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Conserved domains on  [gi|518970782|ref|WP_020126657|]
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hypothetical protein [Streptomyces sp. 303MFCol5.2]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VMAP-C pfam20028
vWA-MoxR associated protein C-terminal domain; C-terminal region of the VMAP protein of the ...
 262-497 2.09e-31

vWA-MoxR associated protein C-terminal domain; C-terminal region of the VMAP protein of the classical ternary system (vWA-MoxR-VMAP) in NTP-dependent conflict systems. Mixed alpha+beta domain with no apparent structural similarity to known protein folds. Contains several, nearly universally polar residues, suggesting a conserved interaction interface. Enzymatic function for VMAP-C though possible appears unlikely. Sensing of invasive elements by VMAP-Ms are predicted to trigger a sequence of conformational changes, which is communicated to the switch-component (MoxR) of the system via the more constant VMAP-C.


:

Pssm-ID: 437860  Cd Length: 237  Bit Score: 121.15  E-value: 2.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518970782  262 VRPWLNTVPGRWAPLPAEP---VTTTLEDLGVAIDEVLRQLARLSPPADGPtstvsaAPPCVEFVLPYDLLNHDVAGLNH 338
Cdd:pfam20028   5 VRVWLYRDGGGWHPRPLVGeddRGLPREELPEALAELLAELEEAFRRLDEP------APLVVEFFLPRELLGLPVDEWRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518970782  339 RSGDSGSLPLGLKYGVHLRSLERMRTDDtsLRRRWRERWSVLRTHGIAVHGWRDADEQRPDEWQAALVAEPRITAAVLDA 418
Cdd:pfam20028  79 PDDRDEPRPLGVEYPVVVRSLERLRRGR--RRPRWRRRWRALLDAGLLRLDRGDCDLGDLDGPPRPAELEARLRDRDVGV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518970782  419 PVGG--PAMAALKEAIAAGIGLAVWDRRGEFLEERREVVSAVFASVptPAQLPLAVHRLRSRAAVDQTL--LGRHIAFFW 494
Cdd:pfam20028 157 PVLCrpPGGEALLAALRAGVPVALWRRRGCDPPAFHDELAELLAGV--LAQLPERVRELRADAGAGDPEahWGRHLALLW 234


                  ...
gi 518970782  495 DDP 497
Cdd:pfam20028 235 DDP 237
VMAP-M0 super family cl45304
vWA-MoxR associated protein middle region 0; Highly variable central region of the vWA-MoxR ...
 149-228 7.52e-08

vWA-MoxR associated protein middle region 0; Highly variable central region of the vWA-MoxR associated protein (VMAP) of the classical ternary system (vWA-MoxR-VMAP) in NTP-dependent conflict systems. VMAP-Ms may be involved in sensing of invasive entities.


The actual alignment was detected with superfamily member pfam19916:

Pssm-ID: 437748  Cd Length: 104  Bit Score: 50.34  E-value: 7.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518970782  149 AELRDRLAQELRIDFPSD-LSPVQLFEYVMEFNVQPDGLPPAVLLMDQAAASVRiPGRRASLSGWAEDWASRAGLLTRLE 227
Cdd:pfam19916  22 RDLYRRAAGPRGPPLPAGcTTAWQVFLHLAGLNAPPDGLPPALAFLEHLAARLG-GELAGELRRWNDRQARRLGLTDELA 100


                  .
gi 518970782  228 E 228
Cdd:pfam19916 101 A 101
EAD2 super family cl45342
Effector-associated domain 2; Effector-associated domains (EADs) are predicted to function as ...
 32-103 9.05e-05

Effector-associated domain 2; Effector-associated domains (EADs) are predicted to function as adaptor domains mediating protein-protein interactions. The EADs show a characteriztic architectural pattern. One copy is always fused, typically to the N- or C-terminus, of a core component of a biological conflict system; examples include VMAP, iSTAND, or GAP1. Further copies of the same EAD are fused to either effector or signal-transducing domains, or additional EADs. EAD pairs are frequently observed together on the genome in conserved gene neighborhoods, but can also be severed from such neighborhoods and located in distant regions, indicating the EAD-EAD coupling approximates the advantages of collinear transcription.


