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Conserved domains on  [gi|221039926|dbj|BAH11726|]
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unnamed protein product [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
24-186 2.59e-12

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 2.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  24 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 103
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 104 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-AQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 182
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeELLEALRAAAELAAQLEELEEAEEALLERLERL 419

                 ....
gi 221039926 183 NSQL 186
Cdd:COG1196  420 EEEL 423
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
24-186 2.59e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 2.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  24 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 103
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 104 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-AQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 182
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeELLEALRAAAELAAQLEELEEAEEALLERLERL 419

                 ....
gi 221039926 183 NSQL 186
Cdd:COG1196  420 EEEL 423
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
23-178 5.38e-12

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: 68.93  E-value: 5.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTN-------LQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKK 95
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    96 CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 175
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940

                   ...
gi 221039926   176 MKD 178
Cdd:TIGR02168  941 LQE 943
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
32-186 3.26e-11

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 62.26  E-value: 3.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   32 DLKEKEDTIKQRTsevQDLQDEVQRE-NTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 110
Cdd:pfam08614  11 RLLDRTALLEAEN---AKLQSEPESVlPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  111 TSQESQISTYEEELAKAREELSRLQQETAELEESVEsGKAQLeplqqhLQDSQQEISSMQMKL--ME--MKDLENHNSQL 186
Cdd:pfam08614  88 QELEKKLREDERRLAALEAERAQLEEKLKDREEELR-EKRKL------NQDLQDELVALQLQLnmAEekLRKLEKENREL 160
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
23-180 4.65e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.23  E-value: 4.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRT-SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQLEEQLKEVRKKCAEEAQ 101
Cdd:PRK03918 562 EKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KLEEELDKAFEELAETEK 640
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221039926 102 LISSLKAELTSQESQIStyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 180
Cdd:PRK03918 641 RLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
83-186 4.02e-04

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 41.87  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  83 AQLEEQLKEVRKKCAEEAQLISSLKAEltsQESQISTYEEeLAKAREELSRLQ-QETAELEESVESGKAQLEPLQQHLQD 161
Cdd:cd16855    4 LEIRQQLEELRQRTQETENDLRNLQQK---QESFVIQYQE-SQKIQAQLQQLQqQPQNERIELEQQLQQQKEQLEQLLNA 79
                         90       100
                 ....*....|....*....|....*.
gi 221039926 162 SQQEISSMQMKLME-MKDLENHNSQL 186
Cdd:cd16855   80 KAQELLQLRMELADkFKKTIQLLSKL 105
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
73-182 5.97e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.31  E-value: 5.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    73 ELLDELDEQKAQL---EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-EEELAKAREELSRLQQE-------TAEL 141
Cdd:smart00787 151 ENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEimikvkkLEEL 230
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 221039926   142 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 182
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK 271
growth_prot_Scy NF041483
polarized growth protein Scy;
33-170 8.22e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.42  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   33 LKEKEDTIKQR-TSEVQDLQDEVQRENTnlQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAqliSSLK-AEL 110
Cdd:NF041483 1119 IRERAEELRDRiTGEIEELHERARRESA--EQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANSEA---SKVRiAAV 1193
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221039926  111 TSQESQISTYEEELAKAREELSRLQQET-AELEESVESGKAQLEPLQQHLQDSQQEISSMQ 170
Cdd:NF041483 1194 KKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQ 1254
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
24-186 2.59e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 2.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  24 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 103
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 104 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-AQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 182
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeELLEALRAAAELAAQLEELEEAEEALLERLERL 419

                 ....
gi 221039926 183 NSQL 186
Cdd:COG1196  420 EEEL 423
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
23-178 5.38e-12

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: 68.93  E-value: 5.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTN-------LQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKK 95
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    96 CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 175
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940

                   ...
gi 221039926   176 MKD 178
Cdd:TIGR02168  941 LQE 943
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
11-175 5.52e-12

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: 68.93  E-value: 5.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    11 SQHRDPHcdPSDKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 90
Cdd:TIGR02168  270 EELRLEV--SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    91 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 170
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427

                   ....*
gi 221039926   171 MKLME 175
Cdd:TIGR02168  428 KKLEE 432
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
24-166 6.73e-12

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: 65.33  E-value: 6.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  24 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKkcAEEAQli 103
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELE--------------IEEVEARIKKYEEQLGNVRN--NKEYE-- 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221039926 104 sSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 166
Cdd:COG1579   93 -ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
29-180 7.76e-12

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 67.23  E-value: 7.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  29 VEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA 108
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221039926 109 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 180
Cdd:COG4372  109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
32-186 3.26e-11

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 62.26  E-value: 3.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   32 DLKEKEDTIKQRTsevQDLQDEVQRE-NTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 110
Cdd:pfam08614  11 RLLDRTALLEAEN---AKLQSEPESVlPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  111 TSQESQISTYEEELAKAREELSRLQQETAELEESVEsGKAQLeplqqhLQDSQQEISSMQMKL--ME--MKDLENHNSQL 186
Cdd:pfam08614  88 QELEKKLREDERRLAALEAERAQLEEKLKDREEELR-EKRKL------NQDLQDELVALQLQLnmAEekLRKLEKENREL 160
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
23-170 4.78e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 64.54  E-value: 4.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:COG4372   51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL--EPLQQHLQDSQQEISSMQ 170
Cdd:COG4372  131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANRNAEKEE 200
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
23-187 7.26e-11

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 65.04  E-value: 7.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSmqmKLMEMKDLENH 182
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS---KEKELKKLNEE 504

                  ....*
gi 221039926  183 NSQLN 187
Cdd:TIGR04523 505 KKELE 509
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
23-187 7.30e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 7.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME-MKDLEN 181
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEaLRAAAE 397

                 ....*.
gi 221039926 182 HNSQLN 187
Cdd:COG1196  398 LAAQLE 403
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
24-187 3.69e-10

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: 63.16  E-value: 3.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    24 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAE-EAQL 102
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----------LKELEARIEELEEDLHKLEEALNDlEARL 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   103 ----ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK- 177
Cdd:TIGR02169  789 shsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEe 868
                          170
                   ....*....|
gi 221039926   178 DLENHNSQLN 187
Cdd:TIGR02169  869 ELEELEAALR 878
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
24-178 3.97e-10

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: 62.77  E-value: 3.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    24 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRkkcaeeaQLI 103
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK-------EEL 798
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221039926   104 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 178
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
80-169 4.83e-10

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: 61.70  E-value: 4.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  80 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHL 159
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                         90
                 ....*....|
gi 221039926 160 QDSQQEISSM 169
Cdd:COG4942  100 EAQKEELAEL 109
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
23-187 9.28e-10

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: 61.61  E-value: 9.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK-DLEN 181
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLElQIAS 397

                   ....*.
gi 221039926   182 HNSQLN 187
Cdd:TIGR02168  398 LNNEIE 403
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
23-170 1.01e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.47  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:COG4913   301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDR-------------LEQLEREIERLERELEERERRRARLEAL 367
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221039926  103 ISSLKAELTSQESQistYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 170
Cdd:COG4913   368 LAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
23-168 2.24e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEEELAELE--------------EELEELEEELEELEEELEEAEEELEEAEAE 359
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221039926 103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 168
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
23-166 2.24e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221039926 103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 166
Cdd:COG1196  388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
24-170 2.49e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  24 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 103
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221039926 104 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 170
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
23-185 2.66e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 182
Cdd:COG1196  325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404

                 ...
gi 221039926 183 NSQ 185
Cdd:COG1196  405 LEE 407
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
22-187 2.98e-09

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: 60.07  E-value: 2.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    22 DKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQ 101
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   102 LISSLKAELTSQESQISTYEEELAKA------------REELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 169
Cdd:TIGR02168  408 RLERLEDRRERLQQEIEELLKKLEEAelkelqaeleelEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
                          170
                   ....*....|....*...
gi 221039926   170 QMKLMEMKDLENHNSQLN 187
Cdd:TIGR02168  488 QARLDSLERLQENLEGFS 505
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
75-164 3.03e-09

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: 59.01  E-value: 3.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  75 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 154
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
                         90
                 ....*....|
gi 221039926 155 LQQHLQDSQQ 164
Cdd:COG4942  109 LLRALYRLGR 118
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-181 6.07e-09

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: 58.93  E-value: 6.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVqRENTNLqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDASRKI-GEIEKE-------------IEQLEQEEEKLKERLEELEEDLSSLEQE 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   103 ISSLKAELTSQESQISTYEEELAKAREELSRL------------QQETAELEESVESGKAQLEPLQQHLQDSQQEI---- 166
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKeyle 832
                          170
                   ....*....|....*
gi 221039926   167 SSMQMKLMEMKDLEN 181
Cdd:TIGR02169  833 KEIQELQEQRIDLKE 847
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
23-170 7.63e-09

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: 57.85  E-value: 7.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAE---E 99
Cdd:COG4942   47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAELEAQKEELAEllrA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 100 AQLISS-------LKAELTSQESQISTYEEELAKAR----EELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 168
Cdd:COG4942  113 LYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192

                 ..
gi 221039926 169 MQ 170
Cdd:COG4942  193 LK 194
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
22-182 9.75e-09

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: 58.53  E-value: 9.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    22 DKREKNNVEqdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQ 101
Cdd:TIGR02168  768 ERLEEAEEE--LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   102 LISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLEN 181
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925

                   .
gi 221039926   182 H 182
Cdd:TIGR02168  926 Q 926
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
73-187 1.16e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.22  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 152
Cdd:COG4372   24 ILIAALSEQLRKALFELDKLQEE-------LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 221039926 153 EPLQQHLQDSQQEISSMQMKLM----EMKDLENHNSQLN 187
Cdd:COG4372   97 AQAQEELESLQEEAEELQEELEelqkERQDLEQQRKQLE 135
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
23-165 1.60e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQK--QQVQELLDELDEQKAQLEEQLKEVRKKCAEEA 100
Cdd:COG4717   94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAelAELPERLEELEERLEELRELEEELEELEAELA 173
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221039926 101 QLISSLKAEL----TSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 165
Cdd:COG4717  174 ELQEELEELLeqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
31-173 1.69e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  31 QDLKEKEDTIKQ--RTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA 108
Cdd:COG1196  216 RELKEELKELEAelLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221039926 109 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 173
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
20-180 1.75e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  20 PSDKREKNNVEQ--DLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELD---------EQKAQLEEQ 88
Cdd:COG4717   61 PQGRKPELNLKElkELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAE 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  89 LKEVR---KKCAEEAQLISSLKAELTSQESQISTYEEELAKA--------REELSRLQQETAELEESVESGKAQLEPLQQ 157
Cdd:COG4717  141 LAELPerlEELEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRLAELEEELEEAQE 220
                        170       180
                 ....*....|....*....|...
gi 221039926 158 HLQDSQQEISSMQMKLMEMKDLE 180
Cdd:COG4717  221 ELEELEEELEQLENELEAAALEE 243
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
23-170 2.15e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:COG1196  364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221039926 103 ISSLKAELTSQEsqistyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 170
Cdd:COG1196  444 LEEAAEEEAELE-------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
75-182 2.79e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 56.56  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  75 LDELDEQKAQLEEQLKEVRKKCAE--EAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 152
Cdd:COG3206  177 LEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAL 256
                         90       100       110
                 ....*....|....*....|....*....|....
gi 221039926 153 EPLQQH--LQDSQQEISSMQMKLMEMKD--LENH 182
Cdd:COG3206  257 PELLQSpvIQQLRAQLAELEAELAELSAryTPNH 290
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
78-177 3.60e-08

