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Conserved domains on  [gi|2296792722|ref|XP_050450954|]
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very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase [Cataglyphis hispanica]

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 ...
209-371 2.75e-67

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: 209.68  E-value: 2.75e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722 209 QLLQFLEVMHPLFGYTKSSTLVSFLQVGGRGFVLFLMIDAEPRMQTKPVVFYLFLIWSIIEIVRYPYYITQLLKIEI-SF 287
Cdd:pfam04387   1 QTLAVLEVLHALLGLVRSPVLTTFMQVASRLFVVWGVIYSFPEVQTKPVVFLLLLAWSITEVIRYPYYALNLLGIEVpYF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722 288 LTWLRYTLWIPLYPLGFVCEGIIILRNIPYFEETQKFTVSLPNTYNFALHFPSVMRlYLLLLLLPGIYTIMSRMNQLRSR 367
Cdd:pfam04387  81 LTWLRYTLFIVLYPLGVLSEALLIYQALPYFEETGLYSVSLPNPFNFSFSYPYFLI-LLLLLYIPGFYVLYTHMLKQRRK 159

                  ....
gi 2296792722 368 KLGK 371
Cdd:pfam04387 160 VLGK 163
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
18-125 1.55e-38

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: 133.49  E-value: 1.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722  18 PFVYWAQTENQITLKVDLTDVKDFNVDLKETTLQVTAYGQGarGLNNYSFNLNLHLPIDPNESNYKVIDRQVDFVLKKK- 96
Cdd:cd06465     1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGG--GGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKKe 78
                          90       100
                  ....*....|....*....|....*....
gi 2296792722  97 CSSWWPRLISQPQKPSWLKIDFDKWKSED 125
Cdd:cd06465    79 AGEYWPRLTKEKGKLPWLKVDFDKWVDED 107
 
Name Accession Description Interval E-value
PTPLA pfam04387
Protein tyrosine phosphatase-like protein, PTPLA; This family includes the mammalian protein ...
209-371 2.75e-67

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: 209.68  E-value: 2.75e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722 209 QLLQFLEVMHPLFGYTKSSTLVSFLQVGGRGFVLFLMIDAEPRMQTKPVVFYLFLIWSIIEIVRYPYYITQLLKIEI-SF 287
Cdd:pfam04387   1 QTLAVLEVLHALLGLVRSPVLTTFMQVASRLFVVWGVIYSFPEVQTKPVVFLLLLAWSITEVIRYPYYALNLLGIEVpYF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722 288 LTWLRYTLWIPLYPLGFVCEGIIILRNIPYFEETQKFTVSLPNTYNFALHFPSVMRlYLLLLLLPGIYTIMSRMNQLRSR 367
Cdd:pfam04387  81 LTWLRYTLFIVLYPLGVLSEALLIYQALPYFEETGLYSVSLPNPFNFSFSYPYFLI-LLLLLYIPGFYVLYTHMLKQRRK 159

                  ....
gi 2296792722 368 KLGK 371
Cdd:pfam04387 160 VLGK 163
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
18-125 1.55e-38

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: 133.49  E-value: 1.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722  18 PFVYWAQTENQITLKVDLTDVKDFNVDLKETTLQVTAYGQGarGLNNYSFNLNLHLPIDPNESNYKVIDRQVDFVLKKK- 96
Cdd:cd06465     1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGG--GGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKKe 78
                          90       100
                  ....*....|....*....|....*....
gi 2296792722  97 CSSWWPRLISQPQKPSWLKIDFDKWKSED 125
Cdd:cd06465    79 AGEYWPRLTKEKGKLPWLKVDFDKWVDED 107
PLN02838 PLN02838
3-hydroxyacyl-CoA dehydratase subunit of elongase
159-372 4.98e-29

