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Conserved domains on  [gi|664806051|ref|NP_001287743|]
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keratin, type II cytoskeletal 78 isoform 2 [Homo sapiens]

Protein Classification

intermediate filament family protein( domain architecture ID 705869)

intermediate filament (IF) family protein is a primordial component of the cytoskeleton and the nuclear envelope; such as type I keratins

CATH:  1.20.5.170
Gene Ontology:  GO:0005882

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
18-313 2.43e-93

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 282.96  E-value: 2.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   18 KVRFLEQQNKVLETKWhLLQQQGLSGSQQGLEPVFEACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHR 97
Cdd:pfam00038  19 KVRFLEQQNKLLETKI-SELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   98 RATLENDFVVLKKDVDGVFLSKMELEGKLEALREYLYFLKHLNEEELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRA 177
Cdd:pfam00038  98 RTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRA 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  178 RYEEIARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGELA 257
Cdd:pfam00038 178 QYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQ 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 664806051  258 LKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEECR 313
Cdd:pfam00038 258 LADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
18-313 2.43e-93

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 282.96  E-value: 2.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   18 KVRFLEQQNKVLETKWhLLQQQGLSGSQQGLEPVFEACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHR 97
Cdd:pfam00038  19 KVRFLEQQNKLLETKI-SELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   98 RATLENDFVVLKKDVDGVFLSKMELEGKLEALREYLYFLKHLNEEELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRA 177
Cdd:pfam00038  98 RTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRA 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  178 RYEEIARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGELA 257
Cdd:pfam00038 178 QYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQ 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 664806051  258 LKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEECR 313
Cdd:pfam00038 258 LADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
56-308 1.26e-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: 56.99  E-value: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051    56 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDgvflskmELEGKLEALREYLYF 135
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-------RLEAEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   136 LKHLNEEELGQLQTQASDtsvvLSMDNNRYLDFSSIITEVRARYEEIARSSKAEAEAL--YQTKYQELQVSAQLHGDRMQ 213
Cdd:TIGR02168  752 LSKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNEEAANLRERLE 827
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   214 ETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGElalkDAQAKVDELEAALRMAKQNLARLLCEYQELTSTK 293
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNERASLEEALALLRSELEELSEEL 903
                          250
                   ....*....|....*
gi 664806051   294 LSLDVEIATYRRLLE 308
Cdd:TIGR02168  904 RELESKRSELRRELE 918
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
56-311 1.26e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  56 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREylyf 135
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---- 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 136 LKHLNEEELGQLQTQASDTSVVLSMDNNRyldfssiITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLhgdrmQET 215
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEE-------LEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEA 377
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 216 KVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQR---GELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTST 292
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERlerLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
                        250
                 ....*....|....*....
gi 664806051 293 KLSLDVEIATYRRLLEGEE 311
Cdd:COG1196  458 EEALLELLAELLEEAALLE 476
PRK09039 PRK09039
peptidoglycan -binding protein;
141-281 7.59e-06

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.65  E-value: 7.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 141 EEELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARyeeiARSSKAEAEALyQTKYQELQVSAQLHGDRMQETKVQIS 220
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAS----LSAAEAERSRL-QALLAELAGAGAAAEGRAGELAQELD 126
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664806051 221 QLHQEIQR-------LQSQTENLKKQNASLQAAITDAEQRGelalKDAQAKVD----ELEAALRMAKQNLAR 281
Cdd:PRK09039 127 SEKQVSARalaqvelLNQQIAALRRQLAALEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
18-313 2.43e-93