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 54.06  E-value: 3.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  78 LDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEE--ELA--KAREELSR--LQQEtAELEESVESGKAQ 151
Cdd:COG1842   28 LDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEkaRLAleKGREDLAReaLERK-AELEAQAEALEAQ 106
                         90       100
                 ....*....|....*....|....*.
gi 221039926 152 LEPLQQHLQDSQQEISSMQMKLMEMK 177
Cdd:COG1842  107 LAQLEEQVEKLKEALRQLESKLEELK 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
23-181 4.45e-08

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: 56.22  E-value: 4.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    23 KREKNNVE-----QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLqklqaqkQQVQELLDELDEQKAQLEEQLKEVRKKCA 97
Cdd:TIGR02168  219 KAELRELElallvLRLEELREELEELQEELKEAEEELEELTAEL-------QELEEKLEELRLEVSELEEEIEELQKELY 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    98 EEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK 177
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371

                   ....
gi 221039926   178 DLEN 181
Cdd:TIGR02168  372 SRLE 375
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
23-180 4.65e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.23  E-value: 4.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRT-SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQLEEQLKEVRKKCAEEAQ 101
Cdd:PRK03918 562 EKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KLEEELDKAFEELAETEK 640
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221039926 102 LISSLKAELTSQESQIStyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 180
Cdd:PRK03918 641 RLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
23-146 5.43e-08

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: 53.78  E-value: 5.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTS---------EVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVR 93
Cdd:COG1579   58 EKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKE---------------------IESLKRRISDLEDEILELM 116
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 221039926  94 KKCAEEAQLISSLKAELTSQESQIST----YEEELAKAREELSRLQQETAELEESVE 146
Cdd:COG1579  117 ERIEELEEELAELEAELAELEAELEEkkaeLDEELAELEAELEELEAEREELAAKIP 173
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
29-180 7.51e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 55.41  E-value: 7.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  29 VEQDLKEKEDTIKQRTS----EVQDLQDEVQ---------RENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKK 95
Cdd:COG3206  162 LEQNLELRREEARKALEfleeQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  96 CAE-EAQL---------------ISSLKAELTSQESQI----STY----------EEELAKAREEL-SRLQQETAELEES 144
Cdd:COG3206  242 LAAlRAQLgsgpdalpellqspvIQQLRAQLAELEAELaelsARYtpnhpdvialRAQIAALRAQLqQEAQRILASLEAE 321
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 221039926 145 VESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 180
Cdd:COG3206  322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLE 357
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
73-175 8.26e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 8.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   73 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ--------ESQISTYEEELAKAREELSRLQQETAELEES 144
Cdd:COG4913   295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLP 374
                          90       100       110
                  ....*....|....*....|....*....|.
gi 221039926  145 VESGKAQLEPLQQHLQDSQQEISSMQMKLME 175
Cdd:COG4913   375 LPASAEEFAALRAEAAALLEALEEELEALEE 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
23-170 8.46e-08

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: 55.45  E-value: 8.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221039926   103 ISSLKAELTSQESQIS-------TYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 170
Cdd:TIGR02168  756 LTELEAEIEELEERLEeaeeelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
19-150 8.49e-08

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 55.25  E-value: 8.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  19 DPSDKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR-ENTnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCA 97
Cdd:COG2433  394 EPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEElEAE---------------LEEKDERIERLERELSEARSEER 458
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 221039926  98 EEAQL---ISSLKAELTSQESQISTYEEELAKAREELSRLQqetaELEESVESGKA 150
Cdd:COG2433  459 REIRKdreISRLDREIERLERELEEERERIEELKRKLERLK----ELWKLEHSGEL 510
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
73-168 1.06e-07

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: 54.38  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 152
Cdd:COG4942  150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
                         90
                 ....*....|....*.
gi 221039926 153 EPLQQHLQDSQQEISS 168
Cdd:COG4942  230 ARLEAEAAAAAERTPA 245
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
80-186 1.18e-07

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 50.72  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   80 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQeSQIST-----YEEELAK----------AREELSRLQQETAELEES 144
Cdd:pfam07926   1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQ-AEIAReaqqnYERELVLhaedikalqaLREELNELKAEIAELKAE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 221039926  145 VESGKAQLEPLQQHLQDS----QQEISSMQMKLmemKDLENHNSQL 186
Cdd:pfam07926  80 AESAKAELEESEESWEEQkkelEKELSELEKRI---EDLNEQNKLL 122
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
38-141 1.26e-07

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: 54.00  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  38 DTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQI 117
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELE--------------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
                         90       100
                 ....*....|....*....|....
gi 221039926 118 STYEEELAKAREELSRLQQETAEL 141
Cdd:COG4942   86 AELEKEIAELRAELEAQKEELAEL 109
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-160 1.75e-07

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: 54.30  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelldeLDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR02169  398 KREINELKRELDRLQEELQRLSEELADLNAAIAG---------------------IEAKINELEEEKEDKALEIKKQEWK 456
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221039926   103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE-------ESVESGKAQLEPLQQHLQ 160
Cdd:TIGR02169  457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaqaraseERVRGGRAVEEVLKASIQ 521
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
25-178 1.88e-07

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 53.11  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   25 EKNN-VEQDLKEKEDTIKQRTSEVQ---DL-----QDEVQRENTNLQKLQAQKQQVQEL------LDELDEQKAQLEEQL 89
Cdd:pfam04849 101 ERNEaLEEQLGSAREEILQLRHELSkkdDLlqiysNDAEESETESSCSTPLRRNESFSSlhgcvqLDALQEKLRGLEEEN 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   90 KEVRKKC-----------AEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETA-------ELEESVESGKAQ 151
Cdd:pfam04849 181 LKLRSEAshlktetdtyeEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITsllaqivDLQHKCKELGIE 260
                         170       180
                  ....*....|....*....|....*..
gi 221039926  152 LEPLQQHLQDSQQEISSMQMKLMEMKD 178
Cdd:pfam04849 261 NEELQQHLQASKEAQRQLTSELQELQD 287
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-173 1.97e-07

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: 54.30  E-value: 1.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR02169  293 KEKIGELEAEIASLERSIAEKERELEDAEERLA-----------------KLEAEIDKLLAEIEELEREIEEERKRRDKL 355
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221039926   103 ---ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 173
Cdd:TIGR02169  356 teeYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
29-148 2.06e-07

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: 53.23  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  29 VEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA 108
Cdd:COG4942  144 LAPARREQAEELRADLAELAALRAELEAE-----------------RAELEALLAELEEERAALEALKAERQKLLARLEK 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 221039926 109 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESG 148
Cdd:COG4942  207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
32-169 4.31e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 4.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  32 DLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDEL------DEQKAQLEEQLKEVRKKCAEEAQLI-- 103
Cdd:COG4717  341 ELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELraaleqAEEYQELKEELEELEEQLEELLGELee 420
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221039926 104 -------SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqLEPLQQHLQDSQQEISSM 169
Cdd:COG4717  421 llealdeEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELREL 488
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
33-275 4.50e-07

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 52.90  E-value: 4.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   33 LKEKEDTIKQRTSEVQDLQDEvqrentnlqkLQAQKQQVQELLDELD--EQKA--------QLEEQLKEVRKKCAEEAQL 102
Cdd:pfam10174 354 LEEKESFLNKKTKQLQDLTEE----------KSTLAGEIRDLKDMLDvkERKInvlqkkieNLQEQLRDKDKQLAGLKER 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETaELEESVEsgKAQLEPLQQHLQDSQQEISSMQMKLME----MKD 178
Cdd:pfam10174 424 VKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQR-EREDRER--LEELESLKKENKDLKEKVSALQPELTEkessLID 500
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  179 LENHNSQLNwcSSPHSIlvngatdycsLSTSSSETANLNEHVEGQSNLESE--PIHQ-ESPARSSPELLPSGVTDENEVT 255
Cdd:pfam10174 501 LKEHASSLA--SSGLKK----------DSKLKSLEIAVEQKKEECSKLENQlkKAHNaEEAVRTNPEINDRIRLLEQEVA 568
                         250       260       270
                  ....*....|....*....|....*....|..
gi 221039926  256 TAVTE--KVCSELD----------NNRHSKEE 275
Cdd:pfam10174 569 RYKEEsgKAQAEVErllgilreveNEKNDKDK 600
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
33-185 5.23e-07

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 50.29  E-value: 5.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   33 LKEKEDTIKQRTSEVQDLQ---DEVQRENtnlqklqaqkqqvqELLDELdeQKAQlEEQLKEVRKKCAEEAQLISSLKAE 109
Cdd:pfam15619   6 LSARLHKIKELQNELAELQsklEELRKEN--------------RLLKRL--QKRQ-EKALGKYEGTESELPQLIARHNEE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  110 L--------------TSQESQISTYEEELAKAREELSRLQQ--------ETAELEEsvesgkaQLEPLQQHLQDSQQEIS 167
Cdd:pfam15619  69 VrvlrerlrrlqekeRDLERKLKEKEAELLRLRDQLKRLEKlsedknlaEREELQK-------KLEQLEAKLEDKDEKIQ 141
                         170
                  ....*....|....*...
gi 221039926  168 SMQMKLmemkDLENHNSQ 185
Cdd:pfam15619 142 DLERKL----ELENKSFR 155
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
23-168 5.76e-07

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 52.53  E-value: 5.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLqDEVQRENtnlqklqaqkqqvqelldelDEQKAQLEEQLKEVRKKCAEEA-- 100
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQEL-LESEEKN--------------------REEVEQLKDLYRELRKSLLANRfs 162
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221039926 101 --QLISSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 168
Cdd:PRK04778 163 fgPALDELEKQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKA 237
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
23-186 5.80e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 5.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 103 ISSLKAELTSQESQIstyeEELAKAREEL-SRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLEN 181
Cdd:COG1196  332 LEELEEELEELEEEL----EEAEEELEEAeAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                 ....*
gi 221039926 182 HNSQL 186
Cdd:COG1196  408 AEEAL 412
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
25-187 7.15e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.33  E-value: 7.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   25 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKlqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 104
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK---------SELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  105 SLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS-------QQEISSMQ----MKL 173
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklnqqkDEQIKKLQqekeLLE 425
                         170
                  ....*....|....
gi 221039926  174 MEMKDLENHNSQLN 187
Cdd:TIGR04523 426 KEIERLKETIIKNN 439
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
25-186 7.53e-07

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 52.48  E-value: 7.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    25 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 104
Cdd:pfam01576   97 EKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAK 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   105 SLKAELTSQESQISTYEEEL---AKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME-- 175
Cdd:pfam01576  177 SLSKLKNKHEAMISDLEERLkkeEKGRQELEkakrKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEet 256
                          170       180
                   ....*....|....*....|
gi 221039926   176 ---------MKDLENHNSQL 186
Cdd:pfam01576  257 aqknnalkkIRELEAQISEL 276
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-180 8.48e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 8.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  28 NVEQDLKEKED---TIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 104
Cdd:PRK03918 190 NIEELIKEKEKeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221039926 105 SLKAELTSQESQISTYEE--ELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 180
Cdd:PRK03918 270 ELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL 347
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
23-167 1.15e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.56  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221039926  103 ISSLKAELTSQESQISTYEEELAKAREELSR---------LQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 167
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK 599
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
73-168 1.47e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.17  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQKAQLEEqlkevrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL---QQETAELEESVESGK 149
Cdd:COG3206  295 ALRAQIAALRAQLQQ----------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVAR 364
                         90
                 ....*....|....*....
gi 221039926 150 AQLEPLQQHLQDSQQEISS 168
Cdd:COG3206  365 ELYESLLQRLEEARLAEAL 383
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
29-161 1.70e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.19  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  29 VEQDLKEKEDTIKQRTSEVQDLQDEV--QRENTNLQKLQAQKQQVQELLDELD-----EQKAQLEEQLKEVRKKCAEEAQ 101
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVrdLRERLEELEEERDDLLAEAGLDDADaeaveARREELEDRDEELRDRLEECRV 335
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 102 LISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQD 161
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
13-175 1.72e-06

