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Conserved domains on  [gi|171184435|ref|NP_067320|]
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very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 [Mus musculus]

Protein Classification

p23/wos2 family protein( domain architecture ID 10158053)

p23/wos2 family protein similar to Arabidopsis thaliana co-chaperone protein p23, Saccharomyces cerevisiae Sba1 and Schizosaccharomyces pombe protein wos2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPLA pfam04387
Protein tyrosine phosphatase-like protein, PTPLA; This family includes the mammalian protein ...
 195-355 5.56e-64

Protein tyrosine phosphatase-like protein, PTPLA; This family includes the mammalian protein tyrosine phosphatase-like protein, PTPLA. A significant variation of PTPLA from other protein tyrosine phosphatases is the presence of proline instead of catalytic arginine at the active site. It is thought that PTPLA proteins have a role in the development, differentiation, and maintenance of a number of tissue types.


:

Pssm-ID: 461286  Cd Length: 163  Bit Score: 200.82  E-value: 5.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435  195 QMLALVETLNAAIGVTSTPVLPALIQFLGRNFILFLVFGTMEEMQNKAVVFFVFYSWSAIEIFRYPFYMLSCIDMDW-KV 273
Cdd:pfam04387   1 QTLAVLEVLHALLGLVRSPVLTTFMQVASRLFVVWGVIYSFPEVQTKPVVFLLLLAWSITEVIRYPYYALNLLGIEVpYF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435  274 LTWLRYTMWIPLYPLGCLSEAVAVIQSIPVFNESGRFSFTLPYPVKMKVRFSFFLQVYLVMLFLGLYINFRHLYKQRRRR 353
Cdd:pfam04387  81 LTWLRYTLFIVLYPLGVLSEALLIYQALPYFEETGLYSVSLPNPFNFSFSYPYFLILLLLLYIPGFYVLYTHMLKQRRKV 160


                  ..
gi 171184435  354 YG 355
Cdd:pfam04387 161 LG 162
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 8-115 7.67e-42

p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. hB-ind1 participates in signaling by the small GTPase Rac1. It binds to Rac1 and enhances different Rac1 effects including activation of nuclear factor (NF) kappaB and activation of c-Jun N-terminal kinase (JNK). hB-ind1 also plays a part in the RNA replication and particle production of Hepatitis C virus (HCV) through its interaction with heat shock protein Hsp90, HCV nonstructural protein 5A (NS5A), and the immunophilin FKBP8. hB-ind1 is upregulated in the outer layer of Chinese hamster V79 cells grown as multicell spheroids, versus in the same cells grown as monolayers. This group includes the Saccharomyces cerevisiae Sba1, a co-chaperone of the Hsp90. Sba1 has been shown to be is required for telomere length maintenance, and may modulate telomerase DNA-binding activity.


:

Pssm-ID: 107222 [Multi-domain]  Cd Length: 108  Bit Score: 141.96  E-value: 7.67e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435   8 PHVYWAQRHRELYLRVELSDVQNPAISITDNVLHFKAQGHGakGDNVYEFHLEFLDLVKPE-PAYRLTQRQVNITVQKK- 85
Cdd:cd06465    1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGG--GGKKYEFDLEFYKEIDPEeSKYKVTGRQIEFVLRKKe 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 171184435  86 GSHWWERLTKQEKRPLFLAPDFDRWLDESD 115
Cdd:cd06465   79 AGEYWPRLTKEKGKLPWLKVDFDKWVDEDE 108
 
Name Accession Description Interval E-value
PTPLA pfam04387
Protein tyrosine phosphatase-like protein, PTPLA; This family includes the mammalian protein ...
 195-355 5.56e-64

Protein tyrosine phosphatase-like protein, PTPLA; This family includes the mammalian protein tyrosine phosphatase-like protein, PTPLA. A significant variation of PTPLA from other protein tyrosine phosphatases is the presence of proline instead of catalytic arginine at the active site. It is thought that PTPLA proteins have a role in the development, differentiation, and maintenance of a number of tissue types.