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 282.96  E-value: 2.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   18 KVRFLEQQNKVLETKWhLLQQQGLSGSQQGLEPVFEACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHR 97
Cdd:pfam00038  19 KVRFLEQQNKLLETKI-SELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   98 RATLENDFVVLKKDVDGVFLSKMELEGKLEALREYLYFLKHLNEEELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRA 177
Cdd:pfam00038  98 RTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRA 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  178 RYEEIARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGELA 257
Cdd:pfam00038 178 QYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQ 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 664806051  258 LKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEECR 313
Cdd:pfam00038 258 LADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
56-308 1.26e-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: 56.99  E-value: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051    56 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDgvflskmELEGKLEALREYLYF 135
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-------RLEAEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   136 LKHLNEEELGQLQTQASDtsvvLSMDNNRYLDFSSIITEVRARYEEIARSSKAEAEAL--YQTKYQELQVSAQLHGDRMQ 213
Cdd:TIGR02168  752 LSKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNEEAANLRERLE 827
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   214 ETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGElalkDAQAKVDELEAALRMAKQNLARLLCEYQELTSTK 293
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNERASLEEALALLRSELEELSEEL 903
                          250
                   ....*....|....*
gi 664806051   294 LSLDVEIATYRRLLE 308
Cdd:TIGR02168  904 RELESKRSELRRELE 918
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
56-311 1.26e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  56 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREylyf 135
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---- 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 136 LKHLNEEELGQLQTQASDTSVVLSMDNNRyldfssiITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLhgdrmQET 215
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEE-------LEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEA 377
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 216 KVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQR---GELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTST 292
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERlerLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
                        250
                 ....*....|....*....
gi 664806051 293 KLSLDVEIATYRRLLEGEE 311
Cdd:COG1196  458 EEALLELLAELLEEAALLE 476
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
53-281 2.38e-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: 52.46  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  53 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREY 132
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 133 LyflkhlnEEELGQLQTQASDTSVVLSMDNNRYLDFSSIItevrARYEEIARSSKAEAEALYQTKyQELQVSAQLHGDRM 212
Cdd:COG4942  106 L-------AELLRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAEELRADL-AELAALRAELEAER 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664806051 213 QETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLAR 281
Cdd:COG4942  174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE----LAELQQEAEELEALIARLEAEAAA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
56-308 1.29e-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: 50.83  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051    56 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREYLYF 135
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   136 LKHLNEE----------ELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARYEEIARSSKAEAEAL--YQTKYQELQV 203
Cdd:TIGR02168  314 LERQLEEleaqleelesKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetLRSKVAQLEL 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   204 SAQLHGDRMQETKVQISQLHQEIQRLQSQTENL--KKQNASLQAAITDAEQRGElALKDAQAKVDELEAALRMAKQNLAR 281
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEE-ELEELQEELERLEEALEELREELEE 472
                          250       260
                   ....*....|....*....|....*..
gi 664806051   282 LLCEYQELTSTKLSLDVEIATYRRLLE 308
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDSLERLQE 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
53-289 1.97e-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: 50.06  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051    53 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALREy 132
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE- 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   133 lyfLKHLNEEELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARYEEiARSSKAEAEALYQTKYQELQVSAQLHGD-- 210
Cdd:TIGR02168  776 ---ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN-LRERLESLERRIAATERRLEDLEEQIEEls 851
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   211 -RMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGELA---LKDAQAKVDELEAALRMAKQNLARLLCEY 286
Cdd:TIGR02168  852 eDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELRL 931

                   ...
gi 664806051   287 QEL 289
Cdd:TIGR02168  932 EGL 934
PRK09039 PRK09039
peptidoglycan -binding protein;
141-281 7.59e-06

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.65  E-value: 7.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 141 EEELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARyeeiARSSKAEAEALyQTKYQELQVSAQLHGDRMQETKVQIS 220
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAS----LSAAEAERSRL-QALLAELAGAGAAAEGRAGELAQELD 126
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664806051 221 QLHQEIQR-------LQSQTENLKKQNASLQAAITDAEQRGelalKDAQAKVD----ELEAALRMAKQNLAR 281
Cdd:PRK09039 127 SEKQVSARalaqvelLNQQIAALRRQLAALEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
176-282 7.97e-06

