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Conserved domains on  [gi|1039793990|ref|XP_017169026|]
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dynein axonemal assembly factor 4 isoform X1 [Mus musculus]

Protein Classification

p23_DYX1C1_like and 3a0801s09 domain-containing protein( domain architecture ID 12950641)

protein containing domains p23_DYX1C1_like, PTZ00121, and 3a0801s09

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
p23_DYX1C1_like cd06469
p23_like domain found in proteins similar to dyslexia susceptibility 1 (DYX1) candidate 1 (C1) ...
 10-87 1.36e-37

p23_like domain found in proteins similar to dyslexia susceptibility 1 (DYX1) candidate 1 (C1) protein, DYX1C1. The human gene encoding this protein is a positional candidate gene for developmental dyslexia (DD), it is located on 15q21.3 by the DYX1 DD susceptibility locus (15q15-21). Independent association studies have reported conflicting results. However, association of short-term memory, which plays a role in DD, with a variant within the DYX1C1 gene has been reported. Most proteins belonging to this group contain a C-terminal tetratricopeptide repeat (TPR) protein binding region.


:

Pssm-ID: 107226  Cd Length: 78  Bit Score: 128.16  E-value: 1.36e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039793990  10 WQQTPATIFLSLPLRGVCVRDADVFCGESYLKVNFPPFLFELFLYAPIDDGKSKAKIGNDTILFTLYKKEPVLWDSLS 87
Cdd:cd06469     1 WSQTDEDVKISVPLKGVKTSKVDIFCSDLYLKVNFPPYLFELDLAAPIDDEKSSAKIGNGVLVFTLVKKEPGIWEALC 78
3a0801s09 super family cl36792
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 93-270 3.19e-13

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


The actual alignment was detected with superfamily member TIGR00990:

Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 69.63  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990  93 KEMMQRIREKSILQAQEKAKEATEAKAVAKREDQRYALGEMMKWLHKQAEARRAmstdlpeffDLKEEERN--PDWLKDK 170
Cdd:TIGR00990  63 RESKPKISKKERRKRKQAEKETEGKTEEKKSTAPKNAPVEPADELPEIDESSVA---------NLSEEERKkyAAKLKEK 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 171 GNKLFATENYLAAVDAYNLAIRLNcKIPLLYLNRAACHLKLKNLHKAIEDSSKALELltppvadnANARMKAHVRRGTAF 250
Cdd:TIGR00990 134 GNKAYRNKDFNKAIKLYSKAIECK-PDPVYYSNRAACHNALGDWEKVVEDTTAALEL--------DPDYSKALNRRANAY 204

                         170       180
                  ....*....|....*....|
gi 1039793990 251 CQLELYVEGLQDYEAALKID 270
Cdd:TIGR00990 205 DGLGKYADALLDLTASCIID 224
 
Name Accession Description Interval E-value
p23_DYX1C1_like cd06469
p23_like domain found in proteins similar to dyslexia susceptibility 1 (DYX1) candidate 1 (C1) ...
 10-87 1.36e-37

p23_like domain found in proteins similar to dyslexia susceptibility 1 (DYX1) candidate 1 (C1) protein, DYX1C1. The human gene encoding this protein is a positional candidate gene for developmental dyslexia (DD), it is located on 15q21.3 by the DYX1 DD susceptibility locus (15q15-21). Independent association studies have reported conflicting results. However, association of short-term memory, which plays a role in DD, with a variant within the DYX1C1 gene has been reported. Most proteins belonging to this group contain a C-terminal tetratricopeptide repeat (TPR) protein binding region.


Pssm-ID: 107226  Cd Length: 78  Bit Score: 128.16  E-value: 1.36e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039793990  10 WQQTPATIFLSLPLRGVCVRDADVFCGESYLKVNFPPFLFELFLYAPIDDGKSKAKIGNDTILFTLYKKEPVLWDSLS 87
Cdd:cd06469     1 WSQTDEDVKISVPLKGVKTSKVDIFCSDLYLKVNFPPYLFELDLAAPIDDEKSSAKIGNGVLVFTLVKKEPGIWEALC 78
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 93-270 3.19e-13