The actual alignment was detected with superfamily member pfam19956:

Pssm-ID: 437788  Cd Length: 82  Bit Score: 41.04  E-value: 9.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518970782   32 TEALCELSCVETPADRVRFADVLGRQLGIAVSLRGGRR-RDDVISLVRAAQSVSDGERALLTVVRILEGAVAA 103
Cdd:pfam19956   1 VDALLAVPALRDPDGRRLLLDLLERELGRALPVPEHPRaRLDLLALVRTCLRYPGGLAALVDAVRLLEPGSRA 73
 
Name Accession Description Interval E-value
VMAP-C pfam20028
vWA-MoxR associated protein C-terminal domain; C-terminal region of the VMAP protein of the ...
 262-497 2.09e-31

vWA-MoxR associated protein C-terminal domain; C-terminal region of the VMAP protein of the classical ternary system (vWA-MoxR-VMAP) in NTP-dependent conflict systems. Mixed alpha+beta domain with no apparent structural similarity to known protein folds. Contains several, nearly universally polar residues, suggesting a conserved interaction interface. Enzymatic function for VMAP-C though possible appears unlikely. Sensing of invasive elements by VMAP-Ms are predicted to trigger a sequence of conformational changes, which is communicated to the switch-component (MoxR) of the system via the more constant VMAP-C.


Pssm-ID: 437860  Cd Length: 237  Bit Score: 121.15  E-value: 2.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518970782  262 VRPWLNTVPGRWAPLPAEP---VTTTLEDLGVAIDEVLRQLARLSPPADGPtstvsaAPPCVEFVLPYDLLNHDVAGLNH 338
Cdd:pfam20028   5 VRVWLYRDGGGWHPRPLVGeddRGLPREELPEALAELLAELEEAFRRLDEP------APLVVEFFLPRELLGLPVDEWRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518970782  339 RSGDSGSLPLGLKYGVHLRSLERMRTDDtsLRRRWRERWSVLRTHGIAVHGWRDADEQRPDEWQAALVAEPRITAAVLDA 418
Cdd:pfam20028  79 PDDRDEPRPLGVEYPVVVRSLERLRRGR--RRPRWRRRWRALLDAGLLRLDRGDCDLGDLDGPPRPAELEARLRDRDVGV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518970782  419 PVGG--PAMAALKEAIAAGIGLAVWDRRGEFLEERREVVSAVFASVptPAQLPLAVHRLRSRAAVDQTL--LGRHIAFFW 494
Cdd:pfam20028 157 PVLCrpPGGEALLAALRAGVPVALWRRRGCDPPAFHDELAELLAGV--LAQLPERVRELRADAGAGDPEahWGRHLALLW 234


                  ...
gi 518970782  495 DDP 497
Cdd:pfam20028 235 DDP 237
VMAP-M0 pfam19916
vWA-MoxR associated protein middle region 0; Highly variable central region of the vWA-MoxR ...
 149-228 7.52e-08

vWA-MoxR associated protein middle region 0; Highly variable central region of the vWA-MoxR associated protein (VMAP) of the classical ternary system (vWA-MoxR-VMAP) in NTP-dependent conflict systems. VMAP-Ms may be involved in sensing of invasive entities.


Pssm-ID: 437748  Cd Length: 104  Bit Score: 50.34  E-value: 7.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518970782  149 AELRDRLAQELRIDFPSD-LSPVQLFEYVMEFNVQPDGLPPAVLLMDQAAASVRiPGRRASLSGWAEDWASRAGLLTRLE 227
Cdd:pfam19916  22 RDLYRRAAGPRGPPLPAGcTTAWQVFLHLAGLNAPPDGLPPALAFLEHLAARLG-GELAGELRRWNDRQARRLGLTDELA 100


                  .
gi 518970782  228 E 228
Cdd:pfam19916 101 A 101
EAD2 pfam19956
Effector-associated domain 2; Effector-associated domains (EADs) are predicted to function as ...
 32-103 9.05e-05

Effector-associated domain 2; Effector-associated domains (EADs) are predicted to function as adaptor domains mediating protein-protein interactions. The EADs show a characteriztic architectural pattern. One copy is always fused, typically to the N- or C-terminus, of a core component of a biological conflict system; examples include VMAP, iSTAND, or GAP1. Further copies of the same EAD are fused to either effector or signal-transducing domains, or additional EADs. EAD pairs are frequently observed together on the genome in conserved gene neighborhoods, but can also be severed from such neighborhoods and located in distant regions, indicating the EAD-EAD coupling approximates the advantages of collinear transcription.


