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Conserved domains on  [gi|446625043|ref|WP_000702389|]
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MULTISPECIES: phage head closure protein [Enterobacteriaceae]

Protein Classification

head-tail adaptor protein( domain architecture ID 10009478)

phage head-tail adaptor is a phage head-tail joining protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5614 COG5614
Phage head-tail adaptor [Mobilome: prophages, transposons];
16-117 1.87e-22

Phage head-tail adaptor [Mobilome: prophages, transposons];


:

Pssm-ID: 444345  Cd Length: 107  Bit Score: 84.99  E-value: 1.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446625043  16 DPGELNKRVLIRLRVDMPADNFGVEPQYPVTFRTWAKVIQTSATTWQETAQTGDAITHYITIRYRRGITADYEVVCGDSV 95
Cdd:COG5614    2 SAGRLRHRITLQRPTETPDGAGGPIETWEDLATVWAEVEPLSGREYFAAGAEQAEVTHRITIRYRPGITPDMRIVYGGRI 81

                         90       100
                 ....*....|....*....|..
gi 446625043  96 YRVKRQRDLNGARRFLLLECTE 117
Cdd:COG5614   82 FNIRAVIDPDGRGRYLEILCEE 103
 
Name Accession Description Interval E-value
COG5614 COG5614
Phage head-tail adaptor [Mobilome: prophages, transposons];
16-117 1.87e-22

Phage head-tail adaptor [Mobilome: prophages, transposons];


Pssm-ID: 444345  Cd Length: 107  Bit Score: 84.99  E-value: 1.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446625043  16 DPGELNKRVLIRLRVDMPADNFGVEPQYPVTFRTWAKVIQTSATTWQETAQTGDAITHYITIRYRRGITADYEVVCGDSV 95
Cdd:COG5614    2 SAGRLRHRITLQRPTETPDGAGGPIETWEDLATVWAEVEPLSGREYFAAGAEQAEVTHRITIRYRPGITPDMRIVYGGRI 81

                         90       100
                 ....*....|....*....|..
gi 446625043  96 YRVKRQRDLNGARRFLLLECTE 117
Cdd:COG5614   82 FNIRAVIDPDGRGRYLEILCEE 103
Phage_H_T_join pfam05521
Phage head-tail joining protein;
21-115 8.46e-21

Phage head-tail joining protein;


Pssm-ID: 428506  Cd Length: 96  Bit Score: 80.44  E-value: 8.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446625043   21 NKRVLIRLRV-DMPADNFGVEPQYPVTFRTWAKVIQTSATTWQETAQTGDAITHYITIRYRRGITADYEVVCGDSVYRVK 99
Cdd:pfam05521   1 NHRITIQRPVvDVPDGGGGPVETWVDVGTVWAAVEPLSGREFIAAGAAQAEVTVRITIRYRPDITADMRIRFGGRIYDIK 80

                          90
                  ....*....|....*.
gi 446625043  100 RQRDLNGARRFLLLEC 115
Cdd:pfam05521  81 SVDDPDERGRYLELTC 96
gp16_SPP1 TIGR01563
phage head-tail adaptor, putative, SPP1 family; This family describes a small protein of about ...
 19-117 6.80e-09

phage head-tail adaptor, putative, SPP1 family; This family describes a small protein of about 100 amino acids found in bacteriophage and in bacterial prophage regions. Examples include gp9 of phage HK022 and gp16 of phage SPP1. This minor structural protein is suggested to be a head-tail adaptor protein (although the source of this annotation was not traced during construction of this model). [Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 273692  Cd Length: 101  Bit Score: 50.06  E-value: 6.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446625043   19 ELNKRVLIRLRVDMPADNFGVE-PQYPVTFRTWAKVIQTSATTWQETAQTGDAITHYITIRYRRGITADYEVVCGDSVYR 97
Cdd:TIGR01563   1 KFNDRITFQTYETTGRDGRGQKiTKWVDYFTLWAAVKPMSGQEFYRAGQEGVEITHVILIRYRKDVTNKMRVIYDGRIYT 80