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 47.35  E-value: 7.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 176 RARYEEIARSSKAEAEALYQTKYQELQVsAQLHGDRMQE-------TKVQISQLHQEIQRLQSQTENLKKQNASLQAAIT 248
Cdd:COG1566  101 RLEAELGAEAEIAAAEAQLAAAQAQLDL-AQRELERYQAlykkgavSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLR 179
                         90       100       110
                 ....*....|....*....|....*....|....
gi 664806051 249 DAEQrgelaLKDAQAKVDELEAALRMAKQNLARL 282
Cdd:COG1566  180 EEEE-----LAAAQAQVAQAEAALAQAELNLART 208
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
52-308 2.08e-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: 46.98  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051    52 FEACLDQLRKQLEQLQGERgalDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDGVFLSKMELEGKLEALRE 131
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRRER---EKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   132 YLyflkHLNEEELGQLQTQASDtsvvlsMDNNRYLDFSSIITEVRAryeEIARSSKAEAEalyqtKYQELQVSAQlhgdR 211
Cdd:TIGR02169  266 RL----EEIEQLLEELNKKIKD------LGEEEQLRVKEKIGELEA---EIASLERSIAE-----KERELEDAEE----R 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   212 MQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLARLLCEYQELTS 291
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE----LEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
                          250
                   ....*....|....*..
gi 664806051   292 TKLSLDVEIatyRRLLE 308
Cdd:TIGR02169  400 EINELKREL---DRLQE 413
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
201-307 3.64e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 201 LQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLA 280
Cdd:COG4942   11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELA 86
                         90       100
                 ....*....|....*....|....*..
gi 664806051 281 RLLceyQELTSTKLSLDVEIATYRRLL 307
Cdd:COG4942   87 ELE---KEIAELRAELEAQKEELAELL 110
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
59-302 9.36e-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: 44.67  E-value: 9.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051    59 LRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDfvvlkkdvdgvflsKMELEGKLEALREYLYFLK- 137
Cdd:TIGR02169  721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR--------------IEELEEDLHKLEEALNDLEa 786
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   138 HLNEEELGQLQTQASDtsvvlsmdnnryldfssiITEVRARYEEIARSSKAEAEALYQTKyqelqvsaQLHGDRMQETKV 217
Cdd:TIGR02169  787 RLSHSRIPEIQAELSK------------------LEEEVSRIEARLREIEQKLNRLTLEK--------EYLEKEIQELQE 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   218 QISQLHQEIQRLQSQTENLKKQNASLQAAItdAEQRGELA-----LKDAQAKVDELEAALRMAKQNLARLLCEYQELTST 292
Cdd:TIGR02169  841 QRIDLKEQIKSIEKEIENLNGKKEELEEEL--EELEAALRdlesrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
                          250
                   ....*....|
gi 664806051   293 KLSLDVEIAT 302
Cdd:TIGR02169  919 LSELKAKLEA 928
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
56-288 9.60e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 9.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   56 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDfvvlkKDVDGVFLSKMELEGKLEALREYLYF 135
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-----IDVASAEREIAELEAELERLDASSDD 686
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  136 LKHLNEE------ELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAqlHG 209
Cdd:COG4913   687 LAALEEQleeleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA--VE 764
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664806051  210 DRMQEtkvqisQLHQEIQRLQSQTENLKKQnasLQAAITDAEQRGELALKDAQAKVDELEAALRMAKQNLARLLCEYQE 288
Cdd:COG4913   765 RELRE------NLEERIDALRARLNRAEEE---LERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYEE 834
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
122-308 1.75e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 122 LEGKLEALREYLYFLkhlnEEELGQLQTQASDTSVVLS--MDNNRYLDFSSIITEVRARYEEI------ARSSKAEAEAL 193
Cdd:COG3206  166 LELRREEARKALEFL----EEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELesqlaeARAELAEAEAR 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 194 YQTKYQEL----QVSAQLHGD--------RMQETKVQISQL-------HQEIQRLQSQTENLKKQnasLQAAITDAEQRG 254
Cdd:COG3206  242 LAALRAQLgsgpDALPELLQSpviqqlraQLAELEAELAELsarytpnHPDVIALRAQIAALRAQ---LQQEAQRILASL 318
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 664806051 255 ELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTStkLSLDVEIA--TYRRLLE 308
Cdd:COG3206  319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRR--LEREVEVAreLYESLLQ 372
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
195-283 2.53e-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: 42.83  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 195 QTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRM 274
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEIAELRAELEA 101