Pssm-ID: 437788  Cd Length: 82  Bit Score: 41.04  E-value: 9.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518970782   32 TEALCELSCVETPADRVRFADVLGRQLGIAVSLRGGRR-RDDVISLVRAAQSVSDGERALLTVVRILEGAVAA 103
Cdd:pfam19956   1 VDALLAVPALRDPDGRRLLLDLLERELGRALPVPEHPRaRLDLLALVRTCLRYPGGLAALVDAVRLLEPGSRA 73
 
Name Accession Description Interval E-value
VMAP-C pfam20028
vWA-MoxR associated protein C-terminal domain; C-terminal region of the VMAP protein of the ...
 262-497 2.09e-31

vWA-MoxR associated protein C-terminal domain; C-terminal region of the VMAP protein of the classical ternary system (vWA-MoxR-VMAP) in NTP-dependent conflict systems. Mixed alpha+beta domain with no apparent structural similarity to known protein folds. Contains several, nearly universally polar residues, suggesting a conserved interaction interface. Enzymatic function for VMAP-C though possible appears unlikely. Sensing of invasive elements by VMAP-Ms are predicted to trigger a sequence of conformational changes, which is communicated to the switch-component (MoxR) of the system via the more constant VMAP-C.


Pssm-ID: 437860  Cd Length: 237  Bit Score: 121.15  E-value: 2.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518970782  262 VRPWLNTVPGRWAPLPAEP---VTTTLEDLGVAIDEVLRQLARLSPPADGPtstvsaAPPCVEFVLPYDLLNHDVAGLNH 338
Cdd:pfam20028   5 VRVWLYRDGGGWHPRPLVGeddRGLPREELPEALAELLAELEEAFRRLDEP------APLVVEFFLPRELLGLPVDEWRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518970782  339 RSGDSGSLPLGLKYGVHLRSLERMRTDDtsLRRRWRERWSVLRTHGIAVHGWRDADEQRPDEWQAALVAEPRITAAVLDA 418
Cdd:pfam20028  79 PDDRDEPRPLGVEYPVVVRSLERLRRGR--RRPRWRRRWRALLDAGLLRLDRGDCDLGDLDGPPRPAELEARLRDRDVGV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518970782  419 PVGG--PAMAALKEAIAAGIGLAVWDRRGEFLEERREVVSAVFASVptPAQLPLAVHRLRSRAAVDQTL--LGRHIAFFW 494
Cdd:pfam20028 157 PVLCrpPGGEALLAALRAGVPVALWRRRGCDPPAFHDELAELLAGV--LAQLPERVRELRADAGAGDPEahWGRHLALLW 234


                  ...
gi 518970782  495 DDP 497
Cdd:pfam20028 235 DDP 237
VMAP-M0 pfam19916
vWA-MoxR associated protein middle region 0; Highly variable central region of the vWA-MoxR ...
 149-228 7.52e-08

vWA-MoxR associated protein middle region 0; Highly variable central region of the vWA-MoxR associated protein (VMAP) of the classical ternary system (vWA-MoxR-VMAP) in NTP-dependent conflict systems. VMAP-Ms may be involved in sensing of invasive entities.


Pssm-ID: 437748  Cd Length: 104  Bit Score: 50.34  E-value: 7.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518970782  149 AELRDRLAQELRIDFPSD-LSPVQLFEYVMEFNVQPDGLPPAVLLMDQAAASVRiPGRRASLSGWAEDWASRAGLLTRLE 227
Cdd:pfam19916  22 RDLYRRAAGPRGPPLPAGcTTAWQVFLHLAGLNAPPDGLPPALAFLEHLAARLG-GELAGELRRWNDRQARRLGLTDELA 100


                  .
gi 518970782  228 E 228
Cdd:pfam19916 101 A 101
EAD2 pfam19956
Effector-associated domain 2; Effector-associated domains (EADs) are predicted to function as ...
 32-103 9.05e-05

Effector-associated domain 2; Effector-associated domains (EADs) are predicted to function as adaptor domains mediating protein-protein interactions. The EADs show a characteriztic architectural pattern. One copy is always fused, typically to the N- or C-terminus, of a core component of a biological conflict system; examples include VMAP, iSTAND, or GAP1. Further copies of the same EAD are fused to either effector or signal-transducing domains, or additional EADs. EAD pairs are frequently observed together on the genome in conserved gene neighborhoods, but can also be severed from such neighborhoods and located in distant regions, indicating the EAD-EAD coupling approximates the advantages of collinear transcription.


Pssm-ID: 437788  Cd Length: 82  Bit Score: 41.04  E-value: 9.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518970782   32 TEALCELSCVETPADRVRFADVLGRQLGIAVSLRGGRR-RDDVISLVRAAQSVSDGERALLTVVRILEGAVAA 103
Cdd:pfam19956   1 VDALLAVPALRDPDGRRLLLDLLERELGRALPVPEHPRaRLDLLALVRTCLRYPGGLAALVDAVRLLEPGSRA 73
 
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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