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Conserved domains on  [gi|2169827764|ref|NP_001385711|]
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gamma-taxilin isoform 1 [Rattus norvegicus]

Protein Classification

taxilin( domain architecture ID 12101238)

taxilin is a myosin-like coiled-coil protein involved in intracellular vesicle traffic

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
140-447 1.72e-106

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


:

Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 320.36  E-value: 1.72e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 140 KEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQ 219
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 220 RHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKH 299
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 300 KELQQQLVDAKLQQTTqlikEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFT 379
Cdd:pfam09728 161 KELEVQLAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2169827764 380 TFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTE 447
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
140-447 1.72e-106

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 320.36  E-value: 1.72e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 140 KEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQ 219
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 220 RHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKH 299
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 300 KELQQQLVDAKLQQTTqlikEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFT 379
Cdd:pfam09728 161 KELEVQLAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2169827764 380 TFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTE 447
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
168-454 1.61e-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: 54.29  E-value: 1.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  168 DLLEEsrnVQKQMKIL--QKKQAQIVKEKVHLQSEHSKAILARSkLESLCRELQRHNKTLKEENMQQAREEEERRKEATA 245
Cdd:TIGR02168  193 DILNE---LERQLKSLerQAEKAERYKELKAELRELELALLVLR-LEELREELEELQEELKEAEEELEELTAELQELEEK 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  246 HFQI---------TLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQ 316
Cdd:TIGR02168  269 LEELrlevseleeEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  317 LIKEAD------EKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTK 390
Cdd:TIGR02168  349 LKEELEsleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2169827764  391 KIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEykafqIKLERLEKLCRALQTERNELNEK 454
Cdd:TIGR02168  429 KLEEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALDAAERELAQL 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
241-461 2.78e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 241 KEATAHFqitLNEIQAQLEqhdihnaKLRQENIELGEKLKKLIEQYALREEHIDKV-FKHKELQQQLvdAKLQQTTQLIK 319
Cdd:COG1196   227 AELLLLK---LRELEAELE-------ELEAELEELEAELEELEAELAELEAELEELrLELEELELEL--EEAQAEEYELL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 320 EADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKET 399
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2169827764 400 IIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEVLKEQ 461
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
PRK11281 PRK11281
mechanosensitive channel MscK;
100-459 1.32e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.90  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  100 SSVFCTQETREEIPGREartgppDGQQDSEcSRNKEKTLGKEVLLLMQALN-TLST------PEEKLAALCKKYADLLEE 172
Cdd:PRK11281    23 SSAFARAASNGDLPTEA------DVQAQLD-ALNKQKLLEAEDKLVQQDLEqTLALldkidrQKEETEQLKQQLAQAPAK 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  173 SRNVQKQMKILQKKQAQIVKEkvhlqsEHSKAILAR--SKLESLCRELQRHNKTLKEENMQQAREEEerrkeATAHFQIT 250
Cdd:PRK11281    96 LRQAQAELEALKDDNDEETRE------TLSTLSLRQleSRLAQTLDQLQNAQNDLAEYNSQLVSLQT-----QPERAQAA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  251 LNEIQAQLEQhdIHNaklrqenielgeKLKKL-IEQYALREEHIDKVfkhkELQQQLVDAKLQQTTQLIKEADekhqrer 329
Cdd:PRK11281   165 LYANSQRLQQ--IRN------------LLKGGkVGGKALRPSQRVLL----QAEQALLNAQNDLQRKSLEGNT------- 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  330 efLLKEATESRHKYEQMK----QQEVQLKQQ------LSLYMDKFEEFQ----TTMAKSNELFttfRQEMEKMTKKIKKL 395
Cdd:PRK11281   220 --QLQDLLQKQRDYLTARiqrlEHQLQLLQEainskrLTLSEKTVQEAQsqdeAARIQANPLV---AQELEINLQLSQRL 294
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2169827764  396 EKETiiwrtkwENNNkALLQmaeeKTVRDKEYkafqiklerlekLCRALQTERNeLNEKVEVLK 459
Cdd:PRK11281   295 LKAT-------EKLN-TLTQ----QNLRVKNW------------LDRLTQSERN-IKEQISVLK 333
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
140-447 1.72e-106

