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Conserved domains on  [gi|2296133024|dbj|BDR26881|]
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hypothetical protein RVBP20_1220 [Pseudomonas phage sp. NK1]

Protein Classification

phiKZ_IP domain-containing protein( domain architecture ID 10577437)

phiKZ_IP domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
phiKZ_IP pfam12699
phiKZ-like phage internal head proteins; Phage internal head proteins (IP) are proteins that ...
164-482 9.33e-88

phiKZ-like phage internal head proteins; Phage internal head proteins (IP) are proteins that are encoded by a bacteriophage and assembled into the mature virion inside the capsid head. The most analogous characterized IP proteins are those of bacteriophage T4, which are known to be proteolytically processed during phage maturation, and then subsequently injected into the host cell during infection. The phiKZ_IP family consists of internal head proteins encoded by phiKZ-like phages. Each phage encodes three to six members of this family. Members of the family reside in the head and are cleaved during phage maturation to separate an N-terminal propeptide from a C-terminal domain. The C-terminal domain remains in the mature capsid. The N-terminal propeptide domain is either mostly or completely removed from the mature capsid. In one case, an unrelated polypeptide is embedded in the propeptide and also remains in the mature capsid. The phiKZ-like IP proteins are not discernibly homologous to the T4 IP proteins, and it is not known if the phiKZ-like IP proteins are injected into the host cell, or have some other function within the head. The alignment and HMM model exclude most of the propeptide region, but include the cleavage sites. The first 100 residues, including the cleavage sites, constitute the most conservative part of the seed alignment.


:

Pssm-ID: 403791  Cd Length: 323  Bit Score: 272.37  E-value: 9.33e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296133024 164 AGDRGITKQSAAFMHVTLESIDKLIGFEK--ISIEDFNATPSSAMRFVNISQEEIKERIESIGKKILALIVHVIEQAKVA 241
Cdd:pfam12699   1 AGGNGISLQAAAFIHSGLESIDKDLGDEKtsTGLESYDATPRVKLESIAVSLEDLKEKLKNAGKKAKELIKKIIETLKDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296133024 242 AQRVLTGIKSVEDKTDELIEKAKSLinkptvsnerVTPDFDMSIKIDNPKMLFIGDEFVLD-DLTNETKVSQFLAKEWPN 320
Cdd:pfam12699  81 AVRITSGIERLDERVDKLMRRAKSL----------KKPDEKKEITIKNPQRLFIDGEFILPyDLDNYPKIVGNIASNYSK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296133024 321 IARSNIDKVVKLIKDYDLEDNELDKFKEAFEFIGE---ANQLDKVKDTSLPGNSKLIFQKDKYAPRL-----GEDKHGDG 392
Cdd:pfam12699 151 QALSLLDKLGKLLNNYELEDKLLDSFAEIFERIGKdrfGANVYLVRSTKLPGNRALYYTGSKVGPTEisfsvIEGAAEDG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296133024 393 PDTITIEPRPPVEVRKTLEVNKEAIRRLGDLFKAEKD---VLEQLKKVAQGIEDMELRRSKAIWKGARDDANEIISLVNG 469
Cdd:pfam12699 231 EEEITVEVPTASEIRARLKALKNLLKRLGDVKGGAKKikaVDDRIKQLADAVRQNERRMGDAAAKVLTEDSIKLVRAVSN 310
                         330
                  ....*....|...
gi 2296133024 470 FITDMSPEYATLI 482
Cdd:pfam12699 311 IITDLAPMVNNLI 323
 
Name Accession Description Interval E-value
phiKZ_IP pfam12699
phiKZ-like phage internal head proteins; Phage internal head proteins (IP) are proteins that ...
164-482 9.33e-88

phiKZ-like phage internal head proteins; Phage internal head proteins (IP) are proteins that are encoded by a bacteriophage and assembled into the mature virion inside the capsid head. The most analogous characterized IP proteins are those of bacteriophage T4, which are known to be proteolytically processed during phage maturation, and then subsequently injected into the host cell during infection. The phiKZ_IP family consists of internal head proteins encoded by phiKZ-like phages. Each phage encodes three to six members of this family. Members of the family reside in the head and are cleaved during phage maturation to separate an N-terminal propeptide from a C-terminal domain. The C-terminal domain remains in the mature capsid. The N-terminal propeptide domain is either mostly or completely removed from the mature capsid. In one case, an unrelated polypeptide is embedded in the propeptide and also remains in the mature capsid. The phiKZ-like IP proteins are not discernibly homologous to the T4 IP proteins, and it is not known if the phiKZ-like IP proteins are injected into the host cell, or have some other function within the head. The alignment and HMM model exclude most of the propeptide region, but include the cleavage sites. The first 100 residues, including the cleavage sites, constitute the most conservative part of the seed alignment.


