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Conserved domains on  [gi|229577185|ref|NP_001153441|]
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epidermal growth factor receptor substrate 15 isoform B [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]; ...
33-195 1.98e-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: 70.35  E-value: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 113 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-AQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 191
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeELLEALRAAAELAAQLEELEEAEEALLERLERL 419

                 ....
gi 229577185 192 NSQL 195
Cdd:COG1196  420 EEEL 423
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
33-195 1.98e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.35  E-value: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 113 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-AQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 191
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeELLEALRAAAELAAQLEELEEAEEALLERLERL 419

                 ....
gi 229577185 192 NSQL 195
Cdd:COG1196  420 EEEL 423
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
33-187 5.40e-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: 5.40e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTN-------LQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKC 105
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   106 AEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM 185
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941

                   ..
gi 229577185   186 KD 187
Cdd:TIGR02168  942 QE 943
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
41-195 1.13e-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: 63.41  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   41 DLKEKEDTIKQRTsevQDLQDEVQRE-NTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 119
Cdd:pfam08614  11 RLLDRTALLEAEN---AKLQSEPESVlPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  120 TSQESQISTYEEELAKAREELSRLQQETAELEESVEsGKAQLeplqqhLQDSQQEISSMQMKL--ME--MKDLENHNSQL 195
Cdd:pfam08614  88 QELEKKLREDERRLAALEAERAQLEEKLKDREEELR-EKRKL------NQDLQDELVALQLQLnmAEekLRKLEKENREL 160
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-189 4.89e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.23  E-value: 4.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRT-SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQLEEQLKEVRKKCAEEAQL 111
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KLEEELDKAFEELAETEKR 641
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 229577185 112 ISSLKAELTSQESQIStyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 189
Cdd:PRK03918 642 LEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
92-195 2.46e-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: 42.25  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  92 AQLEEQLKEVRKKCAEEAQLISSLKAEltsQESQISTYEEeLAKAREELSRLQ-QETAELEESVESGKAQLEPLQQHLQD 170
Cdd:cd16855    4 LEIRQQLEELRQRTQETENDLRNLQQK---QESFVIQYQE-SQKIQAQLQQLQqQPQNERIELEQQLQQQKEQLEQLLNA 79
                         90       100
                 ....*....|....*....|....*.
gi 229577185 171 SQQEISSMQMKLME-MKDLENHNSQL 195
Cdd:cd16855   80 KAQELLQLRMELADkFKKTIQLLSKL 105
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
82-191 4.13e-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: 42.70  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    82 ELLDELDEQKAQL---EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-EEELAKAREELSRLQQE-------TAEL 150
Cdd:smart00787 151 ENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEimikvkkLEEL 230
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 229577185   151 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 191
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK 271
growth_prot_Scy NF041483
polarized growth protein Scy;
42-179 4.66e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.19  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   42 LKEKEDTIKQR-TSEVQDLQDEVQRENTnlqklqAQKQQVQELLDEL----DEQKAQLEEQLKEVRKKCAEEAqliSSLK 116
Cdd:NF041483 1119 IRERAEELRDRiTGEIEELHERARRESA------EQMKSAGERCDALvkaaEEQLAEAEAKAKELVSDANSEA---SKVR 1189
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229577185  117 -AELTSQESQISTYEEELAKAREELSRLQQET-AELEESVESGKAQLEPLQQHLQDSQQEISSMQ 179
Cdd:NF041483 1190 iAAVKKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQ 1254
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
33-195 1.98e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.35  E-value: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 113 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-AQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 191
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeELLEALRAAAELAAQLEELEEAEEALLERLERL 419

                 ....
gi 229577185 192 NSQL 195
Cdd:COG1196  420 EEEL 423
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
33-175 2.90e-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: 66.49  E-value: 2.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKkcAEEAQli 112
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELE--------------IEEVEARIKKYEEQLGNVRN--NKEYE-- 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229577185 113 sSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 175
Cdd:COG1579   93 -ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
38-189 3.46e-12

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 68.39  E-value: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  38 VEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA 117
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 229577185 118 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 189
Cdd:COG4372  109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
33-187 5.40e-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: 5.40e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTN-------LQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKC 105
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   106 AEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM 185
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941

                   ..
gi 229577185   186 KD 187
Cdd:TIGR02168  942 QE 943
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
41-195 1.13e-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: 63.41  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   41 DLKEKEDTIKQRTsevQDLQDEVQRE-NTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 119
Cdd:pfam08614  11 RLLDRTALLEAEN---AKLQSEPESVlPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  120 TSQESQISTYEEELAKAREELSRLQQETAELEESVEsGKAQLeplqqhLQDSQQEISSMQMKL--ME--MKDLENHNSQL 195
Cdd:pfam08614  88 QELEKKLREDERRLAALEAERAQLEEKLKDREEELR-EKRKL------NQDLQDELVALQLQLnmAEekLRKLEKENREL 160
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
32-184 1.17e-11

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: 67.77  E-value: 1.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    32 SREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 111
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229577185   112 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 184
Cdd:TIGR02168  360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
33-179 3.25e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 65.31  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:COG4372   52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 229577185 113 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL--EPLQQHLQDSQQEISSMQ 179
Cdd:COG4372  132 KQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANRNAEKEE 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
30-196 3.74e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 3.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  30 WSSREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEA 109
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 110 QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME-MKDL 188
Cdd:COG1196  316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEaLRAA 395

                 ....*...
gi 229577185 189 ENHNSQLN 196
Cdd:COG1196  396 AELAAQLE 403
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
31-187 1.06e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 63.77  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  31 SSREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcaeeaq 110
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE--------------LEQARSELEQLEEELEELNEQ------ 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229577185 111 lISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 187
Cdd:COG4372   89 -LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
32-187 1.46e-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: 64.31  E-value: 1.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    32 SREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRkkcaeeaQL 111
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK-------EE 797
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229577185   112 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 187
Cdd:TIGR02168  798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
33-196 1.65e-10

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: 63.89  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  113 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSmqmKLMEMKDLENHN 192
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS---KEKELKKLNEEK 505

                  ....
gi 229577185  193 SQLN 196
Cdd:TIGR04523 506 KELE 509
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
32-194 1.74e-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: 63.92  E-value: 1.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    32 SREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 111
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   112 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-----AQLEPLQQHLQDSQQEISSMQMKLMEMK 186
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQEELERLEEALEELR 467

                   ....*...
gi 229577185   187 DLENHNSQ 194
Cdd:TIGR02168  468 EELEEAEQ 475
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
33-196 2.10e-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: 63.93  E-value: 2.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAE-EAQL 111
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----------LKELEARIEELEEDLHKLEEALNDlEARL 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   112 ----ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK- 186
Cdd:TIGR02169  789 shsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEe 868
                          170
                   ....*....|
gi 229577185   187 DLENHNSQLN 196
Cdd:TIGR02169  869 ELEELEAALR 878
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
89-178 4.95e-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: 4.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  89 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHL 168
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                         90
                 ....*....|
gi 229577185 169 QDSQQEISSM 178
Cdd:COG4942  100 EAQKEELAEL 109
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
33-179 8.60e-10

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.85  E-value: 8.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:COG4913   302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDR-------------LEQLEREIERLERELEERERRRARLEALL 368
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229577185  113 SSLKAELTSQESQistYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 179
Cdd:COG4913   369 AALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
33-196 1.29e-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: 61.23  E-value: 1.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   113 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK-DLENH 191
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLElQIASL 398

                   ....*
gi 229577185   192 NSQLN 196
Cdd:TIGR02168  399 NNEIE 403
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
32-177 1.62e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  32 SREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQL 111
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEEELAELE--------------EELEELEEELEELEEELEEAEEELEEAEAE 359
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229577185 112 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 177
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
33-179 2.11e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229577185 113 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 179
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
33-175 2.83e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 2.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229577185 113 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 175
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
33-194 2.96e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 113 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENHN 192
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405

                 ..
gi 229577185 193 SQ 194
Cdd:COG1196  406 EE 407
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
84-173 3.11e-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: 3.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  84 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 163
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
                         90
                 ....*....|
gi 229577185 164 LQQHLQDSQQ 173
Cdd:COG4942  109 LLRALYRLGR 118
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
82-196 4.13e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 58.76  E-value: 4.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 161
Cdd:COG4372   24 ILIAALSEQLRKALFELDKLQEE-------LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 229577185 162 EPLQQHLQDSQQEISSMQMKLM----EMKDLENHNSQLN 196
Cdd:COG4372   97 AQAQEELESLQEEAEELQEELEelqkERQDLEQQRKQLE 135
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
39-190 1.09e-08

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: 58.16  E-value: 1.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    39 EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQElldELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 118
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE---QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   119 LTSQESQISTYEEELAKAREELSRL------------QQETAELEESVESGKAQLEPLQQHLQDSQQEI----SSMQMKL 182
Cdd:TIGR02169  760 LKELEARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKeyleKEIQELQ 839

                   ....*...
gi 229577185   183 MEMKDLEN 190
Cdd:TIGR02169  840 EQRIDLKE 847
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
33-174 1.24e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.86  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQK--QQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQ 110
Cdd:COG4717   95 EELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAelAELPERLEELEERLEELRELEEELEELEAELAE 174
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 229577185 111 LISSLKAEL----TSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 174
Cdd:COG4717  175 LQEELEELLeqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
40-182 1.32e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  40 QDLKEKEDTIKQ--RTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA 117
Cdd:COG1196  216 RELKEELKELEAelLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229577185 118 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 182
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
87-186 1.79e-08

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 55.22  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  87 LDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEE--ELA--KAREELSR--LQQEtAELEESVESGKAQ 160
Cdd:COG1842   28 LDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEkaRLAleKGREDLAReaLERK-AELEAQAEALEAQ 106
                         90       100
                 ....*....|....*....|....*.
gi 229577185 161 LEPLQQHLQDSQQEISSMQMKLMEMK 186
Cdd:COG1842  107 LAQLEEQVEKLKEALRQLESKLEELK 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
34-191 1.84e-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: 57.76  E-value: 1.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    34 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 113
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 229577185   114 SLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 191
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
33-179 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 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:COG1196  365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229577185 113 SSLKAELTSQEsqistyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 179
Cdd:COG1196  445 EEAAEEEAELE-------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
32-160 2.51e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.70  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  32 SREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQK-----QQVQELLDELDEQKAQLEEQLKEVRKKCA 106
Cdd:COG4717  101 EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPErleelEERLEELRELEEELEELEAELAELQEELE 180
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 229577185 107 EEAQL--------ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 160
Cdd:COG4717  181 ELLEQlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
84-191 2.86e-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: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  84 LDELDEQKAQLEEQLKEVRKKCAE--EAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 161
Cdd:COG3206  177 LEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAL 256
                         90       100       110
                 ....*....|....*....|....*....|....
gi 229577185 162 EPLQQH--LQDSQQEISSMQMKLMEMKD--LENH 191
Cdd:COG3206  257 PELLQSpvIQQLRAQLAELEAELAELSAryTPNH 290
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
41-190 4.22e-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: 4.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    41 DLKEKEDTIKQRTSEVQDLQDEVQRENTNLqklqaqkQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELT 120
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAEL-------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   121 SQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLEN 190
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
89-195 4.85e-08

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: 51.87  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   89 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQeSQIST-----YEEELAK----------AREELSRLQQETAELEES 153
Cdd:pfam07926   1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQ-AEIAReaqqnYERELVLhaedikalqaLREELNELKAEIAELKAE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 229577185  154 VESGKAQLEPLQQHLQDS----QQEISSMQMKLmemKDLENHNSQL 195
Cdd:pfam07926  80 AESAKAELEESEESWEEQkkelEKELSELEKRI---EDLNEQNKLL 122
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-189 4.89e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.23  E-value: 4.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRT-SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQLEEQLKEVRKKCAEEAQL 111
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KLEEELDKAFEELAETEKR 641
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 229577185 112 ISSLKAELTSQESQIStyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 189
Cdd:PRK03918 642 LEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
31-187 5.87e-08

