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Conserved domains on  [gi|7949018|ref|NP_058022|]
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hsp90 co-chaperone Cdc37 isoform 2 [Mus musculus]

Protein Classification

CDC37_N and CDC37_M domain-containing protein( domain architecture ID 10660770)

protein containing domains CDC37_N, CDC37_M, and CDC37_C

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDC37_M smart01070
Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of ...
 134-276 7.03e-60

Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the Hsp90 chaperone (Heat shocked protein 90) binding domain of Cdc37. It is found between the N terminal Cdc37 domain which is predominantly involved in kinase binding, and the C terminal domain of Cdc37 whose function is unclear.


:

Pssm-ID: 215010  Cd Length: 155  Bit Score: 190.67  E-value: 7.03e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018     134 PEKAEEDSEEAREQKHKTFVEKYEKQIKHFGML--HRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVA 211
Cdd:smart01070   7 KNPPSAPSEEEDEIDDKDFVLKLEPATKKFGMIpaGDYDDSQKFLSEHPHIVSEETADALVMWAFDLELEGKEALMEQVA 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7949018     212 HQTMVMQFILELAKSLKVDPRACFRQFFTKIKTADHQ----YMEGFKYELEAFKERVRGRAKLRIEKAM 276
Cdd:smart01070  87 HQAILMQYILELAKSLKVDPRNCVRLFFQKIKTPSHPakegFLEDVQSEFEHIKTRVRIIAQEQAEEAM 155
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 1-128 8.19e-44

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


:

Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 149.10  E-value: 8.19e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018       1 MVDYSVWDHIEVSDDED-ETHPNIDTASLFRWR----HQARVERMEQFQ-------------KEKEELDRGCREC----- 57
Cdd:smart01071   1 PIDYSKWDKIELSDDSDiEVHPNVDKKSFIRWKqrdiHQARVERMEEIKnlkyelimndhlnKRIDKLLKGLREEelspe 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7949018      58 ----KRKVAECQRKL-KELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKKEKNMPWNVDTlsKDGFSKS 128
Cdd:smart01071  81 tptyNEMLAELQDQLkKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKLDELEKEEKKKIWSVDT--HTGFDKS 154
CDC37_C smart01069
Cdc37 C terminal domain; Cdc37 is a protein required for the activity of numerous eukaryotic ...
 288-378 1.92e-22

Cdc37 C terminal domain; Cdc37 is a protein required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the C terminal domain whose function is unclear. It is found C terminal to the Hsp90 chaperone (Heat shocked protein 90) binding domain pfam08565 and the N terminal kinase binding domain of Cdc37.


:

Pssm-ID: 215009  Cd Length: 93  Bit Score: 90.54  E-value: 1.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018     288 LGPGGL--DPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKSGEAKEGEEAGPGDPLL 365
Cdd:smart01069   1 NLPGGLslDPEEVFESLPPELQKAFETKDLDMLNKVLAKMPVEEAEYHLERCIESGLWGVPNAIEDETEFKELQEQYEVE 80

                           90
                   ....*....|...
gi 7949018     366 EAVPKAGNEKDVS 378
Cdd:smart01069  81 EEAEKEDEEEEDD 93
 
Name Accession Description Interval E-value
CDC37_M smart01070
Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of ...
 134-276 7.03e-60

Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the Hsp90 chaperone (Heat shocked protein 90) binding domain of Cdc37. It is found between the N terminal Cdc37 domain which is predominantly involved in kinase binding, and the C terminal domain of Cdc37 whose function is unclear.


