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Conserved domains on  [gi|19923830|ref|NP_065385|]
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pre-B-cell leukemia transcription factor-interacting protein 1 isoform 1 [Homo sapiens]

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];
272-403 4.61e-07

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: 53.38  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  272 LDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQgeafqraLESELQQLRARLQGLEADCVRGPDg 351
Cdd:COG4913  677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-------AEEELDELQDRLEAAEDLARLELR- 748

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19923830  352 vclsggrgPQGDKAIREQGPREQEPELS--FLKQKEQLEAEAQALRQELERQRR 403
Cdd:COG4913  749 --------ALLEERFAAALGDAVERELRenLEERIDALRARLNRAEEELERAMR 794
PRK11281 super family cl46976
mechanosensitive channel MscK;
378-449 3.08e-04

mechanosensitive channel MscK;


The actual alignment was detected with superfamily member PRK11281:

Pssm-ID: 481316 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 3.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923830   378 LSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLER---SLQDASRGDPAHAGLAELGHRLAQKLQGLENWGQD 449
Cdd:PRK11281   69 LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAlkdDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQND 143
 
Name Accession Description Interval E-value
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
272-403 4.61e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  272 LDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQgeafqraLESELQQLRARLQGLEADCVRGPDg 351
Cdd:COG4913  677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-------AEEELDELQDRLEAAEDLARLELR- 748

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19923830  352 vclsggrgPQGDKAIREQGPREQEPELS--FLKQKEQLEAEAQALRQELERQRR 403
Cdd:COG4913  749 --------ALLEERFAAALGDAVERELRenLEERIDALRARLNRAEEELERAMR 794
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 271-438 2.12e-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: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    271 LLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRGpd 350
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL-- 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    351 gvclsggrgpQGDKAIREQGPREQEPELSFLKQK-EQLEAEAQALRQELERQRRLLgsvqQDLERSLQDASRG-DPAHAG 428
Cdd:TIGR02168  322 ----------EAQLEELESKLDELAEELAELEEKlEELKEELESLEAELEELEAEL----EELESRLEELEEQlETLRSK 387

                          170
                   ....*....|
gi 19923830    429 LAELGHRLAQ 438
Cdd:TIGR02168  388 VAQLELQIAS 397
PRK09039 PRK09039
peptidoglycan -binding protein;
284-444 4.76e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 46.11  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  284 LLQAQLQAQKEELQSLMHQpkgLEEENAQLrgALQQGEAFQraLESELQQLRARLQGLEADCVRGPDgvCLSGGRGpQGD 363
Cdd:PRK09039  43 FLSREISGKDSALDRLNSQ---IAELADLL--SLERQGNQD--LQDSVANLRASLSAAEAERSRLQA--LLAELAG-AGA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  364 KAIREQGPREQEpelsfLKQKEQLEAEAQA----LRQELERQRRLLGSVQQDLERSlqdASRGDPAHAGLAELGHR---- 435
Cdd:PRK09039 113 AAEGRAGELAQE-----LDSEKQVSARALAqvelLNQQIAALRRQLAALEAALDAS---EKRDRESQAKIADLGRRlnva 184


                 ....*....
gi 19923830  436 LAQKLQGLE 444
Cdd:PRK09039 185 LAQRVQELN 193
DUF4175 pfam13779
Domain of unknown function (DUF4175);
226-451 6.84e-05

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 46.52  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830   226 EEVERQVlpdPEVLEAVGDRQDGLREQ-LQAPVPPDSVPSLQNMGLLLDKLAKENQDIRLL-----QAQLQAQKEELQSL 299
Cdd:pfam13779 509 EEIAKLM---QELREALDDYMQALAEQaQQNPQDLQQPDDPNAQEMTQQDLQRMLDRIEELarsgrRAEAQQMLSQLQQM 585

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830   300 MhqpkgleeENAQL-RGALQQGEAFQRALES--ELQQLRARLQGL-------------EADCVRGPDGVCLSGGRGPQGD 363
Cdd:pfam13779 586 L--------ENLQAgQPQQQQQQGQSEMQQAmdELGDLLREQQQLldetfrqlqqqggQQQGQPGQQGQQGQGQQPGQGG 657

