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Conserved domains on  [gi|857274631|gb|AKO59841|]
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hypothetical protein p106619_42 [Brucella phage 1066_19]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 159-257 7.23e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 7.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631  159 IAELQAKAKDYREYSERL---VKRLESEEATRSQVEELLAAERADHDNTIatlSSLIEDNAALTARIKELERVETELCTS 235
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKdeqIKKLQQEKELLEKEIERLKETIIKNNSEI---KDLTNQDSVKELIIKNLDNTRESLETQ 469

                          90       100
                  ....*....|....*....|..
gi 857274631  236 IGLLEDKLNAANGKIEALVQSL 257
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKEL 491
 
Name Accession Description Interval E-value
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 159-257 7.23e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 7.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631  159 IAELQAKAKDYREYSERL---VKRLESEEATRSQVEELLAAERADHDNTIatlSSLIEDNAALTARIKELERVETELCTS 235
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKdeqIKKLQQEKELLEKEIERLKETIIKNNSEI---KDLTNQDSVKELIIKNLDNTRESLETQ 469

                          90       100
                  ....*....|....*....|..
gi 857274631  236 IGLLEDKLNAANGKIEALVQSL 257
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKEL 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-268 2.80e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631 159 IAELQAKAKDYREYSERLVKRLESEEATRSQVEELLAAERADHDNTIATLSSLIEDNAALTARIKELERVETELCTSIGL 238
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                         90       100       110
                 ....*....|....*....|....*....|
gi 857274631 239 LEDKLNAANGKIEALVQSLAYETAHEATKR 268
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELE 343
Rabaptin pfam03528
Rabaptin;
137-267 3.53e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 42.01  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631  137 AHATSSE-MRTEALCR-RSQAGSIIAELQAKAKD-YREYSERLVKRLESEEATRSQVEELLAAERAD----------HDN 203
Cdd:pfam03528  82 AVATVSEnTKQEAIDEvKSQWQEEVASLQAIMKEtVREYEVQFHRRLEQERAQWNQYRESAEREIADlrrrlsegqeEEN 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857274631  204 TIATLSSLIEDNAALTARIKELERvetelctSIGLLEDKLNAANGKIEALVQSLAYETAH--EATK 267
Cdd:pfam03528 162 LEDEMKKAQEDAEKLRSVVMPMEK-------EIAALKAKLTEAEDKIKELEASKMKELNHylEAEK 220
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 116-262 6.66e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 37.73  E-value: 6.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631 116 KCGELVTVGYGYVNSLGElEYAHATSSEMRTEAlcrRSQAGSIIAELQAKAKDYREYSERLVKRLES-EEATRSQVEELL 194
Cdd:cd22656   84 NAGGTIDSYYAEILELID-DLADATDDEELEEA---KKTIKALLDDLLKEAKKYQDKAAKVVDKLTDfENQTEKDQTALE 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631 195 AAERAdHDNTIATLSSLIEDN--AALTARIKELERVETELctsiglLEDKLNAANGKIEALVQSLAYETA 262
Cdd:cd22656  160 TLEKA-LKDLLTDEGGAIARKeiKDLQKELEKLNEEYAAK------LKAKIDELKALIADDEAKLAAALR 222
 
Name Accession Description Interval E-value
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 159-257 7.23e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 7.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631  159 IAELQAKAKDYREYSERL---VKRLESEEATRSQVEELLAAERADHDNTIatlSSLIEDNAALTARIKELERVETELCTS 235
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKdeqIKKLQQEKELLEKEIERLKETIIKNNSEI---KDLTNQDSVKELIIKNLDNTRESLETQ 469

