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Conserved domains on  [gi|515952392|ref|WP_017382975|]
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MULTISPECIES: GPO family capsid scaffolding protein [Enterobacter]

Protein Classification

GPO family capsid scaffolding protein( domain architecture ID 10531835)

GPO family capsid scaffolding protein such as Escherichia virus P2 capsid assembly scaffolding protein GpO that is involved in the icosahedric procapsid assembly and functions as a scaffolding protein and protease

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Phage_GPO pfam05929
Phage capsid scaffolding protein (GPO) serine peptidase; This family consists of several ...
6-284 6.88e-136

Phage capsid scaffolding protein (GPO) serine peptidase; This family consists of several bacteriophage capsid scaffolding proteins (GPO) and some related bacterial sequences. GPO is thought to function in both the assembly of proheads and the cleavage of GPN. The family is found to function as a serine peptidase, with a conserved Asp, His and Ser catalytic triad, as in subtilisin, and as represented in MEROPS:S73. The family includes SwissProt:P25478 from Enterobacteria phage P2 which cleaves itself and then becomes the scaffold protein upon which the bacteriophage prohead is built - a mechanism quite common amongst phages.


:

Pssm-ID: 428677  Cd Length: 271  Bit Score: 384.76  E-value: 6.88e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392    6 SKWFRIGVEGDTCDGRVISADDIQEMADTFDPRVYGCRINLEHIKSLIPDSPFKRYGDVTALKAEIIsDDSALNGKKALF 85
Cdd:pfam05929   1 SKFFRVAVEGATTDGREIQREWLQQMAANYDPAVYGARINLEHIRGWLPDSPFRAYGDVTALKAEEI-EDGPLKGKLALY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392   86 AKIAPLDELVSMVRAGQKVYTSMEIRPNFSNSGKCYLIGLAVTDDPASLGTEYLEFCSRATQNPLAGKKDQPGDLFSVAS 165
Cdd:pfam05929  80 AQIDPTDDLVALNKARQKIYTSIEIHPDFADTGKAYLVGLAVTDTPASLGTEMLQFSARAAANPLAGRKQSPENLFTAAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392  166 LAELEFEDVPDTMLNSLTDKVKAIFSRKQASDDARLADVHEAVTTVTELVQTNLTATDQRVtELETELAQLKQDVtskaE 245
Cdd:pfam05929 160 ETVLEFEEEPEDPAKSLFERIKAIFGKKRQSDDARFADVHEAVELVAESVAELLEQFTQLL-ALETELAALKKEV----A 234
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 515952392  246 ESAQAFNDLKNSLDNTESQrQPRRELSKGGTGdELLTNC 284
Cdd:pfam05929 235 TLTADLSALKTKLSSTDAN-YTQRPPATGGNG-SLLTDC 271
 
Name Accession Description Interval E-value
Phage_GPO pfam05929
Phage capsid scaffolding protein (GPO) serine peptidase; This family consists of several ...
6-284 6.88e-136

Phage capsid scaffolding protein (GPO) serine peptidase; This family consists of several bacteriophage capsid scaffolding proteins (GPO) and some related bacterial sequences. GPO is thought to function in both the assembly of proheads and the cleavage of GPN. The family is found to function as a serine peptidase, with a conserved Asp, His and Ser catalytic triad, as in subtilisin, and as represented in MEROPS:S73. The family includes SwissProt:P25478 from Enterobacteria phage P2 which cleaves itself and then becomes the scaffold protein upon which the bacteriophage prohead is built - a mechanism quite common amongst phages.


Pssm-ID: 428677  Cd Length: 271  Bit Score: 384.76  E-value: 6.88e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392    6 SKWFRIGVEGDTCDGRVISADDIQEMADTFDPRVYGCRINLEHIKSLIPDSPFKRYGDVTALKAEIIsDDSALNGKKALF 85
Cdd:pfam05929   1 SKFFRVAVEGATTDGREIQREWLQQMAANYDPAVYGARINLEHIRGWLPDSPFRAYGDVTALKAEEI-EDGPLKGKLALY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392   86 AKIAPLDELVSMVRAGQKVYTSMEIRPNFSNSGKCYLIGLAVTDDPASLGTEYLEFCSRATQNPLAGKKDQPGDLFSVAS 165
Cdd:pfam05929  80 AQIDPTDDLVALNKARQKIYTSIEIHPDFADTGKAYLVGLAVTDTPASLGTEMLQFSARAAANPLAGRKQSPENLFTAAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392  166 LAELEFEDVPDTMLNSLTDKVKAIFSRKQASDDARLADVHEAVTTVTELVQTNLTATDQRVtELETELAQLKQDVtskaE 245
Cdd:pfam05929 160 ETVLEFEEEPEDPAKSLFERIKAIFGKKRQSDDARFADVHEAVELVAESVAELLEQFTQLL-ALETELAALKKEV----A 234
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 515952392  246 ESAQAFNDLKNSLDNTESQrQPRRELSKGGTGdELLTNC 284
Cdd:pfam05929 235 TLTADLSALKTKLSSTDAN-YTQRPPATGGNG-SLLTDC 271
O PHA02529
capsid-scaffolding protein; Provisional
2-279 1.92e-122

