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Conserved domains on  [gi|66472620|ref|NP_001018401|]
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apolipoprotein Ea precursor [Danio rerio]

Protein Classification

apolipoprotein A1/A4/E family protein( domain architecture ID 12019813)

apolipoprotein A1/A4/E family protein associates with lipid particles and may function in lipoprotein-mediated lipid transport

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 67-241 3.78e-42

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


:

Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 142.02  E-value: 3.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620    67 LISDSMMELQMYRDDLHSKLAPYAQERAQKFNEDLQLLVTKLRTHMEEAKDRVTEYTEELRTMVEQNSDELKNKANSYAK 146
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620   147 KLRKRFNKDIQEINKKMSTYLEEVQSRASQSVEDVKDRLEPYFTSMHERAQQKLVNLREALRSQAEEIKERLDSRMQELR 226
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160

                         170
                  ....*....|....*
gi 66472620   227 DQVEKTKENVHNTLQ 241
Cdd:pfam01442 161 EKLEPQAEDLREKLD 175
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 67-241 3.78e-42

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 142.02  E-value: 3.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620    67 LISDSMMELQMYRDDLHSKLAPYAQERAQKFNEDLQLLVTKLRTHMEEAKDRVTEYTEELRTMVEQNSDELKNKANSYAK 146
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620   147 KLRKRFNKDIQEINKKMSTYLEEVQSRASQSVEDVKDRLEPYFTSMHERAQQKLVNLREALRSQAEEIKERLDSRMQELR 226
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160

                         170
                  ....*....|....*
gi 66472620   227 DQVEKTKENVHNTLQ 241
Cdd:pfam01442 161 EKLEPQAEDLREKLD 175
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 63-266 1.54e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 43.12  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620    63 ELDTLISDSMMELQMYRDDLHSKlapyaqeRAQKFNEDLQLLVTKLRTHMEEAKDRVTEYTEelrtMVEQNSDELknkAN 142
Cdd:PRK10929  193 ELAQLSANNRQELARLRSELAKK-------RSQQLDAYLQALRNQLNSQRQREAERALESTE----LLAEQSGDL---PK 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620   143 SYAKKLRKrfNKDIQEINKKMSTYLEEVQSRASQSVED---VKDRLepyfTSMHERAQQKLVN--LREALRSQAEEIKE- 216
Cdd:PRK10929  259 SIVAQFKI--NRELSQALNQQAQRMDLIASQQRQAASQtlqVRQAL----NTLREQSQWLGVSnaLGEALRAQVARLPEm 332

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 66472620   217 ----RLDSRMQELRdqVEKTK-ENVHNTLQQKAEDVQKWFEPYVSHIQKQMEPVW 266
Cdd:PRK10929  333 pkpqQLDTEMAQLR--VQRLRyEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQL 385
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
157-236 3.47e-04

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 39.18  E-value: 3.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620 157 QEINKKMSTYLEEVQSRASQSVEDVKDRLEPYFTSmherAQQKLVNLREALRSQAEEIKERLDSRMQELRDQVEKTKENV 236
Cdd:COG4980  30 KETRKKLKDKADDLKDKAEDLKDELKEKASELSEE----AKEKLDELIEEIKEKIEELKEEVEPKIEELKEEAEKLQKEV 105
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 31-261 6.68e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 38.11  E-value: 6.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620     31 EEAVDQFWNHVSELTTRAEEMRDNIKA--TQLGRELDTLIS-DSMMELQMYRDDLHSKL--APYAQERAQKFNEDLQLlV 105
Cdd:TIGR01612 1124 DQKIDHHIKALEEIKKKSENYIDEIKAqiNDLEDVADKAISnDDPEEIEKKIENIVTKIdkKKNIYDEIKKLLNEIAE-I 1202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620    106 TKLRTHMEEAKDRVTEYTEELRTMVEQNSDELKNKANSYAKKLRKrFNKDIQEINKKmstyleevqsraSQSVEDvkdrl 185
Cdd:TIGR01612 1203 EKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEA-YIEDLDEIKEK------------SPEIEN----- 1264

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66472620    186 ePYFTSMHERAQQKLVNLREALRSQAEEIKERLDSRMQELRDQVEKTKENvhNTLQQKAEDVQKWFEPYVSHIQKQ 261
Cdd:TIGR01612 1265 -EMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIED--FSEESDINDIKKELQKNLLDAQKH 1337
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 74-187 6.77e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 37.35  E-value: 6.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620  74 ELQMYRDDLHSKLAPYaQERAQKFNEDLQLLVTKLRTH---MEEAKDRVTE-YTEELRTMVEQNSDELKNKANSYAKKLR 149
Cdd:cd22656 118 TIKALLDDLLKEAKKY-QDKAAKVVDKLTDFENQTEKDqtaLETLEKALKDlLTDEGGAIARKEIKDLQKELEKLNEEYA 196

