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Conserved domains on  [gi|581787918|gb|EVR91125|]
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SPP1 family phage portal protein, partial [Staphylococcus aureus M1472]

Protein Classification

phage portal protein( domain architecture ID 10524044)

phage portal protein belonging to the SPP1-like portal protein family forms the portal vertex of the capsid; the portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection

Gene Ontology:  GO:0019028|GO:0099001
PubMed:  17363899
TCDB:  1.W.7.3.7

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Phage_prot_Gp6 pfam05133
Phage portal protein, SPP1 Gp6-like; This bacteriophage protein forms a gateway that enables ...
6-441 3.97e-122

Phage portal protein, SPP1 Gp6-like; This bacteriophage protein forms a gateway that enables DNA passage during packaging and ejection of the phage genome. It also forms the junction between the phage head (capsid) and the tail proteins. During SPP1 morphogenesis, the portal protein, Gp6, participates in the procapsid assembly reaction. In the mature SPP1 virion, Gp6 exists as a dodecamer, while recombinant SPP1 Gp6 has been shown to form 13-subunit assemblies. This protein is common to Siphoviridae (phages with long non-contractile tails) and Myoviridae (phages with contractile tails). It is also found in a number of bacterial species. This family also includes the old Pfam family Phage_min_cap (PF:PF05126). RC Paper describing PDB structure 2jes


:

Pssm-ID: 398687  Cd Length: 416  Bit Score: 362.42  E-value: 3.97e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918    6 YIEHHMDYQRPRLKVLSDYYEGKTKnLVELTRRKEEYMADNRVAHDYASYISDFINGYFLGNPIQYQDDDKDVLEAIEAF 85
Cdd:pfam05133   1 KIIDHHEEEKPRIQKLYRYYKGKHD-ILNRTVKNPPNKANNRIVLNFAKYIVDQKAGYLFGNPITYIVDDDDDNEEILDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918   86 NDLNDVESHNRSLGLDLSIYGKAYELMIRNQDDETRLYKSDAMSTFIIYDNTVERNSIAGVRYLrtkpiDKTDEDEVFTV 165
Cdd:pfam05133  80 LLNNNFDKNDKELLKDASIYGRAYELVYVDEEGEFKIKVVDPEEAFPIYDDSIEREPLAFVRYY-----GDKDEDTITYV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  166 DLFTSHGVYRYLTSRTNGlkLTPRENGFESHSFERMPITEFSNNERRKGDYEKVITLIDLYDNAESDTANYMSDLNDAML 245
Cdd:pfam05133 155 EVYTDNEVYKFTKDGGGG--LNEEYISDEPHGFGRVPLIEFYNNNERLGDLENVKTLIDAYNKTLSDFANEIEDFQDAIL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  246 LIKGNLnLDPVEVRKQKEANVLFLEPtvyenrdtgIETEGSVDGGYIYKQYDVQGTEAYKDRLNSDIHMFTNTPNMKDDN 325
Cdd:pfam05133 233 VLTGMT-LDDEDLAKLKDYGAIKVEP---------GGDGDNGDVKFLTKPIPDEARENLLDRLEKDIHQFSMVPNISDEN 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  326 FSGTQSGEAMKYKLFGLEQRTKTKEGLFTKGLRRRAKLLETILKNTRSIDANKDfnTVRYVYNRNLPKSLIEELKAYIDS 405
Cdd:pfam05133 303 FSGNASGVALKYKYSGLEQKANLKEREFKKALKRRIRLIFEILNILDLGSGDDV--DIKVTFTRNIPKNDLETADIAGKL 380
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 581787918  406 GGKISQTTLMSLFSFFQDPELEVKKIEEDEKESIKK 441
Cdd:pfam05133 381 AGIISKKTLLSKLPFVDDPEEEIERIKEEKEEAQEK 416
 
Name Accession Description Interval E-value
Phage_prot_Gp6 pfam05133
Phage portal protein, SPP1 Gp6-like; This bacteriophage protein forms a gateway that enables ...
6-441 3.97e-122