3-hydroxyacyl-CoA dehydratase subunit of elongase


Pssm-ID: 166479  Cd Length: 221  Bit Score: 112.20  E-value: 4.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722 159 LTKVYLVIYNLCQFVGFIYVLAVMGIRYSRDGPDfmkETYAAVGSPLKFIQLLQFLEVMHPLFGYTKSSTLVSFLQVGGR 238
Cdd:PLN02838    8 LRRLYLTVYNWVVFIGWAQVLYLAVTTLKESGHE---AVYAAVERPLQLAQTAAVLEILHGLVGLVRSPVSATLPQIGSR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722 239 GFVLFLMIDAEPRMQTKPVVFYLFLIWSIIEIVRYPYY-ITQLLKIEISFLTWLRYTLWIPLYPLGFVCEGIIILRNIPY 317
Cdd:PLN02838   85 LFLTWGILWSFPEVRSHILVTSLVISWSITEIIRYSFFgMKEAFGFAPSWLLWLRYSTFLLLYPTGITSEVGLIYIALPY 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2296792722 318 FEETQKFTVSLPNTYNFALHF--PSVMRLYLLLLLLPGIYTIMSRMnqlRSRKLGKS 372
Cdd:PLN02838  165 MKASEKYCLRMPNKWNFSFDYfyASILVLAIYVPGSPHMYSYMLGQ---RKKALSKS 218
Ptpl COG5198
Protein tyrosine phosphatase-like protein (contains Pro instead of catalytic Arg) [General ...
163-312 3.28e-15

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


Pssm-ID: 227525  Cd Length: 209  Bit Score: 73.79  E-value: 3.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722 163 YLVIYNLCQFVGFIYVLAVMGIRYSRDG-PDFMKETYAAVGsplkFIQLLQFLEVMHPLFGYTKSSTLVSFLQVGGRGFV 241
Cdd:COG5198     9 YLRLYNTASCFIWCIVLLLASLVFYKTMdPAVFHETLRVAG----LVQTFAIMEAANSSAGKVNSRYLTTVMQVISRLFI 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2296792722 242 LFLMIDAEPRMQTKPVVFYLFLIWSIIEIVRYPYYITQLLKIEiSFLTWLRYTLWIPLYPLGFVCEGIIIL 312
Cdd:COG5198    85 VWGVFYPYCGIINSWTYPSITTAWSITEIVRYAFYTFRLNGIP-NTLRVLRYNLFLILYPIGFVSEMYCLR 154
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
20-95 7.16e-07

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 46.48  E-value: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722  20 VYWAQTENQITLKVDLTDV----KDFNVDLKETTLQVTAYGQGArglnnySFNLNLHLPIDPNESNYKVIDRQVDFVLKK 95
Cdd:pfam04969   3 YDWYQTLDEVTITIPVKGAgikkKDVKVNIKPRSLKVKIKGGYE------LIDGELFHPIDPEESSWTIEGKKVEITLKK 76
 
Name Accession Description Interval E-value
PTPLA pfam04387
Protein tyrosine phosphatase-like protein, PTPLA; This family includes the mammalian protein ...
209-371 2.75e-67

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: 209.68  E-value: 2.75e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722 209 QLLQFLEVMHPLFGYTKSSTLVSFLQVGGRGFVLFLMIDAEPRMQTKPVVFYLFLIWSIIEIVRYPYYITQLLKIEI-SF 287
Cdd:pfam04387   1 QTLAVLEVLHALLGLVRSPVLTTFMQVASRLFVVWGVIYSFPEVQTKPVVFLLLLAWSITEVIRYPYYALNLLGIEVpYF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722 288 LTWLRYTLWIPLYPLGFVCEGIIILRNIPYFEETQKFTVSLPNTYNFALHFPSVMRlYLLLLLLPGIYTIMSRMNQLRSR 367
Cdd:pfam04387  81 LTWLRYTLFIVLYPLGVLSEALLIYQALPYFEETGLYSVSLPNPFNFSFSYPYFLI-LLLLLYIPGFYVLYTHMLKQRRK 159

                  ....
gi 2296792722 368 KLGK 371
Cdd:pfam04387 160 VLGK 163
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
18-125 1.55e-38