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 66472620 150 KRFNKDIQEINKKMSTYLEEVQS---------RASQSVEDVKDRLEP 187
Cdd:cd22656 197 AKLKAKIDELKALIADDEAKLAAalrliadltAADTDLDNLLALIGP 243
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 67-241 3.78e-42

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 142.02  E-value: 3.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620    67 LISDSMMELQMYRDDLHSKLAPYAQERAQKFNEDLQLLVTKLRTHMEEAKDRVTEYTEELRTMVEQNSDELKNKANSYAK 146
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620   147 KLRKRFNKDIQEINKKMSTYLEEVQSRASQSVEDVKDRLEPYFTSMHERAQQKLVNLREALRSQAEEIKERLDSRMQELR 226
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160

                         170
                  ....*....|....*
gi 66472620   227 DQVEKTKENVHNTLQ 241
Cdd:pfam01442 161 EKLEPQAEDLREKLD 175
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 24-149 7.92e-05

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 42.25  E-value: 7.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620    24 DEPRSRWEEAVDQFWNHVSELTTRAEEmRDNIKATQLGRELDTLISDSMMELQMYRDDLHSKLAPYAQEraqkfnedlql 103
Cdd:pfam01442  58 EELQAKLGQNVEELRQRLEPYTEELRK-RLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEE----------- 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 66472620   104 LVTKLRTHMEEAKDRVTEYTEELRTMVEQNSDELKNKANSYAKKLR 149
Cdd:pfam01442 126 LRQKLAERLEELKESLAPYAEEVQAQLSQRLQELREKLEPQAEDLR 171
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 63-266 1.54e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 43.12  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620    63 ELDTLISDSMMELQMYRDDLHSKlapyaqeRAQKFNEDLQLLVTKLRTHMEEAKDRVTEYTEelrtMVEQNSDELknkAN 142
Cdd:PRK10929  193 ELAQLSANNRQELARLRSELAKK-------RSQQLDAYLQALRNQLNSQRQREAERALESTE----LLAEQSGDL---PK 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620   143 SYAKKLRKrfNKDIQEINKKMSTYLEEVQSRASQSVED---VKDRLepyfTSMHERAQQKLVN--LREALRSQAEEIKE- 216
Cdd:PRK10929  259 SIVAQFKI--NRELSQALNQQAQRMDLIASQQRQAASQtlqVRQAL----NTLREQSQWLGVSnaLGEALRAQVARLPEm 332

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 66472620   217 ----RLDSRMQELRdqVEKTK-ENVHNTLQQKAEDVQKWFEPYVSHIQKQMEPVW 266
Cdd:PRK10929  333 pkpqQLDTEMAQLR--VQRLRyEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQL 385
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
157-236 3.47e-04

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 39.18  E-value: 3.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620 157 QEINKKMSTYLEEVQSRASQSVEDVKDRLEPYFTSmherAQQKLVNLREALRSQAEEIKERLDSRMQELRDQVEKTKENV 236
Cdd:COG4980  30 KETRKKLKDKADDLKDKAEDLKDELKEKASELSEE----AKEKLDELIEEIKEKIEELKEEVEPKIEELKEEAEKLQKEV 105
ElaB COG4575
Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD ...
 160-237 7.31e-04

Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD/DUF883 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443632 [Multi-domain]  Cd Length: 108  Bit Score: 38.39  E-value: 7.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620 160 NKKMSTYLEEVQSRASQSVEDVKDRLEPYFTSMHERAQQKLVNLREALRSQAEEIKERLDSRMQELRDQ----VEKTKEN 235
Cdd:COG4575   3 NTKTTTSVEDSKEDLEADLKALVDDLEELLKSTADDAGEKAAELREKAEAALDEARERLSEAEDAAVERareaADAADDY 82


                ..
gi 66472620 236 VH 237
Cdd:COG4575  83 VH 84
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 156-263 1.02e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 38.78  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620   156 IQEINKKMSTYLEEVQSRASQSVEDVKDRLEpyftsmheraqqklvnlrealrSQAEEIKERLDSRMQELRDQVEKTKEN 235
Cdd:pfam01442   2 LEDSLDELSTYAEELQEQLGPVAQELVDRLE----------------------KETEALRERLQKDLEEVRAKLEPYLEE 59

                          90       100
                  ....*....|....*....|....*...
gi 66472620   236 VHNTLQQKAEDVQKWFEPYVSHIQKQME 263
Cdd:pfam01442  60 LQAKLGQNVEELRQRLEPYTEELRKRLN 87
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
124-218 1.32e-03