Pssm-ID: 403791  Cd Length: 323  Bit Score: 272.37  E-value: 9.33e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296133024 164 AGDRGITKQSAAFMHVTLESIDKLIGFEK--ISIEDFNATPSSAMRFVNISQEEIKERIESIGKKILALIVHVIEQAKVA 241
Cdd:pfam12699   1 AGGNGISLQAAAFIHSGLESIDKDLGDEKtsTGLESYDATPRVKLESIAVSLEDLKEKLKNAGKKAKELIKKIIETLKDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296133024 242 AQRVLTGIKSVEDKTDELIEKAKSLinkptvsnerVTPDFDMSIKIDNPKMLFIGDEFVLD-DLTNETKVSQFLAKEWPN 320
Cdd:pfam12699  81 AVRITSGIERLDERVDKLMRRAKSL----------KKPDEKKEITIKNPQRLFIDGEFILPyDLDNYPKIVGNIASNYSK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296133024 321 IARSNIDKVVKLIKDYDLEDNELDKFKEAFEFIGE---ANQLDKVKDTSLPGNSKLIFQKDKYAPRL-----GEDKHGDG 392
Cdd:pfam12699 151 QALSLLDKLGKLLNNYELEDKLLDSFAEIFERIGKdrfGANVYLVRSTKLPGNRALYYTGSKVGPTEisfsvIEGAAEDG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296133024 393 PDTITIEPRPPVEVRKTLEVNKEAIRRLGDLFKAEKD---VLEQLKKVAQGIEDMELRRSKAIWKGARDDANEIISLVNG 469
Cdd:pfam12699 231 EEEITVEVPTASEIRARLKALKNLLKRLGDVKGGAKKikaVDDRIKQLADAVRQNERRMGDAAAKVLTEDSIKLVRAVSN 310
                         330
                  ....*....|...
gi 2296133024 470 FITDMSPEYATLI 482
Cdd:pfam12699 311 IITDLAPMVNNLI 323
 
Name Accession Description Interval E-value
phiKZ_IP pfam12699
phiKZ-like phage internal head proteins; Phage internal head proteins (IP) are proteins that ...
164-482 9.33e-88

phiKZ-like phage internal head proteins; Phage internal head proteins (IP) are proteins that are encoded by a bacteriophage and assembled into the mature virion inside the capsid head. The most analogous characterized IP proteins are those of bacteriophage T4, which are known to be proteolytically processed during phage maturation, and then subsequently injected into the host cell during infection. The phiKZ_IP family consists of internal head proteins encoded by phiKZ-like phages. Each phage encodes three to six members of this family. Members of the family reside in the head and are cleaved during phage maturation to separate an N-terminal propeptide from a C-terminal domain. The C-terminal domain remains in the mature capsid. The N-terminal propeptide domain is either mostly or completely removed from the mature capsid. In one case, an unrelated polypeptide is embedded in the propeptide and also remains in the mature capsid. The phiKZ-like IP proteins are not discernibly homologous to the T4 IP proteins, and it is not known if the phiKZ-like IP proteins are injected into the host cell, or have some other function within the head. The alignment and HMM model exclude most of the propeptide region, but include the cleavage sites. The first 100 residues, including the cleavage sites, constitute the most conservative part of the seed alignment.


Pssm-ID: 403791  Cd Length: 323  Bit Score: 272.37  E-value: 9.33e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296133024 164 AGDRGITKQSAAFMHVTLESIDKLIGFEK--ISIEDFNATPSSAMRFVNISQEEIKERIESIGKKILALIVHVIEQAKVA 241
Cdd:pfam12699   1 AGGNGISLQAAAFIHSGLESIDKDLGDEKtsTGLESYDATPRVKLESIAVSLEDLKEKLKNAGKKAKELIKKIIETLKDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296133024 242 AQRVLTGIKSVEDKTDELIEKAKSLinkptvsnerVTPDFDMSIKIDNPKMLFIGDEFVLD-DLTNETKVSQFLAKEWPN 320
Cdd:pfam12699  81 AVRITSGIERLDERVDKLMRRAKSL----------KKPDEKKEITIKNPQRLFIDGEFILPyDLDNYPKIVGNIASNYSK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296133024 321 IARSNIDKVVKLIKDYDLEDNELDKFKEAFEFIGE---ANQLDKVKDTSLPGNSKLIFQKDKYAPRL-----GEDKHGDG 392
Cdd:pfam12699 151 QALSLLDKLGKLLNNYELEDKLLDSFAEIFERIGKdrfGANVYLVRSTKLPGNRALYYTGSKVGPTEisfsvIEGAAEDG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296133024 393 PDTITIEPRPPVEVRKTLEVNKEAIRRLGDLFKAEKD---VLEQLKKVAQGIEDMELRRSKAIWKGARDDANEIISLVNG 469
Cdd:pfam12699 231 EEEITVEVPTASEIRARLKALKNLLKRLGDVKGGAKKikaVDDRIKQLADAVRQNERRMGDAAAKVLTEDSIKLVRAVSN 310
                         330
                  ....*....|...
gi 2296133024 470 FITDMSPEYATLI 482
Cdd:pfam12699 311 IITDLAPMVNNLI 323
 
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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