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Conserved domains on  [gi|1085787102|emb|SDS93950|]
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Uncharacterized membrane protein [Mucilaginibacter mallensis]

Protein Classification

COG5637 family protein( domain architecture ID 11475738)

COG5637 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
87-227 1.99e-58

Uncharacterized protein, contains SRPBCC domain [Function unknown];


:

Pssm-ID: 444363  Cd Length: 154  Bit Score: 182.03  E-value: 1.99e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085787102  87 INIRSSFIIHKPRKDVYDFWRRFDNLPLFMTHLKNVELLNNDHSRWVLRLPIGVaSISWEAEVVKDKPNEMIGWRSLPGS 166
Cdd:COG5637     2 TTVEKSITINAPVEEVYAYWRDFENLPRFMKGVESVTVLDDTRSHWVAKGPLGV-TVEWDAEITEQVPGERIAWRSVEGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085787102 167 IlDNSGKVRFKDTeDGESTRVDVVISYQPPVGTVGASIARVFNPVFKKMVEKDVRNFKHYM 227
Cdd:COG5637    81 I-PNAGVVRFEPA-GGRGTRVTVTIEYDPPGGLLGKALAKLFGGVPERQLREDLERFKQLI 139
 
Name Accession Description Interval E-value
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
87-227 1.99e-58

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 182.03  E-value: 1.99e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085787102  87 INIRSSFIIHKPRKDVYDFWRRFDNLPLFMTHLKNVELLNNDHSRWVLRLPIGVaSISWEAEVVKDKPNEMIGWRSLPGS 166
Cdd:COG5637     2 TTVEKSITINAPVEEVYAYWRDFENLPRFMKGVESVTVLDDTRSHWVAKGPLGV-TVEWDAEITEQVPGERIAWRSVEGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085787102 167 IlDNSGKVRFKDTeDGESTRVDVVISYQPPVGTVGASIARVFNPVFKKMVEKDVRNFKHYM 227
Cdd:COG5637    81 I-PNAGVVRFEPA-GGRGTRVTVTIEYDPPGGLLGKALAKLFGGVPERQLREDLERFKQLI 139
SRPBCC_8 cd07817
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 88-227 2.54e-57

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176859  Cd Length: 139  Bit Score: 178.57  E-value: 2.54e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085787102  88 NIRSSFIIHKPRKDVYDFWRRFDNLPLFMTHLKNVELLNNDHSRWVLRLPIGVaSISWEAEVVKDKPNEMIGWRSLPGSI 167
Cdd:cd07817     1 TVEKSITVNVPVEEVYDFWRDFENLPRFMSHVESVEQLDDTRSHWKAKGPAGL-SVEWDAEITEQVPNERIAWRSVEGAD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085787102 168 lDNSGKVRFKDTeDGESTRVDVVISYQPPVGTVGASIARVFNPVFKKMVEKDVRNFKHYM 227
Cdd:cd07817    80 -PNAGSVRFRPA-PGRGTRVTLTIEYEPPGGAEGAAVAGLLGGEPERQLREDLRRFKQLV 137
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 95-224 5.24e-15

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. The family also includes proteins which are involved in the binding/transport of lipids.


Pssm-ID: 397441  Cd Length: 125  Bit Score: 69.06  E-value: 5.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085787102  95 IHKPRKDVYDFWRRFDNLPLFMTHLKNVELLNNDHSRWVLRLPIGVASISWEAEVVKDKPnEMIGWRSLPGSILDNSGKV 174
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSLADWRVAFGGLRRSFTARVTLQPP-ERIEMVLVDGDFKRLEGSW 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1085787102 175 RFKDTEDGESTRVDVVISYQPPVGTVGAsiarVFNPVFKKMVEKDVRNFK 224
Cdd:pfam03364  80 RFEPGGPGTRVKVTLELDFEFASPLPGA----LLGFVFRRVLRTLLEAFR 125
 
Name Accession Description Interval E-value
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
87-227 1.99e-58