Pssm-ID: 215010  Cd Length: 155  Bit Score: 190.67  E-value: 7.03e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018     134 PEKAEEDSEEAREQKHKTFVEKYEKQIKHFGML--HRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVA 211
Cdd:smart01070   7 KNPPSAPSEEEDEIDDKDFVLKLEPATKKFGMIpaGDYDDSQKFLSEHPHIVSEETADALVMWAFDLELEGKEALMEQVA 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7949018     212 HQTMVMQFILELAKSLKVDPRACFRQFFTKIKTADHQ----YMEGFKYELEAFKERVRGRAKLRIEKAM 276
Cdd:smart01070  87 HQAILMQYILELAKSLKVDPRNCVRLFFQKIKTPSHPakegFLEDVQSEFEHIKTRVRIIAQEQAEEAM 155
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 1-128 8.19e-44

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 149.10  E-value: 8.19e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018       1 MVDYSVWDHIEVSDDED-ETHPNIDTASLFRWR----HQARVERMEQFQ-------------KEKEELDRGCREC----- 57
Cdd:smart01071   1 PIDYSKWDKIELSDDSDiEVHPNVDKKSFIRWKqrdiHQARVERMEEIKnlkyelimndhlnKRIDKLLKGLREEelspe 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7949018      58 ----KRKVAECQRKL-KELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKKEKNMPWNVDTlsKDGFSKS 128
Cdd:smart01071  81 tptyNEMLAELQDQLkKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKLDELEKEEKKKIWSVDT--HTGFDKS 154
CDC37_M pfam08565
Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of ...
 163-276 4.51e-23

Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the Hsp90 chaperone (Heat shocked protein 90) binding domain of Cdc37. It is found between the N terminal Cdc37 domain pfam03234, which is predominantly involved in kinase binding, and the C terminal domain of Cdc37 pfam08564 whose function is unclear.


Pssm-ID: 430078  Cd Length: 113  Bit Score: 92.64  E-value: 4.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018    163 FGMLHR--WDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTMVMQFILELAkslkvDPRACFRQFFT 240
Cdd:pfam08565   2 FAKIPSgdYKASEQFLLKHPEILSEQQKDALLMEAFDAQLEGKTKYARQCVHQSLLLQYCRQLD-----GRINGVKLFFK 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 7949018    241 KIKTADHQYMEGFKYELEAFKERVRGRAKLRIEKAM 276
Cdd:pfam08565  77 RITTKDHQAKKLFLDDVQSTYNHIKTRAEEIKQEQA 112
CDC37_C smart01069
Cdc37 C terminal domain; Cdc37 is a protein required for the activity of numerous eukaryotic ...
 288-378 1.92e-22

Cdc37 C terminal domain; Cdc37 is a protein required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the C terminal domain whose function is unclear. It is found C terminal to the Hsp90 chaperone (Heat shocked protein 90) binding domain pfam08565 and the N terminal kinase binding domain of Cdc37.


Pssm-ID: 215009  Cd Length: 93  Bit Score: 90.54  E-value: 1.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018     288 LGPGGL--DPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKSGEAKEGEEAGPGDPLL 365
Cdd:smart01069   1 NLPGGLslDPEEVFESLPPELQKAFETKDLDMLNKVLAKMPVEEAEYHLERCIESGLWGVPNAIEDETEFKELQEQYEVE 80

                           90
                   ....*....|...
gi 7949018     366 EAVPKAGNEKDVS 378
Cdd:smart01069  81 EEAEKEDEEEEDD 93
CDC37_C pfam08564
Cdc37 C terminal domain; Cdc37 is a protein required for the activity of numerous eukaryotic ...
 291-343 1.31e-13

Cdc37 C terminal domain; Cdc37 is a protein required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the C terminal domain whose function is unclear. It is found C terminal to the Hsp90 chaperone (Heat shocked protein 90) binding domain pfam08565 and the N terminal kinase binding domain of Cdc37 pfam03234.