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: 54.65  E-value: 5.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   31 SSREKNN-VEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKC---- 105
Cdd:pfam04849 112 SAREEILqLRHELSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEAshlk 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  106 -------AEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETA-------ELEESVESGKAQLEPLQQHLQDS 171
Cdd:pfam04849 192 tetdtyeEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITsllaqivDLQHKCKELGIENEELQQHLQAS 271
                         170
                  ....*....|....*.
gi 229577185  172 QQEISSMQMKLMEMKD 187
Cdd:pfam04849 272 KEAQRQLTSELQELQD 287
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
82-184 6.02e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 6.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ--------ESQISTYEEELAKAREELSRLQQETAELEES 153
Cdd:COG4913   295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLP 374
                          90       100       110
                  ....*....|....*....|....*....|.
gi 229577185  154 VESGKAQLEPLQQHLQDSQQEISSMQMKLME 184
Cdd:COG4913   375 LPASAEEFAALRAEAAALLEALEEELEALEE 405
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
40-189 6.11e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 6.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  40 QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELD---------EQKAQLEEQLKEVR---KKCAE 107
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPerlEELEE 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 108 EAQLISSLKAELTSQESQISTYEEELAKA--------REELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 179
Cdd:COG4717  154 RLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
                        170
                 ....*....|
gi 229577185 180 MKLMEMKDLE 189
Cdd:COG4717  234 NELEAAALEE 243
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
33-155 6.55e-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: 6.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTS---------EVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRK 103
Cdd:COG1579   59 KEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKE---------------------IESLKRRISDLEDEILELME 117
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 229577185 104 KCAEEAQLISSLKAELTSQESQIST----YEEELAKAREELSRLQQETAELEESVE 155
Cdd:COG1579  118 RIEELEEELAELEAELAELEAELEEkkaeLDEELAELEAELEELEAEREELAAKIP 173
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
38-189 7.70e-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: 7.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  38 VEQDLKEKEDTIKQRTS----EVQDLQDEVQ---------RENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKK 104
Cdd:COG3206  162 LEQNLELRREEARKALEfleeQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 105 CAE-EAQL---------------ISSLKAELTSQESQI----STY----------EEELAKAREEL-SRLQQETAELEES 153
Cdd:COG3206  242 LAAlRAQLgsgpdalpellqspvIQQLRAQLAELEAELaelsARYtpnhpdvialRAQIAALRAQLqQEAQRILASLEAE 321
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 229577185 154 VESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 189
Cdd:COG3206  322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLE 357
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
42-284 9.63e-08

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: 55.21  E-value: 9.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   42 LKEKEDTIKQRTSEVQDLQDEvqrentnlqkLQAQKQQVQELLDELD--EQKA--------QLEEQLKEVRKKCAEEAQL 111
Cdd:pfam10174 354 LEEKESFLNKKTKQLQDLTEE----------KSTLAGEIRDLKDMLDvkERKInvlqkkieNLQEQLRDKDKQLAGLKER 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  112 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETaELEESVEsgKAQLEPLQQHLQDSQQEISSMQMKLME----MKD 187
Cdd:pfam10174 424 VKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQR-EREDRER--LEELESLKKENKDLKEKVSALQPELTEkessLID 500
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  188 LENHNSQLNwcSSPHSIlvngatdycsLSTSSSETANLNEHVEGQSNLESE--PIHQ-ESPARSSPELLPSGVTDENEVT 264
Cdd:pfam10174 501 LKEHASSLA--SSGLKK----------DSKLKSLEIAVEQKKEECSKLENQlkKAHNaEEAVRTNPEINDRIRLLEQEVA 568
                         250       260       270
                  ....*....|....*....|....*....|..
gi 229577185  265 TAVTE--KVCSELD----------NNRHSKEE 284
Cdd:pfam10174 569 RYKEEsgKAQAEVErllgilreveNEKNDKDK 600
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
42-194 9.98e-08

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: 52.60  E-value: 9.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   42 LKEKEDTIKQRTSEVQDLQ---DEVQRENtnlqklqaqkqqvqELLDELdeQKAQlEEQLKEVRKKCAEEAQLISSLKAE 118
Cdd:pfam15619   6 LSARLHKIKELQNELAELQsklEELRKEN--------------RLLKRL--QKRQ-EKALGKYEGTESELPQLIARHNEE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  119 L--------------TSQESQISTYEEELAKAREELSRLQQ--------ETAELEEsvesgkaQLEPLQQHLQDSQQEIS 176
Cdd:pfam15619  69 VrvlrerlrrlqekeRDLERKLKEKEAELLRLRDQLKRLEKlsedknlaEREELQK-------KLEQLEAKLEDKDEKIQ 141
                         170
                  ....*....|....*...
gi 229577185  177 SMQMKLmemkDLENHNSQ 194
Cdd:pfam15619 142 DLERKL----ELENKSFR 155
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
32-179 1.05e-07

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: 55.06  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    32 SREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 111
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229577185   112 ISSLKAELTSQESQIS-------TYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 179
Cdd:TIGR02168  756 LTELEAEIEELEERLEeaeeelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
82-177 1.09e-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: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 161
Cdd:COG4942  150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
                         90
                 ....*....|....*.
gi 229577185 162 EPLQQHLQDSQQEISS 177
Cdd:COG4942  230 ARLEAEAAAAAERTPA 245
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
47-150 1.29e-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: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  47 DTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQI 126
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELE--------------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
                         90       100
                 ....*....|....*....|....
gi 229577185 127 STYEEELAKAREELSRLQQETAEL 150
Cdd:COG4942   86 AELEKEIAELRAELEAQKEELAEL 109
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
33-179 1.47e-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: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQqvqELLDELDEQKAQLEEQL-------------- 98
Cdd:COG4942   48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEELAELLralyrlgrqpplal 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  99 ----------------------------KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAEL 150
Cdd:COG4942  125 llspedfldavrrlqylkylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL 204
                        170       180
                 ....*....|....*....|....*....
gi 229577185 151 EESVESGKAQLEPLQQHLQDSQQEISSMQ 179
Cdd:COG4942  205 EKELAELAAELAELQQEAEELEALIARLE 233
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
38-157 2.11e-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: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  38 VEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA 117
Cdd:COG4942  144 LAPARREQAEELRADLAELAALRAELEAE-----------------RAELEALLAELEEERAALEALKAERQKLLARLEK 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 229577185 118 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESG 157
Cdd:COG4942  207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
38-182 2.30e-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: 53.92  E-value: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    38 VEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQL---ISS 114
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLA-----------------KLEAEIDKLLAEIEELEREIEEERKRRDKLteeYAE 361
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 229577185   115 LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 182
Cdd:TIGR02169  362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
41-178 2.68e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.62  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  41 DLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDEL------DEQKAQLEEQLKEVRKKCAEEAQLI-- 112
Cdd:COG4717  341 ELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELraaleqAEEYQELKEELEELEEQLEELLGELee 420
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229577185 113 -------SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqLEPLQQHLQDSQQEISSM 178
Cdd:COG4717  421 llealdeEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELREL 488
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
33-169 3.13e-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: 53.53  E-value: 3.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelldeLDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:TIGR02169  399 REINELKRELDRLQEELQRLSEELADLNAAIAG---------------------IEAKINELEEEKEDKALEIKKQEWKL 457
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229577185   113 SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE-------ESVESGKAQLEPLQQHLQ 169
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaqaraseERVRGGRAVEEVLKASIQ 521
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
33-159 3.26e-07

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 53.32  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR-ENTnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQL 111
Cdd:COG2433  399 REKEHEERELTEEEEEIRRLEEQVERLEAEVEElEAE---------------LEEKDERIERLERELSEARSEERREIRK 463
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 229577185 112 ---ISSLKAELTSQESQISTYEEELAKAREELSRLQqetaELEESVESGKA 159
Cdd:COG2433  464 dreISRLDREIERLERELEEERERIEELKRKLERLK----ELWKLEHSGEL 510
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
34-196 3.59e-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: 53.10  E-value: 3.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   34 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKlqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 113
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK---------SELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  114 SLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS-------QQEISSMQ----MKL 182
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklnqqkDEQIKKLQqekeLLE 425
                         170
                  ....*....|....
gi 229577185  183 MEMKDLENHNSQLN 196
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 ...
34-195 3.69e-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: 53.26  E-value: 3.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    34 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 113
Cdd:pfam01576   97 EKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAK 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   114 SLKAELTSQESQISTYEEEL---AKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME-- 184
Cdd:pfam01576  177 SLSKLKNKHEAMISDLEERLkkeEKGRQELEkakrKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEet 256
                          170       180
                   ....*....|....*....|
gi 229577185   185 ---------MKDLENHNSQL 195
Cdd:pfam01576  257 aqknnalkkIRELEAQISEL 276
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
37-189 6.49e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 6.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  37 NVEQDLKEKED---TIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 113
Cdd:PRK03918 190 NIEELIKEKEKeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 229577185 114 SLKAELTSQESQISTYEE--ELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 189
Cdd:PRK03918 270 ELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL 347
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
36-196 6.83e-07

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 52.15  E-value: 6.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  36 NNVEQDLKEKEDTIKQRTSEVQDLqDEVQRENtnlqklqaqkqqvqelldelDEQKAQLEEQLKEVRKKCAEEA----QL 111
Cdd:PRK04778 108 NEIESLLDLIEEDIEQILEELQEL-LESEEKN--------------------REEVEQLKDLYRELRKSLLANRfsfgPA 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 112 ISSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS----MQMK- 181
Cdd:PRK04778 167 LDELEKQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreLVEEg 246
                        170       180
                 ....*....|....*....|...
gi 229577185 182 --------LMEMKDLENHNSQLN 196
Cdd:PRK04778 247 yhldhldiEKEIQDLKEQIDENL 269
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
32-176 9.16e-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: 51.94  E-value: 9.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   32 SREKNNVEQDLKEKEDTIKQRTSEvqdlqdevqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQL 111
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKE----------------------------LKKLNEEKKELEEKVKDLTKKISSLKEK 525
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229577185  112 ISSLKAELTSQESQISTYEEELAKAREELSR---------LQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 176
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK 599
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
38-170 1.05e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.96  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  38 VEQDLKEKEDTIKQRTSEVQDLQDEV--QRENTNLQKLQAQKQQVQELLDELD-----EQKAQLEEQLKEVRKKCAEEAQ 110
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVrdLRERLEELEEERDDLLAEAGLDDADaeaveARREELEDRDEELRDRLEECRV 335
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 111 LISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQD 170
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
33-196 1.18e-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: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   33 REKNN-VEQDLKEKE---DTIKQRTSEVQDLQDEVQ---RENTNLQKLQAQKQQVQELLDE----LDEQKAQLEEQLKEV 101
Cdd:TIGR04523 366 EEKQNeIEKLKKENQsykQEIKNLESQINDLESKIQnqeKLNQQKDEQIKKLQQEKELLEKeierLKETIIKNNSEIKDL 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  102 RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMK 181
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
                         170
                  ....*....|....*
gi 229577185  182 lmeMKDLENHNSQLN 196
Cdd:TIGR04523 526 ---IEKLESEKKEKE 537
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
82-177 1.51e-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: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEqlkevrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL---QQETAELEESVESGK 158
Cdd:COG3206  295 ALRAQIAALRAQLQQ----------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVAR 364
                         90
                 ....*....|....*....
gi 229577185 159 AQLEPLQQHLQDSQQEISS 177
Cdd:COG3206  365 ELYESLLQRLEEARLAEAL 383
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
40-178 1.51e-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: 49.05  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   40 QDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkael 119
Cdd:pfam06785  83 EGFKILEETLEELQSEEERLEEELSQKE--------------EELRRLTEENQQLQIQLQQISQDFAEF----------- 137
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 229577185  120 tSQESqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 178
Cdd:pfam06785 138 -RLES-----EEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTL 190
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
82-189 1.71e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYE---EELAKAREELSRLQQETAELEESVESGK 158
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGSKRKLE 258
                         90       100       110
                 ....*....|....*....|....*....|.
gi 229577185 159 AQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 189
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKELK 289
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
39-175 1.78e-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: 51.22  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    39 EQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLisslKAE 118
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSLQSELRRIENR-------------LDELSQELSDASRKIGEIEKEIEQLEQEEEKL----KER 738
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 229577185   119 LTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ-QEI 175
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEI 796
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
88-187 1.93e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  88 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 167
Cdd:COG4372    2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
                         90       100
                 ....*....|....*....|
gi 229577185 168 LQDSQQEISSMQMKLMEMKD 187
Cdd:COG4372   82 LEELNEQLQAAQAELAQAQE 101
TMF_DNA_bd pfam12329
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ...
82-151 1.98e-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: 45.76  E-value: 1.98e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE 151
Cdd:pfam12329   5 KLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
33-179 2.31e-06