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 182.03  E-value: 1.99e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085787102  87 INIRSSFIIHKPRKDVYDFWRRFDNLPLFMTHLKNVELLNNDHSRWVLRLPIGVaSISWEAEVVKDKPNEMIGWRSLPGS 166
Cdd:COG5637     2 TTVEKSITINAPVEEVYAYWRDFENLPRFMKGVESVTVLDDTRSHWVAKGPLGV-TVEWDAEITEQVPGERIAWRSVEGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085787102 167 IlDNSGKVRFKDTeDGESTRVDVVISYQPPVGTVGASIARVFNPVFKKMVEKDVRNFKHYM 227
Cdd:COG5637    81 I-PNAGVVRFEPA-GGRGTRVTVTIEYDPPGGLLGKALAKLFGGVPERQLREDLERFKQLI 139
SRPBCC_8 cd07817
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 88-227 2.54e-57

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176859  Cd Length: 139  Bit Score: 178.57  E-value: 2.54e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085787102  88 NIRSSFIIHKPRKDVYDFWRRFDNLPLFMTHLKNVELLNNDHSRWVLRLPIGVaSISWEAEVVKDKPNEMIGWRSLPGSI 167
Cdd:cd07817     1 TVEKSITVNVPVEEVYDFWRDFENLPRFMSHVESVEQLDDTRSHWKAKGPAGL-SVEWDAEITEQVPNERIAWRSVEGAD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085787102 168 lDNSGKVRFKDTeDGESTRVDVVISYQPPVGTVGASIARVFNPVFKKMVEKDVRNFKHYM 227
Cdd:cd07817    80 -PNAGSVRFRPA-PGRGTRVTLTIEYEPPGGAEGAAVAGLLGGEPERQLREDLRRFKQLV 137
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 95-224 5.24e-15

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. The family also includes proteins which are involved in the binding/transport of lipids.


Pssm-ID: 397441  Cd Length: 125  Bit Score: 69.06  E-value: 5.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085787102  95 IHKPRKDVYDFWRRFDNLPLFMTHLKNVELLNNDHSRWVLRLPIGVASISWEAEVVKDKPnEMIGWRSLPGSILDNSGKV 174
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSLADWRVAFGGLRRSFTARVTLQPP-ERIEMVLVDGDFKRLEGSW 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1085787102 175 RFKDTEDGESTRVDVVISYQPPVGTVGAsiarVFNPVFKKMVEKDVRNFK 224
Cdd:pfam03364  80 RFEPGGPGTRVKVTLELDFEFASPLPGA----LLGFVFRRVLRTLLEAFR 125
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 89-217 2.51e-12

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 62.19  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085787102  89 IRSSFIIHKPRKDVYDFWRRFDNLPLFMTHLKNVELLNNDHSRWVLRLPIGVASI--SWEAEVVKDkPNEMIGWRSLPGS 166
Cdd:COG2867     4 ISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLreSFTTRNTLD-PPERIDFELVDGP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1085787102 167 ILDNSGKVRFKDTEDGeSTRVDVVISYQPPVGTVGASIARVFNPVFKKMVE 217
Cdd:COG2867    83 FKHLEGRWRFEPLGEG-GTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVD 132
SRPBCC_10 cd08865
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 89-224 2.78e-08

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176874  Cd Length: 140  Bit Score: 51.13  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085787102  89 IRSSFIIHKPRKDVYDFWRRFDNLPLFMTHLKNVELLNNDH----SRWVLRLPIGVASISWEAEVVKDKPNEMIGWRSlp 164
Cdd:cd08865     1 VEESIVIERPVEEVFAYLADFENAPEWDPGVVEVEKITDGPvgvgTRYHQVRKFLGRRIELTYEITEYEPGRRVVFRG-- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085787102 165 gsildNSGKVRFKDT----EDGESTRVDVVISYQPpvGTVGASIARVFNPVFKKMVEKDVRNFK 224
Cdd:cd08865    79 -----SSGPFPYEDTytfePVGGGTRVRYTAELEP--GGFARLLDPLMAPAFRRRARAALENLK 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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