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830   364 KAIREQGPREQEPElsflkQKEQLEAEAQALRQELERQRRLLGSVQQ--------DLERSLQDA----SRGDPAHA---- 427
Cdd:pfam13779 658 QQPGAQMPPQGGAE-----ALGDLAERQQALRRRLEELQDELKELGGkepgqalgDAGRAMRDAeealGQGDLAGAvdaq 732

                         250       260
                  ....*....|....*....|....*....
gi 19923830   428 -----GLAELGHRLAQKLQGLENWGQDPG 451
Cdd:pfam13779 733 graleALRKGAQQLAEAMQQQQGQGQQPG 761
PRK11281 PRK11281
mechanosensitive channel MscK;
378-449 3.08e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 3.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923830   378 LSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLER---SLQDASRGDPAHAGLAELGHRLAQKLQGLENWGQD 449
Cdd:PRK11281   69 LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAlkdDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQND 143
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 308-418 9.95e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.18  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    308 EENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRgpDGVCLSggrgpqgdKAIREQgpREQEpelsFLKQKEQL 387
Cdd:smart00935  11 QESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQK--DAATLS--------EAAREK--KEKE----LQKKVQEF 74

                           90       100       110
                   ....*....|....*....|....*....|..
gi 19923830    388 EAEAQALRQELE-RQRRLLGSVQQDLERSLQD 418
Cdd:smart00935  75 QRKQQKLQQDLQkRQQEELQKILDKINKAIKE 106
 
Name Accession Description Interval E-value
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
272-403 4.61e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  272 LDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQgeafqraLESELQQLRARLQGLEADCVRGPDg 351
Cdd:COG4913  677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-------AEEELDELQDRLEAAEDLARLELR- 748

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19923830  352 vclsggrgPQGDKAIREQGPREQEPELS--FLKQKEQLEAEAQALRQELERQRR 403
Cdd:COG4913  749 --------ALLEERFAAALGDAVERELRenLEERIDALRARLNRAEEELERAMR 794
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
269-445 8.95e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 8.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 269 GLLLDKLAKENQDI--------RLLQAQLQAQKEELQSLmhqpKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQG 340
Cdd:COG4717  45 AMLLERLEKEADELfkpqgrkpELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEK 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 341 LEADCVRGPDGVCLSGGRGPQGDKAIR-EQGPREQEPELSFLKQKEQLEAEAQALRQELERQRRLLG-SVQQDLERSLQD 418
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAELPERlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEE 200

                       170       180
                ....*....|....*....|....*..
gi 19923830 419 ASRGDPAHAGLAELGHRLAQKLQGLEN 445
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEE 227
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 273-441 9.06e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 9.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 273 DKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADcvrgpdgv 352
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE-------- 345

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 353 clsggrgpqgdkaIREQGPREQEPELSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLQDASRGDPAHAGLAEL 432
Cdd:COG1196 346 -------------LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412


                ....*....
gi 19923830 433 GHRLAQKLQ 441
Cdd:COG1196 413 LERLERLEE 421
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
272-446 1.19e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  272 LDKLAKENQDIRLLQAQLQAQKEELQSLMhqpkgLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEAdcvrgpdg 351
Cdd:COG4913  264 YAAARERLAELEYLRAALRLWFAQRRLEL-----LEAELEELRAELARLEAELERLEARLDALREELDELEA-------- 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  352 vclsggrgpqgdkAIREQGpreqepelsfLKQKEQLEAEAQALRQELERQRRLLgsvqQDLERSLQDASRGDPAHA-GLA 430
Cdd:COG4913  331 -------------QIRGNG----------GDRLEQLEREIERLERELEERERRR----ARLEALLAALGLPLPASAeEFA 383