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: 50.15  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALER-------RIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 113 SSLKAE-------------------LTSQES-----QISTYEEELAKAR----EELSRLQQETAELEESVESGKAQLEPL 164
Cdd:COG4942  100 EAQKEElaellralyrlgrqpplalLLSPEDfldavRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEAL 179
                        170
                 ....*....|....*
gi 229577185 165 QQHLQDSQQEISSMQ 179
Cdd:COG4942  180 LAELEEERAALEALK 194
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
33-150 2.35e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR----ENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEE 108
Cdd:COG4913   338 DRLEQLEREIERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 229577185  109 AQLISSLKAELTSQESQISTYEEELAKAREELSR-LQQETAEL 150
Cdd:COG4913   418 RRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAEL 460
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
34-197 2.42e-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: 50.40  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   34 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 113
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK 471
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  114 SLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD-LENHN 192
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDeLNKDD 551

                  ....*
gi 229577185  193 SQLNW 197
Cdd:TIGR04523 552 FELKK 556
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
44-174 2.54e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  44 EKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEqkAQLEEQLKEVRKKCAEEAQLISSLKAELTSQE 123
Cdd:COG4717  382 EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELE 459
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 229577185 124 SQISTYEE--ELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 174
Cdd:COG4717  460 AELEQLEEdgELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
35-171 3.27e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 49.83  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  35 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDeqkaQLEEQLKEVRKKCAEEAQLISS 114
Cdd:PRK04778 305 RKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLE----SLEKQYDEITERIAEQEIAYSE 380
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 229577185 115 LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS 171
Cdd:PRK04778 381 LQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKS 437
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
83-195 3.78e-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: 48.38  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  83 LLD--ELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 160
Cdd:COG1579    9 LLDlqELDSELDRLEHRLKELPAE-------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 229577185 161 L---------EPLQQHLQDSQQEISSMQMKLME-MKDLENHNSQL 195
Cdd:COG1579   82 LgnvrnnkeyEALQKEIESLKRRISDLEDEILElMERIEELEEEL 126
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
83-196 4.49e-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: 49.67  E-value: 4.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    83 LLDELDEQKAQLEEQLKEV----RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE--- 155
Cdd:TIGR02168  194 ILNELERQLKSLERQAEKAerykELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEelr 273
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 229577185   156 ----SGKAQLEPLQQHLQDSQQEISSMQMKLM----EMKDLENHNSQLN 196
Cdd:TIGR02168  274 levsELEEEIEELQKELYALANEISRLEQQKQilreRLANLERQLEELE 322
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
82-184 4.50e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 4.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLE-EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 160
Cdd:COG1196  217 ELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
                         90       100
                 ....*....|....*....|....
gi 229577185 161 LEPLQQHLQDSQQEISSMQMKLME 184
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEE 320
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
82-182 4.96e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 4.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQL---------ISSLKAELTSQESQISTYEE---ELAKAREELSRLQQETAE 149
Cdd:COG4913   624 EELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEE 703
                          90       100       110
                  ....*....|....*....|....*....|...
gi 229577185  150 LEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 182
Cdd:COG4913   704 LEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
PRK12704 PRK12704
phosphodiesterase; Provisional
85-190 5.17e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.39  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  85 DELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPL 164
Cdd:PRK12704  64 EEIHKLRNEFEKELRERRNE-------LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136
                         90       100
                 ....*....|....*....|....*....
gi 229577185 165 QQHLQDSQQEISSMQM---KLMEMKDLEN 190
Cdd:PRK12704 137 IEEQLQELERISGLTAeeaKEILLEKVEE 165
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
39-178 5.89e-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: 5.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    39 EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE-EAQL------ 111
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDlESRLgdlkke 890
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   112 ISSLKAELTSQESQISTYEEELAKAREELSRLQ-------QETAELEESVESGK------AQLEPLQQHLQDSQQEISSM 178
Cdd:TIGR02169  891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKaklealeEELSEIEDPKGEDEeipeeeLSLEDVQAELQRVEEEIRAL 970
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
33-164 7.15e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 7.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:COG4372   73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 229577185 113 SSLKAELTSQESQISTYEEEL-----AKAREELSRLQQETAELEESVESGKAQLEPL 164
Cdd:COG4372  153 KELEEQLESLQEELAALEQELqalseAEAEQALDELLKEANRNAEKEEELAEAEKLI 209
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
84-195 7.17e-06

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: 49.18  E-value: 7.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   84 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ--- 160
Cdd:COG3096   524 LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapa 603
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 229577185  161 -------LEPLQQH----LQDSQQEISSMQMKLMEMKDLENHNSQL 195
Cdd:COG3096   604 wlaaqdaLERLREQsgeaLADSQEVTAAMQQLLEREREATVERDEL 649
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
32-189 7.36e-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: 7.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    32 SREKNNVE--QDLK-EKEDT-IKQRTSEVQDLqdEVQRENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAE 107
Cdd:TIGR02169  204 RREREKAEryQALLkEKREYeGYELLKEKEAL--ERQKEAIERQ------------LASLEEELEKLTEEISELEKRLEE 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   108 EAQLISSLKAELTSQEsqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSmqmKLMEMKD 187
Cdd:TIGR02169  270 IEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK---LLAEIEE 340

                   ..
gi 229577185   188 LE 189
Cdd:TIGR02169  341 LE 342
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
34-192 8.07e-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: 48.86  E-value: 8.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   34 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 113
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK--------------YNDLKKQKEELENELNLLEKEKLNIQKNID 190
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 229577185  114 SLKAELTSQESQISTYEEELAKAREelsrLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENHN 192
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQKNKS----LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
118-188 8.76e-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: 8.76e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 229577185 118 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDL 188
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
39-181 1.06e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  39 EQDLKEKEDTIKQRTSEVQDLQDE------------VQRENtnlqkLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCA 106
Cdd:PRK02224 369 ESELEEAREAVEDRREEIEELEEEieelrerfgdapVDLGN-----AEDFLEELREERDELREREAELEATLRTARERVE 443
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229577185 107 EEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQhLQDSQQEISSMQMK 181
Cdd:PRK02224 444 EAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEER 517
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
40-192 1.14e-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: 48.31  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   40 QDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKA---QLEEQLKEVRKKCAEEA----QLI 112
Cdd:pfam06160  86 KALDEIEELLDDIEEDIKQILEELD-----------------ELLESEEKNREeveELKDKYRELRKTLLANRfsygPAI 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  113 SSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK- 186
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGy 228

                  ....*.
gi 229577185  187 DLENHN 192
Cdd:pfam06160 229 ALEHLN 234
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
40-179 1.22e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   40 QDLKEKEDTIKQRTSEVQDLQDEVQR-ENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 118
Cdd:COG4913   654 AEYSWDEIDVASAEREIAELEAELERlDASSDD------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 229577185  119 LTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 179
Cdd:COG4913   722 LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARL 782
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
82-177 1.30e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 161
Cdd:COG3883  154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
                         90
                 ....*....|....*.
gi 229577185 162 EPLQQHLQDSQQEISS 177
Cdd:COG3883  234 AAAAAAAAAAASAAGA 249
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
40-188 1.47e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  40 QDLKEKEDTIKQRTSEVQDLQdevqrentnlqklqaqkqqvqELLDELDEQKAQLEEqLKEVRKKCAEEAQLISSLKA-- 117
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYA---------------------ELQEELEELEEELEE-LEAELEELREELEKLEKLLQll 128
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229577185 118 ----ELTSQESQISTYEEELAKAREELsrlqQETAELEESVESGKAQLEPLQQHLQDSQQEISsmQMKLMEMKDL 188
Cdd:COG4717  129 plyqELEALEAELAELPERLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQDL 197
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
82-182 1.51e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.46  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETA---- 148
Cdd:COG1579   24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIEslkr 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 229577185 149 ----------ELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 182
Cdd:COG1579  104 risdledeilELMERIEELEEELAELEAELAELEAELEEKKAEL 147
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
84-191 1.51e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  84 LDELDEQKAQLEEqLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELS--RLQQETAELEESVESGKAQL 161
Cdd:COG4717   70 LKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERL 148
                         90       100       110
                 ....*....|....*....|....*....|
gi 229577185 162 EPLQQHLQDSQQEISSMQMKLMEMKDLENH 191
Cdd:COG4717  149 EELEERLEELRELEEELEELEAELAELQEE 178
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
83-195 1.55e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  83 LLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE 162
Cdd:COG4717   47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 229577185 163 P---------LQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 195
Cdd:COG4717  127 LlplyqeleaLEAELAELPERLEELEERLEELRELEEELEEL 168
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-195 1.65e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE----- 107
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkelk 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 108 -EAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEE---SVESGKAQLEPLQQHLQDSQQEISSMQMKLM 183
Cdd:PRK03918 290 eKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEERHELYEEAKA 369
                        170
                 ....*....|..
gi 229577185 184 EMKDLENHNSQL 195
Cdd:PRK03918 370 KKEELERLKKRL 381
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
35-182 2.21e-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: 45.83  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   35 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEaqLISS 114
Cdd:pfam04012  10 RANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEE--LARE 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 229577185  115 LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQqhlqdSQQEISSMQMKL 182
Cdd:pfam04012  88 ALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLK-----ARLKAAKAQEAV 150
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
41-190 3.03e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  41 DLKEKEDTIKQRTSEVQDLQ---DEVQRENTNLQKLQaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEeaqlissLKA 117
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVeaeDRIERLEERREDLE-------ELIAERRETIEEKRERAEELRERAAE-------LEA 551
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229577185 118 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESgKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLEN 190
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAEDEIERLREKREALAELND 623
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
34-154 3.03e-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: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  34 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 113
Cdd:COG0542  405 EIDSKPEELDELERRLEQLEIEKEALKKEQD-------------EASFERLAELRDELAELEEELEALKARWEAEKELIE 471
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 229577185 114 ---SLKAELTSQESQISTYEEELAKAREELSrlqQETAELEESV 154
Cdd:COG0542  472 eiqELKEELEQRYGKIPELEKELAELEEELA---ELAPLLREEV 512
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
112-185 3.12e-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: 3.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229577185 112 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM 185
Cdd:COG3883   18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
85-175 3.43e-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: 45.69  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   85 DELDEQKAQLEEQLKevrkkcaeeaqlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEEsvesGKAQLEPL 164
Cdd:pfam11932  37 DKWDDEKQELLAEYR--------------ALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIER----TERELVPL 98
                          90
                  ....*....|.
gi 229577185  165 QQHLQDSQQEI 175
Cdd:pfam11932  99 MLKMLDRLEQF 109
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
39-176 3.45e-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: 45.37  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   39 EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK--EVRKKCAEEAQLIsSLK 116
Cdd:pfam12795  77 SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNgpAPPGEPLSEAQRW-ALQ 155
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 229577185  117 AELTSQESQISTYEEELAKA--REELSRLQQETAeleesvesgKAQLEPLQQHLQDSQQEIS 176
Cdd:pfam12795 156 AELAALKAQIDMLEQELLSNnnRQDLLKARRDLL---------TLRIQRLEQQLQALQELLN 208
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
82-180 3.73e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 46.87  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   82 ELLDELDEQKAQLEEQLKEVrkkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAEleesvesgkAQL 161
Cdd:PRK11448  146 ALQQEVLTLKQQLELQAREK----AQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE---------TSQ 212
                          90
                  ....*....|....*....
gi 229577185  162 EPLQQHLQDSQQEISSMQM 180
Cdd:PRK11448  213 ERKQKRKEITDQAAKRLEL 231
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
33-175 3.83e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 45.67  E-value: 3.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVE-QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDEL-----------DEQK------AQL 94
Cdd:COG1340   66 RDELNEKvKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewrqqtevlspEEEKelvekiKEL 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  95 EEQLKEvRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 174
Cdd:COG1340  146 EKELEK-AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK 224

                 .
gi 229577185 175 I 175
Cdd:COG1340  225 A 225
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
40-190 4.36e-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: 46.60  E-value: 4.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    40 QDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 119
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQ-----------------LERLRREREKAERYQALLKEKREYEGYELLKEKEAL 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   120 TSQ----ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPL--------QQHLQDSQQEISSMQ----MKLM 183
Cdd:TIGR02169  236 ERQkeaiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLErsiaEKER 315