Pssm-ID: 461286  Cd Length: 163  Bit Score: 200.82  E-value: 5.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435  195 QMLALVETLNAAIGVTSTPVLPALIQFLGRNFILFLVFGTMEEMQNKAVVFFVFYSWSAIEIFRYPFYMLSCIDMDW-KV 273
Cdd:pfam04387   1 QTLAVLEVLHALLGLVRSPVLTTFMQVASRLFVVWGVIYSFPEVQTKPVVFLLLLAWSITEVIRYPYYALNLLGIEVpYF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435  274 LTWLRYTMWIPLYPLGCLSEAVAVIQSIPVFNESGRFSFTLPYPVKMKVRFSFFLQVYLVMLFLGLYINFRHLYKQRRRR 353
Cdd:pfam04387  81 LTWLRYTLFIVLYPLGVLSEALLIYQALPYFEETGLYSVSLPNPFNFSFSYPYFLILLLLLYIPGFYVLYTHMLKQRRKV 160


                  ..
gi 171184435  354 YG 355
Cdd:pfam04387 161 LG 162
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 8-115 7.67e-42

p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. hB-ind1 participates in signaling by the small GTPase Rac1. It binds to Rac1 and enhances different Rac1 effects including activation of nuclear factor (NF) kappaB and activation of c-Jun N-terminal kinase (JNK). hB-ind1 also plays a part in the RNA replication and particle production of Hepatitis C virus (HCV) through its interaction with heat shock protein Hsp90, HCV nonstructural protein 5A (NS5A), and the immunophilin FKBP8. hB-ind1 is upregulated in the outer layer of Chinese hamster V79 cells grown as multicell spheroids, versus in the same cells grown as monolayers. This group includes the Saccharomyces cerevisiae Sba1, a co-chaperone of the Hsp90. Sba1 has been shown to be is required for telomere length maintenance, and may modulate telomerase DNA-binding activity.


Pssm-ID: 107222 [Multi-domain]  Cd Length: 108  Bit Score: 141.96  E-value: 7.67e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435   8 PHVYWAQRHRELYLRVELSDVQNPAISITDNVLHFKAQGHGakGDNVYEFHLEFLDLVKPE-PAYRLTQRQVNITVQKK- 85
Cdd:cd06465    1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGG--GGKKYEFDLEFYKEIDPEeSKYKVTGRQIEFVLRKKe 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 171184435  86 GSHWWERLTKQEKRPLFLAPDFDRWLDESD 115
Cdd:cd06465   79 AGEYWPRLTKEKGKLPWLKVDFDKWVDEDE 108
PLN02838 PLN02838
3-hydroxyacyl-CoA dehydratase subunit of elongase
 145-359 1.37e-20

3-hydroxyacyl-CoA dehydratase subunit of elongase


Pssm-ID: 166479  Cd Length: 221  Bit Score: 89.08  E-value: 1.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435 145 LKKGYLFMYNLVQLLGFSWIFVNLTVRFFILGKESFYDTfhnVADMMYFCQMLALVETLNAAIGVTSTPVLPALIQFLGR 224
Cdd:PLN02838   8 LRRLYLTVYNWVVFIGWAQVLYLAVTTLKESGHEAVYAA---VERPLQLAQTAAVLEILHGLVGLVRSPVSATLPQIGSR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435 225 NFILFLVFGTMEEMQNKAVVFFVFYSWSAIEIFRYPFY-MLSCIDMDWKVLTWLRYTMWIPLYPLGCLSEAVAVIQSIPV 303
Cdd:PLN02838  85 LFLTWGILWSFPEVRSHILVTSLVISWSITEIIRYSFFgMKEAFGFAPSWLLWLRYSTFLLLYPTGITSEVGLIYIALPY 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184435 304 FNESGRFSFTLPYpvKMKVRFSFFlqvYLVMLFLGLYIN-----FRHLYKQRRRRYGQKKK 359
Cdd:PLN02838 165 MKASEKYCLRMPN--KWNFSFDYF---YASILVLAIYVPgsphmYSYMLGQRKKALSKSKR 220
Ptpl COG5198
Protein tyrosine phosphatase-like protein (contains Pro instead of catalytic Arg) [General ...
 145-361 8.63e-15

Protein tyrosine phosphatase-like protein (contains Pro instead of catalytic Arg) [General function prediction only];


Pssm-ID: 227525  Cd Length: 209  Bit Score: 72.24  E-value: 8.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435 145 LKKGYLFMYNLVQLLGFSWIFVNLTVRFFILGKESFYDTFHNVADMMyfcQMLALVETLNAAIGVTSTPVLPALIQFLGR 224
Cdd:COG5198    5 LPISYLRLYNTASCFIWCIVLLLASLVFYKTMDPAVFHETLRVAGLV---QTFAIMEAANSSAGKVNSRYLTTVMQVISR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435 225 NFILFLVFGTMEEMQNKAVVFFVFYSWSAIEIFRYPFYMLScIDMDWKVLTWLRYTMWIPLYPLGCLSEAVAVIQSipvF 304
Cdd:COG5198   82 LFIVWGVFYPYCGIINSWTYPSITTAWSITEIVRYAFYTFR-LNGIPNTLRVLRYNLFLILYPIGFVSEMYCLRAL---Y 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171184435 305 NESGRfsftlpypvkmkvRFSFFLQVYLVMLFL---GLYINFRHLYKQRRR-----RYGQKKKKL 361
Cdd:COG5198  158 NAAGK-------------IFSLLKVVLPIVMLLyipGFIFLFSHMLAQRKKsrkvkRYKSNRKDL 209
 