Pssm-ID: 430077  Cd Length: 87  Bit Score: 65.81  E-value: 1.31e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 7949018    291 GGLDP-----VEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLW 343
Cdd:pfam08564   6 GSEDPeeqkaVEIFESLPPEMQKALKTKSLDEVNKVLGKMPVEEAEEIVELFGEAGIL 63
CDC37_N pfam03234
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 7-50 1.56e-10

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain pfam08565. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 427208 [Multi-domain]  Cd Length: 124  Bit Score: 58.39  E-value: 1.56e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 7949018      7 WDHIEVSDDED-ETHPNIDTASLFRWR----HQARVERMEQFQKEKEEL 50
Cdd:pfam03234   2 WDALELSDDSDiEVHPNVDKRSFIRWKqrdiHEKREQRKAEIKTLKYER 50
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 41-155 3.61e-06

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 48.86  E-value: 3.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018    41 EQFQKEKEELDRGCRECKRKVAECQRKLK------------------ELEVAESDGQV---ELERLRAEAQQLRKEERSW 99
Cdd:NF033838 128 EQFKKDTLEPGKKVAEATKKVEEAEKKAKdqkeedrrnyptntyktlELEIAESDVEVkkaELELVKEEAKEPRDEEKIK 207

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 7949018   100 EQKLEDMRKKEknmpwNVDTLSKdgfsksmVNTKPEKAEEDSEEAREQKHKTFVEK 155
Cdd:NF033838 208 QAKAKVESKKA-----EATRLEK-------IKTDREKAEEEAKRRADAKLKEAVEK 251
PTZ00121 PTZ00121
MAEBL; Provisional
 37-159 4.89e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018     37 VERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAE--------------------AQQLRKEE 96
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakkaeelkkkeaeekkkAEELKKAE 1725

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7949018     97 RSWEQKLEDMRKKEKNMPWNVDTLSKDGFSKSMVNTKPEKAEEDSEEAREQKHKTFVEKYEKQ 159
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-105 1.27e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7949018    38 ERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLED 105
Cdd:COG4913  338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 38-109 3.78e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 3.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7949018      38 ERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKK 109
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
 
Name Accession Description Interval E-value
CDC37_M smart01070
Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of ...
 134-276 7.03e-60

Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the Hsp90 chaperone (Heat shocked protein 90) binding domain of Cdc37. It is found between the N terminal Cdc37 domain which is predominantly involved in kinase binding, and the C terminal domain of Cdc37 whose function is unclear.


Pssm-ID: 215010  Cd Length: 155  Bit Score: 190.67  E-value: 7.03e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018     134 PEKAEEDSEEAREQKHKTFVEKYEKQIKHFGML--HRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVA 211
Cdd:smart01070   7 KNPPSAPSEEEDEIDDKDFVLKLEPATKKFGMIpaGDYDDSQKFLSEHPHIVSEETADALVMWAFDLELEGKEALMEQVA 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7949018     212 HQTMVMQFILELAKSLKVDPRACFRQFFTKIKTADHQ----YMEGFKYELEAFKERVRGRAKLRIEKAM 276
Cdd:smart01070  87 HQAILMQYILELAKSLKVDPRNCVRLFFQKIKTPSHPakegFLEDVQSEFEHIKTRVRIIAQEQAEEAM 155
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 1-128 8.19e-44

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 149.10  E-value: 8.19e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018       1 MVDYSVWDHIEVSDDED-ETHPNIDTASLFRWR----HQARVERMEQFQ-------------KEKEELDRGCREC----- 57
Cdd:smart01071   1 PIDYSKWDKIELSDDSDiEVHPNVDKKSFIRWKqrdiHQARVERMEEIKnlkyelimndhlnKRIDKLLKGLREEelspe 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7949018      58 ----KRKVAECQRKL-KELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKKEKNMPWNVDTlsKDGFSKS 128
Cdd:smart01071  81 tptyNEMLAELQDQLkKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKLDELEKEEKKKIWSVDT--HTGFDKS 154
CDC37_M pfam08565
Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of ...
 163-276 4.51e-23

Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the Hsp90 chaperone (Heat shocked protein 90) binding domain of Cdc37. It is found between the N terminal Cdc37 domain pfam03234, which is predominantly involved in kinase binding, and the C terminal domain of Cdc37 pfam08564 whose function is unclear.