                   ....*..
gi 229577185   184 EMKDLEN 190
Cdd:TIGR02169  316 ELEDAEE 322
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
39-187 4.71e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 4.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  39 EQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAE 118
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAE---------------------LDALQAELEELNEEYNELQAE-------LEALQAE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 119 LTSQESQISTYEEELAKAREEL------------------------------------SRLQQETAELEESVESGKAQLE 162
Cdd:COG3883   67 IDKLQAEIAEAEAEIEERREELgeraralyrsggsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELE 146
                        170       180
                 ....*....|....*....|....*
gi 229577185 163 PLQQHLQDSQQEISSMQMKLMEMKD 187
Cdd:COG3883  147 AKKAELEAKLAELEALKAELEAAKA 171
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
82-179 5.13e-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: 46.22  E-value: 5.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQ----------ISTYEEELAKAREELSRLQQETAELE 151
Cdd:pfam05622 311 QLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssllkqkLEEHLEKLHEAQSELQKKKEQIEELE 390
                          90       100
                  ....*....|....*....|....*....
gi 229577185  152 ESVESGKAQ-LEPLQQHLQDSQQEISSMQ 179
Cdd:pfam05622 391 PKQDSNLAQkIDELQEALRKKDEDMKAME 419
PRK12704 PRK12704
phosphodiesterase; Provisional
33-186 5.17e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 5.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQdlqdevQRENtnlqklqaqkqqvqelldeldeqkaQLEEQLKEVRKKcaeeaqli 112
Cdd:PRK12704  68 KLRNEFEKELRERRNELQKLEKRLL------QKEE-------------------------NLDRKLELLEKR-------- 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 229577185 113 sslKAELTSQESQISTYEEELAKAREELSRLQQET-AELEE----SVESGKAQLepLQQHLQDSQQEISSMqMKLMEMK 186
Cdd:PRK12704 109 ---EEELEKKEKELEQKQQELEKKEEELEELIEEQlQELERisglTAEEAKEIL--LEKVEEEARHEAAVL-IKEIEEE 181
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
32-194 5.24e-05

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: 46.25  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   32 SREK-NNVEQDLKEKEDTIKQR-------TSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaqlEEQLKEVRK 103
Cdd:pfam05483 266 SRDKaNQLEEKTKLQDENLKELiekkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK---EAQMEELNK 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  104 KCAEEAQLISSLKAELTSQESQISTYEEELAKAREELS----RLQQETAELEESVE-----------------------S 156
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKfknnkeveleelkkilaedekllD 422
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 229577185  157 GKAQLEPLQQHLQDSQQ-----------EISSMQMKLMEMKDLENHNSQ 194
Cdd:pfam05483 423 EKKQFEKIAEELKGKEQelifllqarekEIHDLEIQLTAIKTSEEHYLK 471
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
83-190 5.34e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 5.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  83 LLDELDEQKAQLEEQlkevRKKcAEEAQlisSLKAELTSQESQISTYEeeLAKAREELSRLQQETAELEESVESGKAQLE 162
Cdd:COG1196  194 ILGELERQLEPLERQ----AEK-AERYR---ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELA 263
                         90       100
                 ....*....|....*....|....*...
gi 229577185 163 PLQQHLQDSQQEISSMQMKLMEMKDLEN 190
Cdd:COG1196  264 ELEAELEELRLELEELELELEEAQAEEY 291
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
84-187 5.69e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 5.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    84 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 163
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100
                   ....*....|....*....|....
gi 229577185   164 LQQHLQDSQQEISSMQMKLMEMKD 187
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEA 782
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
40-173 5.79e-05

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: 43.79  E-value: 5.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   40 QDLKEK-----EDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelldeLDEQKAQLEEQLKEVRKKCAEEAQLiss 114
Cdd:pfam01442  14 EELQEQlgpvaQELVDRLEKETEALRERLQKD--------------------LEEVRAKLEPYLEELQAKLGQNVEE--- 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 229577185  115 LKAELtsqESQISTYEEELAKAREELSR-LQQETAELEESVESG----KAQLEP--------LQQHLQDSQQ 173
Cdd:pfam01442  71 LRQRL---EPYTEELRKRLNADAEELQEkLAPYGEELRERLEQNvdalRARLAPyaeelrqkLAERLEELKE 139
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
84-175 6.99e-05

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: 43.79  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   84 LDELDEQKAQLEEQL----KEVRKKCAEEAQ-LISSLKAELTSQESQISTYEEEL-AKAREELSRLQQETAEL-EESVES 156
Cdd:pfam01442   6 LDELSTYAEELQEQLgpvaQELVDRLEKETEaLRERLQKDLEEVRAKLEPYLEELqAKLGQNVEELRQRLEPYtEELRKR 85
                          90
                  ....*....|....*....
gi 229577185  157 GKAQLEPLQQHLQDSQQEI 175
Cdd:pfam01442  86 LNADAEELQEKLAPYGEEL 104
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
36-166 9.02e-05

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: 42.19  E-value: 9.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   36 NNVEQDLKekeDTIKQrtseVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRkkcaeeaqlissl 115
Cdd:pfam18595  29 QVVEKDLR---SCIKL----LEEIEAELAKLE--------------EAKKKLKELRDALEEKEIELR------------- 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 229577185  116 kaELTSQESQIstyEEELAKAREELSRLQQETaelEESVESGKAQLEPLQQ 166
Cdd:pfam18595  75 --ELERREERL---QRQLENAQEKLERLREQA---EEKREAAQARLEELRE 117
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
90-196 1.25e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 44.27  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  90 QKAQLEEQLKEVrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSR---LQQETAELEESVESGKAQLEPLQQ 166
Cdd:COG1566   88 AEAQLAAAEAQL-----ARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERyqaLYKKGAVSQQELDEARAALDAAQA 162
                         90       100       110
                 ....*....|....*....|....*....|
gi 229577185 167 HLQDSQQEISSMQMKLMEMKDLENHNSQLN 196
Cdd:COG1566  163 QLEAAQAQLAQAQAGLREEEELAAAQAQVA 192
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
83-196 1.46e-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: 44.73  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   83 LLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKA--- 159
Cdd:pfam05557  91 KLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeq 170
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 229577185  160 QLEPLQQHLQ---DSQQEISSMQMKLMEMKDLEN-------HNSQLN 196
Cdd:pfam05557 171 RIKELEFEIQsqeQDSEIVKNSKSELARIPELEKelerlreHNKHLN 217
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
90-189 1.60e-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: 41.44  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   90 QKAQLEEQLKEVRkkcaEEAQLIsslKAELTSQESQISTYEEELAKAREELSRLQQ-------ETAELEESVESGKAQLE 162
Cdd:pfam20492   7 EKQELEERLKQYE----EETKKA---QEELEESEETAEELEEERRQAEEEAERLEQkrqeaeeEKERLEESAEMEAEEKE 79
                          90       100
                  ....*....|....*....|....*..
gi 229577185  163 PLQQHLQDSQQEISSMQMKlMEMKDLE 189
Cdd:pfam20492  80 QLEAELAEAQEEIARLEEE-VERKEEE 105
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
30-178 1.67e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  30 WSSREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR-------ENTNLQKLQAQKQQVQELLDELDEQKAQLE-EQLKEV 101
Cdd:COG4717  292 LLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQlEELEQE 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 102 RK---------------KCAEEAQLISSLKAELTSQESQISTYEEEL--AKAREELSRLQQETAELEESVESGKAQLEPL 164
Cdd:COG4717  372 IAallaeagvedeeelrAALEQAEEYQELKEELEELEEQLEELLGELeeLLEALDEEELEEELEELEEELEELEEELEEL 451
                        170
                 ....*....|....
gi 229577185 165 QQHLQDSQQEISSM 178
Cdd:COG4717  452 REELAELEAELEQL 465
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
83-182 1.72e-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: 42.97  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   83 LLDELDEQKaQLEEQLKEVRKKCAEEAQLISSlkaelTSQESQISTyeEELAKAREELSRLQQETAELE---ESVESGKA 159
Cdd:pfam13851  21 TRNNLELIK-SLKEEIAELKKKEERNEKLMSE-----IQQENKRLT--EPLQKAQEEVEELRKQLENYEkdkQSLKNLKA 92
                          90       100
                  ....*....|....*....|...
gi 229577185  160 QLEPLQQHLQDSQQEISSMQMKL 182
Cdd:pfam13851  93 RLKVLEKELKDLKWEHEVLEQRF 115
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
34-187 1.75e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  34 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQ--- 110
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaly 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 111 --------------------LISSLKA-------------ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESG 157
Cdd:COG3883   97 rsggsvsyldvllgsesfsdFLDRLSAlskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
                        170       180       190
                 ....*....|....*....|....*....|
gi 229577185 158 KAQLEPLQQHLQDSQQEISSMQMKLMEMKD 187
Cdd:COG3883  177 QAEQEALLAQLSAEEAAAEAQLAELEAELA 206
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
35-197 1.77e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  35 KNNVEQDLKEKEDTIKqRTSEVQDLQDEVQRENTnlqklqaqkqqvqELLDELDE---QKAQLEEQLKEVRK---KCAEE 108
Cdd:PRK03918 171 IKEIKRRIERLEKFIK-RTENIEELIKEKEKELE-------------EVLREINEissELPELREELEKLEKevkELEEL 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 109 AQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE-----SGKAQ----LEPLQQHLQDSQQEISSMQ 179
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkelKEKAEeyikLSEFYEEYLDELREIEKRL 316
                        170       180
                 ....*....|....*....|....*.
gi 229577185 180 MKLME--------MKDLENHNSQLNW 197
Cdd:PRK03918 317 SRLEEeingieerIKELEEKEERLEE 342
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
86-159 1.79e-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: 1.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 229577185   86 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ-----ESQISTYEEELAKAREELSRLQQETAELEESVESGKA 159
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQlppekREQLEKLLETKNKLSEELEELEEELKELKEELESLLG 231
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
32-191 1.88e-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: 44.12  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   32 SREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqkLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 111
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTLTQRVLERETELER-------MKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  112 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESvesgKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 191
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLNASERKVEGLGEELSSMAAQRDR 269
mukB PRK04863
chromosome partition protein MukB;
84-190 2.17e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.56  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   84 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKaeltsqeSQISTYEEELAKAREELSRLQ-QETAELEESVESGKaqlE 162
Cdd:PRK04863  994 LEQAEQERTRAREQLRQAQAQLAQYNQVLASLK-------SSYDAKRQMLQELKQELQDLGvPADSGAEERARARR---D 1063
                          90       100       110
                  ....*....|....*....|....*....|..
gi 229577185  163 PLQQHLQDSQQEISSMQMKL----MEMKDLEN 190
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLtfceAEMDNLTK 1095
PRK09039 PRK09039
peptidoglycan -binding protein;
40-196 2.33e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.42  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  40 QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 119
Cdd:PRK09039  46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL 125
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229577185 120 TSQEsQIStyeeelAKAREELSRLQQETAELeesvesgKAQLEPLQQHLQDSQQEISSMQMKLmemKDLenhNSQLN 196
Cdd:PRK09039 126 DSEK-QVS------ARALAQVELLNQQIAAL-------RRQLAALEAALDASEKRDRESQAKI---ADL---GRRLN 182
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
88-188 2.36e-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: 41.51  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   88 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL-TSQESQ------ISTYEEELAKAREELSRLQQETAELEESVESGKAQ 160
Cdd:pfam10473   2 EKKQLHVLEKLKESERKADSLKDKVENLERELeMSEENQelaileAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81
                          90       100
                  ....*....|....*....|....*...
gi 229577185  161 LEPLQQHLQDSQQEISSMQMKLMEMKDL 188
Cdd:pfam10473  82 KENLTKELQKKQERVSELESLNSSLENL 109
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
82-166 2.42e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 161
Cdd:COG3883  147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226