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: 133.49  E-value: 1.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722  18 PFVYWAQTENQITLKVDLTDVKDFNVDLKETTLQVTAYGQGarGLNNYSFNLNLHLPIDPNESNYKVIDRQVDFVLKKK- 96
Cdd:cd06465     1 PPVLWAQRSDVVYLTIELPDAKDPKIKLEPTSLSFKAKGGG--GGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKKe 78
                          90       100
                  ....*....|....*....|....*....
gi 2296792722  97 CSSWWPRLISQPQKPSWLKIDFDKWKSED 125
Cdd:cd06465    79 AGEYWPRLTKEKGKLPWLKVDFDKWVDED 107
PLN02838 PLN02838
3-hydroxyacyl-CoA dehydratase subunit of elongase
159-372 4.98e-29

3-hydroxyacyl-CoA dehydratase subunit of elongase


Pssm-ID: 166479  Cd Length: 221  Bit Score: 112.20  E-value: 4.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722 159 LTKVYLVIYNLCQFVGFIYVLAVMGIRYSRDGPDfmkETYAAVGSPLKFIQLLQFLEVMHPLFGYTKSSTLVSFLQVGGR 238
Cdd:PLN02838    8 LRRLYLTVYNWVVFIGWAQVLYLAVTTLKESGHE---AVYAAVERPLQLAQTAAVLEILHGLVGLVRSPVSATLPQIGSR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722 239 GFVLFLMIDAEPRMQTKPVVFYLFLIWSIIEIVRYPYY-ITQLLKIEISFLTWLRYTLWIPLYPLGFVCEGIIILRNIPY 317
Cdd:PLN02838   85 LFLTWGILWSFPEVRSHILVTSLVISWSITEIIRYSFFgMKEAFGFAPSWLLWLRYSTFLLLYPTGITSEVGLIYIALPY 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2296792722 318 FEETQKFTVSLPNTYNFALHF--PSVMRLYLLLLLLPGIYTIMSRMnqlRSRKLGKS 372
Cdd:PLN02838  165 MKASEKYCLRMPNKWNFSFDYfyASILVLAIYVPGSPHMYSYMLGQ---RKKALSKS 218
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
22-105 9.67e-17

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: 74.63  E-value: 9.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722  22 WAQTENQITLKVDLTDV--KDFNVDLKETTLQVTAYGQGArglNNYSFNLNLHLPIDPNESNYKVIDRQVDFVLKKKCSS 99
Cdd:cd06463     1 WYQTLDEVTITIPLKDVtkKDVKVEFTPKSLTVSVKGGGG---KEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPG 77

                  ....*..
gi 2296792722 100 -WWPRLI 105
Cdd:cd06463    78 eWWPRLE 84
Ptpl COG5198
Protein tyrosine phosphatase-like protein (contains Pro instead of catalytic Arg) [General ...
163-312 3.28e-15

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


Pssm-ID: 227525  Cd Length: 209  Bit Score: 73.79  E-value: 3.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722 163 YLVIYNLCQFVGFIYVLAVMGIRYSRDG-PDFMKETYAAVGsplkFIQLLQFLEVMHPLFGYTKSSTLVSFLQVGGRGFV 241
Cdd:COG5198     9 YLRLYNTASCFIWCIVLLLASLVFYKTMdPAVFHETLRVAG----LVQTFAIMEAANSSAGKVNSRYLTTVMQVISRLFI 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2296792722 242 LFLMIDAEPRMQTKPVVFYLFLIWSIIEIVRYPYYITQLLKIEiSFLTWLRYTLWIPLYPLGFVCEGIIIL 312
Cdd:COG5198    85 VWGVFYPYCGIINSWTYPSITTAWSITEIVRYAFYTFRLNGIP-NTLRVLRYNLFLILYPIGFVSEMYCLR 154
p23 cd00237
p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 ...
22-122 8.93e-10