                 ....*....
gi 664806051 275 AKQNLARLL 283
Cdd:COG4942  102 QKEELAELL 110
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
180-308 2.90e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  180 EEIARSSKAEAEAlyQTKYQELQVS-AQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASL--------------Q 244
Cdd:COG4913   309 AELERLEARLDAL--REELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglplpasaeefaalR 386
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664806051  245 AAITDAEQRGELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLE 308
Cdd:COG4913   387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
57-293 3.95e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  57 DQLRKQLEQLQGERGALDAELKACRDQEEEykskyeeeaHRRatlENDFVVLKKDVDGVFLSKMELEGKLEALREYLYFL 136
Cdd:COG3206  171 EEARKALEFLEEQLPELRKELEEAEAALEE---------FRQ---KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEA 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 137 khlnEEELGQLQTQASDTSVVLSMDNNryldfSSIITEVRARYEEiARSSKAEAEALYQTKYQELQvSAQlhgDRMQETK 216
Cdd:COG3206  239 ----EARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAE-LEAELAELSARYTPNHPDVI-ALR---AQIAALR 304
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664806051 217 VQISQLHQEI-QRLQSQTENLKKQNASLQAAITDAEQRGeLALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTK 293
Cdd:COG3206  305 AQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
141-311 1.56e-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: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 141 EEELGQLQTQASDTSvvlsmdnnRYLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQIS 220
Cdd:COG1196  199 ERQLEPLERQAEKAE--------RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 221 QLHQEIQRLQSQTENLKKQNASLQAAITDAEQ---RGELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLD 297
Cdd:COG1196  271 ELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
                        170
                 ....*....|....
gi 664806051 298 VEIATYRRLLEGEE 311
Cdd:COG1196  351 EELEEAEAELAEAE 364
GrpE COG0576
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein ...
212-278 2.02e-03

Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440341 [Multi-domain]  Cd Length: 147  Bit Score: 38.21  E-value: 2.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664806051 212 MQETKVQISQLHQEIQRLQSQTENLKKQnaslqaaitdAEQRGELALKDAQAKV--------DELEAALRMAKQN 278
Cdd:COG0576    1 MEELEAELAELKDRLLRLQAEFENYRKR----------TEREREEARKYALEKLaedllpvlDNLERALAAAEED 65
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
56-312 2.86e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  56 LDQLRKQLEQ------------LQGERGALDAELKACRDQEEEYKSKYEE-----EAHRR-----ATLENDFVVLKKDVD 113
Cdd:PRK02224 189 LDQLKAQIEEkeekdlherlngLESELAELDEEIERYEEQREQARETRDEadevlEEHEErreelETLEAEIEDLRETIA 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 114 GVFLSKMELEGKLEALREYLYFLKHLNEEELGQLQ-TQASDTSVVLSMDnnrylDFSSIITEVRARYEEIARSSKA---E 189
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEARRE-----ELEDRDEELRDRLEECRVAAQAhneE 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 190 AEALYQtkyqelqvSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELE 269
Cdd:PRK02224 344 AESLRE--------DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER----FGDAPVDLGNAE 411
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 664806051 270 AALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEEC 312
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKC 454
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
172-282 4.55e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 172 ITEVRARYEEI-ARSSKAEAEALYQTKYQEL-QVSAQLHG--DRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAI 247
Cdd:COG4717  104 LEELEAELEELrEELEKLEKLLQLLPLYQELeALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 664806051 248 TDAEQRGELALKDAQAKVDELEAALRMAKQNLARL 282
Cdd:COG4717  184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
193-281 4.59e-03

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 38.77  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 193 LYQTKYQELQVSAQLhgdRMQETKVQISQLHQEIQRLQSqtenLKKQNASLQAAITDAEQrgelALKDAQAKVDELEAAL 272
Cdd:COG0845   54 LDPPDLQAALAQAQA---QLAAAQAQLELAKAELERYKA----LLKKGAVSQQELDQAKA----ALDQAQAALAAAQAAL 122