                        170
                 ....*....|....*.
gi 19923830  431 ELGHRLAQKLQGLENW 446
Cdd:COG4913  384 ALRAEAAALLEALEEE 399
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 271-418 1.58e-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: 46.84  E-value: 1.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 271 LLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADcvrgpd 350
Cdd:COG1579   8 ALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ------ 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923830 351 gvcLSGGRGP--------QGDKAIREQGPREQEpELSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLQD 418
Cdd:COG1579  82 ---LGNVRNNkeyealqkEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 271-438 2.12e-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: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    271 LLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRGpd 350
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL-- 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    351 gvclsggrgpQGDKAIREQGPREQEPELSFLKQK-EQLEAEAQALRQELERQRRLLgsvqQDLERSLQDASRG-DPAHAG 428
Cdd:TIGR02168  322 ----------EAQLEELESKLDELAEELAELEEKlEELKEELESLEAELEELEAEL----EELESRLEELEEQlETLRSK 387

                          170
                   ....*....|
gi 19923830    429 LAELGHRLAQ 438
Cdd:TIGR02168  388 VAQLELQIAS 397
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 274-445 2.49e-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: 47.74  E-value: 2.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    274 KLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRgpdgvc 353
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ------ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    354 LSGGRGP-QGDKAIREQGPREQEPELSFLKQK-EQLEAEAQALRQELERQRRLLGSVQQDLERslqdasrgdpahagLAE 431
Cdd:TIGR02168  752 LSKELTElEAEIEELEERLEEAEEELAEAEAEiEELEAQIEQLKEELKALREALDELRAELTL--------------LNE 817

                          170
                   ....*....|....
gi 19923830    432 LGHRLAQKLQGLEN 445
Cdd:TIGR02168  818 EAANLRERLESLER 831
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
273-433 2.82e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  273 DKLAKENQDIRLLQAQLQAQKEELQSLmhqpKGLEEENAQLRGALQQGEAFQ------RALESELQQLRARLQGLEADcv 346
Cdd:COG4913  610 AKLAALEAELAELEEELAEAEERLEAL----EAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDAS-- 683

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  347 rgpdgvclsggrgpqgdkaireqgpreqEPELSFLK-QKEQLEAEAQALRQELERQRRLLGSVQQDLERSLQDASRGDPA 425
Cdd:COG4913  684 ----------------------------SDDLAALEeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735


                 ....*...
gi 19923830  426 HAGLAELG 433
Cdd:COG4913  736 LEAAEDLA 743
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 270-444 2.96e-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: 2.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 270 LLLDKLAKENQDIRLLQAQLQAQKEELQSlmhqpkgLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEAdcvrgp 349
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEE-------LEAELAELEAELEELRLELEELELELEEAQAEEYELLA------ 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 350 dgvclsggrgpqgdKAIREQGPREQEpelsfLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLQDASRGDPAHAGL 429
Cdd:COG1196 296 --------------ELARLEQDIARL-----EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                       170
                ....*....|....*
gi 19923830 430 AELGHRLAQKLQGLE 444
Cdd:COG1196 357 EAELAEAEEALLEAE 371
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 273-460 4.48e-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: 46.97  E-value: 4.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    273 DKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEAdcvrgpdgv 352
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED--------- 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    353 clsggRGPQGDKAIREQGPREQEPELSFLKQK-EQLEAEAQALRQELERQRRLLGSVQQDLERSLQDAsrgDPAHAGLAE 431
Cdd:TIGR02168  415 -----RRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQAL---DAAERELAQ 486

                          170       180
                   ....*....|....*....|....*....
gi 19923830    432 LGHRLAQkLQGLENWGQDPGVSANASKAW 460
Cdd:TIGR02168  487 LQARLDS-LERLQENLEGFSEGVKALLKN 514
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-444 4.50e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 4.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 274 KLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADcvrgpdgvc 353
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE--------- 373

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 354 LSGGRGPQGDKAIREQgpREQEPELSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLQDASRGDPAHAGLAELG 433
Cdd:COG1196 374 LAEAEEELEELAEELL--EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451