                 ....*
gi 229577185 162 EPLQQ 166
Cdd:COG3883  227 AAAAA 231
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
92-195 2.46e-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: 42.25  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  92 AQLEEQLKEVRKKCAEEAQLISSLKAEltsQESQISTYEEeLAKAREELSRLQ-QETAELEESVESGKAQLEPLQQHLQD 170
Cdd:cd16855    4 LEIRQQLEELRQRTQETENDLRNLQQK---QESFVIQYQE-SQKIQAQLQQLQqQPQNERIELEQQLQQQKEQLEQLLNA 79
                         90       100
                 ....*....|....*....|....*.
gi 229577185 171 SQQEISSMQMKLME-MKDLENHNSQL 195
Cdd:cd16855   80 KAQELLQLRMELADkFKKTIQLLSKL 105
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-190 2.60e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  46 EDTIKQRTSEVQDLQDEVQREntnLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRkkcaEEAqlisslkAELtsqESQ 125
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDR---LEECRVAAQAHNEEAESLREDADDLEERAEELR----EEA-------AEL---ESE 371
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229577185 126 ISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK-DLEN 190
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEaTLRT 437
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
33-194 2.62e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRtsEVQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEEQL---KEVRKKCAEEA 109
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEK--EEKDLHERLNGLES-------ELAELDEEIERYEEQREQARETRdeaDEVLEEHEERR 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 110 QLISSLKAELTSQESQISTYE-------EELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 182
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETErereelaEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330
                        170
                 ....*....|...
gi 229577185 183 MEMK-DLENHNSQ 194
Cdd:PRK02224 331 EECRvAAQAHNEE 343
DUF1090 pfam06476
Protein of unknown function (DUF1090); This family consists of several bacterial proteins of ...
90-175 2.70e-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: 40.69  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   90 QKAQLEEQLKEVRKKCAEEaqlisSLKAEltsqesqistYEEELAKAREELSRLQqetAELEESVESGKAQL-EPLQQHL 168
Cdd:pfam06476  39 RVAGLEKALAEVRAHCTDA-----GLRAE----------RQQKVAEKREEVAERE---AELAEAQAKGDADKiAKRQRKL 100

                  ....*..
gi 229577185  169 QDSQQEI 175
Cdd:pfam06476 101 AEARQEL 107
PTZ00121 PTZ00121
MAEBL; Provisional
34-278 2.98e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   34 EKNNVEQdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK----------EVRK 103
Cdd:PTZ00121 1631 EKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaeeakkaeELKK 1709
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  104 KCAEE---------AQLISSLKAE-LTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 173
Cdd:PTZ00121 1710 KEAEEkkkaeelkkAEEENKIKAEeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  174 EISSMQMKlMEMKDLENHNSQLNWCSSPHSILVN-------GATDYCSLSTSS--SETANLNEHVEGQSNLESEPIHQES 244
Cdd:PTZ00121 1790 EKRRMEVD-KKIKDIFDNFANIIEGGKEGNLVINdskemedSAIKEVADSKNMqlEEADAFEKHKFNKNNENGEDGNKEA 1868
                         250       260       270
                  ....*....|....*....|....*....|....
gi 229577185  245 PARSSPELLPSgvtDENEVTTAvteKVCSELDNN 278
Cdd:PTZ00121 1869 DFNKEKDLKED---DEEEIEEA---DEIEKIDKD 1896
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
32-196 3.48e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  32 SREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ-------------RENTNLQKLQAQKQQVQEL------LDELDEQKA 92
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKELLEEYTAELkriekeLKEIEEKER 476
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  93 QLEEQLKEVRKKCAEEAQLIS--SLKAELTSQESQISTYE-EELAKAREELSRLQQETAELEESVESGKAQLEPLQQhLQ 169
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE-LK 555
                        170       180
                 ....*....|....*....|....*..
gi 229577185 170 DSQQEISSmqmklmEMKDLENHNSQLN 196
Cdd:PRK03918 556 KKLAELEK------KLDELEEELAELL 576
mukB PRK04863
chromosome partition protein MukB;
89-195 3.57e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.79  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   89 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ-------- 160
Cdd:PRK04863  530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaq 609
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 229577185  161 --LEPLQQH----LQDSQQEISSMQMKLMEMKDLENHNSQL 195
Cdd:PRK04863  610 daLARLREQsgeeFEDSQDVTEYMQQLLERERELTVERDEL 650
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
82-184 3.84e-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: 41.36  E-value: 3.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQK---AQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQEtaeleesvesgk 158
Cdd:COG2825   33 RILQESPEGKaaqKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLS--EEERQKKERELQKKQQE------------ 98
                         90       100
                 ....*....|....*....|....*.
gi 229577185 159 aqlepLQQHLQDSQQEISSMQMKLME 184
Cdd:COG2825   99 -----LQRKQQEAQQDLQKRQQELLQ 119
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
37-152 3.99e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  37 NVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqQVQELLDELDE-QKAQLEEQLKEVRKKCAEEAQLISSL 115
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEK----------RLEELRKELEElEKKYSEEEYEELREEYLELSRELAGL 678
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 229577185 116 KAELTSQESQISTYE----------EELAKAREELSRLQQETAELEE 152
Cdd:PRK03918 679 RAELEELEKRREEIKktleklkeelEEREKAKKELEKLEKALERVEE 725
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
32-168 4.13e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  32 SREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqKQQVQELLDELDEqkaqLEEQLKEVRKKCAEE-AQ 110
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKE----LEEKLKKYNLEELEKkAE 525
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 229577185 111 LISSLKAELTSQESQISTYEEELakarEELSRLQQETAELEESVESGKAQLEPLQQHL 168
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELAELLKEL 579
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
82-191 4.13e-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: 42.70  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    82 ELLDELDEQKAQL---EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-EEELAKAREELSRLQQE-------TAEL 150
Cdd:smart00787 151 ENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEimikvkkLEEL 230
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 229577185   151 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 191
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK 271
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
82-189 4.38e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 161
Cdd:COG1340    8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
                         90       100
                 ....*....|....*....|....*...
gi 229577185 162 EPLQQHLQDSQQEISSMQMKLMEMKDLE 189
Cdd:COG1340   88 NELREELDELRKELAELNKAGGSIDKLR 115
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
35-180 4.62e-04

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: 41.68  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   35 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKkcaEEAQL--- 111
Cdd:pfam14988  10 AKKTEEKQKKIEKLWNQYVQECEEIERRRQ-----------------ELASRYTQQTAELQTQLLQKEK---EQASLkke 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229577185  112 ------ISSLKAeltSQESQISTYEEELAKAREELSRLQQETaeleesvesgKAQLEPLQQHLQDSQQEISSMQM 180
Cdd:pfam14988  70 lqalrpFAKLKE---SQEREIQDLEEEKEKVRAETAEKDREA----------HLQFLKEKALLEKQLQELRILEL 131
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
33-175 4.87e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCA--EEAQ 110
Cdd:COG4372  101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalSEAE 180
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229577185 111 LISSLKAELTSQESQISTYEE--ELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 175
Cdd:COG4372  181 AEQALDELLKEANRNAEKEEElaEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
123-196 5.21e-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: 5.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229577185 123 ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM-KDLENHNSQLN 196
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeAEIEERREELG 89
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
117-196 5.37e-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: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 117 AELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL----MEMKDLENHN 192
Cdd:COG4942   13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaaleAELAELEKEI 92

                 ....
gi 229577185 193 SQLN 196
Cdd:COG4942   93 AELR 96
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
33-172 5.71e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQvqELLDELDEQKAQL--EEQLKEVRKKCAEEAQ 110
Cdd:COG4913   699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAAlgDAVERELRENLEERID 776
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  111 LISSLKAELTSQ-ESQISTY-----------------------------EEELAKAREELSRLQQET---------AELE 151
Cdd:COG4913   777 ALRARLNRAEEElERAMRAFnrewpaetadldadleslpeylalldrleEDGLPEYEERFKELLNENsiefvadllSKLR 856
                         170       180
                  ....*....|....*....|.
gi 229577185  152 ESVESGKAQLEPLQQHLQDSQ 172
Cdd:COG4913   857 RAIREIKERIDPLNDSLKRIP 877
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
33-161 5.74e-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: 5.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQ------------------------------------ 76
Cdd:COG3883   44 AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraralyrsggsvsyldvllgsesfsdfldrlsa 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  77 ----KQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEE 152
Cdd:COG3883  124 lskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203

                 ....*....
gi 229577185 153 SVESGKAQL 161
Cdd:COG3883  204 ELAAAEAAA 212
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
40-160 6.83e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 6.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  40 QDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 119
Cdd:COG3883  136 EELKADKAELEAKKAELEAKLAELEAL----------KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 229577185 120 TSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 160
Cdd:COG3883  206 AAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
34-187 6.94e-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: 6.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    34 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVqrentnlqklqaqkqqvqellDELDEQKAQLEEQLKEVRKKCAEEAQLIS 113
Cdd:TIGR02169  862 KKEELEEELEELEAALRDLESRLGDLKKER---------------------DELEAQLRELERKIEELEAQIEKKRKRLS 920
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   114 SLKAELTSQESQISTYEEELAKAREE------LSRLQQETAELEESVESgkaqLEPL-----QQH--LQDSQQEISSMQM 180
Cdd:TIGR02169  921 ELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRA----LEPVnmlaiQEYeeVLKRLDELKEKRA 996

                   ....*..
gi 229577185   181 KLMEMKD 187
Cdd:TIGR02169  997 KLEEERK 1003
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
82-196 7.66e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.82  E-value: 7.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 161
Cdd:COG1340   22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 229577185 162 EPLQ-------------QHLQDSQQ--------------EISSMQMKLMEMKDLENHNSQLN 196
Cdd:COG1340  102 AELNkaggsidklrkeiERLEWRQQtevlspeeekelveKIKELEKELEKAKKALEKNEKLK 163
PRK11637 PRK11637
AmiB activator; Provisional
97-180 8.28e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.99  E-value: 8.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  97 QLKEVRKKCAE-------EAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVesgkAQLEplQQhlQ 169
Cdd:PRK11637  48 QLKSIQQDIAAkeksvrqQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASI----AKLE--QQ--Q 119
                         90
                 ....*....|.
gi 229577185 170 DSQQEISSMQM 180
Cdd:PRK11637 120 AAQERLLAAQL 130
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
34-271 8.43e-04

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: 41.67  E-value: 8.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   34 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRkkcaeeaqlis 113
Cdd:pfam09787  55 ERDLLREEIQKLRGQIQQLRTELQELEAQQQEE-----------------AESSREQLQELEEQLATER----------- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  114 SLKAELtsqESQISTYEEELAKAREELSR----LQQETAELEESVESGKAQLEPLQQHlQDSQQEISSMQMKLMEmkDLE 189
Cdd:pfam09787 107 SARREA---EAELERLQEELRYLEEELRRskatLQSRIKDREAEIEKLRNQLTSKSQS-SSSQSELENRLHQLTE--TLI 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  190 NHNSQLNWCSSPHSILVngatdyCSLSTSSSETANLNEHVEGQSNLESEPIHQESPARSSPelLPSGVTDENEVTTAVTE 269
Cdd:pfam09787 181 QKQTMLEALSTEKNSLV------LQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLRN--VPGLFSESDSDRAGMYG 252

                  ..
gi 229577185  270 KV 271
Cdd:pfam09787 253 KV 254
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
31-188 8.72e-04

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: 42.26  E-value: 8.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    31 SSREKNNVEQDLkEKEDTIKQRTSEVQDLQDEVQRE-NTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEA 109
Cdd:TIGR00618  161 KSKEKKELLMNL-FPLDQYTQLALMEFAKKKSLHGKaELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   110 QLISSLKAELTSQESQiSTYEEELAKAREELSRLQQETAELEESVES-----GKAQLEPLQQHLQDSQQEISSMQMKLME 184
Cdd:TIGR00618  240 QSHAYLTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVLEETQERinrarKAAPLAAHIKAVTQIEQQAQRIHTELQS 318

