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Conserved domains on  [gi|1622830029|ref|XP_028684358|]
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pre-B-cell leukemia transcription factor-interacting protein 1 isoform X3 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
266-397 1.81e-06

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  266 LDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQgeafqraLESELQQLRARLQGLEADCVRGMDg 345
Cdd:COG4913    677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-------AEEELDELQDRLEAAEDLARLELR- 748
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622830029  346 vclsggrgPQGDKAIKEQGPREQEPELS--FLKQKEQLEAEAQALRQELERQRR 397
Cdd:COG4913    749 --------ALLEERFAAALGDAVERELRenLEERIDALRARLNRAEEELERAMR 794
PRK11281 super family cl46976
mechanosensitive channel MscK;
372-443 1.01e-03

mechanosensitive channel MscK;


The actual alignment was detected with superfamily member PRK11281:

Pssm-ID: 481316 [Multi-domain]  Cd Length: 1113  Bit Score: 42.59  E-value: 1.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622830029  372 LSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERsLKDAGHGDP----AHAGLAELGHRLAQKLQSLENWGQD 443
Cdd:PRK11281    69 LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA-LKDDNDEETretlSTLSLRQLESRLAQTLDQLQNAQND 143
 
Name Accession Description Interval E-value
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
266-397 1.81e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  266 LDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQgeafqraLESELQQLRARLQGLEADCVRGMDg 345
Cdd:COG4913    677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-------AEEELDELQDRLEAAEDLARLELR- 748
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622830029  346 vclsggrgPQGDKAIKEQGPREQEPELS--FLKQKEQLEAEAQALRQELERQRR 397
Cdd:COG4913    749 --------ALLEERFAAALGDAVERELRenLEERIDALRARLNRAEEELERAMR 794
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
265-413 1.72e-05

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: 48.51  E-value: 1.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  265 LLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRGmd 344
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL-- 321
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  345 gvclsggrgpQGDKAIKEQGPREQEPELSFLKQK-EQLEAEAQALRQELERQRRLLgsvqQDLERSLKDA 413
Cdd:TIGR02168  322 ----------EAQLEELESKLDELAEELAELEEKlEELKEELESLEAELEELEAEL----EELESRLEEL 377
PRK09039 PRK09039
peptidoglycan -binding protein;
278-438 5.74e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 45.73  E-value: 5.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 278 LLQAQLQAQKEELQSLMHQpkgLEEENAQLrgALQQGEAFQraLESELQQLRARLQGLEADCVRGMDgvCLSGGRGpQGD 357
Cdd:PRK09039   43 FLSREISGKDSALDRLNSQ---IAELADLL--SLERQGNQD--LQDSVANLRASLSAAEAERSRLQA--LLAELAG-AGA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 358 KAIKEQGPREQEpelsfLKQKEQLEAEAQA----LRQELERQRRLLGSVQQDLERSLKdagHGDPAHAGLAELGHR---- 429
Cdd:PRK09039  113 AAEGRAGELAQE-----LDSEKQVSARALAqvelLNQQIAALRRQLAALEAALDASEK---RDRESQAKIADLGRRlnva 184

                  ....*....
gi 1622830029 430 LAQKLQSLE 438
Cdd:PRK09039  185 LAQRVQELN 193
DUF4175 pfam13779
Domain of unknown function (DUF4175);
231-458 1.08e-04

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 45.75  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 231 ELLDAVGDRQDGLREQLQSSVPPDHVPSLQNMGLL-LDKLAKENQDIRLL-----QAQLQAQKEELQSLMhqpkgleeEN 304
Cdd:pfam13779 517 ELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMtQQDLQRMLDRIEELarsgrRAEAQQMLSQLQQML--------EN 588
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 305 AQL-RGALQQGEAFQRALES--ELQQLRARLQGL-------------EADCVRGMDGVCLSGGRGPQGDKAIKEQGPREQ 368
Cdd:pfam13779 589 LQAgQPQQQQQQGQSEMQQAmdELGDLLREQQQLldetfrqlqqqggQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQG 668
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 369 EPElsflkQKEQLEAEAQALRQELERQRRLLGSVQQ--------DLERSLKDA----GHGDPAHA---------GLAELG 427
Cdd:pfam13779 669 GAE-----ALGDLAERQQALRRRLEELQDELKELGGkepgqalgDAGRAMRDAeealGQGDLAGAvdaqgraleALRKGA 743
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1622830029 428 HRLAQKLQSLENWGQDPGVSANASEAWHQKP 458
Cdd:pfam13779 744 QQLAEAMQQQQGQGQQPGQGGQGGRQAGQDP 774
PRK11281 PRK11281
mechanosensitive channel MscK;
372-443 1.01e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.59  E-value: 1.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622830029  372 LSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERsLKDAGHGDP----AHAGLAELGHRLAQKLQSLENWGQD 443
Cdd:PRK11281    69 LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA-LKDDNDEETretlSTLSLRQLESRLAQTLDQLQNAQND 143
 