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: 51.22  E-value: 1.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    13 HRDPHCDPSDKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqVQELLDELDEQKAQLEEQLKEV 92
Cdd:TIGR02169  659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENR-------------LDELSQELSDASRKIGEIEKEI 725
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    93 RKKCAEEAQLisslKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMK 172
Cdd:TIGR02169  726 EQLEQEEEKL----KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS 801

                   ...
gi 221039926   173 LME 175
Cdd:TIGR02169  802 KLE 804
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
24-187 2.06e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.79  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   24 REKNN-VEQDLKEKE---DTIKQRTSEVQDLQDEVQ---RENTNLQKLQAQKQQVQELLDE----LDEQKAQLEEQLKEV 92
Cdd:TIGR04523 366 EEKQNeIEKLKKENQsykQEIKNLESQINDLESKIQnqeKLNQQKDEQIKKLQQEKELLEKeierLKETIIKNNSEIKDL 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   93 RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMK 172
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
                         170
                  ....*....|....*
gi 221039926  173 lmeMKDLENHNSQLN 187
Cdd:TIGR04523 526 ---IEKLESEKKEKE 537
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
23-188 2.21e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.79  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD-LEN 181
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDeLNK 549

                  ....*..
gi 221039926  182 HNSQLNW 188
Cdd:TIGR04523 550 DDFELKK 556
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
73-180 2.38e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYE---EELAKAREELSRLQQETAELEESVESGK 149
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGSKRKLE 258
                         90       100       110
                 ....*....|....*....|....*....|.
gi 221039926 150 AQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 180
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKELK 289
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
31-169 2.56e-06

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 48.28  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   31 QDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkael 110
Cdd:pfam06785  83 EGFKILEETLEELQSEEERLEEELSQKE--------------EELRRLTEENQQLQIQLQQISQDFAEF----------- 137
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 221039926  111 tSQESqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 169
Cdd:pfam06785 138 -RLES-----EEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTL 190
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
9-141 2.87e-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: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    9 LKSQHRDphcdpSDKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR----ENTNLQKLQAQKQQVQELLDELDEQKAQ 84
Cdd:COG4913   328 LEAQIRG-----NGGDRLEQLEREIERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEA 402
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221039926   85 LEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR-LQQETAEL 141
Cdd:COG4913   403 LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAEL 460
TMF_DNA_bd pfam12329
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ...
73-142 3.03e-06

TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.


Pssm-ID: 372049 [Multi-domain]  Cd Length: 74  Bit Score: 44.99  E-value: 3.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   73 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE 142
Cdd:pfam12329   5 KLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
35-165 3.57e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  35 EKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEqkAQLEEQLKEVRKKCAEEAQLISSLKAELTSQE 114
Cdd:COG4717  382 EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELE 459
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 221039926 115 SQISTYEE--ELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 165
Cdd:COG4717  460 AELEQLEEdgELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-178 3.98e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  79 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 158
Cdd:COG4372    2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
                         90       100
                 ....*....|....*....|
gi 221039926 159 LQDSQQEISSMQMKLMEMKD 178
Cdd:COG4372   82 LEELNEQLQAAQAELAQAQE 101
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
26-162 4.43e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 49.45  E-value: 4.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  26 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDeqkaQLEEQLKEVRKKCAEEAQLISS 105
Cdd:PRK04778 305 RKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLE----SLEKQYDEITERIAEQEIAYSE 380
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 221039926 106 LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS 162
Cdd:PRK04778 381 LQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKS 437
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
22-172 5.70e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 5.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  22 DKREK-NNVEQDLKEKEDTIKQRTSEVQDLQDE------------VQRENtnlqkLQAQKQQVQELLDELDEQKAQLEEQ 88
Cdd:PRK02224 360 ELREEaAELESELEEAREAVEDRREEIEELEEEieelrerfgdapVDLGN-----AEDFLEELREERDELREREAELEAT 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  89 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQhLQDSQQEISS 168
Cdd:PRK02224 435 LRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIER 513

                 ....
gi 221039926 169 MQMK 172
Cdd:PRK02224 514 LEER 517
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
23-155 5.71e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 5.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:COG4372   72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 221039926 103 ISSLKAELTSQESQISTYEEEL-----AKAREELSRLQQETAELEESVESGKAQLEPL 155
Cdd:COG4372  152 LKELEEQLESLQEELAALEQELqalseAEAEQALDELLKEANRNAEKEEELAEAEKLI 209
PRK12704 PRK12704
phosphodiesterase; Provisional
76-181 6.01e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.01  E-value: 6.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  76 DELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPL 155
Cdd:PRK12704  64 EEIHKLRNEFEKELRERRNE-------LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136
                         90       100
                 ....*....|....*....|....*....
gi 221039926 156 QQHLQDSQQEISSMQM---KLMEMKDLEN 181
Cdd:PRK12704 137 IEEQLQELERISGLTAeeaKEILLEKVEE 165
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
73-175 6.19e-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: 6.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQKAQLE-EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 151
Cdd:COG1196  217 ELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
                         90       100
                 ....*....|....*....|....
gi 221039926 152 LEPLQQHLQDSQQEISSMQMKLME 175
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEE 320
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-169 6.38e-06

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: 49.30  E-value: 6.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE-EAQ 101
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDlESR 883
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   102 L------ISSLKAELTSQESQISTYEEELAKAREELSRLQ-------QETAELEESVESGK------AQLEPLQQHLQDS 162
Cdd:TIGR02169  884 LgdlkkeRDELEAQLRELERKIEELEAQIEKKRKRLSELKaklealeEELSEIEDPKGEDEeipeeeLSLEDVQAELQRV 963

                   ....*..
gi 221039926   163 QQEISSM 169
Cdd:TIGR02169  964 EEEIRAL 970
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
74-187 6.67e-06

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: 49.28  E-value: 6.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    74 LLDELDEQKAQLEEQLKEV----RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE--- 146
Cdd:TIGR02168  194 ILNELERQLKSLERQAEKAerykELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEelr 273
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 221039926   147 ----SGKAQLEPLQQHLQDSQQEISSMQMKLM----EMKDLENHNSQLN 187
Cdd:TIGR02168  274 levsELEEEIEELQKELYALANEISRLEQQKQilreRLANLERQLEELE 322
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
73-173 7.37e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 7.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   73 ELLDELDEQKAQLEEQLKEVRKKCAEEAQL---------ISSLKAELTSQESQISTYEE---ELAKAREELSRLQQETAE 140
Cdd:COG4913   624 EELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEE 703
                          90       100       110
                  ....*....|....*....|....*....|...
gi 221039926  141 LEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 173
Cdd:COG4913   704 LEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
109-179 7.58e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 7.58e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221039926 109 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDL 179
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
74-186 7.71e-06

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: 47.61  E-value: 7.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  74 LLD--ELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 151
Cdd:COG1579    9 LLDlqELDSELDRLEHRLKELPAE-------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 221039926 152 L---------EPLQQHLQDSQQEISSMQMKLME-MKDLENHNSQL 186
Cdd:COG1579   82 LgnvrnnkeyEALQKEIESLKRRISDLEDEILElMERIEELEEEL 126
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-180 9.78e-06

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: 48.53  E-value: 9.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    23 KREKNNVE--QDLK-EKEDT-IKQRTSEVQDLqdEVQRENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAE 98
Cdd:TIGR02169  204 RREREKAEryQALLkEKREYeGYELLKEKEAL--ERQKEAIERQ------------LASLEEELEKLTEEISELEKRLEE 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    99 EAQLISSLKAELTSQEsqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSmqmKLMEMKD 178
Cdd:TIGR02169  270 IEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK---LLAEIEE 340

                   ..
gi 221039926   179 LE 180
Cdd:TIGR02169  341 LE 342
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
75-186 1.01e-05

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: 48.80  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   75 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ--- 151
Cdd:COG3096   524 LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapa 603
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 221039926  152 -------LEPLQQH----LQDSQQEISSMQMKLMEMKDLENHNSQL 186
Cdd:COG3096   604 wlaaqdaLERLREQsgeaLADSQEVTAAMQQLLEREREATVERDEL 649
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
38-168 1.05e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  38 DTIKQRTSEVQDLQDEVQRENTNLQKLQAqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQI 117
Cdd:COG3883  125 SKIADADADLLEELKADKAELEAKKAELE------AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 221039926 118 STYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 168
Cdd:COG3883  199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
23-183 1.09e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK--------------YNDLKKQKEELENELNLLEKEKLNIQKN 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  103 ISSLKAELTSQESQISTYEEELAKAREelsrLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 182
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNKS----LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264

                  .
gi 221039926  183 N 183
Cdd:TIGR04523 265 I 265
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
23-183 1.22e-05

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 47.93  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   23 KREKNNVEQDLKEKEDTIKQRTSEVQDLqdeVQRENTNlqklqaqkqqvqelldelDEQKAQLEEQLKEVRKKCAEEA-- 100
Cdd:pfam06160  85 KKALDEIEELLDDIEEDIKQILEELDEL---LESEEKN------------------REEVEELKDKYRELRKTLLANRfs 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  101 --QLISSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 173
Cdd:pfam06160 144 ygPAIDELEKQLAEIEEEFSQFEELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREM 223
                         170
                  ....*....|.
gi 221039926  174 MEMK-DLENHN 183
Cdd:pfam06160 224 EEEGyALEHLN 234
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
96-186 1.56e-05

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: 47.45  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  96 CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 175
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
                         90
                 ....*....|..
gi 221039926 176 M-KDLENHNSQL 186
Cdd:COG4942   95 LrAELEAQKEEL 106
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
22-166 1.69e-05

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.83  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  22 DKREKNNVE-QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDEL-----------DEQK------A 83
Cdd:COG1340   64 EKRDELNEKvKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewrqqtevlspEEEKelvekiK 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  84 QLEEQLKEvRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 163
Cdd:COG1340  144 ELEKELEK-AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQ 222

                 ...
gi 221039926 164 QEI 166
Cdd:COG1340  223 EKA 225
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
31-170 1.79e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   31 QDLKEKEDTIKQRTSEVQDLQDEVQR-ENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 109
Cdd:COG4913   654 AEYSWDEIDVASAEREIAELEAELERlDASSDD------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221039926  110 LTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 170
Cdd:COG4913   722 LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARL 782
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
24-186 2.05e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  24 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE----- 98
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkelk 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  99 -EAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEE---SVESGKAQLEPLQQHLQDSQQEISSMQMKLM 174
Cdd:PRK03918 290 eKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEERHELYEEAKA 369
                        170
                 ....*....|..
gi 221039926 175 EMKDLENHNSQL 186
Cdd:PRK03918 370 KKEELERLKKRL 381
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
75-182 2.27e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  75 LDELDEQKAQLEEqLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELS--RLQQETAELEESVESGKAQL 152
Cdd:COG4717   70 LKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERL 148
                         90       100       110
                 ....*....|....*....|....*....|
gi 221039926 153 EPLQQHLQDSQQEISSMQMKLMEMKDLENH 182
Cdd:COG4717  149 EELEERLEELRELEEELEELEAELAELQEE 178
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
74-186 2.35e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  74 LLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE 153
Cdd:COG4717   47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 221039926 154 P---------LQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 186
Cdd:COG4717  127 LlplyqeleaLEAELAELPERLEELEERLEELRELEEELEEL 168
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
103-176 2.87e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 2.87e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221039926 103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM 176
Cdd:COG3883   18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
73-173 2.88e-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: 45.69  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETA---- 139
Cdd:COG1579   24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIEslkr 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 221039926 140 ----------ELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 173
Cdd:COG1579  104 risdledeilELMERIEELEEELAELEAELAELEAELEEKKAEL 147
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
25-145 2.99e-05