Pssm-ID: 430078  Cd Length: 113  Bit Score: 92.64  E-value: 4.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018    163 FGMLHR--WDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTMVMQFILELAkslkvDPRACFRQFFT 240
Cdd:pfam08565   2 FAKIPSgdYKASEQFLLKHPEILSEQQKDALLMEAFDAQLEGKTKYARQCVHQSLLLQYCRQLD-----GRINGVKLFFK 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 7949018    241 KIKTADHQYMEGFKYELEAFKERVRGRAKLRIEKAM 276
Cdd:pfam08565  77 RITTKDHQAKKLFLDDVQSTYNHIKTRAEEIKQEQA 112
CDC37_C smart01069
Cdc37 C terminal domain; Cdc37 is a protein required for the activity of numerous eukaryotic ...
 288-378 1.92e-22

Cdc37 C terminal domain; Cdc37 is a protein required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the C terminal domain whose function is unclear. It is found C terminal to the Hsp90 chaperone (Heat shocked protein 90) binding domain pfam08565 and the N terminal kinase binding domain of Cdc37.


Pssm-ID: 215009  Cd Length: 93  Bit Score: 90.54  E-value: 1.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018     288 LGPGGL--DPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKSGEAKEGEEAGPGDPLL 365
Cdd:smart01069   1 NLPGGLslDPEEVFESLPPELQKAFETKDLDMLNKVLAKMPVEEAEYHLERCIESGLWGVPNAIEDETEFKELQEQYEVE 80

                           90
                   ....*....|...
gi 7949018     366 EAVPKAGNEKDVS 378
Cdd:smart01069  81 EEAEKEDEEEEDD 93
CDC37_C pfam08564
Cdc37 C terminal domain; Cdc37 is a protein required for the activity of numerous eukaryotic ...
 291-343 1.31e-13

Cdc37 C terminal domain; Cdc37 is a protein required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the C terminal domain whose function is unclear. It is found C terminal to the Hsp90 chaperone (Heat shocked protein 90) binding domain pfam08565 and the N terminal kinase binding domain of Cdc37 pfam03234.


Pssm-ID: 430077  Cd Length: 87  Bit Score: 65.81  E-value: 1.31e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 7949018    291 GGLDP-----VEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLW 343
Cdd:pfam08564   6 GSEDPeeqkaVEIFESLPPEMQKALKTKSLDEVNKVLGKMPVEEAEEIVELFGEAGIL 63
CDC37_N pfam03234
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 7-50 1.56e-10

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain pfam08565. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 427208 [Multi-domain]  Cd Length: 124  Bit Score: 58.39  E-value: 1.56e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 7949018      7 WDHIEVSDDED-ETHPNIDTASLFRWR----HQARVERMEQFQKEKEEL 50
Cdd:pfam03234   2 WDALELSDDSDiEVHPNVDKRSFIRWKqrdiHEKREQRKAEIKTLKYER 50
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 41-155 3.61e-06

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 48.86  E-value: 3.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018    41 EQFQKEKEELDRGCRECKRKVAECQRKLK------------------ELEVAESDGQV---ELERLRAEAQQLRKEERSW 99
Cdd:NF033838 128 EQFKKDTLEPGKKVAEATKKVEEAEKKAKdqkeedrrnyptntyktlELEIAESDVEVkkaELELVKEEAKEPRDEEKIK 207

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 7949018   100 EQKLEDMRKKEknmpwNVDTLSKdgfsksmVNTKPEKAEEDSEEAREQKHKTFVEK 155
Cdd:NF033838 208 QAKAKVESKKA-----EATRLEK-------IKTDREKAEEEAKRRADAKLKEAVEK 251
PTZ00121 PTZ00121
MAEBL; Provisional
 37-159 4.89e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018     37 VERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAE--------------------AQQLRKEE 96
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakkaeelkkkeaeekkkAEELKKAE 1725