                          90       100
                  ....*....|....*....|..
gi 857274631  236 IGLLEDKLNAANGKIEALVQSL 257
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKEL 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-268 2.80e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631 159 IAELQAKAKDYREYSERLVKRLESEEATRSQVEELLAAERADHDNTIATLSSLIEDNAALTARIKELERVETELCTSIGL 238
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                         90       100       110
                 ....*....|....*....|....*....|
gi 857274631 239 LEDKLNAANGKIEALVQSLAYETAHEATKR 268
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELE 343
Rabaptin pfam03528
Rabaptin;
137-267 3.53e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 42.01  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631  137 AHATSSE-MRTEALCR-RSQAGSIIAELQAKAKD-YREYSERLVKRLESEEATRSQVEELLAAERAD----------HDN 203
Cdd:pfam03528  82 AVATVSEnTKQEAIDEvKSQWQEEVASLQAIMKEtVREYEVQFHRRLEQERAQWNQYRESAEREIADlrrrlsegqeEEN 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857274631  204 TIATLSSLIEDNAALTARIKELERvetelctSIGLLEDKLNAANGKIEALVQSLAYETAH--EATK 267
Cdd:pfam03528 162 LEDEMKKAQEDAEKLRSVVMPMEK-------EIAALKAKLTEAEDKIKELEASKMKELNHylEAEK 220
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
151-253 8.81e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631  151 RRSQAGSIIAELQAKAKDYREYSE---RLVKRLESEEATRSQVEEL--LAAERADHDNTIATLSSLIEDNAALTARIKEL 225
Cdd:COG4913   625 ELAEAEERLEALEAELDALQERREalqRLAEYSWDEIDVASAEREIaeLEAELERLDASSDDLAALEEQLEELEAELEEL 704

                          90       100
                  ....*....|....*....|....*...
gi 857274631  226 ERVETELCTSIGLLEDKLNAANGKIEAL 253
Cdd:COG4913   705 EEELDELKGEIGRLEKELEQAEEELDEL 732
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
139-287 1.37e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631 139 ATSSEMRTEALCRRSQAGSIIAELQAKAKDYREYSERLVKRLESE----EATRSQVEEL-----------------LAAE 197
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArselEQLEEELEELneqlqaaqaelaqaqeeLESL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631 198 RADHDNTIATLSSLIEDNAALTARIKELERVETELCTSIGLLEDKLNAANGKIEALVQSLAyetAHEATKRAEALEAKLA 277
Cdd:COG4372  107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA---ALEQELQALSEAEAEQ 183

                        170
                 ....*....|
gi 857274631 278 AAEQALKTAR 287
Cdd:COG4372  184 ALDELLKEAN 193
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 161-258 1.64e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631   161 ELQA-KAKDYREYSERL--------VKRLESEEATRSQVEELLAAERADHDNTIATLssliednAALTARIKELERVETE 231
Cdd:TIGR02168  206 ERQAeKAERYKELKAELrelelallVLRLEELREELEELQEELKEAEEELEELTAEL-------QELEEKLEELRLEVSE 278

                           90       100
                   ....*....|....*....|....*..
gi 857274631   232 LCTSIGLLEDKLNAANGKIEALVQSLA 258
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRLEQQKQ 305
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 125-287 1.69e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631 125 YGYVNSLGELEYAHATSSEMRTEALCRRSQAGSIIAELQAKAKDYREYSERLVKRLESEEATRSQVEELLAAERADHDNT 204
Cdd:COG1196  291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631 205 IATLSSLIEDNAALTARIKELERVETELCTSIGLLEDKLNAANGKIEALVQSLAYETAHEATKRAEALEAKLAAAEQALK 284
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450


                 ...
gi 857274631 285 TAR 287
Cdd:COG1196  451 EAE 453
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-262 4.20e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631 158 IIAEL---------QA-KAKDYREYSERLvKRLESEEA--TRSQVEELLAAERADHDNTIATLSSLIEDNAALTARIKEL 225
Cdd:COG1196  194 ILGELerqleplerQAeKAERYRELKEEL-KELEAELLllKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 857274631 226 ERVETELCTSIGLLEDKLNAANGKIEALVQSLAYETA 262
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 116-262 6.66e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 37.73  E-value: 6.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631 116 KCGELVTVGYGYVNSLGElEYAHATSSEMRTEAlcrRSQAGSIIAELQAKAKDYREYSERLVKRLES-EEATRSQVEELL 194
Cdd:cd22656   84 NAGGTIDSYYAEILELID-DLADATDDEELEEA---KKTIKALLDDLLKEAKKYQDKAAKVVDKLTDfENQTEKDQTALE 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631 195 AAERAdHDNTIATLSSLIEDN--AALTARIKELERVETELctsiglLEDKLNAANGKIEALVQSLAYETA 262
Cdd:cd22656  160 TLEKA-LKDLLTDEGGAIARKeiKDLQKELEKLNEEYAAK------LKAKIDELKALIADDEAKLAAALR 222
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 174-258 8.03e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.44  E-value: 8.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857274631 174 ERLVKRLESEEATRSQVEELLAAERADHDNTIATLSSLIEDNAALTARIKELERVETELCTSIGLLEDKLNAANGKIEAL 253
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102


                 ....*
gi 857274631 254 VQSLA 258
Cdd:COG4942  103 KEELA 107
 
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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