                   ....
gi 229577185   185 MKDL 188
Cdd:TIGR00618  319 KMRS 322
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
82-195 9.03e-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: 9.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEqlkevrkkcaEEAQLIsslkaeltsQESQISTYEEeLAKAREELSRLQQETAELEESVESGKAQL 161
Cdd:COG0542  411 EELDELERRLEQLEI----------EKEALK---------KEQDEASFER-LAELRDELAELEEELEALKARWEAEKELI 470
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 229577185 162 EPLQ---QHLQDSQQEISSMQMKLMEMKDLENHNSQL 195
Cdd:COG0542  471 EEIQelkEELEQRYGKIPELEKELAELEEELAELAPL 507
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
44-192 1.08e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  44 EKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRkkcaeeaqlISSLKAELTSQE 123
Cdd:PRK02224 589 ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR---------IEEAREDKERAE 659
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229577185 124 SQISTYEEELAKAREELSRLQQETAELEESVESGKA------QLEPLQQHLQDSQQEISSMQMKLMEMK-DLENHN 192
Cdd:PRK02224 660 EYLEQVEEKLDELREERDDLQAEIGAVENELEELEElrerreALENRVEALEALYDEAEELESMYGDLRaELRQRN 735
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
93-195 1.13e-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: 41.96  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    93 QLEEQLKEVRKKCAEEAQLISslKAELtsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE---PLQQHLQ 169
Cdd:TIGR00606  710 KLKSTESELKKKEKRRDEMLG--LAPG--RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimPEEESAK 785
                           90       100
                   ....*....|....*....|....*.
gi 229577185   170 DSQQEISSMQMKLMEMKDLENHNSQL 195
Cdd:TIGR00606  786 VCLTDVTIMERFQMELKDVERKIAQQ 811
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
114-174 1.14e-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: 38.32  E-value: 1.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 229577185 114 SLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQqhLQDSQQE 174
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQ--IENNLLE 59
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
39-150 1.14e-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: 39.64  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   39 EQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelLDEldEQKAQLEEQLKEVRKKCAEEAQlisslkAE 118
Cdd:pfam05672  39 EEERLRKEELRRRAEEERARREEEARR------------------LEE--ERRREEEERQRKAEEEAEEREQ------RE 92
                          90       100       110
                  ....*....|....*....|....*....|..
gi 229577185  119 LTSQESQISTYEEELAKAREELSRLQQETAEL 150
Cdd:pfam05672  93 QEEQERLQKQKEEAEAKAREEAERQRQEREKI 124
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
33-174 1.20e-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: 39.13  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   33 REKNnvEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDEQKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:pfam20492   1 REEA--EREKQELEERLKQYEEETKKAQEELEES--------------EETAEELEEERRQAEEEAERLEQKRQEAEEEK 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 229577185  113 SSLKaeltsqESQISTyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 174
Cdd:pfam20492  65 ERLE------ESAEME-AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
39-194 1.22e-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: 41.96  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    39 EQDLKEKEDTIKQRTSEVQ--DLQDEVQRENTNLqklqaqkqqvqellDELDEQKAQLEEQLKEVRKKCAEEAQLISSLK 116
Cdd:TIGR00606  798 QMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEK--------------QEKQHELDTVVSKIELNRKLIQDQQEQIQHLK 863
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   117 A---ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEissmQMKLMEMKDLENHNS 193
Cdd:TIGR00606  864 SktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE----KEELISSKETSNKKA 939

                   .
gi 229577185   194 Q 194
Cdd:TIGR00606  940 Q 940
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
32-155 1.22e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  32 SREKNNVEQDLKEKEDTiKQRTSEVQDLQDEVQREntnlqklqaqKQQVQELLDELDEQKaQLEEQLKEVRKKCAEEAql 111
Cdd:PRK03918 320 EEEINGIEERIKELEEK-EERLEELKKKLKELEKR----------LEELEERHELYEEAK-AKKEELERLKKRLTGLT-- 385
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 229577185 112 ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE 155
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
39-196 1.24e-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: 42.08  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    39 EQDLKEKEDTIKQrtseVQDLQDEVQRENTNLQKLQAqkqqvqelldELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 118
Cdd:pfam01576    4 EEEMQAKEEELQK----VKERQQKAESELKELEKKHQ----------QLCEEKNALQEQLQAETELCAEAEEMRARLAAR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   119 -------LTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDlenH 191
Cdd:pfam01576   70 kqeleeiLHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED---Q 146

                   ....*
gi 229577185   192 NSQLN 196
Cdd:pfam01576  147 NSKLS 151
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
34-189 1.58e-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: 41.42  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   34 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE---EQLKEVRKKCAEEAQ 110
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEallEELRSLQERLNASER 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  111 LISSLKAELTSQESQISTYEEELAKAR------------------EELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 172
Cdd:pfam07888 252 KVEGLGEELSSMAAQRDRTQAELHQARlqaaqltlqladaslalrEGRARWAQERETLQQSAEADKDRIEKLSAELQRLE 331
                         170
                  ....*....|....*..
gi 229577185  173 QeisSMQMKLMEMKDLE 189
Cdd:pfam07888 332 E---RLQEERMEREKLE 345
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
96-195 1.63e-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: 38.53  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   96 EQLKEVRKKCAEEAQLISSLKAELTSQESQIstyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 175
Cdd:pfam04871   1 AKKSELESEASSLKNENTELKAELQELSKQY----NSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
                          90       100
                  ....*....|....*....|
gi 229577185  176 SSMqmkLMEMKDLENHNSQL 195
Cdd:pfam04871  77 DDL---LLLLGDLEEKVEKY 93
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
96-188 1.63e-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: 41.28  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   96 EQLKEVRKKCAEEAQLisslKAELTSQEsqISTYEEELAKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDS 171
Cdd:pfam07111 484 EQLREERNRLDAELQL----SAHLIQQE--VGRAREQGEAERQQLSevaqQLEQELQRAQESLASVGQQLEVARQGQQES 557
                          90
                  ....*....|....*..
gi 229577185  172 QQEISSMQMKLMEMKDL 188
Cdd:pfam07111 558 TEEAASLRQELTQQQEI 574
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
33-196 1.67e-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: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ-RENTNLqklqaqkqqvqELLDELDEQKAQLEEQLKEvrkkcaeeaql 111
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTnSESENS-----------EKQRELEEKQNEIEKLKKE----------- 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  112 ISSLKAELTSQESQISTYEEELAKAreelsrlQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQmklMEMKDLENH 191
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQ-------EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN---SEIKDLTNQ 448

                  ....*
gi 229577185  192 NSQLN 196
Cdd:TIGR04523 449 DSVKE 453
Filament pfam00038
Intermediate filament protein;
40-194 1.68e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 40.67  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   40 QDLKEK-EDTIKQRTS---EVQDLQDEVQRENTNLQKLQAQKQqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS-- 113
Cdd:pfam00038  85 EDFRQKyEDELNLRTSaenDLVGLRKDLDEATLARVDLEAKIE---SLKEELAFLKKNHEEEVRELQAQVSDTQVNVEmd 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  114 -SLKAELTSQESQI-STYEEELAKAREELSRL-QQETAELEESVESGKAQleplqqhLQDSQQEISSMQMKLMEMK-DLE 189
Cdd:pfam00038 162 aARKLDLTSALAEIrAQYEEIAAKNREEAEEWyQSKLEELQQAAARNGDA-------LRSAKEEITELRRTIQSLEiELQ 234

                  ....*
gi 229577185  190 NHNSQ 194
Cdd:pfam00038 235 SLKKQ 239
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
39-194 1.72e-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: 41.26  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   39 EQDlKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqKQQVQELLDELDEQKAQLEEQLKEVRKKC-------AEEAQL 111
Cdd:pfam05557 183 EQD-SEIVKNSKSELARIPELEKELER-----------LREHNKHLNENIENKLLLKEEVEDLKRKLereekyrEEAATL 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  112 ---ISSLKAELTSQESQISTYEEELAK---AREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM 185
Cdd:pfam05557 251 eleKEKLEQELQSWVKLAQDTGLNLRSpedLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDL 330
                         170
                  ....*....|
gi 229577185  186 -KDLENHNSQ 194
Cdd:pfam05557 331 nKKLKRHKAL 340
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
85-196 1.78e-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: 41.59  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    85 DELDEQKAQLEEQLKEVRKKcAEEAQLISSLKAE----LTSQESQISTYEEELAKARE-ELSRLQQETAELEESVESGKA 159
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEEN-IERLDLIIDEKRQqlerLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIER 244
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 229577185   160 QLEPLQQHLQDSQQEISSMQMKLMEM-KDLENHNSQLN 196
Cdd:TIGR02169  245 QLASLEEELEKLTEEISELEKRLEEIeQLLEELNKKIK 282
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
48-195 1.80e-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: 41.26  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    48 TIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDEL-DEQKAQLEEQLKEVRKKcAEEAQLISSLKAELTSQesqi 126
Cdd:pfam15921  413 TIDHLRRELDDRNMEVQR--------------LEALLKAMkSECQGQMERQMAAIQGK-NESLEKVSSLTAQLEST---- 473
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229577185   127 styEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ----MKLMEMKDLENHNSQL 195
Cdd:pfam15921  474 ---KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRsrvdLKLQELQHLKNEGDHL 543
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
33-187 1.93e-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: 39.43  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEeaqli 112
Cdd:pfam16789  32 KEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTSDK------------ILQMKRYIKVVKERLKQEEKKVQD----- 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229577185  113 sslkaeltsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 187
Cdd:pfam16789  95 ---------QKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEEREQDEIGSALHLANQRK 160
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
94-196 1.95e-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: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  94 LEEQLKEVRKKcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 173
Cdd:COG2433  378 IEEALEELIEK--ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS 455
                         90       100
                 ....*....|....*....|...
gi 229577185 174 EISSMQMKLMEMKDLENHNSQLN 196
Cdd:COG2433  456 EERREIRKDREISRLDREIERLE 478
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
39-176 1.99e-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: 40.56  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   39 EQDLKEKEDTIKQRTSEVQdLQdEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkae 118
Cdd:pfam15905 167 KLEAKMKEVMAKQEGMEGK-LQ-VTQKN-----------------LEHSKGKVAQLEEKLVSTEKEKIEE---------- 217
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 229577185  119 lTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 176
Cdd:pfam15905 218 -KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELS 274
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
38-190 2.07e-03

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.


Pssm-ID: 464053 [Multi-domain]  Cd Length: 294  Bit Score: 40.30  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   38 VEQDLKEKEDTIKQRTSEVQDLQDEV--QRENTNLQKLQAQKQQVQELLDELDE---QKAQLEEQLKEVRKKCAEEAQLI 112
Cdd:pfam13949  98 VRSKFREHEEDLELLSGPDEDLEAFLpsSRRAKNSPSVEEQVAKLRELLNKLNElkrEREQLLKDLKEKARNDDISPKLL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  113 SSLKAEL-TSQESQIstYEEELAKAREELSRLQQETA---ELEESVESGKAQLEPLQQHLQDSQQEISSMqmklmeMKDL 188
Cdd:pfam13949 178 LEKARLIaPNQEEQL--FEEELEKYDPLQNRLEQNLHkqeELLKEITEANNEFLQDKRVDSEKQRQREEA------LQKL 249

                  ..
gi 229577185  189 EN 190
Cdd:pfam13949 250 EN 251
mukB PRK04863
chromosome partition protein MukB;
39-179 2.23e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   39 EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA- 117
Cdd:PRK04863  515 LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAr 594
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229577185  118 --ELTSQESQISTYEEELAKARE----------ELSRLQQETAELEESVESGKAQLEPLQQHLqdsQQEISSMQ 179
Cdd:PRK04863  595 iqRLAARAPAWLAAQDALARLREqsgeefedsqDVTEYMQQLLERERELTVERDELAARKQAL---DEEIERLS 665
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
32-189 2.24e-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: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    32 SREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqelldELDEQKAQLEEQLKEVRKKCAEEaql 111
Cdd:TIGR00606  240 VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKK--------------QMEKDNSELELKMEKVFQGTDEQ--- 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   112 issLKAELTSQESQISTYEEELAKAREELSRLQQETAEL-----EESVESGKAQL--EPLQQHLQDSQQEISSMQMKLmE 184
Cdd:TIGR00606  303 ---LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLnqektELLVEQGRLQLqaDRHQEHIRARDSLIQSLATRL-E 378