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7949018     97 RSWEQKLEDMRKKEKNMPWNVDTLSKDGFSKSMVNTKPEKAEEDSEEAREQKHKTFVEKYEKQ 159
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
PTZ00121 PTZ00121
MAEBL; Provisional
 32-161 1.23e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018     32 RHQARVERMEQFQKEKEElDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKKEK 111
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 7949018    112 NMPWNVDTLSKDGFSKSMVNTKPEKAEEDSEEAREQKHKTFVEKYEKQIK 161
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-105 1.27e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7949018    38 ERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLED 105
Cdd:COG4913  338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
PRK12704 PRK12704
phosphodiesterase; Provisional
 41-162 1.89e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018    41 EQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDgqvELERLRAEAQQLRKEERSWEQKLEDMRKKEKNMpwnvdtl 120
Cdd:PRK12704  64 EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR---KLELLEKREEELEKKEKELEQKQQELEKKEEEL------- 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 7949018   121 skdgfsKSMVNTKPEKAEE----DSEEAREQkhktFVEKYEKQIKH 162
Cdd:PRK12704 134 ------EELIEEQLQELERisglTAEEAKEI----LLEKVEEEARH 169
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 38-155 1.97e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.26  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018     38 ERMEQfQKEKEELDRGcRECKR-KVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEdmrkKEKNMPWN 116
Cdd:pfam07888 337 ERMER-EKLEVELGRE-KDCNRvQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLE----TVADAKWS 410

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 7949018    117 VDTLSKDGFSKSMVNTKPEKAEEDSEEAREQKHKTFVEK 155
Cdd:pfam07888 411 EAALTSTERPDSPLSDSEDENPEALQPPRPLGHYSLCEQ 449
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 34-113 3.69e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 3.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018   34 QARVERMEQFQKEKEELdrgcRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQ----LRKEERSWEQKLEDMRKK 109
Cdd:COG4942 146 PARREQAEELRADLAEL----AALRAELEAERAELEALLAELEEERAALEALKAERQKllarLEKELAELAAELAELQQE 221


                ....
gi 7949018  110 EKNM 113
Cdd:COG4942 222 AEEL 225
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 38-109 3.78e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 3.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7949018      38 ERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKK 109
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 23-150 5.97e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.91  E-value: 5.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018   23 IDTASlfrwrhqARVeRMEQFQKEkEELDrgcreckrkvaECQRKLKELEVaesdgqvELERLRAE--------AQQLRK 94
Cdd:COG0542 395 IDEAA-------ARV-RMEIDSKP-EELD-----------ELERRLEQLEI-------EKEALKKEqdeasferLAELRD 447

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7949018   95 EERSWEQKLEDMR---KKEKNMPWNVDTLSKDGFSKSMVNTKPEKAEEDSEEAREQKHK 150
Cdd:COG0542 448 ELAELEEELEALKarwEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 58-122 8.54e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.50  E-value: 8.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7949018      58 KRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKKEKNMPWNVDTLSK 122
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
34-112 9.04e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 9.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018   34 QARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAES---------DGQVELERLRAEAQQLRKEERSWEQKLE 104
Cdd:COG4717  84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyqeleALEAELAELPERLEELEERLEELRELEE 163


                ....*...
gi 7949018  105 DMRKKEKN 112
Cdd:COG4717 164 ELEELEAE 171
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 34-146 9.55e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.13  E-value: 9.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018      34 QARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKKEKNM 113
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901

                           90       100       110
                   ....*....|....*....|....*....|....
gi 7949018     114 PWNVDTLSKDGFSK-SMVNTKPEKAEEDSEEARE 146
Cdd:TIGR02169  902 ERKIEELEAQIEKKrKRLSELKAKLEALEEELSE 935
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 23-111 9.60e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.89  E-value: 9.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018   23 IDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQK 102
Cdd:COG3883 118 LDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQ 197


                ....*....
gi 7949018  103 LEDMRKKEK 111
Cdd:COG3883 198 LAELEAELA 206
PTZ00121 PTZ00121
MAEBL; Provisional
 11-155 9.92e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 9.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7949018     11 EVSDDEDETHPNIDTASLFRWRHQARVERM----EQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLR 86
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7949018     87 aEAQQLRKEERSWEQKLEDMRKKEKNMPWNVDTLSKDGFSKSMVNTKPEKAEEDSEEAREQKHKTFVEK 155
Cdd:PTZ00121 1648 -KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
 
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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