                       170
                ....*....|.
gi 19923830 434 HRLAQKLQGLE 444
Cdd:COG1196 452 AELEEEEEALL 462
PRK09039 PRK09039
peptidoglycan -binding protein;
284-444 4.76e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 46.11  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  284 LLQAQLQAQKEELQSLMHQpkgLEEENAQLrgALQQGEAFQraLESELQQLRARLQGLEADCVRGPDgvCLSGGRGpQGD 363
Cdd:PRK09039  43 FLSREISGKDSALDRLNSQ---IAELADLL--SLERQGNQD--LQDSVANLRASLSAAEAERSRLQA--LLAELAG-AGA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  364 KAIREQGPREQEpelsfLKQKEQLEAEAQA----LRQELERQRRLLGSVQQDLERSlqdASRGDPAHAGLAELGHR---- 435
Cdd:PRK09039 113 AAEGRAGELAQE-----LDSEKQVSARALAqvelLNQQIAALRRQLAALEAALDAS---EKRDRESQAKIADLGRRlnva 184


                 ....*....
gi 19923830  436 LAQKLQGLE 444
Cdd:PRK09039 185 LAQRVQELN 193
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 286-445 5.78e-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: 46.59  E-value: 5.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    286 QAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEadcvRGPDGVCLSGGRGPQGDKA 365
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    366 IREQGPREQEPELSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLQDA----SRGDPAHAGLAELGHRLAQKLQ 441
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalrEALDELRAELTLLNEEAANLRE 824


                   ....
gi 19923830    442 GLEN 445
Cdd:TIGR02168  825 RLES 828
DUF4175 pfam13779
Domain of unknown function (DUF4175);
226-451 6.84e-05

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 46.52  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830   226 EEVERQVlpdPEVLEAVGDRQDGLREQ-LQAPVPPDSVPSLQNMGLLLDKLAKENQDIRLL-----QAQLQAQKEELQSL 299
Cdd:pfam13779 509 EEIAKLM---QELREALDDYMQALAEQaQQNPQDLQQPDDPNAQEMTQQDLQRMLDRIEELarsgrRAEAQQMLSQLQQM 585

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830   300 MhqpkgleeENAQL-RGALQQGEAFQRALES--ELQQLRARLQGL-------------EADCVRGPDGVCLSGGRGPQGD 363
Cdd:pfam13779 586 L--------ENLQAgQPQQQQQQGQSEMQQAmdELGDLLREQQQLldetfrqlqqqggQQQGQPGQQGQQGQGQQPGQGG 657

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830   364 KAIREQGPREQEPElsflkQKEQLEAEAQALRQELERQRRLLGSVQQ--------DLERSLQDA----SRGDPAHA---- 427
Cdd:pfam13779 658 QQPGAQMPPQGGAE-----ALGDLAERQQALRRRLEELQDELKELGGkepgqalgDAGRAMRDAeealGQGDLAGAvdaq 732

                         250       260
                  ....*....|....*....|....*....
gi 19923830   428 -----GLAELGHRLAQKLQGLENWGQDPG 451
Cdd:pfam13779 733 graleALRKGAQQLAEAMQQQQGQGQQPG 761
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 271-445 9.24e-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: 46.20  E-value: 9.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    271 LLDKLAKENQDIRLLQAQLQAQKEELQSLmhqpkglEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRGPD 350
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEEL-------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    351 GVCLSGGRGPQGDKAIREQGPREQEPELSFLKQKEQLEA------EAQALRQELERQRRLLGSVQQDLERSLQDASRG-D 423
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleseleALLNERASLEEALALLRSELEELSEELRELESKrS 911

                          170       180
                   ....*....|....*....|....*
gi 19923830    424 PAHAGLAELGHRLAQ---KLQGLEN 445
Cdd:TIGR02168  912 ELRRELEELREKLAQlelRLEGLEV 936
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 274-444 1.10e-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: 45.14  E-value: 1.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 274 KLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRGPD--- 350
Cdd:COG4942  28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEela 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 351 ---GVCLSGGRGPQGDKAIREQGPREQEPELSFLKQ-KEQLEAEAQALR---QELERQRRLLGSVQQDLERSLQDASRgd 423
Cdd:COG4942 108 ellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRadlAELAALRAELEAERAELEALLAELEE-- 185