Phage portal protein, SPP1 Gp6-like; This bacteriophage protein forms a gateway that enables DNA passage during packaging and ejection of the phage genome. It also forms the junction between the phage head (capsid) and the tail proteins. During SPP1 morphogenesis, the portal protein, Gp6, participates in the procapsid assembly reaction. In the mature SPP1 virion, Gp6 exists as a dodecamer, while recombinant SPP1 Gp6 has been shown to form 13-subunit assemblies. This protein is common to Siphoviridae (phages with long non-contractile tails) and Myoviridae (phages with contractile tails). It is also found in a number of bacterial species. This family also includes the old Pfam family Phage_min_cap (PF:PF05126). RC Paper describing PDB structure 2jes


Pssm-ID: 398687  Cd Length: 416  Bit Score: 362.42  E-value: 3.97e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918    6 YIEHHMDYQRPRLKVLSDYYEGKTKnLVELTRRKEEYMADNRVAHDYASYISDFINGYFLGNPIQYQDDDKDVLEAIEAF 85
Cdd:pfam05133   1 KIIDHHEEEKPRIQKLYRYYKGKHD-ILNRTVKNPPNKANNRIVLNFAKYIVDQKAGYLFGNPITYIVDDDDDNEEILDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918   86 NDLNDVESHNRSLGLDLSIYGKAYELMIRNQDDETRLYKSDAMSTFIIYDNTVERNSIAGVRYLrtkpiDKTDEDEVFTV 165
Cdd:pfam05133  80 LLNNNFDKNDKELLKDASIYGRAYELVYVDEEGEFKIKVVDPEEAFPIYDDSIEREPLAFVRYY-----GDKDEDTITYV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  166 DLFTSHGVYRYLTSRTNGlkLTPRENGFESHSFERMPITEFSNNERRKGDYEKVITLIDLYDNAESDTANYMSDLNDAML 245
Cdd:pfam05133 155 EVYTDNEVYKFTKDGGGG--LNEEYISDEPHGFGRVPLIEFYNNNERLGDLENVKTLIDAYNKTLSDFANEIEDFQDAIL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  246 LIKGNLnLDPVEVRKQKEANVLFLEPtvyenrdtgIETEGSVDGGYIYKQYDVQGTEAYKDRLNSDIHMFTNTPNMKDDN 325
Cdd:pfam05133 233 VLTGMT-LDDEDLAKLKDYGAIKVEP---------GGDGDNGDVKFLTKPIPDEARENLLDRLEKDIHQFSMVPNISDEN 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  326 FSGTQSGEAMKYKLFGLEQRTKTKEGLFTKGLRRRAKLLETILKNTRSIDANKDfnTVRYVYNRNLPKSLIEELKAYIDS 405
Cdd:pfam05133 303 FSGNASGVALKYKYSGLEQKANLKEREFKKALKRRIRLIFEILNILDLGSGDDV--DIKVTFTRNIPKNDLETADIAGKL 380
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 581787918  406 GGKISQTTLMSLFSFFQDPELEVKKIEEDEKESIKK 441
Cdd:pfam05133 381 AGIISKKTLLSKLPFVDDPEEEIERIKEEKEEAQEK 416
portal_SPP1 TIGR01538
phage portal protein, SPP1 family; This model represents one of several distantly related ...
3-424 7.09e-94