                   ....*
gi 229577185   185 MKDLE 189
Cdd:TIGR00606  379 LDGFE 383
PRK11281 PRK11281
mechanosensitive channel MscK;
39-196 2.54e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.05  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   39 EQDLKEKEDTIKQRTSE-------VQDLQDEV----QRENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcae 107
Cdd:PRK11281   38 EADVQAQLDALNKQKLLeaedklvQQDLEQTLalldKIDRQKEE------------TEQLKQQLAQAPAKLRQAQAE--- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  108 eaqlISSLKAELTSQESQ------ISTYEEELAKAREELSRLQQETAELEesvesgkAQLEPLQQHLQDSQQEISSMQMK 181
Cdd:PRK11281  103 ----LEALKDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYN-------SQLVSLQTQPERAQAALYANSQR 171
                         170
                  ....*....|....*
gi 229577185  182 LMEMkdlenhNSQLN 196
Cdd:PRK11281  172 LQQI------RNLLK 180
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
82-178 2.64e-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: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 161
Cdd:COG1196  683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
                         90
                 ....*....|....*..
gi 229577185 162 EPLQQHLQDSQQEISSM 178
Cdd:COG1196  763 EELERELERLEREIEAL 779
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
82-184 2.66e-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: 38.33  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   82 ELLDELDEQK---AQLEEQLKEVRKKCAEEAQLISSLKAELtsqESQISTYEEELAKAREELSRLQQEtaeleesvesgk 158
Cdd:pfam03938   9 KILEESPEGKaaqAQLEKKFKKRQAELEAKQKELQKLYEEL---QKDGALLEEEREEKEQELQKKEQE------------ 73
                          90       100
                  ....*....|....*....|....*.
gi 229577185  159 aqlepLQQHLQDSQQEISSMQMKLME 184
Cdd:pfam03938  74 -----LQQLQQKAQQELQKKQQELLQ 94
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
32-187 2.67e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  32 SREKNNVEQ---DLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqeLLDELDEQKAQLEEQLKEVRKKCAEE 108
Cdd:PRK00409 512 GEDKEKLNEliaSLEELERELEQKAEEAEALLKEAEK-----------------LKEELEEKKEKLQEEEDKLLEEAEKE 574
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 109 AQlisslkaeltsqesqistyeEELAKAREELSRLQQETAELE-ESVESGKAQ-LEPLQQHLQDSQQEISSMQMKLMEMK 186
Cdd:PRK00409 575 AQ--------------------QAIKEAKKEADEIIKELRQLQkGGYASVKAHeLIEARKRLNKANEKKEKKKKKQKEKQ 634

                 .
gi 229577185 187 D 187
Cdd:PRK00409 635 E 635
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
84-253 2.81e-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: 40.87  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    84 LDELDEQKAQLEEQLKEVRKkcaeEAQLISSLKAELTSQESQISTYEEELAKAREELS----RLQQETAELEESVESGKA 159
Cdd:pfam15921  743 IDALQSKIQFLEEAMTNANK----EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRsqerRLKEKVANMEVALDKASL 818
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   160 QLEPLQQHLQDSQQEisSMQMKL---MEMKDLENHNSQLNWCSSPHSILVNGATDYCSLSTSSSETANLNEHVEGQSNle 236
Cdd:pfam15921  819 QFAECQDIIQRQEQE--SVRLKLqhtLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHSRKTN-- 894
                          170
                   ....*....|....*..
gi 229577185   237 sepIHQESPARSSPELL 253
Cdd:pfam15921  895 ---ALKEDPTRDLKQLL 908
Rcc_KIF21 cd22248
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ...
131-180 2.82e-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: 36.80  E-value: 2.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 229577185 131 EELAKAREELSRLQQE---TAELEESVESGKAQLEPLQQHLQDSQQEIssMQM 180
Cdd:cd22248   27 EKLEKKRERALDEGKDesvLRDLEEEIDSLKANIDYVQENITECQSNI--MQM 77
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
39-173 2.83e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  39 EQDLKEKEDTIKQRTSEVQDLQDEV----QRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISS 114
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECrvaaQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 229577185 115 LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 173
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
82-173 2.89e-03

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


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 40.02  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEQLKEVRKKcaEEAQLISSL-----KAELTSQESQISTYEEELAKAREELSRL----QQETAELEE 152
Cdd:COG1538   90 EQLALAEENLALAEELLELARAR--YEAGLASRLdvlqaEAQLAQARAQLAQAEAQLAQARNALALLlglpPPAPLDLPD 167
                         90       100
                 ....*....|....*....|.
gi 229577185 153 SVESGKAQLEPLQQHLQDSQQ 173
Cdd:COG1538  168 PLPPLPPLPPSLPGLPSEALE 188
Nnf1 pfam03980
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ...
82-157 2.90e-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: 37.61  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   82 ELLDELDEqkaqLEEQLKEvRKKCAEEAQLISSLKAEltsqesQI------STYEEELAKAREELSRLQQETAELEESVE 155
Cdd:pfam03980  33 AKLNELDE----LIEEAKE-RREEGEGPAWRPSVPPE------ELirahlaPYKQKQLEQLNARLQKLEAENAALAEEVQ 101

                  ..
gi 229577185  156 SG 157
Cdd:pfam03980 102 AQ 103
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
38-186 3.00e-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: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    38 VEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQLEEQLKEVRKKCAEEAQLISSLKA 117
Cdd:TIGR00606  742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIME-RFQMELKDVERKIAQQAAKLQGSDL 820
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 229577185   118 ELTSQEsqistyeeelakareelsrLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK 186
Cdd:TIGR00606  821 DRTVQQ-------------------VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK 870
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
82-197 3.05e-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: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY--EEELAKAREELSRLQQETAEL-EESVESGK 158
Cdd:cd22656  121 ALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDEGGAIARKEIKDLQKELEKLnEEYAAKLK 200
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 229577185 159 AQLEPLQQHLQDSQQEIssmQMKLMEMKDLENHNSQLNW 197
Cdd:cd22656  201 AKIDELKALIADDEAKL---AAALRLIADLTAADTDLDN 236
46 PHA02562
endonuclease subunit; Provisional
33-195 3.09e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENT-NLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL 111
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAA 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 112 ISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ---EISSMQ 179
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdEFNEQS 336
                        170
                 ....*....|....*..
gi 229577185 180 MKLMEMK-DLENHNSQL 195
Cdd:PHA02562 337 KKLLELKnKISTNKQSL 353
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
83-186 3.28e-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: 40.40  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   83 LLDELDEQKAQLEEqlkeVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR----LQQETAELEESVESGK 158
Cdd:pfam05701 326 LRSELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVElpkqLQQAAQEAEEAKSLAQ 401
                          90       100       110
                  ....*....|....*....|....*....|.
gi 229577185  159 AQLEPLQQHLQDSQQ---EISSMQMKLMEMK 186
Cdd:pfam05701 402 AAREELRKAKEEAEQakaAASTVESRLEAVL 432
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
35-196 3.31e-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: 39.12  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   35 KNNVE--QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKAQLEEQLKEVRKkcaeeaqli 112
Cdd:pfam13851  22 RNNLEliKSLKEEIAELKKKEERNEKLMSEIQQENKRLT----------EPLQKAQEEVEELRKQLENYEK--------- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  113 ssLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE-PLQQHLQDSQQEISSMQMKLMEM-KDLEN 190
Cdd:pfam13851  83 --DKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEaAIQDVQQKTGLKNLLLEKKLQALgETLEK 160

                  ....*.
gi 229577185  191 HNSQLN 196
Cdd:pfam13851 161 KEAQLN 166
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
82-192 3.55e-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: 39.03  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   82 ELLDELDEQKAQLEEQLkevRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVES----- 156
Cdd:pfam06785  58 EDALKEKFEKSFLEEKE---AKLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQisqdf 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 229577185  157 ------GKAQLEPLQQHLQDSQQEISSmQMKLMEMKDLENHN 192
Cdd:pfam06785 135 aefrleSEEQLAEKQLLINEYQQTIEE-QRSVLEKRQDQIEN 175
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
40-174 3.57e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.34  E-value: 3.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    40 QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD--------ELDEQKAQLEEQLKEVRKKCAEEAQL 111
Cdd:TIGR00618  732 SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGaelshlaaEIQFFNRLREEDTHLLKTLEAEIGQE 811
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229577185   112 ISSLKAELTSQESQISTYEEELAKAREELSRLQQE-TAELEESVESGKAQLEPLQQHLQDSQQE 174
Cdd:TIGR00618  812 IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEiTHQLLKYEECSKQLAQLTQEQAKIIQLS 875
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
84-196 3.62e-03

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


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 39.21  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   84 LDELDEQKaQLEEQLKEVRKKcAEEAQL----ISSLKAELTSQESQISTYEEELAKAREELSRLQQeTAELEESVESGKA 159
Cdd:pfam12795   2 LDELEKAK-LDEAAKKKLLQD-LQQALSlldkIDASKQRAAAYQKALDDAPAELRELRQELAALQA-KAEAAPKEILASL 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 229577185  160 QLEPLQQHLQDSQQEISSMQmklmemKDLENHNSQLN 196
Cdd:pfam12795  79 SLEELEQRLLQTSAQLQELQ------NQLAQLNSQLI 109
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
87-173 4.03e-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: 40.32  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   87 LDEQKAQLEEQ--LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEEL--------------AKAR 137
Cdd:COG3096   295 FGARRQLAEEQyrLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLeelterleeqeevvEEAA 374
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 229577185  138 EELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 173
Cdd:COG3096   375 EQLAEAEARLEAAEEEVDSLKSQLADYQQAL-DVQQ 409
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
33-161 4.06e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqVQELLDELDEQKAQLEEQLKEVRkkcAEEAQLI 112
Cdd:COG3206  277 AELAELSARYTPNHPDVIALRAQIAALRAQLQQE-------------AQRILASLEAELEALQAREASLQ---AQLAQLE 340
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 229577185 113 SSLKaELTSQESQISTYEEELAKAREELSRLQQ--ETAELEESVESGKAQL 161
Cdd:COG3206  341 ARLA-ELPELEAELRRLEREVEVARELYESLLQrlEEARLAEALTVGNVRV 390
PRK01156 PRK01156
chromosome segregation protein; Provisional
42-194 4.11e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 4.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  42 LKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKkcaEEAQLISSLKaELTS 121
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD---DYNNLKSALN-ELSS 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 122 QESQISTYEEELAKAREELSRLQQETAELEESVE---------------------SGKAQLEPLQQHLQDSQQEISSMQM 180
Cdd:PRK01156 247 LEDMKNRYESEIKTAESDLSMELEKNNYYKELEErhmkiindpvyknrnyindyfKYKNDIENKKQILSNIDAEINKYHA 326
                        170
                 ....*....|....
gi 229577185 181 KLMEMKDLENHNSQ 194
Cdd:PRK01156 327 IIKKLSVLQKDYND 340
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
38-187 4.19e-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: 39.52  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   38 VEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQlEEQLKEVRKKCAEEAQLISSLKA 117
Cdd:pfam13868 157 ILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQ-EEQERKERQKEREEAEKKARQRQ 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  118 ELT-SQESQIS----TYEEELAKAREELSRLQQETAELEEsvesgKAQLEPLQQHLQDSQ--QEISSM-----QMKLMEM 185
Cdd:pfam13868 236 ELQqAREEQIElkerRLAEEAEREEEEFERMLRKQAEDEE-----IEQEEAEKRRMKRLEhrRELEKQieereEQRAAER 310

                  ..
gi 229577185  186 KD 187
Cdd:pfam13868 311 EE 312
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
32-184 4.51e-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: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   32 SREKNNVEQDLKEKEDTIKQRTSEV--QDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEA 109
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKE 609
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229577185  110 QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMqMKLME 184
Cdd:TIGR04523 610 KKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDI-IELMK 683
growth_prot_Scy NF041483
polarized growth protein Scy;
42-179 4.66e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.19  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   42 LKEKEDTIKQR-TSEVQDLQDEVQRENTnlqklqAQKQQVQELLDEL----DEQKAQLEEQLKEVRKKCAEEAqliSSLK 116
Cdd:NF041483 1119 IRERAEELRDRiTGEIEELHERARRESA------EQMKSAGERCDALvkaaEEQLAEAEAKAKELVSDANSEA---SKVR 1189
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229577185  117 -AELTSQESQISTYEEELAKAREELSRLQQET-AELEESVESGKAQLEPLQQHLQDSQQEISSMQ 179
Cdd:NF041483 1190 iAAVKKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQ 1254
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
84-161 5.08e-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: 5.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  84 LDELDEQKAQLEEQLKEVRKKCAE---EAQLISSlKAELTSQEsqisTYEEELAKAREELSRLQQET-AELEESVESGKA 159
Cdd:cd06503   39 LEEAEKAKEEAEELLAEYEEKLAEaraEAQEIIE-EARKEAEK----IKEEILAEAKEEAERILEQAkAEIEQEKEKALA 113