                          90       100
                  ....*....|....*....|
gi 446625043   98 VKRQRDLNGARRFLLLECTE 117
Cdd:TIGR01563  81 IGAVIDPSRTREELDLLTKE 100
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 86-120 8.04e-03

phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319826 [Multi-domain]  Cd Length: 211  Bit Score: 34.62  E-value: 8.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446625043  86 DYEVVCGDSV--YRVKRQRDLNGARRFLLLECTELGE 120
Cdd:cd07524  158 PFIIVIGDSVtdLEAAKEADLVFARDGLILKCEEENL 194
 
Name Accession Description Interval E-value
COG5614 COG5614
Phage head-tail adaptor [Mobilome: prophages, transposons];
16-117 1.87e-22

Phage head-tail adaptor [Mobilome: prophages, transposons];


Pssm-ID: 444345  Cd Length: 107  Bit Score: 84.99  E-value: 1.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446625043  16 DPGELNKRVLIRLRVDMPADNFGVEPQYPVTFRTWAKVIQTSATTWQETAQTGDAITHYITIRYRRGITADYEVVCGDSV 95
Cdd:COG5614    2 SAGRLRHRITLQRPTETPDGAGGPIETWEDLATVWAEVEPLSGREYFAAGAEQAEVTHRITIRYRPGITPDMRIVYGGRI 81

                         90       100
                 ....*....|....*....|..
gi 446625043  96 YRVKRQRDLNGARRFLLLECTE 117
Cdd:COG5614   82 FNIRAVIDPDGRGRYLEILCEE 103
Phage_H_T_join pfam05521
Phage head-tail joining protein;
21-115 8.46e-21

Phage head-tail joining protein;


Pssm-ID: 428506  Cd Length: 96  Bit Score: 80.44  E-value: 8.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446625043   21 NKRVLIRLRV-DMPADNFGVEPQYPVTFRTWAKVIQTSATTWQETAQTGDAITHYITIRYRRGITADYEVVCGDSVYRVK 99
Cdd:pfam05521   1 NHRITIQRPVvDVPDGGGGPVETWVDVGTVWAAVEPLSGREFIAAGAAQAEVTVRITIRYRPDITADMRIRFGGRIYDIK 80

                          90
                  ....*....|....*.
gi 446625043  100 RQRDLNGARRFLLLEC 115
Cdd:pfam05521  81 SVDDPDERGRYLELTC 96
gp16_SPP1 TIGR01563
phage head-tail adaptor, putative, SPP1 family; This family describes a small protein of about ...
 19-117 6.80e-09

phage head-tail adaptor, putative, SPP1 family; This family describes a small protein of about 100 amino acids found in bacteriophage and in bacterial prophage regions. Examples include gp9 of phage HK022 and gp16 of phage SPP1. This minor structural protein is suggested to be a head-tail adaptor protein (although the source of this annotation was not traced during construction of this model). [Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 273692  Cd Length: 101  Bit Score: 50.06  E-value: 6.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446625043   19 ELNKRVLIRLRVDMPADNFGVE-PQYPVTFRTWAKVIQTSATTWQETAQTGDAITHYITIRYRRGITADYEVVCGDSVYR 97
Cdd:TIGR01563   1 KFNDRITFQTYETTGRDGRGQKiTKWVDYFTLWAAVKPMSGQEFYRAGQEGVEITHVILIRYRKDVTNKMRVIYDGRIYT 80

                          90       100
                  ....*....|....*....|
gi 446625043   98 VKRQRDLNGARRFLLLECTE 117
Cdd:TIGR01563  81 IGAVIDPSRTREELDLLTKE 100
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 86-120 8.04e-03

phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319826 [Multi-domain]  Cd Length: 211  Bit Score: 34.62  E-value: 8.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446625043  86 DYEVVCGDSV--YRVKRQRDLNGARRFLLLECTELGE 120
Cdd:cd07524  158 PFIIVIGDSVtdLEAAKEADLVFARDGLILKCEEENL 194
 
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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