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 69.63  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990  93 KEMMQRIREKSILQAQEKAKEATEAKAVAKREDQRYALGEMMKWLHKQAEARRAmstdlpeffDLKEEERN--PDWLKDK 170
Cdd:TIGR00990  63 RESKPKISKKERRKRKQAEKETEGKTEEKKSTAPKNAPVEPADELPEIDESSVA---------NLSEEERKkyAAKLKEK 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 171 GNKLFATENYLAAVDAYNLAIRLNcKIPLLYLNRAACHLKLKNLHKAIEDSSKALELltppvadnANARMKAHVRRGTAF 250
Cdd:TIGR00990 134 GNKAYRNKDFNKAIKLYSKAIECK-PDPVYYSNRAACHNALGDWEKVVEDTTAALEL--------DPDYSKALNRRANAY 204

                         170       180
                  ....*....|....*....|
gi 1039793990 251 CQLELYVEGLQDYEAALKID 270
Cdd:TIGR00990 205 DGLGKYADALLDLTASCIID 224
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 167-269 1.48e-11

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 64.04  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 167 LKDKGNKLFATENYLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALElLTPPVAdnanarmKAHVRR 246
Cdd:PLN03088    5 LEDKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIE-LDPSLA-------KAYLRK 76

                          90       100
                  ....*....|....*....|...
gi 1039793990 247 GTAFCQLELYveglQDYEAALKI 269
Cdd:PLN03088   77 GTACMKLEEY----QTAKAALEK 95
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
171-271 2.23e-10

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 59.54  E-value: 2.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 171 GNKLFATENYLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALELltppvaDNANARmkAHVRRGTAF 250
Cdd:COG4785    80 GVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALEL------DPDYAY--AYLNRGIAL 151

                          90       100
                  ....*....|....*....|.
gi 1039793990 251 CQLELYVEGLQDYEAALKIDP 271
Cdd:COG4785   152 YYLGRYELAIADLEKALELDP 172
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
 7-77 1.40e-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: 48.02  E-value: 1.40e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039793990   7 EFSWQQTPATIFLSLPLRGVCVRDADVFC--GESYLKVNFP--PFLFELFLYAPIDDGKSKAKIGNDTILFTLYK 77
Cdd:pfam04969   2 RYDWYQTLDEVTITIPVKGAGIKKKDVKVniKPRSLKVKIKggYELIDGELFHPIDPEESSWTIEGKKVEITLKK 76
TPR_1 pfam00515
Tetratricopeptide repeat;
198-227 4.93e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 33.93  E-value: 4.93e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1039793990 198 PLLYLNRAACHLKLKNLHKAIEDSSKALEL 227
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALEL 30
 
Name Accession Description Interval E-value
p23_DYX1C1_like cd06469
p23_like domain found in proteins similar to dyslexia susceptibility 1 (DYX1) candidate 1 (C1) ...
 10-87 1.36e-37

p23_like domain found in proteins similar to dyslexia susceptibility 1 (DYX1) candidate 1 (C1) protein, DYX1C1. The human gene encoding this protein is a positional candidate gene for developmental dyslexia (DD), it is located on 15q21.3 by the DYX1 DD susceptibility locus (15q15-21). Independent association studies have reported conflicting results. However, association of short-term memory, which plays a role in DD, with a variant within the DYX1C1 gene has been reported. Most proteins belonging to this group contain a C-terminal tetratricopeptide repeat (TPR) protein binding region.


Pssm-ID: 107226  Cd Length: 78  Bit Score: 128.16  E-value: 1.36e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039793990  10 WQQTPATIFLSLPLRGVCVRDADVFCGESYLKVNFPPFLFELFLYAPIDDGKSKAKIGNDTILFTLYKKEPVLWDSLS 87
Cdd:cd06469     1 WSQTDEDVKISVPLKGVKTSKVDIFCSDLYLKVNFPPYLFELDLAAPIDDEKSSAKIGNGVLVFTLVKKEPGIWEALC 78
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 10-86 1.03e-15

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: 70.78  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990  10 WQQTPATIFLSLPLRGVCVRDADVFCGESYLKVNF-----PPFLFELFLYAPIDDGKSKAKIGNDTILFTLYKKEP-VLW 83
Cdd:cd06463     1 WYQTLDEVTITIPLKDVTKKDVKVEFTPKSLTVSVkggggKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPgEWW 80


                  ...
gi 1039793990  84 DSL 86
Cdd:cd06463    81 PRL 83
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 93-270 3.19e-13