capsid-scaffolding protein; Provisional


Pssm-ID: 222855  Cd Length: 278  Bit Score: 350.97  E-value: 1.92e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392   2 AKKVSKWFRIGVEGDTCDGRVISADDIQEMADTFDPRVYGCRINLEHIKSLIPDSPFKRYGDVTALKAEIISDdsalnGK 81
Cdd:PHA02529   1 MKKKTKFFRIATEGATVDGREISAEWLTQMAETYDPEVYGARINLEHIRWAWPDGEFKNYGDVIELKAEEIED-----GK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392  82 KALFAKIAPLDELVSMVRAGQKVYTSMEIRPNFSNSGKCYLIGLAVTDDPASLGTEYLEFCSRATQNPLAGKKDQPGDLF 161
Cdd:PHA02529  76 LALFAQIAPTDELVELNKAGQKLFTSIEIQPNFADTGKAYLVGLAVTDDPASLGTEYLKFSAKAKHNPLARRKQNPENLF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392 162 SVASLAELEFEdvPDTMLNSLTDKVKAIFSRKQASD---DARLADVHEAVTTVTELVQtnltATDQRVTELETELAQLKQ 238
Cdd:PHA02529 156 SVACEAKEEFE--PEAELAALFEKVKKLFSRKKEDDamtDEQFADVHEAVEGVAEKID----HTSAQVATTETAEPPQEG 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 515952392 239 DVTSKAEESAQAFNDLKNSLDNTESQ-----RQPRRELSKGGTGDE 279
Cdd:PHA02529 230 KDTEENGETAEQFSALKETLDKLASKfneevPAPQRPPATGGGGAY 275
 
Name Accession Description Interval E-value
Phage_GPO pfam05929
Phage capsid scaffolding protein (GPO) serine peptidase; This family consists of several ...
6-284 6.88e-136

Phage capsid scaffolding protein (GPO) serine peptidase; This family consists of several bacteriophage capsid scaffolding proteins (GPO) and some related bacterial sequences. GPO is thought to function in both the assembly of proheads and the cleavage of GPN. The family is found to function as a serine peptidase, with a conserved Asp, His and Ser catalytic triad, as in subtilisin, and as represented in MEROPS:S73. The family includes SwissProt:P25478 from Enterobacteria phage P2 which cleaves itself and then becomes the scaffold protein upon which the bacteriophage prohead is built - a mechanism quite common amongst phages.


Pssm-ID: 428677  Cd Length: 271  Bit Score: 384.76  E-value: 6.88e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392    6 SKWFRIGVEGDTCDGRVISADDIQEMADTFDPRVYGCRINLEHIKSLIPDSPFKRYGDVTALKAEIIsDDSALNGKKALF 85
Cdd:pfam05929   1 SKFFRVAVEGATTDGREIQREWLQQMAANYDPAVYGARINLEHIRGWLPDSPFRAYGDVTALKAEEI-EDGPLKGKLALY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392   86 AKIAPLDELVSMVRAGQKVYTSMEIRPNFSNSGKCYLIGLAVTDDPASLGTEYLEFCSRATQNPLAGKKDQPGDLFSVAS 165
Cdd:pfam05929  80 AQIDPTDDLVALNKARQKIYTSIEIHPDFADTGKAYLVGLAVTDTPASLGTEMLQFSARAAANPLAGRKQSPENLFTAAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392  166 LAELEFEDVPDTMLNSLTDKVKAIFSRKQASDDARLADVHEAVTTVTELVQTNLTATDQRVtELETELAQLKQDVtskaE 245
Cdd:pfam05929 160 ETVLEFEEEPEDPAKSLFERIKAIFGKKRQSDDARFADVHEAVELVAESVAELLEQFTQLL-ALETELAALKKEV----A 234
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 515952392  246 ESAQAFNDLKNSLDNTESQrQPRRELSKGGTGdELLTNC 284
Cdd:pfam05929 235 TLTADLSALKTKLSSTDAN-YTQRPPATGGNG-SLLTDC 271
O PHA02529
capsid-scaffolding protein; Provisional
2-279 1.92e-122

capsid-scaffolding protein; Provisional


Pssm-ID: 222855  Cd Length: 278  Bit Score: 350.97  E-value: 1.92e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392   2 AKKVSKWFRIGVEGDTCDGRVISADDIQEMADTFDPRVYGCRINLEHIKSLIPDSPFKRYGDVTALKAEIISDdsalnGK 81
Cdd:PHA02529   1 MKKKTKFFRIATEGATVDGREISAEWLTQMAETYDPEVYGARINLEHIRWAWPDGEFKNYGDVIELKAEEIED-----GK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392  82 KALFAKIAPLDELVSMVRAGQKVYTSMEIRPNFSNSGKCYLIGLAVTDDPASLGTEYLEFCSRATQNPLAGKKDQPGDLF 161
Cdd:PHA02529  76 LALFAQIAPTDELVELNKAGQKLFTSIEIQPNFADTGKAYLVGLAVTDDPASLGTEYLKFSAKAKHNPLARRKQNPENLF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952392 162 SVASLAELEFEdvPDTMLNSLTDKVKAIFSRKQASD---DARLADVHEAVTTVTELVQtnltATDQRVTELETELAQLKQ 238
Cdd:PHA02529 156 SVACEAKEEFE--PEAELAALFEKVKKLFSRKKEDDamtDEQFADVHEAVEGVAEKID----HTSAQVATTETAEPPQEG 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 515952392 239 DVTSKAEESAQAFNDLKNSLDNTESQ-----RQPRRELSKGGTGDE 279
Cdd:PHA02529 230 KDTEENGETAEQFSALKETLDKLASKfneevPAPQRPPATGGGGAY 275
 
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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