                 ....*....
gi 664806051 273 RMAKQNLAR 281
Cdd:COG0845  123 EQARANLAY 131
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
53-280 4.94e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  53 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKDVDgvflskmELEGKLEALREY 132
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 133 LyflkhlnEEELGQLQTQASDTSVVLSMDNNRylDFSSIITEVRARyEEIARSSKAEAEALYQTK--YQELQVSAQLHGD 210
Cdd:COG3883   88 L-------GERARALYRSGGSVSYLDVLLGSE--SFSDFLDRLSAL-SKIADADADLLEELKADKaeLEAKKAELEAKLA 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 211 RMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGELALKDAQAKVDELEAALRMAKQNLA 280
Cdd:COG3883  158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
157-280 5.61e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 38.55  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  157 VLSMDNNRYLDFSSI-ITEVRARYEEIARSSKAEAEAlyQTKYQELQvsaqlhgDRMQETKVQISQLHQEIQRLQSQTEN 235
Cdd:TIGR04320 230 FVNFNDSYIADGNKFdKTPIPNPPNSLAALQAKLATA--QADLAAAQ-------TALNTAQAALTSAQTAYAAAQAALAT 300
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 664806051  236 LKKQNASLQAAitdAEQRGELALKDAQAKVDELEAALRMAKQNLA 280
Cdd:TIGR04320 301 AQKELANAQAQ---ALQTAQNNLATAQAALANAEARLAKAKEALA 342
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
53-250 6.12e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051   53 EACLDQLRKQLEQLQGERGALDAELKACRDQEEeykskyeeeAHRRATLENDFVVLKkdvdgvflskmELEGKLEALREy 132
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELD---------ELEAQIRGNGGDRLE-----------QLEREIERLER- 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  133 lyflkHLNE--EELGQLQTQASDtsVVLSMDNNRyLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLHgd 210
Cdd:COG4913   353 -----ELEEreRRRARLEALLAA--LGLPLPASA-EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR-- 422
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 664806051  211 rmqetkvqisQLHQEIQRLQSQTENLKKQNASLQAAITDA 250
Cdd:COG4913   423 ----------ELEAEIASLERRKSNIPARLLALRDALAEA 452
PRK12704 PRK12704
phosphodiesterase; Provisional
169-282 6.47e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 6.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051 169 SSIITEVRARYEEIARSSKAEA-----EALYQTKYQELQVSAQLHGD---RMQETKVQISQLHQEIQRLQSQTENLKKQN 240
Cdd:PRK12704  30 EAKIKEAEEEAKRILEEAKKEAeaikkEALLEAKEEIHKLRNEFEKElreRRNELQKLEKRLLQKEENLDRKLELLEKRE 109
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 664806051 241 ASLQAAITDAEQRgELALKDAQAKVDELEAALRMAKQNLARL 282
Cdd:PRK12704 110 EELEKKEKELEQK-QQELEKKEEELEELIEEQLQELERISGL 150
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
218-282 8.95e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 36.52  E-value: 8.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664806051  218 QISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLARL 282
Cdd:pfam11559  60 TIRTLEAEIERLQSKIERLKTQLEDLERELALLQAK----ERQLEKKLKTLEQKLKNEKEELQRL 120
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
126-308 9.05e-03

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: 38.16  E-value: 9.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  126 LEALREYLYFLKHLNEEELGQLQTQASDTSVVLSmDNNRYLDFSSIITEVRARYEEIARSSKAEAEALYQ---------- 195
Cdd:pfam05483 115 IEAQRKAIQELQFENEKVSLKLEEEIQENKDLIK-ENNATRHLCNLLKETCARSAEKTKKYEYEREETRQvymdlnnnie 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806051  196 ---TKYQELQVSAQlhgDRMQETKVQISQLHQEIQRL----QSQTENLKKQNASLQAAITDAEQRGE---LALKDAQAKV 265
Cdd:pfam05483 194 kmiLAFEELRVQAE---NARLEMHFKLKEDHEKIQHLeeeyKKEINDKEKQVSLLLIQITEKENKMKdltFLLEESRDKA 270
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 664806051  266 DELEAALRMAKQNLARLLCEYQELTS----TKLSLDVEIATYRRLLE 308
Cdd:pfam05483 271 NQLEEKTKLQDENLKELIEKKDHLTKeledIKMSLQRSMSTQKALEE 317
 
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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