDSSSKWqrrdylllVMEGTDDGRLLeydTVTKEVK 249
Cdd:cd05819    77 rIQKFDPDGNFLASFGGSGDGDGE--FNGPRGIAVDSSGN-IYVADTGNHR--------IQKFDPDGEFL---TTFGSGG 142
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2171360870 250 VLLDQLQFPNGVQLSPEEDfVLVAETAMARIRRV 283
Cdd:cd05819   143 SGPGQFNGPTGVAVDSDGN-IYVADTGNHRIQVF 175
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
148-283 1.95e-04

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 42.70  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 148 CGRPLGIRVGPNGTLFVVDAYKG-LFEVNPQKRSVklllsseTPIEGKKMSFVNDLTITRDGRkIYFTDSSskwqrrdyl 226
Cdd:COG4257    16 GSGPRDVAVDPDGAVWFTDQGGGrIGRLDPATGEF-------TEYPLGGGSGPHGIAVDPDGN-LWFTDNG--------- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2171360870 227 llvmegtdDGRLLEYDTVTKEVKVLL--DQLQFPNGVQLSPEEDfVLVAETAMARIRRV 283
Cdd:COG4257    79 --------NNRIGRIDPKTGEITTFAlpGGGSNPHGIAFDPDGN-LWFTDQGGNRIGRL 128
 
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 ...
200-287 1.06e-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: 110.22  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 200 NDLTITRDGRKIYFTDSSSKWQRRDYLLLVMEGTDDGRLLEYDTVTKEVKVLLDQLQFPNGVQLSPEEDFVLVAETAMAR 279
Cdd:pfam03088   1 NALDVDPETGVLYFTDSSSRYDRRQVIAAFLEGDATGRLMKYDPTTKVTKVLLDDLYFPNGIALSPDGSFVLFCETPMAR 80

                  ....*...
gi 2171360870 280 IRRVYVSG 287
Cdd:pfam03088  81 ISRYWIKE 88
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
92-319 6.67e-26

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: 105.36  E-value: 6.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870  92 RLFENQLNGPESIVNI--GDVLFTGTADGRVVKL--ENGEIETIARfgsgpcktrddepTCGRPLGIRVGPNGTLFVVDA 167
Cdd:COG3386     1 KLADAGFRLGEGPVWDpdGRLYWVDIPGGRIHRYdpDGGAVEVFAE-------------PSGRPNGLAFDPDGRLLVADH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 168 YKGLFEVNPQKRSVKLLLSSEtpieGKKMSFVNDLTITRDGRkIYFTDSSskwqrrdylllvmEGTDDGRLLEYDTvTKE 247
Cdd:COG3386    68 GRGLVRFDPADGEVTVLADEY----GKPLNRPNDGVVDPDGR-LYFTDMG-------------EYLPTGALYRVDP-DGS 128
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2171360870 248 VKVLLDQLQFPNGVQLSPEEDFVLVAETAMARIRRV-YVSGLMKGGADMFVE--NMPGFPDNIRPSSSGGYWVAA 319
Cdd:COG3386   129 LRVLADGLTFPNGIAFSPDGRTLYVADTGAGRIYRFdLDADGTLGNRRVFADlpDGPGGPDGLAVDADGNLWVAL 203
SGL pfam08450
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
143-318 2.64e-10

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: 60.35  E-value: 2.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 143 DDEPTCGRPlgirvGPNGTLFVVDAYkGLFEVNPQKRSVKLLLSSETPiEGKKMSFvNDLTITRDGRkIYFTDsssKWQR 222
Cdd:pfam08450  40 PGPVGAIAP-----RDDGGLIVALKD-GVALLDLATGELTPLADPEDD-DWPLNRF-NDGKVDPDGR-FWFGT---MGDD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 223 RDylllvmEGTDDGRLLEYDTVTKeVKVLLDQLQFPNGVQLSPEEDFVLVAETAMARIRR--VYVSGLMKGGADMFV--E 298
Cdd:pfam08450 108 EA------PGGDPGALYRLDPDGK-LTRVLDGLTISNGLAWSPDGRTLYFADSPARKIWAydYDLDGGLISNRRVFAdfK 180
                         170       180
                  ....*....|....*....|
gi 2171360870 299 NMPGFPDNIRPSSSGGYWVA 318
Cdd:pfam08450 181 PGLGRPDGMAVDAEGNVWVA 200
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
79-283 6.08e-09

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 56.57  E-value: 6.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870  79 GVLQPNTKlrQAERLFENQLNGPESIV--NIGDVLFTGTADGRVVKL--ENGEIETIArfgsGPCKTRDdeptcgrPLGI 154
Cdd:COG4257    41 GRLDPATG--EFTEYPLGGGSGPHGIAvdPDGNLWFTDNGNNRIGRIdpKTGEITTFA----LPGGGSN-------PHGI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 155 RVGPNGTLFVVDAYKG-LFEVNPQKRSVKLLLSsetpieGKKMSFVNDLTITRDGRkIYFTDSSSkwqrrdylllvmegt 233
Cdd:COG4257   108 AFDPDGNLWFTDQGGNrIGRLDPATGEVTEFPL------PTGGAGPYGIAVDPDGN-LWVTDFGA--------------- 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2171360870 234 ddGRLLEYDTVTKEVKV--LLDQLQFPNGVQLSPeEDFVLVAETAMARIRRV 283
Cdd:COG4257   166 --NAIGRIDPDTGTLTEyaLPTPGAGPRGLAVDP-DGNLWVADTGSGRIGRF 214
SSL_N pfam20067
Strictosidine synthase-like, N-terminal; This domain is found at the N-terminal of ...
79-123 1.48e-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: 44.79  E-value: 1.48e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2171360870  79 GVLQPNTKLRQAERLFENQLNGPESIVnIGD--VLFTGTADGRVVKL 123
Cdd:pfam20067   1 GPFAPNDRLAGAELIALGGEHGPEDIA-VDPdgRLYTGLHDGRIVRM 46
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
108-283 6.19e-06