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 47.00  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  25 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 104
Cdd:COG0542  405 EIDSKPEELDELERRLEQLEIEKEALKKEQD-------------EASFERLAELRDELAELEEELEALKARWEAEKELIE 471
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 221039926 105 ---SLKAELTSQESQISTYEEELAKAREELSrlqQETAELEESV 145
Cdd:COG0542  472 eiqELKEELEQRYGKIPELEKELAELEEELA---ELAPLLREEV 512
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
23-180 3.23e-05

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: 46.30  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcaeeaql 102
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQ---------------------LAALERRIAALARRIRALEQE------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 103 ISSLKAELTSQESQISTYEEELAKAREELSRL--------QQETAEL---EESVESGKAQLEPLQQHLQDSQQEISSMQM 171
Cdd:COG4942   78 LAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRA 157

                 ....*....
gi 221039926 172 KLMEMKDLE 180
Cdd:COG4942  158 DLAELAALR 166
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
26-173 3.28e-05

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 45.44  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   26 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEaqLISS 105
Cdd:pfam04012  10 RANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEE--LARE 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221039926  106 LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQqhlqdSQQEISSMQMKL 173
Cdd:pfam04012  88 ALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLK-----ARLKAAKAQEAV 150
PRK12704 PRK12704
phosphodiesterase; Provisional
23-177 3.34e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQdlqdevQRENtnlqklqaqkqqvqelldeldeqkaQLEEQLKEVRKKcaeeaql 102
Cdd:PRK12704  67 HKLRNEFEKELRERRNELQKLEKRLL------QKEE-------------------------NLDRKLELLEKR------- 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 103 isslKAELTSQESQISTYEEELAKAREELSRLQQET-AELEE----SVESGKAQLepLQQHLQDSQQEISSMqMKLMEMK 177
Cdd:PRK12704 109 ----EEELEKKEKELEQKQQELEKKEEELEELIEEQlQELERisglTAEEAKEIL--LEKVEEEARHEAAVL-IKEIEEE 181
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
30-178 3.80e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  30 EQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAE 109
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAE---------------------LDALQAELEELNEEYNELQAE-------LEALQAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 110 LTSQESQISTYEEELAKAREEL------------------------------------SRLQQETAELEESVESGKAQLE 153
Cdd:COG3883   67 IDKLQAEIAEAEAEIEERREELgeraralyrsggsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELE 146
                        170       180
                 ....*....|....*....|....*
gi 221039926 154 PLQQHLQDSQQEISSMQMKLMEMKD 178
Cdd:COG3883  147 AKKAELEAKLAELEALKAELEAAKA 171
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
11-181 3.96e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  11 SQHRDPHCDPSDKREKNNVE-QDLKEKEDTIKQRTSEVQDLQ---DEVQRENTNLQKLQaqkqqvqELLDELDEQKAQLE 86
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAElEDLEEEVEEVEERLERAEDLVeaeDRIERLEERREDLE-------ELIAERRETIEEKR 536
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  87 EQLKEVRKKCAEeaqlissLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESgKAQLEPLQQHLQDSQQEI 166
Cdd:PRK02224 537 ERAEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAEDEI 608
                        170
                 ....*....|....*
gi 221039926 167 SSMQMKLMEMKDLEN 181
Cdd:PRK02224 609 ERLREKREALAELND 623
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
73-166 4.14e-05

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 45.30  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   73 ELLDELDEQKAQLEEQLKevrkkcaeeaqlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEEsvesGKAQL 152
Cdd:pfam11932  34 KKIDKWDDEKQELLAEYR--------------ALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIER----TEREL 95
                          90
                  ....*....|....
gi 221039926  153 EPLQQHLQDSQQEI 166
Cdd:pfam11932  96 VPLMLKMLDRLEQF 109
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
73-171 4.36e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 46.48  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   73 ELLDELDEQKAQLEEQLKEVrkkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAEleesvesgkAQL 152
Cdd:PRK11448  146 ALQQEVLTLKQQLELQAREK----AQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE---------TSQ 212
                          90
                  ....*....|....*....
gi 221039926  153 EPLQQHLQDSQQEISSMQM 171
Cdd:PRK11448  213 ERKQKRKEITDQAAKRLEL 231
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
23-188 5.78e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 5.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDtIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:PRK03918 175 KRRIERLEKFIKRTEN-IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQ------ETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLmem 176
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI--- 330
                        170
                 ....*....|..
gi 221039926 177 KDLENHNSQLNW 188
Cdd:PRK03918 331 KELEEKEERLEE 342
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
31-181 6.94e-05

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: 45.83  E-value: 6.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    31 QDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 110
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQ-----------------LERLRREREKAERYQALLKEKREYEGYELLKEKEAL 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   111 TSQ----ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPL--------QQHLQDSQQEISSMQ----MKLM 174
Cdd:TIGR02169  236 ERQkeaiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLErsiaEKER 315

                   ....*..
gi 221039926   175 EMKDLEN 181
Cdd:TIGR02169  316 ELEDAEE 322
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
75-178 7.44e-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: 45.82  E-value: 7.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    75 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 154
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100
                   ....*....|....*....|....
gi 221039926   155 LQQHLQDSQQEISSMQMKLMEMKD 178
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEA 782
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
74-181 7.55e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 7.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  74 LLDELDEQKAQLEEQlkevRKKcAEEAQlisSLKAELTSQESQISTYEeeLAKAREELSRLQQETAELEESVESGKAQLE 153
Cdd:COG1196  194 ILGELERQLEPLERQ----AEK-AERYR---ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELA 263
                         90       100
                 ....*....|....*....|....*...
gi 221039926 154 PLQQHLQDSQQEISSMQMKLMEMKDLEN 181
Cdd:COG1196  264 ELEAELEELRLELEELELELEEAQAEEY 291
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
30-167 8.49e-05

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: 44.21  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   30 EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK--EVRKKCAEEAQLIsSLK 107
Cdd:pfam12795  77 SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNgpAPPGEPLSEAQRW-ALQ 155
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221039926  108 AELTSQESQISTYEEELAKA--REELSRLQQETAeleesvesgKAQLEPLQQHLQDSQQEIS 167
Cdd:pfam12795 156 AELAALKAQIDMLEQELLSNnnRQDLLKARRDLL---------TLRIQRLEQQLQALQELLN 208
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
73-170 9.68e-05

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 45.07  E-value: 9.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   73 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQ----------ISTYEEELAKAREELSRLQQETAELE 142
Cdd:pfam05622 311 QLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssllkqkLEEHLEKLHEAQSELQKKKEQIEELE 390
                          90       100
                  ....*....|....*....|....*....
gi 221039926  143 ESVESGKAQ-LEPLQQHLQDSQQEISSMQ 170
Cdd:pfam05622 391 PKQDSNLAQkIDELQEALRKKDEDMKAME 419
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
81-187 1.22e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 44.27  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  81 QKAQLEEQLKEVrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSR---LQQETAELEESVESGKAQLEPLQQ 157
Cdd:COG1566   88 AEAQLAAAEAQL-----ARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERyqaLYKKGAVSQQELDEARAALDAAQA 162
                         90       100       110
                 ....*....|....*....|....*....|
gi 221039926 158 HLQDSQQEISSMQMKLMEMKDLENHNSQLN 187
Cdd:COG1566  163 QLEAAQAQLAQAQAGLREEEELAAAQAQVA 192
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
25-178 1.32e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  25 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQ--- 101
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaly 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 102 --------------------LISSLKA-------------ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESG 148
Cdd:COG3883   97 rsggsvsyldvllgsesfsdFLDRLSAlskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
                        170       180       190
                 ....*....|....*....|....*....|
gi 221039926 149 KAQLEPLQQHLQDSQQEISSMQMKLMEMKD 178
Cdd:COG3883  177 QAEQEALLAQLSAEEAAAEAQLAELEAELA 206
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-177 1.33e-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: 45.06  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   103 ISSLKAELTSQESQISTY-------EEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 175
Cdd:TIGR02169  394 LEKLKREINELKRELDRLqeelqrlSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473

                   ..
gi 221039926   176 MK 177
Cdd:TIGR02169  474 LK 475
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
75-166 1.43e-04

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 42.64  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   75 LDELDEQKAQLEEQL----KEVRKKCAEEAQ-LISSLKAELTSQESQISTYEEEL-AKAREELSRLQQETAEL-EESVES 147
Cdd:pfam01442   6 LDELSTYAEELQEQLgpvaQELVDRLEKETEaLRERLQKDLEEVRAKLEPYLEELqAKLGQNVEELRQRLEPYtEELRKR 85
                          90
                  ....*....|....*....
gi 221039926  148 GKAQLEPLQQHLQDSQQEI 166
Cdd:pfam01442  86 LNADAEELQEKLAPYGEEL 104
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
37-164 1.66e-04

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 42.64  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   37 EDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelldeLDEQKAQLEEQLKEVRKKCAEEAQLissLKAELtsqESQ 116
Cdd:pfam01442  25 QELVDRLEKETEALRERLQKD--------------------LEEVRAKLEPYLEELQAKLGQNVEE---LRQRL---EPY 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221039926  117 ISTYEEELAKAREELSR-LQQETAELEESVESG----KAQLEP--------LQQHLQDSQQ 164
Cdd:pfam01442  79 TEELRKRLNADAEELQEkLAPYGEELRERLEQNvdalRARLAPyaeelrqkLAERLEELKE 139
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
27-170 1.67e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   27 NNVEQdLKEKEDTIKQRTSEVQDLQDEVQRentnlqkLQAQKQQVQELLDELDEQKAQLEEQL--KEVRKKCAEEAQLIS 104
Cdd:COG4913   607 DNRAK-LAALEAELAELEEELAEAEERLEA-------LEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELE 678
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221039926  105 SLKA---ELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaQLEPLQQHLQDSQQEISSMQ 170
Cdd:COG4913   679 RLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLA 743
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
77-150 1.75e-04

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 43.44  E-value: 1.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221039926   77 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ-----ESQISTYEEELAKAREELSRLQQETAELEESVESGKA 150
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQlppekREQLEKLLETKNKLSEELEELEEELKELKEELESLLG 231
PRK09039 PRK09039
peptidoglycan -binding protein;
31-187 2.75e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.42  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  31 QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 110
Cdd:PRK09039  46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL 125
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221039926 111 TSQEsQIStyeeelAKAREELSRLQQETAELeesvesgKAQLEPLQQHLQDSQQEISSMQMKLmemKDLenhNSQLN 187
Cdd:PRK09039 126 DSEK-QVS------ARALAQVELLNQQIAAL-------RRQLAALEAALDASEKRDRESQAKI---ADL---GRRLN 182
mukB PRK04863
chromosome partition protein MukB;
21-181 2.79e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.18  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   21 SDKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREN----TNLQKLQAQKQQVQELL----DELDEQKAQLEEQLKEV 92
Cdd:PRK04863  932 SDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLNEKLrqrlEQAEQERTRAREQLRQA 1011
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   93 RKKCAEEAQLISSLKaeltsqeSQISTYEEELAKAREELSRLQ-QETAELEESVESGKaqlEPLQQHLQDSQQEISSMQM 171
Cdd:PRK04863 1012 QAQLAQYNQVLASLK-------SSYDAKRQMLQELKQELQDLGvPADSGAEERARARR---DELHARLSANRSRRNQLEK 1081
                         170
                  ....*....|....
gi 221039926  172 KL----MEMKDLEN 181
Cdd:PRK04863 1082 QLtfceAEMDNLTK 1095
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
21-187 2.82e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.96  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   21 SDKREKNNVE-------QDLKEKEDTIKQRTSEVQDLQD-EVQRENTNLQK--LQAQKQQVQELLDELDEQKAQLEEQLK 90
Cdd:pfam05557  24 EHKRARIELEkkasalkRQLDRESDRNQELQKRIRLLEKrEAEAEEALREQaeLNRLKKKYLEALNKKLNEKESQLADAR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   91 EV----RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKA---QLEPLQQHLQ--- 160
Cdd:pfam05557 104 EVisclKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQsqe 183
                         170       180       190
                  ....*....|....*....|....*....|....
gi 221039926  161 DSQQEISSMQMKLMEMKDLEN-------HNSQLN 187
Cdd:pfam05557 184 QDSEIVKNSKSELARIPELEKelerlreHNKHLN 217
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
23-185 2.92e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRtsEVQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEEQL---KEVRKKCAEE 99
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEK--EEKDLHERLNGLES-------ELAELDEEIERYEEQREQARETRdeaDEVLEEHEER 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 100 AQLISSLKAELTSQESQISTYE-------EELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMK 172
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETErereelaEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
                        170
                 ....*....|....
gi 221039926 173 LMEMK-DLENHNSQ 185
Cdd:PRK02224 330 LEECRvAAQAHNEE 343
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
73-157 3.09e-04