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: 55.58  E-value: 8.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722  22 WAQTENQITLKVDLTDVKDFNVDLKETTLQVTAYGQGArglNNYSFNLNLHLPIDPNESNYKVIDRQVDFVLKK-KCSSW 100
Cdd:cd00237     6 WYDRRDYVFIEFCVEDSKDVKVDFEKSKLTFSCLNGDN---VKIYNEIELYDRVDPNDSKHKRTDRSILCCLRKgKEGVA 82
                          90       100
                  ....*....|....*....|..
gi 2296792722 101 WPRLISQPQKPSWLKIDFDKWK 122
Cdd:cd00237    83 WPRLTKEKAKPNWLSVDFDNWR 104
p23_CS_hSgt1_like cd06489
p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related ...
22-104 4.79e-08

p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related proteins. hSgt1 is a co-chaperone which has been shown to be elevated in HEp-2 cells as a result of stress conditions such as heat shock. It interacts with the heat shock proteins (HSPs) Hsp70 and Hsp90, and it expression pattern is synchronized with these two Hsps. The interaction with HSP90 has been shown to involve the hSgt1_CS domain, and appears to be required for correct kinetochore assembly and efficient cell division. Some proteins in this subgroup contain a tetratricopeptide repeat (TPR) HSP-binding domain N-terminal to this CS domain, and most proteins in this subgroup contain a Sgt1-specific (SGS) domain C-terminal to the CS domain. The SGS domain interacts with some S100 family proteins. Studies suggest that S100A6 modulates in a Ca2+ dependent manner the interactions of hSgt1 with Hsp90 and Hsp70. The yeast Sgt1 CS domain is not found in this subgroup.


Pssm-ID: 107239  Cd Length: 84  Bit Score: 50.07  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722  22 WAQTENQITLKVDLTDVK--DFNVDLKETTLQVTAYGQGArglNNYSFNLNLHLPIDPNESNYKVIDRQVDFVLKKKCSS 99
Cdd:cd06489     2 WYQTESQVVITILIKNVKpeDVSVEFEKRELSATVKLPSG---NDYSLKLHLLHPIVPEQSSYKILSTKIEIKLKKTEAI 78

                  ....*
gi 2296792722 100 WWPRL 104
Cdd:cd06489    79 RWSKL 83
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
22-95 7.75e-08

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: 49.12  E-value: 7.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722  22 WAQTENQITLKVDLTDV--KDFNVDLKETTLQVTA----YGQGARGLNNYSFNLNLHLPIDPNESNYKVIDRQVDFVLKK 95
Cdd:cd00298     1 WYQTDDEVVVTVDLPGVkkEDIKVEVEDNVLTISGkreeEEERERSYGEFERSFELPEDVDPEKSKASLENGVLEITLPK 80
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
22-104 1.20e-07

p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of Skp1). Sgt1 interacts with multiple protein complexes and has the features of a cochaperone. 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. ScSgt1 is needed for the G1/S and G2/M cell-cycle transitions, and for assembly of the core kinetochore complex (CBF3) via activation of Ctf13, the F-box protein. Binding of Hsp82 (a yeast Hsp90 homologue) to ScSgt1, promotes the binding of Sgt1 to Skp1 and of Skp1 to Ctf13. Some proteins in this group have an SGT1-specific (SGS) domain at the extreme C-terminus. The ScSgt1-SGS domain binds adenylate cyclase. The hSgt1-SGS domain interacts with some S100 family proteins, and studies suggest that the interaction of hSgt1 with Hsp90 and Hsp70 may be regulated by S100A6 in a Ca2+ dependent fashion. This group also includes the p23_like domains of Melusin and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Melusin is a vertebrate protein which interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107223  Cd Length: 84  Bit Score: 48.74  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722  22 WAQTENQITLKV--DLTDVKDFNVDLKETTLQVTAYGQGArglNNYSFNLNLHLPIDPNESNYKVIDRQVDFVLKKKCSS 99
Cdd:cd06466     2 WYQTDTSVTVTIyaKNVDKEDVKVEFNEQSLSVSIILPGG---SEYQLELDLFGPIDPEQSKVSVLPTKVEITLKKAEPG 78

                  ....*
gi 2296792722 100 WWPRL 104
Cdd:cd06466    79 SWPSL 83
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
20-95 7.16e-07