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 37.64  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620 124 EELRTMVEQNSDELKNKANSYAKKLRKRfnkdIQEINKKMSTYLEEVQSRASQSVEDVKDRLEPyftsmheraqqklvnL 203
Cdd:COG4980  30 KETRKKLKDKADDLKDKAEDLKDELKEK----ASELSEEAKEKLDELIEEIKEKIEELKEEVEP---------------K 90

                        90
                ....*....|....*
gi 66472620 204 REALRSQAEEIKERL 218
Cdd:COG4980  91 IEELKEEAEKLQKEV 105
ApoLp-III pfam07464
Apolipophorin-III precursor (apoLp-III); This family consists of several insect ...
 113-242 1.95e-03

Apolipophorin-III precursor (apoLp-III); This family consists of several insect apolipoprotein-III sequences. Exchangeable apolipoproteins constitute a functionally important family of proteins that play critical roles in lipid transport and lipoprotein metabolism. Apolipophorin III (apoLp-III) is a prototypical exchangeable apolipoprotein found in many insect species that functions in transport of diacylglycerol (DAG) from the fat body lipid storage depot to flight muscles in the adult life stage.


Pssm-ID: 462172 [Multi-domain]  Cd Length: 143  Bit Score: 37.73  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620   113 EEAKDRVTEYTEELRTMVEQNSDELKnKANSYAKKLRKRFNKDIQEINKKMSTYLEEVQSRASQSVEDVKDRLEPYFTSM 192
Cdd:pfam07464  23 ETIKENTENLVDQLKQVQKSLQEELK-KASGEAEEALKELNTKIVETADKLSEANPEVVQKANELQEKFQSGVQSLVTES 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 66472620   193 heraqQKLVnlrEALRSQAEEIKERLDSRMQELRDQVEKTKENVHNTLQQ 242
Cdd:pfam07464 102 -----QKLA---KSISENSQGATEKLQKATKQAYDDAVQAAQKLANQLQP 143
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 32-251 3.76e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 38.67  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620     32 EAVDQFWNHVSE---LTTRAEEMRDNIKATQLGRELDTLISDSMMELQMYRDDLHSKLAPYAQERAQKFNEDLQLLVTKL 108
Cdd:pfam12128  418 QALESELREQLEagkLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQA 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620    109 RTHMEEAKDR---VTEYTEELRTMVEQNSDELKNKANSYAKKLRKRFNKDIQEINKKMSTYL----------EEVQSRAS 175
Cdd:pfam12128  498 RKRRDQASEAlrqASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELlhrtdldpevWDGSVGGE 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620    176 QSVEDVKDRLE----PYFTSMHERAQQKLVNLREALRSQAEEIKeRLDSRMQELRDQVEKTK---ENVHNTLQQKAEDVQ 248
Cdd:pfam12128  578 LNLYGVKLDLKridvPEWAASEEELRERLDKAEEALQSAREKQA-AAEEQLVQANGELEKASreeTFARTALKNARLDLR 656


                   ...
gi 66472620    249 KWF 251
Cdd:pfam12128  657 RLF 659
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 31-261 6.68e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 38.11  E-value: 6.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620     31 EEAVDQFWNHVSELTTRAEEMRDNIKA--TQLGRELDTLIS-DSMMELQMYRDDLHSKL--APYAQERAQKFNEDLQLlV 105
Cdd:TIGR01612 1124 DQKIDHHIKALEEIKKKSENYIDEIKAqiNDLEDVADKAISnDDPEEIEKKIENIVTKIdkKKNIYDEIKKLLNEIAE-I 1202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620    106 TKLRTHMEEAKDRVTEYTEELRTMVEQNSDELKNKANSYAKKLRKrFNKDIQEINKKmstyleevqsraSQSVEDvkdrl 185
Cdd:TIGR01612 1203 EKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEA-YIEDLDEIKEK------------SPEIEN----- 1264

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66472620    186 ePYFTSMHERAQQKLVNLREALRSQAEEIKERLDSRMQELRDQVEKTKENvhNTLQQKAEDVQKWFEPYVSHIQKQ 261
Cdd:TIGR01612 1265 -EMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIED--FSEESDINDIKKELQKNLLDAQKH 1337
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 74-187 6.77e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 37.35  E-value: 6.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472620  74 ELQMYRDDLHSKLAPYaQERAQKFNEDLQLLVTKLRTH---MEEAKDRVTE-YTEELRTMVEQNSDELKNKANSYAKKLR 149
Cdd:cd22656 118 TIKALLDDLLKEAKKY-QDKAAKVVDKLTDFENQTEKDqtaLETLEKALKDlLTDEGGAIARKEIKDLQKELEKLNEEYA 196

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 66472620 150 KRFNKDIQEINKKMSTYLEEVQS---------RASQSVEDVKDRLEP 187
Cdd:cd22656 197 AKLKAKIDELKALIADDEAKLAAalrliadltAADTDLDNLLALIGP 243
 
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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