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 40.65  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   73 ELLDELDEQKAQLEEQLKEVrkkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETaelEESVESGKAQL 152
Cdd:pfam18595  40 KLLEEIEAELAKLEEAKKKL----KELRDALEEKEIELRELERREERLQRQLENAQEKLERLREQA---EEKREAAQARL 112

                  ....*
gi 221039926  153 EPLQQ 157
Cdd:pfam18595 113 EELRE 117
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
23-187 3.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ-------------RENTNLQKLQAQKQQVQEL------LDELDEQKA 83
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKELLEEYTAELkriekeLKEIEEKER 476
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  84 QLEEQLKEVRKKCAEEAQLIS--SLKAELTSQESQISTYE-EELAKAREELSRLQQETAELEESVESGKAQLEPLQQhLQ 160
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE-LK 555
                        170       180
                 ....*....|....*....|....*..
gi 221039926 161 DSQQEISSmqmklmEMKDLENHNSQLN 187
Cdd:PRK03918 556 KKLAELEK------KLDELEEELAELL 576
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
22-185 3.24e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.56  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   22 DKREK-NNVEQDLKEKEDTIKQR-------TSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaqlEEQLKEVR 93
Cdd:pfam05483 265 ESRDKaNQLEEKTKLQDENLKELiekkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK---EAQMEELN 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   94 KKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELS----RLQQETAELEESVE----------------------- 146
Cdd:pfam05483 342 KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKfknnkeveleelkkilaedekll 421
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 221039926  147 SGKAQLEPLQQHLQDSQQ-----------EISSMQMKLMEMKDLENHNSQ 185
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQelifllqarekEIHDLEIQLTAIKTSEEHYLK 471
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
5-180 3.39e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.88  E-value: 3.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926     5 VRDCLKSQHRDPHCDPSDKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqelldELDEQKAQ 84
Cdd:TIGR00606  222 IRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKK--------------QMEKDNSE 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    85 LEEQLKEVRKKCAEEaqlissLKAELTSQESQISTYEEELAKAREELSRLQQETAEL-----EESVESGKAQL--EPLQQ 157
Cdd:TIGR00606  288 LELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLnqektELLVEQGRLQLqaDRHQE 361
                          170       180
                   ....*....|....*....|...
gi 221039926   158 HLQDSQQEISSMQMKLmEMKDLE 180
Cdd:TIGR00606  362 HIRARDSLIQSLATRL-ELDGFE 383
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
74-173 3.48e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.82  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   74 LLDELDEQKaQLEEQLKEVRKKCAEEAQLISSlkaelTSQESQISTyeEELAKAREELSRLQQETAELE---ESVESGKA 150
Cdd:pfam13851  21 TRNNLELIK-SLKEEIAELKKKEERNEKLMSE-----IQQENKRLT--EPLQKAQEEVEELRKQLENYEkdkQSLKNLKA 92
                          90       100
                  ....*....|....*....|...
gi 221039926  151 QLEPLQQHLQDSQQEISSMQMKL 173
Cdd:pfam13851  93 RLKVLEKELKDLKWEHEVLEQRF 115
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
23-163 3.84e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQvqELLDELDEQKAQL--EEQLKEVRKKCAEEA 100
Cdd:COG4913   698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAAlgDAVERELRENLEERI 775
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  101 QLISSLKAELTSQ-ESQISTY-----------------------------EEELAKAREELSRLQQET---------AEL 141
Cdd:COG4913   776 DALRARLNRAEEElERAMRAFnrewpaetadldadleslpeylalldrleEDGLPEYEERFKELLNENsiefvadllSKL 855
                         170       180
                  ....*....|....*....|..
gi 221039926  142 EESVESGKAQLEPLQQHLQDSQ 163
Cdd:COG4913   856 RRAIREIKERIDPLNDSLKRIP 877
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
83-186 4.02e-04

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 41.87  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  83 AQLEEQLKEVRKKCAEEAQLISSLKAEltsQESQISTYEEeLAKAREELSRLQ-QETAELEESVESGKAQLEPLQQHLQD 161
Cdd:cd16855    4 LEIRQQLEELRQRTQETENDLRNLQQK---QESFVIQYQE-SQKIQAQLQQLQqQPQNERIELEQQLQQQKEQLEQLLNA 79
                         90       100
                 ....*....|....*....|....*.
gi 221039926 162 SQQEISSMQMKLME-MKDLENHNSQL 186
Cdd:cd16855   80 KAQELLQLRMELADkFKKTIQLLSKL 105
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
23-168 4.17e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 4.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR----------------ENTNLQKLQAQKQQVQELLDELD------E 80
Cdd:COG3883   50 NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelgeraralyrsgGSVSYLDVLLGSESFSDFLDRLSalskiaD 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  81 QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREElsrLQQETAELEESVESGKAQLEPLQQHLQ 160
Cdd:COG3883  130 ADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE---QEALLAQLSAEEAAAEAQLAELEAELA 206

                 ....*...
gi 221039926 161 DSQQEISS 168
Cdd:COG3883  207 AAEAAAAA 214
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
114-187 4.40e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 4.40e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221039926 114 ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM-KDLENHNSQLN 187
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeAEIEERREELG 89
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
79-179 4.66e-04

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 40.74  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   79 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL-TSQESQ------ISTYEEELAKAREELSRLQQETAELEESVESGKAQ 151
Cdd:pfam10473   2 EKKQLHVLEKLKESERKADSLKDKVENLERELeMSEENQelaileAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81
                          90       100
                  ....*....|....*....|....*...
gi 221039926  152 LEPLQQHLQDSQQEISSMQMKLMEMKDL 179
Cdd:pfam10473  82 KENLTKELQKKQERVSELESLNSSLENL 109
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
37-181 4.79e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  37 EDTIKQRTSEVQDLQDEVQREntnLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRkkcaEEAqlisslkAELtsqESQ 116
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDR---LEECRVAAQAHNEEAESLREDADDLEERAEELR----EEA-------AEL---ESE 371
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221039926 117 ISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK-DLEN 181
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEaTLRT 437
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
23-166 4.94e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCA--EEA 100
Cdd:COG4372  100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalSEA 179
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221039926 101 QLISSLKAELTSQESQISTYEE--ELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 166
Cdd:COG4372  180 EAEQALDELLKEANRNAEKEEElaEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
81-180 5.02e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.90  E-value: 5.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   81 QKAQLEEQLKEVRkkcaEEAQLIsslKAELTSQESQISTYEEELAKAREELSRLQQ-------ETAELEESVESGKAQLE 153
Cdd:pfam20492   7 EKQELEERLKQYE----EETKKA---QEELEESEETAEELEEERRQAEEEAERLEQkrqeaeeEKERLEESAEMEAEEKE 79
                          90       100
                  ....*....|....*....|....*..
gi 221039926  154 PLQQHLQDSQQEISSMQMKlMEMKDLE 180
Cdd:pfam20492  80 QLEAELAEAQEEIARLEEE-VERKEEE 105
DUF1090 pfam06476
Protein of unknown function (DUF1090); This family consists of several bacterial proteins of ...
81-166 5.03e-04

Protein of unknown function (DUF1090); This family consists of several bacterial proteins of unknown function and is known as YqjC in E. coli.


Pssm-ID: 428965 [Multi-domain]  Cd Length: 109  Bit Score: 39.92  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   81 QKAQLEEQLKEVRKKCAEEaqlisSLKAEltsqesqistYEEELAKAREELSRLQqetAELEESVESGKAQL-EPLQQHL 159
Cdd:pfam06476  39 RVAGLEKALAEVRAHCTDA-----GLRAE----------RQQKVAEKREEVAERE---AELAEAQAKGDADKiAKRQRKL 100

                  ....*..
gi 221039926  160 QDSQQEI 166
Cdd:pfam06476 101 AEARQEL 107
mukB PRK04863
chromosome partition protein MukB;
80-186 5.12e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 5.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   80 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ-------- 151
Cdd:PRK04863  530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaq 609
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 221039926  152 --LEPLQQH----LQDSQQEISSMQMKLMEMKDLENHNSQL 186
Cdd:PRK04863  610 daLARLREQsgeeFEDSQDVTEYMQQLLERERELTVERDEL 650
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
73-175 5.14e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 40.97  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQK---AQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQEtaeleesvesgk 149
Cdd:COG2825   33 RILQESPEGKaaqKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLS--EEERQKKERELQKKQQE------------ 98
                         90       100
                 ....*....|....*....|....*.
gi 221039926 150 aqlepLQQHLQDSQQEISSMQMKLME 175
Cdd:COG2825   99 -----LQRKQQEAQQDLQKRQQELLQ 119
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
108-187 5.26e-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: 5.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 108 AELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL----MEMKDLENHN 183
Cdd:COG4942   13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaaleAELAELEKEI 92