Name Accession Description Interval E-value
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
266-397 1.81e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  266 LDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQgeafqraLESELQQLRARLQGLEADCVRGMDg 345
Cdd:COG4913    677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-------AEEELDELQDRLEAAEDLARLELR- 748
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622830029  346 vclsggrgPQGDKAIKEQGPREQEPELS--FLKQKEQLEAEAQALRQELERQRR 397
Cdd:COG4913    749 --------ALLEERFAAALGDAVERELRenLEERIDALRARLNRAEEELERAMR 794
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
266-440 4.03e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 4.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  266 LDKLAKENQDIRLLQAQLQAQKEELQSLMhqpkgLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEAdcvrgmdg 345
Cdd:COG4913    264 YAAARERLAELEYLRAALRLWFAQRRLEL-----LEAELEELRAELARLEAELERLEARLDALREELDELEA-------- 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  346 vclsggrgpqgdkAIKEQGpreqepelsfLKQKEQLEAEAQALRQELERQRRLLgsvqQDLERSLKDAGHGDPAHA-GLA 424
Cdd:COG4913    331 -------------QIRGNG----------GDRLEQLEREIERLERELEERERRR----ARLEALLAALGLPLPASAeEFA 383
                          170
                   ....*....|....*.
gi 1622830029  425 ELGHRLAQKLQSLENW 440
Cdd:COG4913    384 ALRAEAAALLEALEEE 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
265-413 1.72e-05

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: 48.51  E-value: 1.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  265 LLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRGmd 344
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL-- 321
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  345 gvclsggrgpQGDKAIKEQGPREQEPELSFLKQK-EQLEAEAQALRQELERQRRLLgsvqQDLERSLKDA 413
Cdd:TIGR02168  322 ----------EAQLEELESKLDELAEELAELEEKlEELKEELESLEAELEELEAEL----EELESRLEEL 377
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
268-439 2.02e-05

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: 48.13  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  268 KLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRgmdgvc 347
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ------ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  348 LSGGRGPQGDKAIKEQGPREQ-EPELSFLKQK-EQLEAEAQALRQELERQRRLLGSVQQDLERslkdaghgdpahagLAE 425
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEaEEELAEAEAEiEELEAQIEQLKEELKALREALDELRAELTL--------------LNE 817
                          170
                   ....*....|....
gi 1622830029  426 LGHRLAQKLQSLEN 439
Cdd:TIGR02168  818 EAANLRERLESLER 831
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
265-412 2.07e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.46  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 265 LLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADcvrgmd 344
Cdd:COG1579     8 ALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ------ 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622830029 345 gvcLSGGRGP--------QGDKAIKEQGPREQEpELSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLKD 412
Cdd:COG1579    82 ---LGNVRNNkeyealqkEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
267-438 2.66e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 267 DKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADcvrgmdgv 346
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE-------- 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 347 clsggrgpqgdkaIKEQGPREQEPELSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLKDAGHGDPAHAGLAEL 426
Cdd:COG1196   346 -------------LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
                         170
                  ....*....|..
gi 1622830029 427 GHRLAQKLQSLE 438
Cdd:COG1196   413 LERLERLEEELE 424
PRK09039 PRK09039
peptidoglycan -binding protein;
278-438 5.74e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 45.73  E-value: 5.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 278 LLQAQLQAQKEELQSLMHQpkgLEEENAQLrgALQQGEAFQraLESELQQLRARLQGLEADCVRGMDgvCLSGGRGpQGD 357
Cdd:PRK09039   43 FLSREISGKDSALDRLNSQ---IAELADLL--SLERQGNQD--LQDSVANLRASLSAAEAERSRLQA--LLAELAG-AGA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 358 KAIKEQGPREQEpelsfLKQKEQLEAEAQA----LRQELERQRRLLGSVQQDLERSLKdagHGDPAHAGLAELGHR---- 429
Cdd:PRK09039  113 AAEGRAGELAQE-----LDSEKQVSARALAqvelLNQQIAALRRQLAALEAALDASEK---RDRESQAKIADLGRRlnva 184