Name Accession Description Interval E-value
PTPLA pfam04387
Protein tyrosine phosphatase-like protein, PTPLA; This family includes the mammalian protein ...
 195-355 5.56e-64

Protein tyrosine phosphatase-like protein, PTPLA; This family includes the mammalian protein tyrosine phosphatase-like protein, PTPLA. A significant variation of PTPLA from other protein tyrosine phosphatases is the presence of proline instead of catalytic arginine at the active site. It is thought that PTPLA proteins have a role in the development, differentiation, and maintenance of a number of tissue types.


Pssm-ID: 461286  Cd Length: 163  Bit Score: 200.82  E-value: 5.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435  195 QMLALVETLNAAIGVTSTPVLPALIQFLGRNFILFLVFGTMEEMQNKAVVFFVFYSWSAIEIFRYPFYMLSCIDMDW-KV 273
Cdd:pfam04387   1 QTLAVLEVLHALLGLVRSPVLTTFMQVASRLFVVWGVIYSFPEVQTKPVVFLLLLAWSITEVIRYPYYALNLLGIEVpYF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435  274 LTWLRYTMWIPLYPLGCLSEAVAVIQSIPVFNESGRFSFTLPYPVKMKVRFSFFLQVYLVMLFLGLYINFRHLYKQRRRR 353
Cdd:pfam04387  81 LTWLRYTLFIVLYPLGVLSEALLIYQALPYFEETGLYSVSLPNPFNFSFSYPYFLILLLLLYIPGFYVLYTHMLKQRRKV 160


                  ..
gi 171184435  354 YG 355
Cdd:pfam04387 161 LG 162
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 8-115 7.67e-42

p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. hB-ind1 participates in signaling by the small GTPase Rac1. It binds to Rac1 and enhances different Rac1 effects including activation of nuclear factor (NF) kappaB and activation of c-Jun N-terminal kinase (JNK). hB-ind1 also plays a part in the RNA replication and particle production of Hepatitis C virus (HCV) through its interaction with heat shock protein Hsp90, HCV nonstructural protein 5A (NS5A), and the immunophilin FKBP8. hB-ind1 is upregulated in the outer layer of Chinese hamster V79 cells grown as multicell spheroids, versus in the same cells grown as monolayers. This group includes the Saccharomyces cerevisiae Sba1, a co-chaperone of the Hsp90. Sba1 has been shown to be is required for telomere length maintenance, and may modulate telomerase DNA-binding activity.


Pssm-ID: 107222 [Multi-domain]  Cd Length: 108  Bit Score: 141.96  E-value: 7.67e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435   8 PHVYWAQRHRELYLRVELSDVQNPAISITDNVLHFKAQGHGakGDNVYEFHLEFLDLVKPE-PAYRLTQRQVNITVQKK- 85
Cdd:cd06465    1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGG--GGKKYEFDLEFYKEIDPEeSKYKVTGRQIEFVLRKKe 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 171184435  86 GSHWWERLTKQEKRPLFLAPDFDRWLDESD 115
Cdd:cd06465   79 AGEYWPRLTKEKGKLPWLKVDFDKWVDEDE 108
PLN02838 PLN02838
3-hydroxyacyl-CoA dehydratase subunit of elongase
 145-359 1.37e-20