phage portal protein, SPP1 family; This model represents one of several distantly related families of phage portal protein. This protein forms a hole, or portal, that enables DNA passage during packaging and ejection. It also forms the junction between the phage head (capsid) and the tail proteins. It functions as a dodecamer of a single polypeptide of average mol. wt. of 40-90 KDa. [Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 273678  Cd Length: 412  Bit Score: 290.21  E-value: 7.09e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918    3 VSKYIEHHMDYQRPRLKVLSDYYEGKTKnlVELTRRKEEYMADNRVAHDYASYISDFINGYFLGNPIQYQDDDKDVLEAI 82
Cdd:TIGR01538   8 IQKLIEEHNPEPVRRYECLNDIEKGRRT--IYDAALKDDTKTDNRTSHNWHKYIVDQKTGYLVGNPVKFTSDDKTLLDYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918   83 EAFNDLNDVESHNRSLGLDLSIYGKAYELMIRNQDDETRLYKSDAMSTFIIYDNTVERNSIAGVRYLRTKPIDKtdeDEV 162
Cdd:TIGR01538  86 NELANQNDFHDILNELVKDLSNKGRAYELLYVDEDDETDVVIFDPEEMFVVYDDNVEQDPLFAVRYYSKKDLMG---ETT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  163 FTVDLFTSHGVYRYLTSRTNGLKLTPRENGFESHSFERMPITEFSNNERRKGDYEKVITLIDLYDNAESDTANYMSDLND 242
Cdd:TIGR01538 163 QKAELYTDTHIYKYEKIDDVYQMDYSEGEYNPRPGFGRVPIIEFKNNEERMSDFEFYISLIDAYDSAQSDTANDFSDFSD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  243 AMLLIKGNlNLDPVEVRKQkEANVLFLEPtvyenrdtgIETEGSVDGGYIYKQYDVQGTEAYKDRLNSDIHMFTNTPNMK 322
Cdd:TIGR01538 243 QQLVYFGK-NYDGEDPKEF-RANLRYHSV---------IRESGDVDVKTLRKEIDVDQTEKLLERIQDDIHKSTQVPDMS 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  323 DDNFSGTQSGEAMKYKLFGLEQRTKTKEGLFTKGLRRRAKLLETILKNTRSIDANkDFNTVRYVYNRNLPKSLIEELKAY 402
Cdd:TIGR01538 312 DEKFGGGASGEALKFKLFGLDNLANMAQRKFRAGLRRRYKLFAEYSRNTGKGDFN-DDKELKITFTRNRPKNLSEIVESL 390
                         410       420
                  ....*....|....*....|..
gi 581787918  403 IDSGGKISQTTLMSLFSFFQDP 424
Cdd:TIGR01538 391 KQLGGIMSQETAVARNPFVQDP 412
 
Name Accession Description Interval E-value
Phage_prot_Gp6 pfam05133
Phage portal protein, SPP1 Gp6-like; This bacteriophage protein forms a gateway that enables ...
6-441 3.97e-122

Phage portal protein, SPP1 Gp6-like; This bacteriophage protein forms a gateway that enables DNA passage during packaging and ejection of the phage genome. It also forms the junction between the phage head (capsid) and the tail proteins. During SPP1 morphogenesis, the portal protein, Gp6, participates in the procapsid assembly reaction. In the mature SPP1 virion, Gp6 exists as a dodecamer, while recombinant SPP1 Gp6 has been shown to form 13-subunit assemblies. This protein is common to Siphoviridae (phages with long non-contractile tails) and Myoviridae (phages with contractile tails). It is also found in a number of bacterial species. This family also includes the old Pfam family Phage_min_cap (PF:PF05126). RC Paper describing PDB structure 2jes