                       170       180
                ....*....|....*....|.
gi 19923830 424 pAHAGLAELGHRLAQKLQGLE 444
Cdd:COG4942 186 -ERAALEALKAERQKLLARLE 205
PRK11281 PRK11281
mechanosensitive channel MscK;
378-449 3.08e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 3.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923830   378 LSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLER---SLQDASRGDPAHAGLAELGHRLAQKLQGLENWGQD 449
Cdd:PRK11281   69 LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAlkdDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQND 143
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 225-414 3.70e-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: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    225 MEEVERQVLPDPEVLEAVGDRQDGLREQLQapvppdsvpslqnmgLLLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPK 304
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELT---------------LLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    305 GLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEAdcvrgpdgvclsggrgpqgdkAIREQgpREQEPELSflKQK 384
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEE---------------------ALALL--RSELEELS--EEL 903

                          170       180       190
                   ....*....|....*....|....*....|
gi 19923830    385 EQLEAEAQALRQELERQRRLLGSVQQDLER 414
Cdd:TIGR02168  904 RELESKRSELRRELEELREKLAQLELRLEG 933
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
271-414 4.82e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 4.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 271 LLDKLAKENQDIRLLQAQLQAQKEELQSL--MHQPKGLEEENAQLRGALQQGEAFQRALES---ELQQLRARLQGLEADC 345
Cdd:COG4717  93 LQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAEL 172

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923830 346 VRGPDgvclsggrgpQGDKAIREQGPREQEPELSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLER 414
Cdd:COG4717 173 AELQE----------ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 227-431 5.66e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 5.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  227 EVERQVLPDPEVLEAVGDRQDGLREQLQApvppdsvpslqnmgllLDKLAKENQDIRLLQAQL-QAQKEELQSLMHQPKG 305
Cdd:COG3096  495 QTARELLRRYRSQQALAQRLQQLRAQLAE----------------LEQRLRQQQNAERLLEEFcQRIGQQLDAAEELEEL 558

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  306 LEEENAQLRGALQQGEAFQ---RALESELQQLRARLQGLEAdcvrgpdgvclsggRGPQGDKA------IREQG--PREQ 374
Cdd:COG3096  559 LAELEAQLEELEEQAAEAVeqrSELRQQLEQLRARIKELAA--------------RAPAWLAAqdalerLREQSgeALAD 624

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 19923830  375 EPEL-SFLKQKEQLEAEAQALRQELERQRRLLgsvQQDLERSLQDASRGDPAHAGLAE 431
Cdd:COG3096  625 SQEVtAAMQQLLEREREATVERDELAARKQAL---ESQIERLSQPGGAEDPRLLALAE 679
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 281-418 8.28e-04

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: 42.75  E-value: 8.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    281 DIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADcvrgpdgvcLSGGRGP 360
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR---------LSHSRIP 794

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923830    361 QGDKAIREQGPREQEPELSF------LKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLQD 418
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEARLreieqkLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 245-344 8.36e-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: 42.44  E-value: 8.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 245 RQDGLREQLQAPVPPDSVPSLQNMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQ 324
Cdd:COG4942 118 RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197

                        90       100
                ....*....|....*....|....
gi 19923830 325 RA----LESELQQLRARLQGLEAD 344
Cdd:COG4942 198 QKllarLEKELAELAAELAELQQE 221
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
271-440 1.14e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  271 LLDKLAKENQDIRLLQAQLQAQKEELQSLmhqpkgleeeNAQLRGA----LQQGEAFQRALESELQQLRARLQGLEADCv 346
Cdd:COG4913  300 LRAELARLEAELERLEARLDALREELDEL----------EAQIRGNggdrLEQLEREIERLERELEERERRRARLEALL- 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830  347 rgpDGVCLSGGRGPQGDKAIREQGPREQEPELSFLKQKEQLEAEAQALRQELERQRRllgSVQQDLErSLQdaSRGDPAH 426
Cdd:COG4913  369 ---AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR---ELEAEIA-SLE--RRKSNIP 439

