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Conserved domains on  [gi|492267852|ref|WP_005794425|]
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MULTISPECIES: phage portal protein [Bacteroidaceae]

Protein Classification

phage portal protein( domain architecture ID 140520)

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; may be partial

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 super family cl19531
Phage portal protein, SPP1 Gp6-like; This bacteriophage protein forms a gateway that enables ...
67-478 6.79e-27

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


The actual alignment was detected with superfamily member pfam05133:

Pssm-ID: 418597  Cd Length: 416  Bit Score: 112.42  E-value: 6.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852   67 YPDRLKYDEEKKRFFREKVfraSFPFQMIITIQQLVHLCGNDIhheLTDTKVDESSREIFLEFQKGWLDKNMEiafyEYA 146
Cdd:pfam05133  24 HDILNRTVKNPPNKANNRI---VLNFAKYIVDQKAGYLFGNPI---TYIVDDDDDNEEILDVLLNNNFDKNDK----ELL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852  147 KSVKITGDAAIVFYMNEGKVFtkNLSYFDGDTLYPHYD-SITGQMTLFARRYSDYDEEGkelISWVEVWDNKKMYRYRQD 225
Cdd:pfam05133  94 KDASIYGRAYELVYVDEEGEF--KIKVVDPEEAFPIYDdSIEREPLAFVRYYGDKDEDT---ITYVEVYTDNEVYKFTKD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852  226 KRGIagainkvkqyfgiEGYTLVEEHDHGFTECPVVYYRDKHGAC--WSFSQDNIDKYELAISHLCQNNMAYAFPIMLLK 303
Cdd:pfam05133 169 GGGG-------------LNEEYISDEPHGFGRVPLIEFYNNNERLgdLENVKTLIDAYNKTLSDFANEIEDFQDAILVLT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852  304 G-----EDVEIQGDmYGAVKAITMGKDDDAG--FMNRPEASQSFELQINTLLKMIFMGSFVV-MPPEVKSGDLPGVAIKL 375
Cdd:pfam05133 236 GmtlddEDLAKLKD-YGAIKVEPGGDGDNGDvkFLTKPIPDEARENLLDRLEKDIHQFSMVPnISDENFSGNASGVALKY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852  376 IYSPSLEKAMIDCKEFDESIDKMKRLFLHGYGTEKGQLTKFLNLKI-FSWAVPyvhQNAAELVSNLVQLvgAGILSKETG 454
Cdd:pfam05133 315 KYSGLEQKANLKEREFKKALKRRIRLIFEILNILDLGSGDDVDIKVtFTRNIP---KNDLETADIAGKL--AGIISKKTL 389
                         410       420
                  ....*....|....*....|....*.
gi 492267852  455 SEESGY--GKNNEWDRIMREYKEQQQ 478
Cdd:pfam05133 390 LSKLPFvdDPEEEIERIKEEKEEAQE 415
 
Name Accession Description Interval E-value
Phage_prot_Gp6 pfam05133
Phage portal protein, SPP1 Gp6-like; This bacteriophage protein forms a gateway that enables ...
67-478 6.79e-27