                 ....
gi 221039926 184 SQLN 187
Cdd:COG4942   93 AELR 96
PTZ00121 PTZ00121
MAEBL; Provisional
22-269 5.38e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 5.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   22 DKREKNNVEQdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK----------E 91
Cdd:PTZ00121 1628 AEEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaeeakkaeE 1706
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   92 VRKKCAEEAQLISSLKA----------ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQD 161
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKaeeenkikaeEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  162 SQQEISSMQMKlMEMKDLENHNSQLNWCSSPHSILVN-------GATDYCSLSTSS--SETANLNEHVEGQSNLESEPIH 232
Cdd:PTZ00121 1787 EEDEKRRMEVD-KKIKDIFDNFANIIEGGKEGNLVINdskemedSAIKEVADSKNMqlEEADAFEKHKFNKNNENGEDGN 1865
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 221039926  233 QESPARSSPELLPSgvtDENEVTTAvteKVCSELDNN 269
Cdd:PTZ00121 1866 KEADFNKEKDLKED---DEEEIEEA---DEIEKIDKD 1896
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-143 5.55e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 5.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  28 NVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqQVQELLDELDE-QKAQLEEQLKEVRKKCAEEAQLISSL 106
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEK----------RLEELRKELEElEKKYSEEEYEELREEYLELSRELAGL 678
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 221039926 107 KAELTSQESQISTYE----------EELAKAREELSRLQQETAELEE 143
Cdd:PRK03918 679 RAELEELEKRREEIKktleklkeelEEREKAKKELEKLEKALERVEE 725
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
31-151 5.57e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  31 QDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 110
Cdd:COG3883  136 EELKADKAELEAKKAELEAKLAELEAL----------KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 221039926 111 TSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 151
Cdd:COG3883  206 AAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
23-159 5.69e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 5.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqKQQVQELLDELDEqkaqLEEQLKEVRKKCAEE-AQ 101
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKE----LEEKLKKYNLEELEKkAE 525
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 221039926 102 LISSLKAELTSQESQISTYEEELakarEELSRLQQETAELEESVESGKAQLEPLQQHL 159
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELAELLKEL 579
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
73-182 5.97e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.31  E-value: 5.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    73 ELLDELDEQKAQL---EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-EEELAKAREELSRLQQE-------TAEL 141
Cdd:smart00787 151 ENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEimikvkkLEEL 230
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 221039926   142 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 182
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK 271
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
21-178 6.08e-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: 6.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    21 SDKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVqrentnlqklqaqkqqvqellDELDEQKAQLEEQLKEVRKKCAEEA 100
Cdd:TIGR02169  858 NLNGKKEELEEELEELEAALRDLESRLGDLKKER---------------------DELEAQLRELERKIEELEAQIEKKR 916
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   101 QLISSLKAELTSQESQISTYEEELAKAREE------LSRLQQETAELEESVESgkaqLEPL-----QQH--LQDSQQEIS 167
Cdd:TIGR02169  917 KRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRA----LEPVnmlaiQEYeeVLKRLDELK 992
                          170
                   ....*....|.
gi 221039926   168 SMQMKLMEMKD 178
Cdd:TIGR02169  993 EKRAKLEEERK 1003
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
73-180 6.62e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.82  E-value: 6.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 152
Cdd:COG1340    8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
                         90       100
                 ....*....|....*....|....*...
gi 221039926 153 EPLQQHLQDSQQEISSMQMKLMEMKDLE 180
Cdd:COG1340   88 NELREELDELRKELAELNKAGGSIDKLR 115
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
24-182 6.91e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.57  E-value: 6.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   24 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqkLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 103
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERETELER-------MKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221039926  104 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESvesgKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 182
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLNASERKVEGLGEELSSMAAQRDR 269
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
73-186 8.84e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 8.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQKAQLEEqlkevrkkcaEEAQLIsslkaeltsQESQISTYEEeLAKAREELSRLQQETAELEESVESGKAQL 152
Cdd:COG0542  411 EELDELERRLEQLEI----------EKEALK---------KEQDEASFER-LAELRDELAELEEELEALKARWEAEKELI 470
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 221039926 153 EPLQ---QHLQDSQQEISSMQMKLMEMKDLENHNSQL 186
Cdd:COG0542  471 EEIQelkEELEQRYGKIPELEKELAELEEELAELAPL 507
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
24-169 9.13e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 9.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  24 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR-------ENTNLQKLQAQKQQVQELLDELDEQKAQLE-EQLKEVRK- 94
Cdd:COG4717  295 REKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQlEELEQEIAa 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  95 --------------KCAEEAQLISSLKAELTSQESQISTYEEEL--AKAREELSRLQQETAELEESVESGKAQLEPLQQH 158
Cdd:COG4717  375 llaeagvedeeelrAALEQAEEYQELKEELEELEEQLEELLGELeeLLEALDEEELEEELEELEEELEELEEELEELREE 454
                        170
                 ....*....|.
gi 221039926 159 LQDSQQEISSM 169
Cdd:COG4717  455 LAELEAELEQL 465
PRK11637 PRK11637
AmiB activator; Provisional
88-171 9.40e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.99  E-value: 9.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  88 QLKEVRKKCAE-------EAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVesgkAQLEplQQhlQ 160
Cdd:PRK11637  48 QLKSIQQDIAAkeksvrqQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASI----AKLE--QQ--Q 119
                         90
                 ....*....|.
gi 221039926 161 DSQQEISSMQM 171
Cdd:PRK11637 120 AAQERLLAAQL 130
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
73-171 1.15e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 40.52  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   73 ELLDELDEQKAQLEEQLKEVRKkcaEEAQL---------ISSLKAeltSQESQISTYEEELAKAREELSRLQQETaelee 143
Cdd:pfam14988  40 ELASRYTQQTAELQTQLLQKEK---EQASLkkelqalrpFAKLKE---SQEREIQDLEEEKEKVRAETAEKDREA----- 108
                          90       100
                  ....*....|....*....|....*...
gi 221039926  144 svesgKAQLEPLQQHLQDSQQEISSMQM 171
Cdd:pfam14988 109 -----HLQFLKEKALLEKQLQELRILEL 131
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
22-178 1.22e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  22 DKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqeLLDELDEQKAQLEEQLKEVRKKCAEEAQ 101
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALLKEAEK-----------------LKEELEEKKEKLQEEEDKLLEEAEKEAQ 576
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221039926 102 lisslkaeltsqesqistyeEELAKAREELSRLQQETAELE-ESVESGKAQ-LEPLQQHLQDSQQEISSMQMKLMEMKD 178
Cdd:PRK00409 577 --------------------QAIKEAKKEADEIIKELRQLQkGGYASVKAHeLIEARKRLNKANEKKEKKKKKQKEKQE 635
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
23-187 1.35e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ-RENTNLqklqaqkqqvqELLDELDEQKAQLEEQLKEvrkkcaeeaq 101
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLNEQISQLKKELTnSESENS-----------EKQRELEEKQNEIEKLKKE---------- 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  102 lISSLKAELTSQESQISTYEEELAKAreelsrlQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQmklMEMKDLEN 181
Cdd:TIGR04523 379 -NQSYKQEIKNLESQINDLESKIQNQ-------EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN---SEIKDLTN 447

                  ....*.
gi 221039926  182 HNSQLN 187
Cdd:TIGR04523 448 QDSVKE 453
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
23-262 1.47e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.90  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRkkcaeeaql 102
Cdd:pfam09787  53 RQERDLLREEIQKLRGQIQQLRTELQELEAQQQEE-----------------AESSREQLQELEEQLATER--------- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  103 isSLKAELtsqESQISTYEEELAKAREELSR----LQQETAELEESVESGKAQLEPLQQHlQDSQQEISSMQMKLMEmkD 178
Cdd:pfam09787 107 --SARREA---EAELERLQEELRYLEEELRRskatLQSRIKDREAEIEKLRNQLTSKSQS-SSSQSELENRLHQLTE--T 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  179 LENHNSQLNWCSSPHSILVngatdyCSLSTSSSETANLNEHVEGQSNLESEPIHQESPARSSPelLPSGVTDENEVTTAV 258
Cdd:pfam09787 179 LIQKQTMLEALSTEKNSLV------LQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLRN--VPGLFSESDSDRAGM 250

                  ....
gi 221039926  259 TEKV 262
Cdd:pfam09787 251 YGKV 254
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-183 1.54e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  35 EKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRkkcaeeaqlISSLKAELTSQE 114
Cdd:PRK02224 589 ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR---------IEEAREDKERAE 659
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221039926 115 SQISTYEEELAKAREELSRLQQETAELEESVESGKA------QLEPLQQHLQDSQQEISSMQMKLMEMK-DLENHN 183
Cdd:PRK02224 660 EYLEQVEEKLDELREERDDLQAEIGAVENELEELEElrerreALENRVEALEALYDEAEELESMYGDLRaELRQRN 735
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
73-187 1.64e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.66  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 152
Cdd:COG1340   22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221039926 153 EPLQ-------------QHLQDSQQ--------------EISSMQMKLMEMKDLENHNSQLN 187
Cdd:COG1340  102 AELNkaggsidklrkeiERLEWRQQtevlspeeekelveKIKELEKELEKAKKALEKNEKLK 163
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
105-165 1.90e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.55  E-value: 1.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221039926 105 SLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQqhLQDSQQE 165
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQ--IENNLLE 59
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
23-146 1.90e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKA---------QLEEQLKEVR 93
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEErhelyeeakAKKEELERLK 378
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 221039926  94 KKCAEEAqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE 146
Cdd:PRK03918 379 KRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
84-186 2.09e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.19  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    84 QLEEQLKEVRKKCAEEAQLISslKAELtsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE---PLQQHLQ 160
Cdd:TIGR00606  710 KLKSTESELKKKEKRRDEMLG--LAPG--RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimPEEESAK 785
                           90       100
                   ....*....|....*....|....*.
gi 221039926   161 DSQQEISSMQMKLMEMKDLENHNSQL 186
Cdd:TIGR00606  786 VCLTDVTIMERFQMELKDVERKIAQQ 811
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
20-119 2.12e-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: 40.52  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  20 PSDKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEE 99
Cdd:COG4942  146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
                         90       100
                 ....*....|....*....|
gi 221039926 100 AQLISSLKAELTSQESQIST 119
Cdd:COG4942  226 EALIARLEAEAAAAAERTPA 245
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
85-187 2.21e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  85 LEEQLKEVRKKcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 164
Cdd:COG2433  378 IEEALEELIEK--ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS 455
                         90       100
                 ....*....|....*....|...
gi 221039926 165 EISSMQMKLMEMKDLENHNSQLN 187
Cdd:COG2433  456 EERREIRKDREISRLDREIERLE 478
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
73-179 2.36e-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: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    73 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQiSTYEEELAKAREELSRLQQETAELEESVES----- 147
Cdd:TIGR00618  212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVLEETQERinrar 290
                           90       100       110
                   ....*....|....*....|....*....|..
gi 221039926   148 GKAQLEPLQQHLQDSQQEISSMQMKLMEMKDL 179
Cdd:TIGR00618  291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
PRK11281 PRK11281
mechanosensitive channel MscK;
30-187 2.40e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.05  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   30 EQDLKEKEDTIKQRTSE-------VQDLQDEV----QRENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcae 98
Cdd:PRK11281   38 EADVQAQLDALNKQKLLeaedklvQQDLEQTLalldKIDRQKEE------------TEQLKQQLAQAPAKLRQAQAE--- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   99 eaqlISSLKAELTSQESQ------ISTYEEELAKAREELSRLQQETAELEesvesgkAQLEPLQQHLQDSQQEISSMQMK 172
Cdd:PRK11281  103 ----LEALKDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYN-------SQLVSLQTQPERAQAALYANSQR 171
                         170
                  ....*....|....*
gi 221039926  173 LMEMkdlenhNSQLN 187
Cdd:PRK11281  172 LQQI------RNLLK 180
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
76-187 2.41e-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: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    76 DELDEQKAQLEEQLKEVRKKcAEEAQLISSLKAE----LTSQESQISTYEEELAKARE-ELSRLQQETAELEESVESGKA 150
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEEN-IERLDLIIDEKRQqlerLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIER 244
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 221039926   151 QLEPLQQHLQDSQQEISSMQMKLMEM-KDLENHNSQLN 187
Cdd:TIGR02169  245 QLASLEEELEKLTEEISELEKRLEEIeQLLEELNKKIK 282
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
30-187 2.58e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    30 EQDLKEKEDTIKQrtseVQDLQDEVQRENTNLQKLQAqkqqvqelldELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 109
Cdd:pfam01576    4 EEEMQAKEEELQK----VKERQQKAESELKELEKKHQ----------QLCEEKNALQEQLQAETELCAEAEEMRARLAAR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   110 LTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD----LENHNSQ 185
Cdd:pfam01576   70 KQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEdillLEDQNSK 149

                   ..
gi 221039926   186 LN 187
Cdd:pfam01576  150 LS 151
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
30-185 2.63e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.80  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    30 EQDLKEKEDTIKQRTSEVQ--DLQDEVQRENTNLqklqaqkqqvqellDELDEQKAQLEEQLKEVRKKCAEEAQLISSLK 107
Cdd:TIGR00606  798 QMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEK--------------QEKQHELDTVVSKIELNRKLIQDQQEQIQHLK 863
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   108 A---ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEissmQMKLMEMKDLENHNS 184
Cdd:TIGR00606  864 SktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE----KEELISSKETSNKKA 939