                 ..
gi 229577185 160 QL 161
Cdd:cd06503  114 EL 115
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-196 5.34e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 5.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  34 EKNNVE---QDLKEKEDTIKQRTSE----VQDLQD----EVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVR 102
Cdd:PRK03918 332 ELEEKEerlEELKKKLKELEKRLEEleerHELYEEakakKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 103 KKCAEEAQLISSLKA-----------------ELTSQESqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQ 165
Cdd:PRK03918 412 ARIGELKKEIKELKKaieelkkakgkcpvcgrELTEEHR-----KELLEEYTAELKRIEKELKEIEEKERKLRKELRELE 486
                        170       180       190
                 ....*....|....*....|....*....|.
gi 229577185 166 QHLQDsQQEISSMQMKLMEMKDLENHNSQLN 196
Cdd:PRK03918 487 KVLKK-ESELIKLKELAEQLKELEEKLKKYN 516
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
83-187 5.36e-03

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 37.19  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   83 LLDELDEQKAQLEEQ-------LKEVRKKCAEEaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEEsve 155
Cdd:pfam17675  10 LLEELDKQLEDAEKErdayisfLKKLEKETPEE---LEELEKELEKLEKEEEELLQELEELEKEREELDAELEALEE--- 83
                          90       100       110
                  ....*....|....*....|....*....|..
gi 229577185  156 sgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD 187
Cdd:pfam17675  84 ----ELEALDEEEEEFWREYNALQLQLLEFQD 111
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
118-184 5.52e-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: 35.70  E-value: 5.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 229577185  118 ELTSQ-ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 184
Cdd:pfam06005   4 ELLEQlETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKLDE 71
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
33-196 5.64e-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: 39.62  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   33 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEqkaqLEEQLKEVRKKCAEEAQLI 112
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQEI 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  113 SSLKAELTSQESQISTYEEELAKAREELSRLQQET-------AELEESVESGKAQLEPL-QQHLQDSQQEISSmQMKLME 184
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqnnkkiKELEKQLNQLKSEISDLnNQKEQDWNKELKS-ELKNQE 320
                         170
                  ....*....|..
gi 229577185  185 mKDLENHNSQLN 196
Cdd:TIGR04523 321 -KKLEEIQNQIS 331
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
89-195 5.75e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 39.78  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   89 EQKAQLEEQLKEVRKK-----------CAEE-----AQLISS--LKAELTSQESQISTYEEELAKAREELSRLQQETAEL 150
Cdd:PRK10246  380 EQLRQWQQQLTHAEQKlnalpaitltlTADEvaaalAQHAEQrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQR 459
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 229577185  151 EESVESGKAQLEPLQQHLQD----SQQEissmqmklMEMKDLENHNSQL 195
Cdd:PRK10246  460 NAALNEMRQRYKEKTQQLADvktiCEQE--------ARIKDLEAQRAQL 500
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
82-196 6.02e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 37.29  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   82 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSlKAELTSQESQISTYEEELAKAREELSRLQQetaeleesvesgkaQL 161
Cdd:TIGR02473  27 AEFERLETQLQQLIKYREEYEQQALEKVGAGTS-ALELSNYQRFIRQLDQRIQQQQQELALLQQ--------------EV 91
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 229577185  162 EPLQQHLQDSQQEIssMQMKLMEMKDLENHNSQLN 196
Cdd:TIGR02473  92 EAKRERLLEARREL--KALEKLKEKKQKEYRAEEA 124
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
45-188 6.12e-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: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   45 KEDTIKQRTSEVQDLQDEVQRENTNLQKLQaqkqqvqellDELDEQKAQLE-------------EQLK-EVRKKCAEEAQ 110
Cdd:pfam10174 238 KDTKISSLERNIRDLEDEVQMLKTNGLLHT----------EDREEEIKQMEvykshskfmknkiDQLKqELSKKESELLA 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  111 LISSLKAeLTSQES----QISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK 186
Cdd:pfam10174 308 LQTKLET-LTNQNSdckqHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLK 386

                  ..
gi 229577185  187 DL 188
Cdd:pfam10174 387 DM 388
MCP2201-like_sensor cd19411
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar ...
88-184 6.29e-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: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  88 DEQKAQLEEQLKEVRKKCAEeaqLISSLKAELTSQESQisTYEEELAKAREELSRLQQETAELeesVESGKA-------- 159
Cdd:cd19411   35 PAERAKELARIAAARARITE---LLKKLEKLITSPEGK--ALLAAIAEARAAYLAARDKVLEL---KKAGDReearalll 106
                         90       100
                 ....*....|....*....|....*.
gi 229577185 160 -QLEPLQQHLQDSQQEISSMQMKLME 184
Cdd:cd19411  107 gELRPAQAAYLAALDALVDYQEELMD 132
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
82-187 6.51e-03

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


Pssm-ID: 128778  Cd Length: 127  Bit Score: 37.24  E-value: 6.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    82 ELLDELDEQKAQLEEQLKEVRKKCaeeaQLISSLKAELTSQ-ESQISTYEEELAKAREEL-SRLQQETAELEESVESGKA 159
Cdd:smart00502   7 ELLTKLRKKAAELEDALKQLISII----QEVEENAADVEAQiKAAFDELRNALNKRKKQLlEDLEEQKENKLKVLEQQLE 82
                           90       100
                   ....*....|....*....|....*...
gi 229577185   160 QLEPLQQHLQDSQQEISsmqmKLMEMKD 187
Cdd:smart00502  83 SLTQKQEKLSHAINFTE----EALNSGD 106
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
33-182 6.54e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.44  E-value: 6.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    33 REKNNVEQDLKEKEDTIKQRTS---EVQDLQDEVQRentnlqklQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEE- 108
Cdd:pfam12128  379 RRRSKIKEQNNRDIAGIKDKLAkirEARDRQLAVAE--------DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELk 450
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 229577185   109 -----AQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 182
Cdd:pfam12128  451 lrlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
85-175 6.54e-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: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   85 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAeLEESVESGKAQLEPL 164
Cdd:COG3096   281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQEDLEEL 359
                          90
                  ....*....|.
gi 229577185  165 QQHLqDSQQEI 175
Cdd:COG3096   360 TERL-EEQEEV 369
PRK01156 PRK01156
chromosome segregation protein; Provisional
34-179 6.80e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.50  E-value: 6.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  34 EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 113
Cdd:PRK01156 588 RSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIP 667
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229577185 114 SlKAELTSQESQIstyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 179
Cdd:PRK01156 668 D-LKEITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK 729
CCDC-167 pfam15188
Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, ...
84-139 6.84e-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: 35.72  E-value: 6.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   84 LDELDEQKAQLEEQLKEVRKKcAEEAQLI----SSLKAELTSQESQISTYEEELAKAREE 139
Cdd:pfam15188   5 IDRLEEKIASCRDRLERIEKK-LRREELSeedrRSLEKELLLLKKRLEKNEEELKLLRKE 63
mukB PRK04863
chromosome partition protein MukB;
86-173 6.99e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   86 ELDEQKAQLEEQ---LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEELAK-------------- 135
Cdd:PRK04863  294 ELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAasdhlnlvqtalrQQEKIERYQADLEEleerleeqnevvee 373
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 229577185  136 AREELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 173
Cdd:PRK04863  374 ADEQQEENEARAEAAEEEVDELKSQLADYQQAL-DVQQ 410
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
35-185 7.32e-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: 7.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    35 KNNVEQDLKEKEDTIKQRtsevQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEE--QLKEVRKKCAEEAQLI 112
Cdd:TIGR00618  320 MRSRAKLLMKRAAHVKQQ----SSIEEQRRLLQT-------LHSQEIHIRDAHEVATSIREIscQQHTLTQHIHTLQQQK 388
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229577185   113 SSLKAELTSQESQISTYEEELAKAREELSR---LQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM 185
Cdd:TIGR00618  389 TTLTQKLQSLCKELDILQREQATIDTRTSAfrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
41-192 7.49e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.05  E-value: 7.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  41 DLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKK---CAEEAQLISSLKA 117
Cdd:PRK04778 276 DLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSytlNESELESVRQLEK 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 118 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ-------DSQQEISSMQMKLMEMK-DLE 189
Cdd:PRK04778 356 QLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQglrkdelEAREKLERYRNKLHEIKrYLE 435

                 ...
gi 229577185 190 NHN 192
Cdd:PRK04778 436 KSN 438
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
21-196 7.90e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 39.27  E-value: 7.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   21 VLKYSCIVCWSSREKNNVeQDLKEKEDTIKqrtseVQDLQDEV-QREN-----TNLQKLQAQKQQVQELLDEL------- 87
Cdd:pfam05911 603 VLELSHILDWISNHCFSL-LDVSSMEDEIK-----KHDCIDKVtLSENkvaqvDNGCSEIDNLSSDPEIPSDGplvsgsn 676
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   88 ----DEQKAQLEEQLK-EVRKKCAEEA-------------------QLISSLKAEL-TSQES------QI-------STY 129
Cdd:pfam05911 677 dlktEENKRLKEEFEQlKSEKENLEVElasctenlestksqlqeseQLIAELRSELaSLKESnslaetQLkcmaesyEDL 756
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229577185  130 EEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQLN 196
Cdd:pfam05911 757 ETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCDADQEDKKLQ 823
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
91-184 8.47e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 36.79  E-value: 8.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185    91 KAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQEtaeleesvesgkaqlepLQQHLQD 170
Cdd:smart00935  20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQE-----------------FQRKQQK 80
                           90
                   ....*....|....
gi 229577185   171 SQQEISSMQMKLME 184
Cdd:smart00935  81 LQQDLQKRQQEELQ 94
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
43-151 8.67e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.14  E-value: 8.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  43 KEKEDTIK--QRTSEVQ--DLQDEVQRENTnlQKLQAQKQQVQELLDEL--DEQKAQ-LEEQLKEVRKKCAEEaqLISSL 115
Cdd:PRK05771  16 SYKDEVLEalHELGVVHieDLKEELSNERL--RKLRSLLTKLSEALDKLrsYLPKLNpLREEKKKVSVKSLEE--LIKDV 91
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 229577185 116 KAELTSQESQISTYEEELAKAREELSRLQQETAELE 151
Cdd:PRK05771  92 EEELEKIEKEIKELEEEISELENEIKELEQEIERLE 127
FliJ pfam02050
Flagellar FliJ protein;
84-179 8.90e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 36.49  E-value: 8.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185   84 LDELDEQKAQLEEQLKEVRKKCAEEA-----QLISSLKAELTSQESQISTYEEELAKAREELSRLQQEtaelEESVE--S 156
Cdd:pfam02050  21 LEELQQYRAEYQQQLSGAGQGISAAElrnyqAFISQLDEAIAQQQQELAQAEAQVEKAREEWQEARQE----RKSLEklR 96
                          90       100
                  ....*....|....*....|....*...
gi 229577185  157 GKAQLEplQQHLQDSQQ-----EISSMQ 179
Cdd:pfam02050  97 EREKKE--ERKEQNRREqkqldELAARL 122
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
36-176 9.63e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 9.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  36 NNVEQDLkekedtikqrtSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLI--- 112
Cdd:PRK02224 401 GDAPVDL-----------GNAEDFLEELREE-----------------RDELREREAELEATLRTARERVEEAEALLeag 452
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229577185 113 -----------SSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKaQLEPLQQHLQDSQQEIS 176
Cdd:PRK02224 453 kcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLEERREDLEELIA 526
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-187 9.79e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  35 KNNVEQDLKEKEDTIKQRT-------SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKkcae 107
Cdd:PRK02224 518 REDLEELIAERRETIEEKReraeelrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER---- 593
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185 108 eaqlISSLKAELTSQESQISTYEEELA-------KAREELSRLQQETAELEESVESgkAQLEPLQQHLQDSQQEISSMQM 180
Cdd:PRK02224 594 ----IRTLLAAIADAEDEIERLREKREalaelndERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEE 667

                 ....*..
gi 229577185 181 KLMEMKD 187
Cdd:PRK02224 668 KLDELRE 674
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
84-161 1.00e-02

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 37.07  E-value: 1.00e-02
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577185  84 LDELDEQKAQLEEQLKEVRKKCAE---EAQLIsslKAELTSQESQIstYEEELAKAREELSRLQQET-AELEESVESGKA 159
Cdd:COG0711   40 LAEAERAKEEAEAALAEYEEKLAEaraEAAEI---IAEARKEAEAI--AEEAKAEAEAEAERIIAQAeAEIEQERAKALA 114

                 ..
gi 229577185 160 QL 161
Cdd:COG0711  115 EL 116
 
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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