Pssm-ID: 398687  Cd Length: 416  Bit Score: 362.42  E-value: 3.97e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918    6 YIEHHMDYQRPRLKVLSDYYEGKTKnLVELTRRKEEYMADNRVAHDYASYISDFINGYFLGNPIQYQDDDKDVLEAIEAF 85
Cdd:pfam05133   1 KIIDHHEEEKPRIQKLYRYYKGKHD-ILNRTVKNPPNKANNRIVLNFAKYIVDQKAGYLFGNPITYIVDDDDDNEEILDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918   86 NDLNDVESHNRSLGLDLSIYGKAYELMIRNQDDETRLYKSDAMSTFIIYDNTVERNSIAGVRYLrtkpiDKTDEDEVFTV 165
Cdd:pfam05133  80 LLNNNFDKNDKELLKDASIYGRAYELVYVDEEGEFKIKVVDPEEAFPIYDDSIEREPLAFVRYY-----GDKDEDTITYV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  166 DLFTSHGVYRYLTSRTNGlkLTPRENGFESHSFERMPITEFSNNERRKGDYEKVITLIDLYDNAESDTANYMSDLNDAML 245
Cdd:pfam05133 155 EVYTDNEVYKFTKDGGGG--LNEEYISDEPHGFGRVPLIEFYNNNERLGDLENVKTLIDAYNKTLSDFANEIEDFQDAIL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  246 LIKGNLnLDPVEVRKQKEANVLFLEPtvyenrdtgIETEGSVDGGYIYKQYDVQGTEAYKDRLNSDIHMFTNTPNMKDDN 325
Cdd:pfam05133 233 VLTGMT-LDDEDLAKLKDYGAIKVEP---------GGDGDNGDVKFLTKPIPDEARENLLDRLEKDIHQFSMVPNISDEN 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  326 FSGTQSGEAMKYKLFGLEQRTKTKEGLFTKGLRRRAKLLETILKNTRSIDANKDfnTVRYVYNRNLPKSLIEELKAYIDS 405
Cdd:pfam05133 303 FSGNASGVALKYKYSGLEQKANLKEREFKKALKRRIRLIFEILNILDLGSGDDV--DIKVTFTRNIPKNDLETADIAGKL 380
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 581787918  406 GGKISQTTLMSLFSFFQDPELEVKKIEEDEKESIKK 441
Cdd:pfam05133 381 AGIISKKTLLSKLPFVDDPEEEIERIKEEKEEAQEK 416
portal_SPP1 TIGR01538
phage portal protein, SPP1 family; This model represents one of several distantly related ...
3-424 7.09e-94

phage portal protein, SPP1 family; This model represents one of several distantly related families of phage portal protein. This protein forms a hole, or portal, that enables DNA passage during packaging and ejection. It also forms the junction between the phage head (capsid) and the tail proteins. It functions as a dodecamer of a single polypeptide of average mol. wt. of 40-90 KDa. [Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 273678  Cd Length: 412  Bit Score: 290.21  E-value: 7.09e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918    3 VSKYIEHHMDYQRPRLKVLSDYYEGKTKnlVELTRRKEEYMADNRVAHDYASYISDFINGYFLGNPIQYQDDDKDVLEAI 82
Cdd:TIGR01538   8 IQKLIEEHNPEPVRRYECLNDIEKGRRT--IYDAALKDDTKTDNRTSHNWHKYIVDQKTGYLVGNPVKFTSDDKTLLDYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918   83 EAFNDLNDVESHNRSLGLDLSIYGKAYELMIRNQDDETRLYKSDAMSTFIIYDNTVERNSIAGVRYLRTKPIDKtdeDEV 162
Cdd:TIGR01538  86 NELANQNDFHDILNELVKDLSNKGRAYELLYVDEDDETDVVIFDPEEMFVVYDDNVEQDPLFAVRYYSKKDLMG---ETT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  163 FTVDLFTSHGVYRYLTSRTNGLKLTPRENGFESHSFERMPITEFSNNERRKGDYEKVITLIDLYDNAESDTANYMSDLND 242
Cdd:TIGR01538 163 QKAELYTDTHIYKYEKIDDVYQMDYSEGEYNPRPGFGRVPIIEFKNNEERMSDFEFYISLIDAYDSAQSDTANDFSDFSD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  243 AMLLIKGNlNLDPVEVRKQkEANVLFLEPtvyenrdtgIETEGSVDGGYIYKQYDVQGTEAYKDRLNSDIHMFTNTPNMK 322
Cdd:TIGR01538 243 QQLVYFGK-NYDGEDPKEF-RANLRYHSV---------IRESGDVDVKTLRKEIDVDQTEKLLERIQDDIHKSTQVPDMS 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787918  323 DDNFSGTQSGEAMKYKLFGLEQRTKTKEGLFTKGLRRRAKLLETILKNTRSIDANkDFNTVRYVYNRNLPKSLIEELKAY 402
Cdd:TIGR01538 312 DEKFGGGASGEALKFKLFGLDNLANMAQRKFRAGLRRRYKLFAEYSRNTGKGDFN-DDKELKITFTRNRPKNLSEIVESL 390
                         410       420
                  ....*....|....*....|..
gi 581787918  403 IDSGGKISQTTLMSLFSFFQDP 424
Cdd:TIGR01538 391 KQLGGIMSQETAVARNPFVQDP 412
 
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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