                   .
gi 221039926   185 Q 185
Cdd:TIGR00606  940 Q 940
mukB PRK04863
chromosome partition protein MukB;
20-170 2.73e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   20 PSDKREKNNVEQdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEE 99
Cdd:PRK04863  506 REQRHLAEQLQQ-LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMAL 584
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  100 AQLISSLKA---ELTSQESQISTYEEELAKARE----------ELSRLQQETAELEESVESGKAQLEPLQQHLqdsQQEI 166
Cdd:PRK04863  585 RQQLEQLQAriqRLAARAPAWLAAQDALARLREqsgeefedsqDVTEYMQQLLERERELTVERDELAARKQAL---DEEI 661

                  ....
gi 221039926  167 SSMQ 170
Cdd:PRK04863  662 ERLS 665
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
73-164 2.83e-03

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 40.02  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQKAQLEEQLKEVRKKcaEEAQLISSL-----KAELTSQESQISTYEEELAKAREELSRL----QQETAELEE 143
Cdd:COG1538   90 EQLALAEENLALAEELLELARAR--YEAGLASRLdvlqaEAQLAQARAQLAQAEAQLAQARNALALLlglpPPAPLDLPD 167
                         90       100
                 ....*....|....*....|.
gi 221039926 144 SVESGKAQLEPLQQHLQDSQQ 164
Cdd:COG1538  168 PLPPLPPLPPSLPGLPSEALE 188
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
87-179 2.84e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 40.51  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   87 EQLKEVRKKCAEEAQLisslKAELTSQEsqISTYEEELAKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDS 162
Cdd:pfam07111 484 EQLREERNRLDAELQL----SAHLIQQE--VGRAREQGEAERQQLSevaqQLEQELQRAQESLASVGQQLEVARQGQQES 557
                          90
                  ....*....|....*..
gi 221039926  163 QQEISSMQMKLMEMKDL 179
Cdd:pfam07111 558 TEEAASLRQELTQQQEI 574
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
25-164 2.95e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.26  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   25 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE---EQLKEVRKKCAEEAQ 101
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEallEELRSLQERLNASER 251
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221039926  102 LISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 164
Cdd:pfam07888 252 KVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAE 314
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
87-186 3.12e-03

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 37.76  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   87 EQLKEVRKKCAEEAQLISSLKAELTSQESQIstyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 166
Cdd:pfam04871   1 AKKSELESEASSLKNENTELKAELQELSKQY----NSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
                          90       100
                  ....*....|....*....|
gi 221039926  167 SSMqmkLMEMKDLENHNSQL 186
Cdd:pfam04871  77 DDL---LLLLGDLEEKVEKY 93
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
73-188 3.12e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.05  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY--EEELAKAREELSRLQQETAEL-EESVESGK 149
Cdd:cd22656  121 ALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDEGGAIARKEIKDLQKELEKLnEEYAAKLK 200
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 221039926 150 AQLEPLQQHLQDSQQEIssmQMKLMEMKDLENHNSQLNW 188
Cdd:cd22656  201 AKIDELKALIADDEAKL---AAALRLIADLTAADTDLDN 236
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
73-169 3.15e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  73 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 152
Cdd:COG1196  683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
                         90
                 ....*....|....*..
gi 221039926 153 EPLQQHLQDSQQEISSM 169
Cdd:COG1196  763 EELERELERLEREIEAL 779
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
23-152 3.24e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 3.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqVQELLDELDEQKAQLEEQLKEVRkkcAEEAQL 102
Cdd:COG3206  276 EAELAELSARYTPNHPDVIALRAQIAALRAQLQQE-------------AQRILASLEAELEALQAREASLQ---AQLAQL 339
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 221039926 103 ISSLKaELTSQESQISTYEEELAKAREELSRLQQ--ETAELEESVESGKAQL 152
Cdd:COG3206  340 EARLA-ELPELEAELRRLEREVEVARELYESLLQrlEEARLAEALTVGNVRV 390
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
39-186 3.32e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.49  E-value: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    39 TIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDEL-DEQKAQLEEQLKEVRKKcAEEAQLISSLKAELTSQesqi 117
Cdd:pfam15921  413 TIDHLRRELDDRNMEVQR--------------LEALLKAMkSECQGQMERQMAAIQGK-NESLEKVSSLTAQLEST---- 473
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221039926   118 styEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ----MKLMEMKDLENHNSQL 186
Cdd:pfam15921  474 ---KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRsrvdLKLQELQHLKNEGDHL 543
Filament pfam00038
Intermediate filament protein;
31-185 3.43e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 39.90  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   31 QDLKEK-EDTIKQRTS---EVQDLQDEVQRENTNLQKLQAQKQqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS-- 104
Cdd:pfam00038  85 EDFRQKyEDELNLRTSaenDLVGLRKDLDEATLARVDLEAKIE---SLKEELAFLKKNHEEEVRELQAQVSDTQVNVEmd 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  105 -SLKAELTSQESQI-STYEEELAKAREELSRL-QQETAELEESVESGKAQleplqqhLQDSQQEISSMQMKLMEMK-DLE 180
Cdd:pfam00038 162 aARKLDLTSALAEIrAQYEEIAAKNREEAEEWyQSKLEELQQAAARNGDA-------LRSAKEEITELRRTIQSLEiELQ 234

                  ....*
gi 221039926  181 NHNSQ 185
Cdd:pfam00038 235 SLKKQ 239
46 PHA02562
endonuclease subunit; Provisional
24-186 3.50e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  24 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENT-NLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAA 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926 103 ISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ---EISSMQ 170
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdEFNEQS 336
                        170
                 ....*....|....*..
gi 221039926 171 MKLMEMK-DLENHNSQL 186
Cdd:PHA02562 337 KKLLELKnKISTNKQSL 353
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
20-177 3.51e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    20 PSDKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQLEEQLKEVRKKCAEE 99
Cdd:TIGR00606  733 PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIME-RFQMELKDVERKIAQQ 811
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221039926   100 AQLISSLKAELTSQEsqistyeeelakareelsrLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK 177
Cdd:TIGR00606  812 AAKLQGSDLDRTVQQ-------------------VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK 870
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
30-167 3.73e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 39.79  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   30 EQDLKEKEDTIKQRTSEVQdLQdEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkae 109
Cdd:pfam15905 167 KLEAKMKEVMAKQEGMEGK-LQ-VTQKN-----------------LEHSKGKVAQLEEKLVSTEKEKIEE---------- 217
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221039926  110 lTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 167
Cdd:pfam15905 218 -KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELS 274
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
24-165 3.80e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.59  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   24 REKNnvEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 103
Cdd:pfam20492   1 REEA--EREKQELEERLKQYEEETKKAQEELEES--------------EETAEELEEERRQAEEEAERLEQKRQEAEEEK 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221039926  104 SSLKaeltsqESQISTyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 165
Cdd:pfam20492  65 ERLE------ESAEME-AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
30-141 3.85e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.10  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   30 EQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelLDEldEQKAQLEEQLKEVRKKCAEEAQlisslkAE 109
Cdd:pfam05672  39 EEERLRKEELRRRAEEERARREEEARR------------------LEE--ERRREEEERQRKAEEEAEEREQ------RE 92
                          90       100       110
                  ....*....|....*....|....*....|..
gi 221039926  110 LTSQESQISTYEEELAKAREELSRLQQETAEL 141
Cdd:pfam05672  93 QEEQERLQKQKEEAEAKAREEAERQRQEREKI 124
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
73-175 3.86e-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: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.94  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   73 ELLDELDEQK---AQLEEQLKEVRKKCAEEAQLISSLKAELtsqESQISTYEEELAKAREELSRLQQEtaeleesvesgk 149
Cdd:pfam03938   9 KILEESPEGKaaqAQLEKKFKKRQAELEAKQKELQKLYEEL---QKDGALLEEEREEKEQELQKKEQE------------ 73
                          90       100
                  ....*....|....*....|....*.
gi 221039926  150 aqlepLQQHLQDSQQEISSMQMKLME 175
Cdd:pfam03938  74 -----LQQLQQKAQQELQKKQQELLQ 94
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
30-185 3.91e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.11  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   30 EQDlKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqKQQVQELLDELDEQKAQLEEQLKEVRKKC-------AEEAQL 102
Cdd:pfam05557 183 EQD-SEIVKNSKSELARIPELEKELER-----------LREHNKHLNENIENKLLLKEEVEDLKRKLereekyrEEAATL 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  103 ---ISSLKAELTSQESQISTYEEELAK---AREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM 176
Cdd:pfam05557 251 eleKEKLEQELQSWVKLAQDTGLNLRSpedLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDL 330
                         170
                  ....*....|
gi 221039926  177 -KDLENHNSQ 185
Cdd:pfam05557 331 nKKLKRHKAL 340
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
30-164 4.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  30 EQDLKEKEDTIKQRTSEVQDLQDEV----QRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISS 105
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECrvaaQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 221039926 106 LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 164
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
23-187 4.05e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEqkaqLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR04523 165 KKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQE 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQET-------AELEESVESGKAQLEPL-QQHLQDSQQEISSmQMKLM 174
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqnnkkiKELEKQLNQLKSEISDLnNQKEQDWNKELKS-ELKNQ 319
                         170
                  ....*....|...
gi 221039926  175 EmKDLENHNSQLN 187
Cdd:TIGR04523 320 E-KKLEEIQNQIS 331
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
74-177 4.15e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 40.01  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   74 LLDELDEQKAQLEEqlkeVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR----LQQETAELEESVESGK 149
Cdd:pfam05701 326 LRSELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVElpkqLQQAAQEAEEAKSLAQ 401
                          90       100       110
                  ....*....|....*....|....*....|.
gi 221039926  150 AQLEPLQQHLQDSQQ---EISSMQMKLMEMK 177
Cdd:pfam05701 402 AAREELRKAKEEAEQakaAASTVESRLEAVL 432
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
24-165 4.76e-03

YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.


Pssm-ID: 435583 [Multi-domain]  Cd Length: 160  Bit Score: 37.89  E-value: 4.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   24 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEeaqli 103
Cdd:pfam16789  32 KEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTSDK------------ILQMKRYIKVVKERLKQEEKKVQD----- 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221039926  104 sslkaeltsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 165
Cdd:pfam16789  95 ---------QKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEEREQD 147
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
73-183 5.22e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 38.26  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   73 ELLDELDEQKAQLEEQLkevRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVES----- 147
Cdd:pfam06785  58 EDALKEKFEKSFLEEKE---AKLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQisqdf 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 221039926  148 ------GKAQLEPLQQHLQDSQQEISSmQMKLMEMKDLENHN 183
Cdd:pfam06785 135 aefrleSEEQLAEKQLLINEYQQTIEE-QRSVLEKRQDQIEN 175
PRK01156 PRK01156
chromosome segregation protein; Provisional
33-146 5.47e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.88  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  33 LKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKkcaEEAQLISSLKaELTS 112
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD---DYNNLKSALN-ELSS 246
                         90       100       110
                 ....*....|....*....|....*....|....
gi 221039926 113 QESQISTYEEELAKAREELSRLQQETAELEESVE 146
Cdd:PRK01156 247 LEDMKNRYESEIKTAESDLSMELEKNNYYKELEE 280
Rcc_KIF21 cd22248
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ...
122-171 5.52e-03

regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


Pssm-ID: 410202 [Multi-domain]  Cd Length: 81  Bit Score: 36.03  E-value: 5.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 221039926 122 EELAKAREELSRLQQE---TAELEESVESGKAQLEPLQQHLQDSQQEIssMQM 171
Cdd:cd22248   27 EKLEKKRERALDEGKDesvLRDLEEEIDSLKANIDYVQENITECQSNI--MQM 77
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
31-165 5.69e-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: 5.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926    31 QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD--------ELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR00618  732 SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGaelshlaaEIQFFNRLREEDTHLLKTLEAEIGQE 811
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221039926   103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQE-TAELEESVESGKAQLEPLQQHLQDSQQE 165
Cdd:TIGR00618  812 IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEiTHQLLKYEECSKQLAQLTQEQAKIIQLS 875
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
75-152 5.70e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.42  E-value: 5.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  75 LDELDEQKAQLEEQLKEVRKKCAE---EAQLISSlKAELTSQEsqisTYEEELAKAREELSRLQQET-AELEESVESGKA 150
Cdd:cd06503   39 LEEAEKAKEEAEELLAEYEEKLAEaraEAQEIIE-EARKEAEK----IKEEILAEAKEEAERILEQAkAEIEQEKEKALA 113

                 ..
gi 221039926 151 QL 152
Cdd:cd06503  114 EL 115
Nnf1 pfam03980
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ...
73-148 5.92e-03

Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is associated with the spindle poles and forms part of a kinetochore subcomplex called MIND.