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 69.63  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990  93 KEMMQRIREKSILQAQEKAKEATEAKAVAKREDQRYALGEMMKWLHKQAEARRAmstdlpeffDLKEEERN--PDWLKDK 170
Cdd:TIGR00990  63 RESKPKISKKERRKRKQAEKETEGKTEEKKSTAPKNAPVEPADELPEIDESSVA---------NLSEEERKkyAAKLKEK 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 171 GNKLFATENYLAAVDAYNLAIRLNcKIPLLYLNRAACHLKLKNLHKAIEDSSKALELltppvadnANARMKAHVRRGTAF 250
Cdd:TIGR00990 134 GNKAYRNKDFNKAIKLYSKAIECK-PDPVYYSNRAACHNALGDWEKVVEDTTAALEL--------DPDYSKALNRRANAY 204

                         170       180
                  ....*....|....*....|
gi 1039793990 251 CQLELYVEGLQDYEAALKID 270
Cdd:TIGR00990 205 DGLGKYADALLDLTASCIID 224
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 167-269 1.48e-11

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 64.04  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 167 LKDKGNKLFATENYLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALElLTPPVAdnanarmKAHVRR 246
Cdd:PLN03088    5 LEDKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIE-LDPSLA-------KAYLRK 76

                          90       100
                  ....*....|....*....|...
gi 1039793990 247 GTAFCQLELYveglQDYEAALKI 269
Cdd:PLN03088   77 GTACMKLEEY----QTAKAALEK 95
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
171-271 2.23e-10

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 59.54  E-value: 2.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 171 GNKLFATENYLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALELltppvaDNANARmkAHVRRGTAF 250
Cdd:COG4785    80 GVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALEL------DPDYAY--AYLNRGIAL 151

                          90       100
                  ....*....|....*....|.
gi 1039793990 251 CQLELYVEGLQDYEAALKIDP 271
Cdd:COG4785   152 YYLGRYELAIADLEKALELDP 172
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
157-273 2.08e-09

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 56.94  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 157 LKEEERNPDWLKDKGNKLFATENYLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALELltppvaDNA 236
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL------DPD 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039793990 237 NARmkAHVRRGTAFCQLELYVEGLQDYEAALKIDPAN 273
Cdd:COG0457    75 DAE--ALNNLGLALQALGRYEEALEDYDKALELDPDD 109
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
 10-86 3.88e-09

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: 52.59  E-value: 3.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990  10 WQQTPATIFLSLPLRGVCVRDADVFCGESYLKVNFP-----PFLFELFLYAPIDDGKSKAKIGNDTILFTLYKKEPVLWD 84
Cdd:cd06466     2 WYQTDTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIIlpggsEYQLELDLFGPIDPEQSKVSVLPTKVEITLKKAEPGSWP 81


                  ..
gi 1039793990  85 SL 86
Cdd:cd06466    82 SL 83
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 92-278 5.68e-09

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 56.93  E-value: 5.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990  92 DKEMMQRIREKSILQAQEKAKEATEAKAVAKREDQRYALGEMMKWLHKQAEARRAMSTDLPEFFDLKEEERNPdWLKDKG 171
Cdd:COG3914     7 LALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAA-LLELAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 172 NKLFATENYLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALELltppVADNANarmkAHVRRGTAFC 251
Cdd:COG3914    86 LLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALAL----NPDFAE----AYLNLGEALR 157

                         170       180
                  ....*....|....*....|....*..
gi 1039793990 252 QLELYVEGLQDYEAALKIDPANTVVQN 278
Cdd:COG3914   158 RLGRLEEAIAALRRALELDPDNAEALN 184
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
104-272 5.02e-08

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 52.70  E-value: 5.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 104 ILQAQEKAKEATEA--KAVAKREDQRYALGEMMKWLHKQAEARRAMstdlpEFFD--LKEEERNPDWLKDKGNKLFATEN 179
Cdd:COG0457    17 AYRRLGRYEEAIEDyeKALELDPDDAEALYNLGLAYLRLGRYEEAL-----ADYEqaLELDPDDAEALNNLGLALQALGR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 180 YLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALELltppvaDNANARmkAHVRRGTAFCQLELYVEG 259
Cdd:COG0457    92 YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL------DPDDAD--ALYNLGIALEKLGRYEEA 163