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 47.32  E-value: 6.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 108 GDVLFTGTADGRVVKL--ENGEIETIARFGSGpcktrddeptcGRPLGIRVGPNGTLFVVDAYKG-LFEVNPQKRSVKLL 184
Cdd:COG4257   113 GNLWFTDQGGNRIGRLdpATGEVTEFPLPTGG-----------AGPYGIAVDPDGNLWVTDFGANaIGRIDPDTGTLTEY 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 185 lssETPIEGkkmSFVNDLTITRDGRkIYFTDssskwqrrdylllvmegTDDGRLLEYDTVTKEVK--VLLDQLQFPNGVQ 262
Cdd:COG4257   182 ---ALPTPG---AGPRGLAVDPDGN-LWVAD-----------------TGSGRIGRFDPKTGTVTeyPLPGGGARPYGVA 237
                         170       180
                  ....*....|....*....|.
gi 2171360870 263 LSPeEDFVLVAETAMARIRRV 283
Cdd:COG4257   238 VDG-DGRVWFAESGANRIVRF 257
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
108-285 6.29e-06

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 47.00  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 108 GDVLF-TGTADGRVVKLENGEIETIARFGSGpcktrddeptcGRPLGIRVGPNG-TLFVVDAYKG-LFEVNPQKRSVKll 184
Cdd:COG3391    79 GRRLYvANSGSGRVSVIDLATGKVVATIPVG-----------GGPRGLAVDPDGgRLYVADSGNGrVSVIDTATGKVV-- 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 185 lsseTPIEGKKMSfvNDLTITRDGRKIYFTDSSSkwqrrDYLLLVmegtddgrLLEYDTVTKEVKVLLDQLQFPNGVQLS 264
Cdd:COG3391   146 ----ATIPVGAGP--HGIAVDPDGKRLYVANSGS-----NTVSVI--------VSVIDTATGKVVATIPVGGGPVGVAVS 206
                         170       180
                  ....*....|....*....|....*
gi 2171360870 265 PEEDFVLVAE----TAMARIRRVYV 285
Cdd:COG3391   207 PDGRRLYVANrgsnTSNGGSNTVSV 231
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
95-283 4.49e-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: 44.62  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870  95 ENQLNGPESIV--NIGDVLFTGTADGRVVKL--ENGEIETIARFGSGPCKTRddeptcgRPLGIRVGPNGTLFVVDAYKG 170
Cdd:cd05819     4 PGELNNPQGIAvdSSGNIYVADTGNNRIQVFdpDGNFITSFGSFGSGDGQFN-------EPAGVAVDSDGNLYVADTGNH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 171 -LFEVNPQKRSVKLLLSSETPIEGkkMSFVNDLTITRDGRkIYFTDSSSKWqrrdylllVMEGTDDGRLLeydTVTKEVK 249
Cdd:cd05819    77 rIQKFDPDGNFLASFGGSGDGDGE--FNGPRGIAVDSSGN-IYVADTGNHR--------IQKFDPDGEFL---TTFGSGG 142
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2171360870 250 VLLDQLQFPNGVQLSPEEDfVLVAETAMARIRRV 283
Cdd:cd05819   143 SGPGQFNGPTGVAVDSDGN-IYVADTGNHRIQVF 175
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
148-283 1.95e-04

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 42.70  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 148 CGRPLGIRVGPNGTLFVVDAYKG-LFEVNPQKRSVklllsseTPIEGKKMSFVNDLTITRDGRkIYFTDSSskwqrrdyl 226
Cdd:COG4257    16 GSGPRDVAVDPDGAVWFTDQGGGrIGRLDPATGEF-------TEYPLGGGSGPHGIAVDPDGN-LWFTDNG--------- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2171360870 227 llvmegtdDGRLLEYDTVTKEVKVLL--DQLQFPNGVQLSPEEDfVLVAETAMARIRRV 283
Cdd:COG4257    79 --------NNRIGRIDPKTGEITTFAlpGGGSNPHGIAFDPDGN-LWFTDQGGNRIGRL 128
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
94-280 2.73e-03

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: 39.20  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870  94 FENQLNGPESI-VNIGDVLFTGTADGRVV--KLENGEIETIARFGSGPCKTRddeptcgRPLGIRVGPNGTLFVVDAYKG 170
Cdd:cd14963     5 FGDPLNKPMGVaVSDGRIYVADTNNHRVQvfDYEGKFKKSFGGPGTGPGEFK-------YPYGIAVDSDGNIYVADLYNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2171360870 171 LFEV-NPQKRSVKLLLSSEtpiEGKKMSFVNDLTItrDGRKIYFTDSSskwqrrdylllvmegtdDGRLLEYDTVTKEVK 249
Cdd:cd14963    78 RIQVfDPDGKFLKYFPEKK---DRVKLISPAGLAI--DDGKLYVSDVK-----------------KHKVIVFDLEGKLLL 135
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2171360870 250 VL------LDQLQFPNGVQLSpEEDFVLVAETAMARI 280
Cdd:cd14963   136 EFgkpgsePGELSYPNGIAVD-EDGNIYVADSGNGRI 171
 
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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