                        170
                 ....*....|....
gi 19923830  427 AGLAELGHRLAQKL 440
Cdd:COG4913  440 ARLLALRDALAEAL 453
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 273-343 1.31e-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: 1.31e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19923830 273 DKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEA 343
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
225-344 1.84e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 225 MEEVERQVLPDPEVLEAVGDRQDGLREQLQApvppdsvpSLQNMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPK 304
Cdd:COG4372  61 LEQLEEELEQARSELEQLEEELEELNEQLQA--------AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19923830 305 GLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEAD 344
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 269-445 1.92e-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: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    269 GLLLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADcvrg 348
Cdd:TIGR02168  228 ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ---- 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    349 pdgvclsggrgpqgdkaIREQGPREQEPElsflKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLQDasrgdpaHAG 428
Cdd:TIGR02168  304 -----------------KQILRERLANLE----RQLEELEAQLEELESKLDELAEELAELEEKLEELKEE-------LES 355

                          170
                   ....*....|....*..
gi 19923830    429 LAELGHRLAQKLQGLEN 445
Cdd:TIGR02168  356 LEAELEELEAELEELES 372
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 266-443 2.07e-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: 41.29  E-value: 2.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 266 QNMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADC 345
Cdd:COG4942  34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 346 VR----GPDGVCLSGGRGPQGDK----------AIREQ--GPREQEPELSFLKQK-EQLEAEAQALRQELERQRRLLGSV 408
Cdd:COG4942 114 YRlgrqPPLALLLSPEDFLDAVRrlqylkylapARREQaeELRADLAELAALRAElEAERAELEALLAELEEERAALEAL 193

                       170       180       190
                ....*....|....*....|....*....|....*
gi 19923830 409 QQDLERSLQDASRGDPAHAGLAELGHRLAQKLQGL 443
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
273-432 2.68e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.81  E-value: 2.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 273 DKLAKEN-QDIRLLQAQLQAQKEELQSLmhqpkglEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEAdcvrgpdg 351
Cdd:COG1842  83 EDLAREAlERKAELEAQAEALEAQLAQL-------EEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKA-------- 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 352 vclsggrgpqgDKAIREQ--GPREQEPELSF--LKQK-EQLEAEAQALRqELERQRrllgsvqqDLERSLQDASRGDPAH 426
Cdd:COG1842 148 -----------QEKVNEAlsGIDSDDATSALerMEEKiEEMEARAEAAA-ELAAGD--------SLDDELAELEADSEVE 207


                ....*.
gi 19923830 427 AGLAEL 432
Cdd:COG1842 208 DELAAL 213
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 249-418 2.86e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 39.98  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830   249 LREQLQAPVPPDSVPSLQnmgllldklAKENQDIRLLQAQLQAQKEELQSLMHQpkgLEEENAQLRGALQQGEAFQRALE 328
Cdd:pfam12795  56 LRQELAALQAKAEAAPKE---------ILASLSLEELEQRLLQTSAQLQELQNQ---LAQLNSQLIELQTRPERAQQQLS 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830   329 S---ELQQLRARLQGleadcvrgpdgvclsggrGPQGDKAIREQGPREQEPELSFLKQK-EQLEAEAQA--LRQELERQR 402
Cdd:pfam12795 124 EarqRLQQIRNRLNG------------------PAPPGEPLSEAQRWALQAELAALKAQiDMLEQELLSnnNRQDLLKAR 185

                         170
                  ....*....|....*..
gi 19923830   403 R-LLGSVQQDLERSLQD 418
Cdd:pfam12795 186 RdLLTLRIQRLEQQLQA 202
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
265-421 3.13e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 3.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 265 LQNMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEAD 344
Cdd:COG4372  37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 345 cvrgpdgvcLSGGRGPQGDKAIREQGPREQEPELSFL-----KQKEQLEAEAQALRQELER-----QRRLLGSVQQDLER 414
Cdd:COG4372 117 ---------LEELQKERQDLEQQRKQLEAQIAELQSEiaereEELKELEEQLESLQEELAAleqelQALSEAEAEQALDE 187