Pssm-ID: 461118  Cd Length: 103  Bit Score: 36.45  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   73 ELLDELDEqkaqLEEQLKEvRKKCAEEAQLISSLKAEltsqesQI------STYEEELAKAREELSRLQQETAELEESVE 146
Cdd:pfam03980  33 AKLNELDE----LIEEAKE-RREEGEGPAWRPSVPPE------ELirahlaPYKQKQLEQLNARLQKLEAENAALAEEVQ 101

                  ..
gi 221039926  147 SG 148
Cdd:pfam03980 102 AQ 103
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
78-164 5.99e-03

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: 39.55  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   78 LDEQKAQLEEQ--LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEEL--------------AKAR 128
Cdd:COG3096   295 FGARRQLAEEQyrLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLeelterleeqeevvEEAA 374
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 221039926  129 EELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 164
Cdd:COG3096   375 EQLAEAEARLEAAEEEVDSLKSQLADYQQAL-DVQQ 409
MCP2201-like_sensor cd19411
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar ...
79-175 6.18e-03

ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar chemoreceptors; This family includes the ligand-binding sensor domain of Comamonas testosteroni transmembrane chemoreceptor CNB-2 MCP2201 and similar chemoreceptors. The C. testosteroni methyl-accepting chemotaxis protein MCP2201 triggers chemotaxis towards tricarboxylic acid cycle intermediates such as citric acid and aromatic compounds. While the apo-form ligand binding domain (LBD) forms a typical four-helix bundle homodimer, similar to other chemoreceptors in the superfamily such as Escherichia coli Tar and Tsr, the citrate-bound LBD reveals a four-helix bundle homotrimer. This type of oligomerization has never been observed in other bacterial chemoreceptor LBD. Site-directed mutations of key amino acid residues have demonstrated the physiological importance of the homotrimer for chemotaxis.


Pssm-ID: 438629 [Multi-domain]  Cd Length: 138  Bit Score: 37.23  E-value: 6.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  79 DEQKAQLEEQLKEVRKKCAEeaqLISSLKAELTSQESQisTYEEELAKAREELSRLQQETAELeesVESGKA-------- 150
Cdd:cd19411   35 PAERAKELARIAAARARITE---LLKKLEKLITSPEGK--ALLAAIAEARAAYLAARDKVLEL---KKAGDReearalll 106
                         90       100
                 ....*....|....*....|....*.
gi 221039926 151 -QLEPLQQHLQDSQQEISSMQMKLME 175
Cdd:cd19411  107 gELRPAQAAYLAALDALVDYQEELMD 132
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
26-187 6.28e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 38.35  E-value: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   26 KNNVE--QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKAQLEEQLKEVRKkcaeeaqli 103
Cdd:pfam13851  22 RNNLEliKSLKEEIAELKKKEERNEKLMSEIQQENKRLT----------EPLQKAQEEVEELRKQLENYEK--------- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  104 ssLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE-PLQQHLQDSQQEISSMQMKLMEM-KDLEN 181
Cdd:pfam13851  83 --DKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEaAIQDVQQKTGLKNLLLEKKLQALgETLEK 160

                  ....*.
gi 221039926  182 HNSQLN 187
Cdd:pfam13851 161 KEAQLN 166
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
11-179 6.42e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.42  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   11 SQHRDPHCDPsDKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQaqkqqvqellDELDEQKAQLE---- 86
Cdd:pfam10174 214 ELHRRNQLQP-DPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHT----------EDREEEIKQMEvyks 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   87 ---------EQLK-EVRKKCAEEAQLISSLKAeLTSQES----QISTYEEELAKAREELSRLQQETAELEESVESGKAQL 152
Cdd:pfam10174 283 hskfmknkiDQLKqELSKKESELLALQTKLET-LTNQNSdckqHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFL 361
                         170       180
                  ....*....|....*....|....*..
gi 221039926  153 EPLQQHLQDSQQEISSMQMKLMEMKDL 179
Cdd:pfam10174 362 NKKTKQLQDLTEEKSTLAGEIRDLKDM 388
PRK01156 PRK01156
chromosome segregation protein; Provisional
23-170 6.49e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.50  E-value: 6.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:PRK01156 586 RSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSI 665
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221039926 103 ISSlKAELTSQESQIstyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 170
Cdd:PRK01156 666 IPD-LKEITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK 729
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
25-137 7.58e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   25 EKNNVEQDLKEKEDTIKQRTSEV--QDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 102
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK 611
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 221039926  103 ISSLKAELTSQESQISTYEEELAKAREELSRLQQE 137
Cdd:TIGR04523 612 ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
25-187 7.68e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  25 EKNNVE---QDLKEKEDTIKQRTSEVQD--------LQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVR 93
Cdd:PRK03918 332 ELEEKEerlEELKKKLKELEKRLEELEErhelyeeaKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  94 KKCAEEAQLISSLKA-----------------ELTSQESqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQ 156
Cdd:PRK03918 412 ARIGELKKEIKELKKaieelkkakgkcpvcgrELTEEHR-----KELLEEYTAELKRIEKELKEIEEKERKLRKELRELE 486
                        170       180       190
                 ....*....|....*....|....*....|.
gi 221039926 157 QHLQDsQQEISSMQMKLMEMKDLENHNSQLN 187
Cdd:PRK03918 487 KVLKK-ESELIKLKELAEQLKELEEKLKKYN 516
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
22-183 7.79e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.05  E-value: 7.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  22 DKREKNN---VEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKK--- 95
Cdd:PRK04778 263 EQIDENLallEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSytl 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  96 CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ-------DSQQEISS 168
Cdd:PRK04778 343 NESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQglrkdelEAREKLER 422
                        170
                 ....*....|....*.
gi 221039926 169 MQMKLMEMK-DLENHN 183
Cdd:PRK04778 423 YRNKLHEIKrYLEKSN 438
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
34-142 8.21e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.14  E-value: 8.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926  34 KEKEDTIK--QRTSEVQ--DLQDEVQRENTnlQKLQAQKQQVQELLDEL--DEQKAQ-LEEQLKEVRKKCAEEaqLISSL 106
Cdd:PRK05771  16 SYKDEVLEalHELGVVHieDLKEELSNERL--RKLRSLLTKLSEALDKLrsYLPKLNpLREEKKKVSVKSLEE--LIKDV 91
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 221039926 107 KAELTSQESQISTYEEELAKAREELSRLQQETAELE 142
Cdd:PRK05771  92 EEELEKIEKEIKELEEEISELENEIKELEQEIERLE 127
growth_prot_Scy NF041483
polarized growth protein Scy;
33-170 8.22e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.42  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   33 LKEKEDTIKQR-TSEVQDLQDEVQRENTnlQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAqliSSLK-AEL 110
Cdd:NF041483 1119 IRERAEELRDRiTGEIEELHERARRESA--EQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANSEA---SKVRiAAV 1193
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221039926  111 TSQESQISTYEEELAKAREELSRLQQET-AELEESVESGKAQLEPLQQHLQDSQQEISSMQ 170
Cdd:NF041483 1194 KKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQ 1254
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
80-186 8.41e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 39.01  E-value: 8.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   80 EQKAQLEEQLKEVRKK-----------CAEE-----AQLISS--LKAELTSQESQISTYEEELAKAREELSRLQQETAEL 141
Cdd:PRK10246  380 EQLRQWQQQLTHAEQKlnalpaitltlTADEvaaalAQHAEQrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQR 459
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 221039926  142 EESVESGKAQLEPLQQHLQD----SQQEissmqmklMEMKDLENHNSQL 186
Cdd:PRK10246  460 NAALNEMRQRYKEKTQQLADvktiCEQE--------ARIKDLEAQRAQL 500
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
75-187 8.42e-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: 38.05  E-value: 8.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   75 LDELDEQKaQLEEQLKEVRKKCaEEAQL----ISSLKAELTSQESQISTYEEELAKAREELSRLQQeTAELEESVESGKA 150
Cdd:pfam12795   2 LDELEKAK-LDEAAKKKLLQDL-QQALSlldkIDASKQRAAAYQKALDDAPAELRELRQELAALQA-KAEAAPKEILASL 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 221039926  151 QLEPLQQHLQDSQQEISSMQmklmemKDLENHNSQLN 187
Cdd:pfam12795  79 SLEELEQRLLQTSAQLQELQ------NQLAQLNSQLI 109
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
76-166 8.94e-03

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: 39.17  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   76 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAeLEESVESGKAQLEPL 155
Cdd:COG3096   281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQEDLEEL 359
                          90
                  ....*....|.
gi 221039926  156 QQHLqDSQQEI 166
Cdd:COG3096   360 TERL-EEQEEV 369
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
114-175 9.06e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 35.32  E-value: 9.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221039926  114 ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 175
Cdd:pfam06005  10 ETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKLDE 71
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
22-175 9.45e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.36  E-value: 9.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   22 DKREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQlEEQLKEVRKKCAEEAQ 101
Cdd:pfam13868 150 EREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQ-EEQERKERQKEREEAE 228
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221039926  102 LISSLKAELTsqesqiSTYEEELAKAREELSRLQQETAELEESVEsgKAQLEPLQQHLQDSQQEissmQMKLME 175
Cdd:pfam13868 229 KKARQRQELQ------QAREEQIELKERRLAEEAEREEEEFERML--RKQAEDEEIEQEEAEKR----RMKRLE 290
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
23-178 9.47e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 9.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   23 KREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqQVQELLDELDE-----QKAQLEEQLKEVRKKCA 97
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES----------KISDLEDELNKddfelKKENLEKEIDEKNKEIE 571
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   98 EEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEplqqhlqdsqqEISSMQMKLMEMK 177
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE-----------KLSSIIKNIKSKK 640

                  .
gi 221039926  178 D 178
Cdd:TIGR04523 641 N 641
CCDC-167 pfam15188
Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, ...
75-130 9.76e-03

Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, has not, as yet, been determined. Members of this family remain uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between and 103 amino acids in length.


Pssm-ID: 464553 [Multi-domain]  Cd Length: 82  Bit Score: 35.33  E-value: 9.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221039926   75 LDELDEQKAQLEEQLKEVRKKcAEEAQLI----SSLKAELTSQESQISTYEEELAKAREE 130
Cdd:pfam15188   5 IDRLEEKIASCRDRLERIEKK-LRREELSeedrRSLEKELLLLKKRLEKNEEELKLLRKE 63
 
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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