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Conserved domains on  [gi|1080984408|gb|OFR41865|]
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hypothetical protein HMPREF2890_08600 [Porphyromonas sp. HMSC065F10]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_2 super family cl44978
START-like superfamily domain; This family of proteins is functionally uncharacterized. This ...
 11-130 2.65e-11

START-like superfamily domain; This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are approximately 130 amino acids in length. This family appears to be distantly related to the START domain.


The actual alignment was detected with superfamily member pfam19569:

Pssm-ID: 437401  Cd Length: 126  Bit Score: 56.73  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080984408  11 KIEIDLD---NASPQSVWNQISTSRGLSEWMAPrvDVSLRN-IHVF-WDetGDDRTATVTDLKKGEYIQWNW-NDHPDSY 84
Cdd:pfam19569   4 KKKFTLEyeiKSSPKILYSFLSEPNGLAQWFAD--DVKYKDqVYTFiWD--DEEQKAKLLSIKENKLVKFKWiDDEPYCY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1080984408  85 VRMEIVVSELSHLVSLLVNDH--DEHLEPTTLqkIWGNHRRKLRLSLG 130
Cdd:pfam19569  80 FEMEIVQDELTNDVALAITDFalDENLKDRKL--IWDNQIEYLISVIG 125
 
Name Accession Description Interval E-value
START_2 pfam19569
START-like superfamily domain; This family of proteins is functionally uncharacterized. This ...
 11-130 2.65e-11

START-like superfamily domain; This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are approximately 130 amino acids in length. This family appears to be distantly related to the START domain.


Pssm-ID: 437401  Cd Length: 126  Bit Score: 56.73  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080984408  11 KIEIDLD---NASPQSVWNQISTSRGLSEWMAPrvDVSLRN-IHVF-WDetGDDRTATVTDLKKGEYIQWNW-NDHPDSY 84
Cdd:pfam19569   4 KKKFTLEyeiKSSPKILYSFLSEPNGLAQWFAD--DVKYKDqVYTFiWD--DEEQKAKLLSIKENKLVKFKWiDDEPYCY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1080984408  85 VRMEIVVSELSHLVSLLVNDH--DEHLEPTTLqkIWGNHRRKLRLSLG 130
Cdd:pfam19569  80 FEMEIVQDELTNDVALAITDFalDENLKDRKL--IWDNQIEYLISVIG 125
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 12-82 1.35e-03

Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.


Pssm-ID: 176856 [Multi-domain]  Cd Length: 139  Bit Score: 36.19  E-value: 1.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080984408  12 IEIDLDnASPQSVWNQISTSRGLSEWMAPRVDVSLR-----NIHVFWDETGDDR---TATVTDLKKGEYIQWNWNDHPD 82
Cdd:cd07814     4 IEREFD-APPELVWRALTDPELLAQWFGPTTTAEMDlrvggRWFFFMTGPDGEEgwvSGEVLEVEPPRRLVFTWAFSDE 81
 
Name Accession Description Interval E-value
START_2 pfam19569
START-like superfamily domain; This family of proteins is functionally uncharacterized. This ...
 11-130 2.65e-11

START-like superfamily domain; This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are approximately 130 amino acids in length. This family appears to be distantly related to the START domain.


Pssm-ID: 437401  Cd Length: 126  Bit Score: 56.73  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080984408  11 KIEIDLD---NASPQSVWNQISTSRGLSEWMAPrvDVSLRN-IHVF-WDetGDDRTATVTDLKKGEYIQWNW-NDHPDSY 84
Cdd:pfam19569   4 KKKFTLEyeiKSSPKILYSFLSEPNGLAQWFAD--DVKYKDqVYTFiWD--DEEQKAKLLSIKENKLVKFKWiDDEPYCY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1080984408  85 VRMEIVVSELSHLVSLLVNDH--DEHLEPTTLqkIWGNHRRKLRLSLG 130
Cdd:pfam19569  80 FEMEIVQDELTNDVALAITDFalDENLKDRKL--IWDNQIEYLISVIG 125
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 12-82 1.35e-03

Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.


Pssm-ID: 176856 [Multi-domain]  Cd Length: 139  Bit Score: 36.19  E-value: 1.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080984408  12 IEIDLDnASPQSVWNQISTSRGLSEWMAPRVDVSLR-----NIHVFWDETGDDR---TATVTDLKKGEYIQWNWNDHPD 82
Cdd:cd07814     4 IEREFD-APPELVWRALTDPELLAQWFGPTTTAEMDlrvggRWFFFMTGPDGEEgwvSGEVLEVEPPRRLVFTWAFSDE 81
 
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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