                ....*..
gi 19923830 415 SLQDASR 421
Cdd:COG4372 188 LLKEANR 194
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
229-445 4.14e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 229 ERQVLPDPEVLEAVGDRQDGLREQLQAPVPPDSVPSL-QNMGLLLDKLAKENQDIRllQAQLQAQKEELQSLMHQPKGLE 307
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELlDRIEELQELLREAEELEE--ELQLEELEQEIAALLAEAGVED 383

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 308 EEnaQLRGALQQGEAFQrALESELQQLRARLQGLeadcvrgpdgvclsggrgpqgDKAIREQGPREQEPELSflKQKEQL 387
Cdd:COG4717 384 EE--ELRAALEQAEEYQ-ELKEELEELEEQLEEL---------------------LGELEELLEALDEEELE--EELEEL 437

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19923830 388 EAEAQALRQELERQRRLLGSVQQDLERSLQDASrgdpahagLAELGHRLAQKLQGLEN 445
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDGE--------LAELLQELEELKAELRE 487
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
239-420 7.34e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 7.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 239 LEAVGDRQDGLREQLQAPvpPDSVPSLQN---MGLLLDKLAKENQDIRLLQAQLQAQKEELQSLMHQpkgLEEENAQLRG 315
Cdd:COG3206 235 LAEAEARLAALRAQLGSG--PDALPELLQspvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQ 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830 316 ALQQGEAfqrALESELQQLRARLQGLEAdcvrgpdgvclsggrgpqgdkaireqgpreqepelsflkQKEQLEAEAQALR 395
Cdd:COG3206 310 EAQRILA---SLEAELEALQAREASLQA---------------------------------------QLAQLEARLAELP 347

                       170       180       190
                ....*....|....*....|....*....|.
gi 19923830 396 Q------ELERQRRLLGSVQQDLERSLQDAS 420
Cdd:COG3206 348 EleaelrRLEREVEVARELYESLLQRLEEAR 378
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 275-427 8.00e-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: 39.57  E-value: 8.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    275 LAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEEnaqlrgalqqgeafqralESELQQLRARLQGLEADCVRGPDGvcl 354
Cdd:TIGR00618  302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ------------------QSSIEEQRRLLQTLHSQEIHIRDA--- 360

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19923830    355 sgGRGPQGDKAIREQGPREQEPELSFLKQKEQLEAEAQALRQELERQRRLLGsvQQDLERSLQDASRGDPAHA 427
Cdd:TIGR00618  361 --HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQA--TIDTRTSAFRDLQGQLAHA 429
PRK11281 PRK11281
mechanosensitive channel MscK;
240-418 8.73e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.51  E-value: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830   240 EAVGDRQDGLREQL-QAPvppdsvPSLQNMGLLLDKLAKENQDI------RLLQAQLQAQKEELQSLMHQ-PKGLEEENA 311
Cdd:PRK11281   76 DRQKEETEQLKQQLaQAP------AKLRQAQAELEALKDDNDEEtretlsTLSLRQLESRLAQTLDQLQNaQNDLAEYNS 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830   312 QLRGALQQGEAFQRALES---ELQQLRARLQGLEAdcvrgpdgvclsggrgpqGDKAIREQgpreqepelsflkQKEQLE 388
Cdd:PRK11281  150 QLVSLQTQPERAQAALYAnsqRLQQIRNLLKGGKV------------------GGKALRPS-------------QRVLLQ 198

                         170       180       190
                  ....*....|....*....|....*....|..
gi 19923830   389 AEAQALRQELERQRRLL-GSVQ-QDLERSLQD 418
Cdd:PRK11281  199 AEQALLNAQNDLQRKSLeGNTQlQDLLQKQRD 230
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 308-418 9.95e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.18  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923830    308 EENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRgpDGVCLSggrgpqgdKAIREQgpREQEpelsFLKQKEQL 387
Cdd:smart00935  11 QESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQK--DAATLS--------EAAREK--KEKE----LQKKVQEF 74

                           90       100       110
                   ....*....|....*....|....*....|..
gi 19923830    388 EAEAQALRQELE-RQRRLLGSVQQDLERSLQD 418
Cdd:smart00935  75 QRKQQKLQQDLQkRQQEELQKILDKINKAIKE 106
 
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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