                  ....*....
gi 1622830029 430 LAQKLQSLE 438
Cdd:PRK09039  185 LAQRVQELN 193
DUF4175 pfam13779
Domain of unknown function (DUF4175);
231-458 1.08e-04

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 45.75  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 231 ELLDAVGDRQDGLREQLQSSVPPDHVPSLQNMGLL-LDKLAKENQDIRLL-----QAQLQAQKEELQSLMhqpkgleeEN 304
Cdd:pfam13779 517 ELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMtQQDLQRMLDRIEELarsgrRAEAQQMLSQLQQML--------EN 588
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 305 AQL-RGALQQGEAFQRALES--ELQQLRARLQGL-------------EADCVRGMDGVCLSGGRGPQGDKAIKEQGPREQ 368
Cdd:pfam13779 589 LQAgQPQQQQQQGQSEMQQAmdELGDLLREQQQLldetfrqlqqqggQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQG 668
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 369 EPElsflkQKEQLEAEAQALRQELERQRRLLGSVQQ--------DLERSLKDA----GHGDPAHA---------GLAELG 427
Cdd:pfam13779 669 GAE-----ALGDLAERQQALRRRLEELQDELKELGGkepgqalgDAGRAMRDAeealGQGDLAGAvdaqgraleALRKGA 743
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1622830029 428 HRLAQKLQSLENWGQDPGVSANASEAWHQKP 458
Cdd:pfam13779 744 QQLAEAMQQQQGQGQQPGQGGQGGRQAGQDP 774
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
263-439 1.13e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 263 GLLLDKLAKENQDI--------RLLQAQLQAQKEELQSLmhqpKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQG 334
Cdd:COG4717    45 AMLLERLEKEADELfkpqgrkpELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 335 LEADCVRGMDGVCLSGGRGPQGDKAIK-EQGPREQEPELSFLKQKEQLEAEAQALRQELERQRRLLG-SVQQDLERSLKD 412
Cdd:COG4717   121 LEKLLQLLPLYQELEALEAELAELPERlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEE 200
                         170       180
                  ....*....|....*....|....*..
gi 1622830029 413 AGHGDPAHAGLAELGHRLAQKLQSLEN 439
Cdd:COG4717   201 LEELQQRLAELEEELEEAQEELEELEE 227
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
267-408 1.78e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  267 DKLAKENQDIRLLQAQLQAQKEELQSLmhqpKGLEEENAQLRGALQQGEAFQ------RALESELQQLRARLQGLEADcv 340
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEAL----EAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDAS-- 683
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622830029  341 rgmdgvclsggrgpqgdkaikeqgpreqEPELSFLK-QKEQLEAEAQALRQELERQRRLLGSVQQDLER 408
Cdd:COG4913    684 ----------------------------SDDLAALEeQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
264-438 1.99e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 264 LLLDKLAKENQDIRLLQAQLQAQKEELQSlmhqpkgLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADcvrgm 343
Cdd:COG1196   229 LLLLKLRELEAELEELEAELEELEAELEE-------LEAELAELEAELEELRLELEELELELEEAQAEEYELLAE----- 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 344 dgvclsggrgpqgdkaiKEQGPREQEPElsfLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLKDAGHGDPAHAGL 423
Cdd:COG1196   297 -----------------LARLEQDIARL---EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
                         170
                  ....*....|....*
gi 1622830029 424 AELGHRLAQKLQSLE 438
Cdd:COG1196   357 EAELAEAEEALLEAE 371
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
266-408 2.14e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 266 LDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQR--ALESELQQLRARLQGLEA------ 337
Cdd:COG4717    80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPERLEELEErleelr 159
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622830029 338 DCVRGMDGVCLSGGRGPQGDKAIKEQGPREQEPELS-FLKQKEQLEAEAQALRQELERQRRLLGSVQQDLER 408
Cdd:COG4717   160 ELEEELEELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
265-438 2.20e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 265 LLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVrgmd 344
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL---- 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 345 gvclsggrgpqgdkaikeqgpREQEPELSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLKDAghgDPAHAGLA 424
Cdd:COG1196   390 ---------------------EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE---EEEEEALE 445
                         170
                  ....*....|....
gi 1622830029 425 ELGHRLAQKLQSLE 438
Cdd:COG1196   446 EAAEEEAELEEEEE 459
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
267-450 2.38e-04