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: 112.42  E-value: 6.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852   67 YPDRLKYDEEKKRFFREKVfraSFPFQMIITIQQLVHLCGNDIhheLTDTKVDESSREIFLEFQKGWLDKNMEiafyEYA 146
Cdd:pfam05133  24 HDILNRTVKNPPNKANNRI---VLNFAKYIVDQKAGYLFGNPI---TYIVDDDDDNEEILDVLLNNNFDKNDK----ELL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852  147 KSVKITGDAAIVFYMNEGKVFtkNLSYFDGDTLYPHYD-SITGQMTLFARRYSDYDEEGkelISWVEVWDNKKMYRYRQD 225
Cdd:pfam05133  94 KDASIYGRAYELVYVDEEGEF--KIKVVDPEEAFPIYDdSIEREPLAFVRYYGDKDEDT---ITYVEVYTDNEVYKFTKD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852  226 KRGIagainkvkqyfgiEGYTLVEEHDHGFTECPVVYYRDKHGAC--WSFSQDNIDKYELAISHLCQNNMAYAFPIMLLK 303
Cdd:pfam05133 169 GGGG-------------LNEEYISDEPHGFGRVPLIEFYNNNERLgdLENVKTLIDAYNKTLSDFANEIEDFQDAILVLT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852  304 G-----EDVEIQGDmYGAVKAITMGKDDDAG--FMNRPEASQSFELQINTLLKMIFMGSFVV-MPPEVKSGDLPGVAIKL 375
Cdd:pfam05133 236 GmtlddEDLAKLKD-YGAIKVEPGGDGDNGDvkFLTKPIPDEARENLLDRLEKDIHQFSMVPnISDENFSGNASGVALKY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852  376 IYSPSLEKAMIDCKEFDESIDKMKRLFLHGYGTEKGQLTKFLNLKI-FSWAVPyvhQNAAELVSNLVQLvgAGILSKETG 454
Cdd:pfam05133 315 KYSGLEQKANLKEREFKKALKRRIRLIFEILNILDLGSGDDVDIKVtFTRNIP---KNDLETADIAGKL--AGIISKKTL 389
                         410       420
                  ....*....|....*....|....*.
gi 492267852  455 SEESGY--GKNNEWDRIMREYKEQQQ 478
Cdd:pfam05133 390 LSKLPFvdDPEEEIERIKEEKEEAQE 415
 
Name Accession Description Interval E-value
Phage_prot_Gp6 pfam05133
Phage portal protein, SPP1 Gp6-like; This bacteriophage protein forms a gateway that enables ...
67-478 6.79e-27

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: 112.42  E-value: 6.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852   67 YPDRLKYDEEKKRFFREKVfraSFPFQMIITIQQLVHLCGNDIhheLTDTKVDESSREIFLEFQKGWLDKNMEiafyEYA 146
Cdd:pfam05133  24 HDILNRTVKNPPNKANNRI---VLNFAKYIVDQKAGYLFGNPI---TYIVDDDDDNEEILDVLLNNNFDKNDK----ELL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852  147 KSVKITGDAAIVFYMNEGKVFtkNLSYFDGDTLYPHYD-SITGQMTLFARRYSDYDEEGkelISWVEVWDNKKMYRYRQD 225
Cdd:pfam05133  94 KDASIYGRAYELVYVDEEGEF--KIKVVDPEEAFPIYDdSIEREPLAFVRYYGDKDEDT---ITYVEVYTDNEVYKFTKD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852  226 KRGIagainkvkqyfgiEGYTLVEEHDHGFTECPVVYYRDKHGAC--WSFSQDNIDKYELAISHLCQNNMAYAFPIMLLK 303
Cdd:pfam05133 169 GGGG-------------LNEEYISDEPHGFGRVPLIEFYNNNERLgdLENVKTLIDAYNKTLSDFANEIEDFQDAILVLT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852  304 G-----EDVEIQGDmYGAVKAITMGKDDDAG--FMNRPEASQSFELQINTLLKMIFMGSFVV-MPPEVKSGDLPGVAIKL 375
Cdd:pfam05133 236 GmtlddEDLAKLKD-YGAIKVEPGGDGDNGDvkFLTKPIPDEARENLLDRLEKDIHQFSMVPnISDENFSGNASGVALKY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492267852  376 IYSPSLEKAMIDCKEFDESIDKMKRLFLHGYGTEKGQLTKFLNLKI-FSWAVPyvhQNAAELVSNLVQLvgAGILSKETG 454
Cdd:pfam05133 315 KYSGLEQKANLKEREFKKALKRRIRLIFEILNILDLGSGDDVDIKVtFTRNIP---KNDLETADIAGKL--AGIISKKTL 389
                         410       420
                  ....*....|....*....|....*.
gi 492267852  455 SEESGY--GKNNEWDRIMREYKEQQQ 478
Cdd:pfam05133 390 LSKLPFvdDPEEEIERIKEEKEEAQE 415
 
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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