                         170
                  ....*....|...
gi 1039793990 260 LQDYEAALKIDPA 272
Cdd:COG0457   164 LELLEKLEAAALA 176
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
 7-77 1.40e-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: 48.02  E-value: 1.40e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039793990   7 EFSWQQTPATIFLSLPLRGVCVRDADVFC--GESYLKVNFP--PFLFELFLYAPIDDGKSKAKIGNDTILFTLYK 77
Cdd:pfam04969   2 RYDWYQTLDEVTITIPVKGAGIKKKDVKVniKPRSLKVKIKggYELIDGELFHPIDPEESSWTIEGKKVEITLKK 76
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 121-273 2.70e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 45.95  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 121 AKREDQRYALGEMMKWLHKQAEARRAMSTDLpeffdlKEEERNPDWLKDKGNKLFATENYLAAVDAYNLAIRLNCKIPLL 200
Cdd:COG4783     1 AACAEALYALAQALLLAGDYDEAEALLEKAL------ELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEA 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039793990 201 YLNRAACHLKLKNLHKAIEDSSKALELltppvaDNANARmkAHVRRGTAFCQLELYVEGLQDYEAALKIDPAN 273
Cdd:COG4783    75 RLNLGLALLKAGDYDEALALLEKALKL------DPEHPE--AYLRLARAYRALGRPDEAIAALEKALELDPDD 139
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 10-77 3.20e-06

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: 44.50  E-value: 3.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990  10 WQQTPATIFLSLPLRGVCVRDADVFCGESYLKV------------NFPPFLFELFLYAPIDDGKSKAKIGNDTILFTLYK 77
Cdd:cd00298     1 WYQTDDEVVVTVDLPGVKKEDIKVEVEDNVLTIsgkreeeeererSYGEFERSFELPEDVDPEKSKASLENGVLEITLPK 80
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 157-288 3.20e-06

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 45.77  E-value: 3.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 157 LKEEERNPDWLKDKGNKLFATENYLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALELltppvaDNA 236
Cdd:COG4235    10 LAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL------DPD 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039793990 237 NARmkAHVRRGTAFCQLELYVEGLQDYEAALKIDPANTvvqnDAEKIRNIIQ 288
Cdd:COG4235    84 NPE--ALYLLGLAAFQQGDYAEAIAAWQKLLALLPADA----PARLLEASIA 129
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
174-273 6.88e-06

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 46.06  E-value: 6.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 174 LFATENYLAAVDAYNLAIR---LNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALELltppvaDNANARmkAHVRRGTAF 250
Cdd:COG4785    46 LALAAAALAAAALAAERIDralALPDLAQLYYERGVAYDSLGDYDLAIADFDQALEL------DPDLAE--AYNNRGLAY 117

                          90       100
                  ....*....|....*....|...
gi 1039793990 251 CQLELYVEGLQDYEAALKIDPAN 273
Cdd:COG4785   118 LLLGDYDAALEDFDRALELDPDY 140
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
191-278 7.38e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 46.15  E-value: 7.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 191 IRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALELltppvaDNANArmKAHVRRGTAFCQLELYVEGLQDYEAALKID 270
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALEL------DPDDA--EALYNLGLAYLRLGRYEEALADYEQALELD 72


                  ....*...
gi 1039793990 271 PANTVVQN 278
Cdd:COG0457    73 PDDAEALN 80
p23_CacyBP cd06468
p23_like domain found in proteins similar to Calcyclin-Binding Protein(CacyBP) ...
 5-86 1.98e-05

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: 42.25  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990   5 VSEFSWQQTPATIFLSLPLRGVcvrdadVFCGESYLKVNFPPFLFELF---------------LYAPIDDGKSKAKIGND 69
Cdd:cd06468     1 ITKYAWDQSDKFVKIYITLKGV------HQLPKENIQVEFTERSFELKvhdlngknyrftinrLLKKIDPEKSSFKVKTD 74

                          90
                  ....*....|....*..
gi 1039793990  70 TILFTLYKKEPVLWDSL 86
Cdd:cd06468    75 RIVITLAKKKEKKWESL 91
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
157-227 8.31e-05

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 42.98  E-value: 8.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039793990 157 LKEEERNPDWLKDKGNKLFATENYLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALEL 227
Cdd:COG4785   100 LELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALEL 170
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 109-283 1.53e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.41  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 109 EKAKEATEaKAVAKREDQRYALGEMMKWLHKQAEARRAMstdlpEFFD--LKEEERNPDWLKDKGNKLFATENYLAAVDA 186
Cdd:COG2956    59 DRAIRIHQ-KLLERDPDRAEALLELAQDYLKAGLLDRAE-----ELLEklLELDPDDAEALRLLAEIYEQEGDWEKAIEV 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 187 YNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALElltppvADNANARmkAHVRRGTAFCQLELYVEGLQDYEAA 266
Cdd:COG2956   133 LERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALK------LDPDCAR--ALLLLAELYLEQGDYEEAIAALERA 204