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: 44.66  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  267 DKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRGMDgv 346
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ-- 421
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  347 clsggRGPQGDKAIKEQGPREQEPELSFLKQ-KEQLEAEAQALRQELERQRRLLGSVQQDLerslkdaghgDPAHAGLAE 425
Cdd:TIGR02168  422 -----EIEELLKKLEEAELKELQAELEELEEeLEELQEELERLEEALEELREELEEAEQAL----------DAAERELAQ 486
                          170       180
                   ....*....|....*....|....*
gi 1622830029  426 LGHRLAQkLQSLENWGQDPGVSANA 450
Cdd:TIGR02168  487 LQARLDS-LERLQENLEGFSEGVKA 510
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
239-338 3.45e-04

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: 43.60  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 239 RQDGLREQLQSSVPPDHVPSLQNMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQ 318
Cdd:COG4942   118 RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
                          90       100
                  ....*....|....*....|....
gi 1622830029 319 RA----LESELQQLRARLQGLEAD 338
Cdd:COG4942   198 QKllarLEKELAELAAELAELQQE 221
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
268-438 3.60e-04

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: 43.60  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 268 KLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESEL-------QQLRARLQGLEADCV 340
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaelekeiAELRAELEAQKEELA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 341 RGMDGVCLSgGRGPQGDKAIKEQGPREQEPELSFLKQ-KEQLEAEAQALR---QELERQRRLLGSVQQDLERSLKDAghg 416
Cdd:COG4942   108 ELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRadlAELAALRAELEAERAELEALLAEL--- 183
                         170       180
                  ....*....|....*....|..
gi 1622830029 417 DPAHAGLAELGHRLAQKLQSLE 438
Cdd:COG4942   184 EEERAALEALKAERQKLLARLE 205
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
265-439 3.64e-04

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: 43.89  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  265 LLDKLAKENQDIRLLQAQLQAQKEELQSLmhqpkglEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRGMD 344
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEEL-------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  345 GVCLSGGRGPQGDKAIKEQGPREQEPELSFLKQKEQLEA------EAQALRQELERQRRLLGSVQQDLERSLKDAGHG-D 417
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleseleALLNERASLEEALALLRSELEELSEELRELESKrS 911
                          170       180
                   ....*....|....*....|....*
gi 1622830029  418 PAHAGLAELGHRLAQ---KLQSLEN 439
Cdd:TIGR02168  912 ELRRELEELREKLAQlelRLEGLEV 936
PRK11281 PRK11281
mechanosensitive channel MscK;
372-443 1.01e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.59  E-value: 1.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622830029  372 LSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERsLKDAGHGDP----AHAGLAELGHRLAQKLQSLENWGQD 443
Cdd:PRK11281    69 LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA-LKDDNDEETretlSTLSLRQLESRLAQTLDQLQNAQND 143
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
267-337 1.46e-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: 41.67  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622830029 267 DKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEA 337
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
263-439 2.27e-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: 41.58  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  263 GLLLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADcvrg 342
Cdd:TIGR02168  228 ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ---- 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  343 mdgvclsggrgpqgdkaIKEQGPREQEPElsflKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLKDaghgdpaHAG 422
Cdd:TIGR02168  304 -----------------KQILRERLANLE----RQLEELEAQLEELESKLDELAEELAELEEKLEELKEE-------LES 355
                          170
                   ....*....|....*..
gi 1622830029  423 LAELGHRLAQKLQSLEN 439
Cdd:TIGR02168  356 LEAELEELEAELEELES 372
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
269-510 2.57e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  269 LAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEEnaqlrgalqqgeafqralESELQQLRARLQGLEADCVRGMDGvcl 348
Cdd:TIGR00618  302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ------------------QSSIEEQRRLLQTLHSQEIHIRDA--- 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  349 sgGRGPQGDKAIKEQGPREQEPELSFLKQKEQLEAEAQALRQELERQRRLLGsvQQDLERSLKDAGHGDPAHAglaelgh 428
Cdd:TIGR00618  361 --HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQA--TIDTRTSAFRDLQGQLAHA------- 429
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  429 RLAQKLQSLENWGQDPGVSANASEAWHQKPHFQNSREWSGKEKWWDGQRDRKAEHWNHKKEEsgRERKKNRGGQEDRELA 508
Cdd:TIGR00618  430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAV--VLARLLELQEEPCPLC 507