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 46.48  E-value: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722  20 VYWAQTENQITLKVDLTDV----KDFNVDLKETTLQVTAYGQGArglnnySFNLNLHLPIDPNESNYKVIDRQVDFVLKK 95
Cdd:pfam04969   3 YDWYQTLDEVTITIPVKGAgikkKDVKVNIKPRSLKVKIKGGYE------LIDGELFHPIDPEESSWTIEGKKVEITLKK 76
p23_CacyBP cd06468
p23_like domain found in proteins similar to Calcyclin-Binding Protein(CacyBP) ...
22-104 7.84e-06

p23_like domain found in proteins similar to Calcyclin-Binding Protein(CacyBP)/Siah-1-interacting protein (SIP). CacyBP/SIP interacts with S100A6 (calcyclin), with some other members of the S100 family, with tubulin, and with Siah-1 and Skp-1. The latter two are components of the ubiquitin ligase that regulates beta-catenin degradation. The beta-catenin gene is an oncogene participating in tumorigenesis in many different cancers. Overexpression of CacyBP/SIP, in part through its effect on the expression of beta-catenin, inhibits the proliferation, tumorigenicity, and invasion of gastric cancer cells. CacyBP/SIP is abundant in neurons and neuroblastoma NB2a cells. An extensive re-organization of microtubules accompanies the differentiation of NB2a cells. CacyBP/SIP may contribute to NB2a cell differentiation through binding to and increasing the oligomerization of tubulin. CacyBP/SIP is also implicated in differentiation of erythroid cells, rat neonatal cardiomyocytes, in mouse endometrial events, and in thymocyte development.


Pssm-ID: 107225  Cd Length: 92  Bit Score: 43.79  E-value: 7.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722  22 WAQTENQITLKVDLTDVKDFN-----VDLKETTLQVTAYGQGARglnNYSFNLN-LHLPIDPNESNYKVIDRQVDFVLKK 95
Cdd:cd06468     6 WDQSDKFVKIYITLKGVHQLPkeniqVEFTERSFELKVHDLNGK---NYRFTINrLLKKIDPEKSSFKVKTDRIVITLAK 82

                  ....*....
gi 2296792722  96 KCSSWWPRL 104
Cdd:cd06468    83 KKEKKWESL 91
p23_NUDC_like cd06467
p23_like domain of NUD (nuclear distribution) C and similar proteins. Aspergillus nidulas (An) ...
21-105 1.29e-04

p23_like domain of NUD (nuclear distribution) C and similar proteins. Aspergillus nidulas (An) NUDC is needed for nuclear movement. AnNUDC is localized at the hyphal cortex, and binds NUDF at spindle pole bodies (SPBs) and in the cytoplasm at different stages in the cell cycle. At the SPBs it is part of the dynein molecular motor/NUDF complex that regulates microtubule dynamics. Mammalian(m) NUDC associates both with the dynein complex and also with an anti-inflammatory enzyme, platelet activating factor acetylhydrolase I, PAF-AH(I) complex, through binding mNUDF, the regulatory beta subunit of PAF-AH(I). mNUDC is important for cell proliferation both in normal and tumor tissues. Its expression is elevated in various cell types undergoing mitosis or stimulated to proliferate, with high expression levels observed in leukemic cells and tumors. For a leukemic cell line, human NUDC was shown to activate the thrombopoietin (TPO) receptor (Mpl) by binding to its extracellular domain, and promoting cell proliferation and differentiation. This group also includes the human broadly immunogenic tumor associated antigen, CML66, which is highly expressed in a variety of solid tumors and in leukemias. In normal tissues high expression of CML66 is limited to testis and heart.


Pssm-ID: 107224  Cd Length: 85  Bit Score: 40.22  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296792722  21 YWAQTENQITLKVDL---TDVKDFNVDLKETTLQVtaygqgarGLNNYSFNLN--LHLPIDPNESNYKVID-RQVDFVL- 93
Cdd:cd06467     2 SWTQTLDEVTVTIPLpegTKSKDVKVEITPKHLKV--------GVKGGEPLLDgeLYAKVKVDESTWTLEDgKLLEITLe 73
                          90
                  ....*....|..
gi 2296792722  94 KKKCSSWWPRLI 105
Cdd:cd06467    74 KRNEGEWWPSLV 85
 
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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