                         170
                  ....*....|....*..
gi 1039793990 267 LKIDPANTVVQNDAEKI 283
Cdd:COG2956   205 LEQDPDYLPALPRLAEL 221
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 94-227 1.66e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.06  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990  94 EMMQRIREKSILQAQEKAKEATEA--KAVAKREDQ---RYALGEMMKWLHKQAEA----RRAmstdlpeffdLKEEERNP 164
Cdd:COG3914    77 LAALLELAALLLQALGRYEEALALyrRALALNPDNaeaLFNLGNLLLALGRLEEAlaalRRA----------LALNPDFA 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039793990 165 DWLKDKGNKLFATENYLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALEL 227
Cdd:COG3914   147 EAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEL 209
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 111-271 2.04e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 41.10  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 111 AKEATEAKAVAKREDQRYALGEMMKWLHKQAEARRAMSTDLPEFFDLKEEERNPDWLKDKGNKLFATENYLAAVDAYNLA 190
Cdd:COG5010     1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 191 IRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALELltppvaDNANARmkAHVRRGTAFCQLELYVEGLQDYEAALKID 270
Cdd:COG5010    81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL------SPDNPN--AYSNLAALLLSLGQDDEAKAALQRALGTS 152


                  .
gi 1039793990 271 P 271
Cdd:COG5010   153 P 153
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
104-286 3.31e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 41.15  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 104 ILQAQEKAKEATEA--KAVAKREDQ---RYALGEMMKWLHKQAEARramstdlpEFFD--LKEEERNPDWLKDKGNKLFA 176
Cdd:COG0457    51 AYLRLGRYEEALADyeQALELDPDDaeaLNNLGLALQALGRYEEAL--------EDYDkaLELDPDDAEALYNLGLALLE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 177 TENYLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALELLTPPVADNANARMKAHVRRGTAFCQLELY 256
Cdd:COG0457   123 LGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLA 202

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039793990 257 VEGLQDYEAALKIDPANTVVQNDAEKIRNI 286
Cdd:COG0457   203 LEQALRKKLAILTLAALAELLLLALALLLA 232
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 7-80 1.97e-03

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: 37.19  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990   7 EFSWQQTPATIFLSLPLRgvCVRDADVFCGESYLK------VNFPPFLFELFLYAPIDDGKSKAKIGNDTILFTLYKKEP 80
Cdd:cd06465     2 PVLWAQRSDVVYLTIELP--DAKDPKIKLEPTSLSfkakggGGGKKYEFDLEFYKEIDPEESKYKVTGRQIEFVLRKKEA 79
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
174-272 4.76e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 35.92  E-value: 4.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 174 LFATENYLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEdSSKALELltppvaDNANARmkAHVRRGTAFCQL 253
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKL------DPNNAE--ALLNLAELLLEL 72

                          90
                  ....*....|....*....
gi 1039793990 254 ELYVEGLQDYEAALKIDPA 272
Cdd:COG3063    73 GDYDEALAYLERALELDPS 91
TPR_1 pfam00515
Tetratricopeptide repeat;
198-227 4.93e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 33.93  E-value: 4.93e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1039793990 198 PLLYLNRAACHLKLKNLHKAIEDSSKALEL 227
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALEL 30
TPR_1 pfam00515
Tetratricopeptide repeat;
241-273 5.82e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 33.93  E-value: 5.82e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1039793990 241 KAHVRRGTAFCQLELYVEGLQDYEAALKIDPAN 273
Cdd:pfam00515   2 KALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 104-227 8.60e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 35.94  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793990 104 ILQAQEKAKEATEA--KAVAKREDQRYALGEMMKWLHKQAEARRAMstdlpEFFD--LKEEERNPDWLKDKGNKLFATEN 179
Cdd:COG4783    13 ALLLAGDYDEAEALleKALELDPDNPEAFALLGEILLQLGDLDEAI-----VLLHeaLELDPDEPEARLNLGLALLKAGD 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1039793990 180 YLAAVDAYNLAIRLNCKIPLLYLNRAACHLKLKNLHKAIEDSSKALEL 227
Cdd:COG4783    88 YDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALEL 135
 
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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