                   ..
gi 1622830029  509 GR 510
Cdd:TIGR00618  508 GS 509
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
275-399 3.18e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  275 DIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADcvRGMDGVCLSGGRGP 354
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELS 801
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1622830029  355 QGDKAIKEQGPREQEPELSfLKQKEQLEAEAQALRQELERQRRLL 399
Cdd:TIGR02169  802 KLEEEVSRIEARLREIEQK-LNRLTLEKEYLEKEIQELQEQRIDL 845
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
260-411 3.33e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 260 QNMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRG--ALQQGEAFQRALESELQQLRARL----- 332
Cdd:COG3206   212 EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYtpnhp 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029 333 --QGLEADCvrgmdgvclsggrgpqgdKAIKEQGPREQEPELSFLK-QKEQLEAEAQALRQELERQRRLLGSVQQ----- 404
Cdd:COG3206   292 dvIALRAQI------------------AALRAQLQQEAQRILASLEaELEALQAREASLQAQLAQLEARLAELPEleael 353

                  ....*...
gi 1622830029 405 -DLERSLK 411
Cdd:COG3206   354 rRLEREVE 361
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
267-338 5.16e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 5.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622830029 267 DKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEAD 338
Cdd:COG4372   101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
265-439 5.59e-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: 5.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  265 LLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEAdcvrgmd 344
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS------- 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  345 gvclsggrgpqgdkaiKEQGPREQEPELSflKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLKDAGHGDPA--HAG 422
Cdd:TIGR02168  387 ----------------KVAQLELQIASLN--NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEelEEE 448
                          170
                   ....*....|....*..
gi 1622830029  423 LAELGHRLAQKLQSLEN 439
Cdd:TIGR02168  449 LEELQEELERLEEALEE 465
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
243-337 7.98e-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: 39.65  E-value: 7.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  243 LREQLQSSVppDHVPSLQNMGLLLDKlAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALE 322
Cdd:TIGR02168  405 LEARLERLE--DRRERLQQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
                           90
                   ....*....|....*
gi 1622830029  323 SELQQLRARLQGLEA 337
Cdd:TIGR02168  482 RELAQLQARLDSLER 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
231-408 8.69e-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: 39.65  E-value: 8.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  231 ELLDAVGDRQDGLREQLQssvppdhvpslqnmgLLLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGA 310
Cdd:TIGR02168  796 EELKALREALDELRAELT---------------LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  311 LQQGEAFQRALESELQQLRARLQGLEAdcvrgmdgvclsggrgpqgdkAIKEQgpREQEPELSflKQKEQLEAEAQALRQ 390
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEE---------------------ALALL--RSELEELS--EELRELESKRSELRR 915
                          170
                   ....*....|....*...
gi 1622830029  391 ELERQRRLLGSVQQDLER 408
Cdd:TIGR02168  916 ELEELREKLAQLELRLEG 933
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
265-439 9.16e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 9.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  265 LLDKLAKENQDIRLLQAQLQAQKEELQSLmhqpkgleeeNAQLRGA----LQQGEAFQRALESELQQLRARLQGLEADCv 340
Cdd:COG4913    300 LRAELARLEAELERLEARLDALREELDEL----------EAQIRGNggdrLEQLEREIERLERELEERERRRARLEALL- 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622830029  341 rgmdgvclsggrgpqgdKAIKEQGPREQEpelSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLKDAghgdpah 420
Cdd:COG4913    369 -----------------AALGLPLPASAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL------- 421
                          170
                   ....*....|....*....
gi 1622830029  421 aglaelgHRLAQKLQSLEN 439
Cdd:COG4913    422 -------RELEAEIASLER 433
 
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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