3-hydroxyacyl-CoA dehydratase subunit of elongase


Pssm-ID: 166479  Cd Length: 221  Bit Score: 89.08  E-value: 1.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435 145 LKKGYLFMYNLVQLLGFSWIFVNLTVRFFILGKESFYDTfhnVADMMYFCQMLALVETLNAAIGVTSTPVLPALIQFLGR 224
Cdd:PLN02838   8 LRRLYLTVYNWVVFIGWAQVLYLAVTTLKESGHEAVYAA---VERPLQLAQTAAVLEILHGLVGLVRSPVSATLPQIGSR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435 225 NFILFLVFGTMEEMQNKAVVFFVFYSWSAIEIFRYPFY-MLSCIDMDWKVLTWLRYTMWIPLYPLGCLSEAVAVIQSIPV 303
Cdd:PLN02838  85 LFLTWGILWSFPEVRSHILVTSLVISWSITEIIRYSFFgMKEAFGFAPSWLLWLRYSTFLLLYPTGITSEVGLIYIALPY 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171184435 304 FNESGRFSFTLPYpvKMKVRFSFFlqvYLVMLFLGLYIN-----FRHLYKQRRRRYGQKKK 359
Cdd:PLN02838 165 MKASEKYCLRMPN--KWNFSFDYF---YASILVLAIYVPgsphmYSYMLGQRKKALSKSKR 220
Ptpl COG5198
Protein tyrosine phosphatase-like protein (contains Pro instead of catalytic Arg) [General ...
 145-361 8.63e-15

Protein tyrosine phosphatase-like protein (contains Pro instead of catalytic Arg) [General function prediction only];


Pssm-ID: 227525  Cd Length: 209  Bit Score: 72.24  E-value: 8.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435 145 LKKGYLFMYNLVQLLGFSWIFVNLTVRFFILGKESFYDTFHNVADMMyfcQMLALVETLNAAIGVTSTPVLPALIQFLGR 224
Cdd:COG5198    5 LPISYLRLYNTASCFIWCIVLLLASLVFYKTMDPAVFHETLRVAGLV---QTFAIMEAANSSAGKVNSRYLTTVMQVISR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435 225 NFILFLVFGTMEEMQNKAVVFFVFYSWSAIEIFRYPFYMLScIDMDWKVLTWLRYTMWIPLYPLGCLSEAVAVIQSipvF 304
Cdd:COG5198   82 LFIVWGVFYPYCGIINSWTYPSITTAWSITEIVRYAFYTFR-LNGIPNTLRVLRYNLFLILYPIGFVSEMYCLRAL---Y 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171184435 305 NESGRfsftlpypvkmkvRFSFFLQVYLVMLFL---GLYINFRHLYKQRRR-----RYGQKKKKL 361
Cdd:COG5198  158 NAAGK-------------IFSLLKVVLPIVMLLyipGFIFLFSHMLAQRKKsrkvkRYKSNRKDL 209
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 12-94 6.78e-12

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 60.76  E-value: 6.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435  12 WAQRHRELYLRVELSDVQ--NPAISITDNVLHFKAQGHGakgDNVYEFHLEFLDLVKPEPA-YRLTQRQVNITVQKK-GS 87
Cdd:cd06463    1 WYQTLDEVTITIPLKDVTkkDVKVEFTPKSLTVSVKGGG---GKEYLLEGELFGPIDPEESkWTVEDRKIEITLKKKePG 77


                 ....*..
gi 171184435  88 HWWERLT 94
Cdd:cd06463   78 EWWPRLE 84
p23 cd00237
p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 ...
 12-112 3.53e-05

p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.


Pssm-ID: 107218  Cd Length: 106  Bit Score: 42.49  E-value: 3.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435  12 WAQRHRELYLRVELSDVQNPAISITDNVLHFKAQGhgakGDNV-YEFHLEFLDLVKPEPA-YRLTQRQVNITVQK-KGSH 88
Cdd:cd00237    6 WYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLN----GDNVkIYNEIELYDRVDPNDSkHKRTDRSILCCLRKgKEGV 81

                         90       100
                 ....*....|....*....|....
gi 171184435  89 WWERLTKQEKRPLFLAPDFDRWLD 112
Cdd:cd00237   82 AWPRLTKEKAKPNWLSVDFDNWRD 105
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 12-84 1.19e-03

This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small heat shock proteins (sHsps) and a similar domain found in p23-like proteins. sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is this ACD. sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps. p23 is a cochaperone of the Hsp90 chaperoning pathway. It binds Hsp90 and participates in the folding of a number of Hsp90 clients including the progesterone receptor. p23 also has a passive chaperoning activity. p23 in addition may act as the cytosolic prostaglandin E2 synthase. Included in this family is the p23-like C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1) and the p23-like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR).


Pssm-ID: 107219  Cd Length: 80  Bit Score: 37.18  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171184435  12 WAQRHRELYLRVELSDVQ--NPAISITDNVLHFKAQGHGAK----GDNVYEFHLEFLDLVKPEPA-YRLTQRQVNITVQK 84
Cdd:cd00298    1 WYQTDDEVVVTVDLPGVKkeDIKVEVEDNVLTISGKREEEEererSYGEFERSFELPEDVDPEKSkASLENGVLEITLPK 80
 
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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