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 320.36  E-value: 1.72e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 140 KEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQ 219
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 220 RHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKH 299
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 300 KELQQQLVDAKLQQTTqlikEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFT 379
Cdd:pfam09728 161 KELEVQLAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2169827764 380 TFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTE 447
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
168-454 1.61e-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: 54.29  E-value: 1.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  168 DLLEEsrnVQKQMKIL--QKKQAQIVKEKVHLQSEHSKAILARSkLESLCRELQRHNKTLKEENMQQAREEEERRKEATA 245
Cdd:TIGR02168  193 DILNE---LERQLKSLerQAEKAERYKELKAELRELELALLVLR-LEELREELEELQEELKEAEEELEELTAELQELEEK 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  246 HFQI---------TLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQ 316
Cdd:TIGR02168  269 LEELrlevseleeEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  317 LIKEAD------EKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTK 390
Cdd:TIGR02168  349 LKEELEsleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2169827764  391 KIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEykafqIKLERLEKLCRALQTERNELNEK 454
Cdd:TIGR02168  429 KLEEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALDAAERELAQL 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
192-456 3.82e-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: 3.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  192 KEKVHLQSEHSKAILARskLESLCRELQRHNKTLKeenmQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQE 271
Cdd:TIGR02168  174 RKETERKLERTRENLDR--LEDILNELERQLKSLE----RQAEKAERYKELKAELRELELALLVLRLEELREELEELQEE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  272 NIELGEKLKKLIEQYALREEHID-KVFKHKELQQQLVDA--KLQQTTQLIKEAD---EKHQREREFLLKEATESRHKYEQ 345
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEeLRLEVSELEEEIEELqkELYALANEISRLEqqkQILRERLANLERQLEELEAQLEE 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  346 MKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKEtiiwrtkWENNNKALLQMAEEKTVRDK 425
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLELQIASLNN 400
                          250       260       270
                   ....*....|....*....|....*....|.
gi 2169827764  426 EYKAFQIKLERLEKLCRALQTERNELNEKVE 456
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLE 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
210-462 1.56e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  210 KLESLCRELQRHNKTLKEENMQ------QAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLI 283
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEEleeeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  284 EQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEADEKHQREREfLLKEATESRHKYEQMKQQEVQLKQQLSLYMDK 363
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  364 FEEFQTTMAKSNElfttfrqEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRA 443
Cdd:TIGR02168  847 IEELSEDIESLAA-------EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
                          250
                   ....*....|....*....
gi 2169827764  444 LQTERNELNEKVEVLKEQV 462
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRI 938
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
241-461 2.78e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 241 KEATAHFqitLNEIQAQLEqhdihnaKLRQENIELGEKLKKLIEQYALREEHIDKV-FKHKELQQQLvdAKLQQTTQLIK 319
Cdd:COG1196   227 AELLLLK---LRELEAELE-------ELEAELEELEAELEELEAELAELEAELEELrLELEELELEL--EEAQAEEYELL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 320 EADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKET 399
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2169827764 400 IIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEVLKEQ 461
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
COG5022 COG5022
Myosin heavy chain [General function prediction only];
164-463 5.49e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 46.22  E-value: 5.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  164 KKYADLLEESRNVQKqmKILQKKQAQIVKEKVHlqsEHSKAILarskLESLCRELQRHNKTL---KEENMQQAREEEERR 240
Cdd:COG5022    810 KEYRSYLACIIKLQK--TIKREKKLRETEEVEF---SLKAEVL----IQKFGRSLKAKKRFSllkKETIYLQSAQRVELA 880
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  241 KEATAHFQITLNEIQAQLEQhdihNAKLRQENIELGEKLKK-LIEQYALREEHIDKVFKH-----------KELQQQLVD 308
Cdd:COG5022    881 ERQLQELKIDVKSISSLKLV----NLELESEIIELKKSLSSdLIENLEFKTELIARLKKLlnnidleegpsIEYVKLPEL 956
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  309 AKLQQTTQLIKEAdekhQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFrQEMEKM 388
Cdd:COG5022    957 NKLHEVESKLKET----SEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV-AELQSA 1031
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2169827764  389 TKKIKKlEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEkVEVLKEQVS 463
Cdd:COG5022   1032 SKIISS-ESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKT-INVKDLEVT 1104
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
156-462 5.72e-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: 46.21  E-value: 5.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  156 EEKLAALckKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILAR--SKLESLCRELQRHNKTLKEENMQqa 233
Cdd:TIGR02169  205 REREKAE--RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKltEEISELEKRLEEIEQLLEELNKK-- 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  234 reEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAklqq 313
Cdd:TIGR02169  281 --IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK---- 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  314 ttqlIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIK 393
Cdd:TIGR02169  355 ----LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2169827764  394 -------KLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEVLKEQV 462
Cdd:TIGR02169  431 gieakinELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
156-395 9.75e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 9.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  156 EEKLAALCKKYADLLEESRNVQKQMKILQK----KQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLK----- 226
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrea 804
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  227 -----------EENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYalreEHIDK 295
Cdd:TIGR02168  805 ldelraeltllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EALLN 880
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  296 VFKHKELQQQLVDAKLQQTTQLIKEADEKHQREREfLLKEATESRHKY----EQMKQQEVQLKQQLS-LYMDKFEEFQTT 370
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRR-ELEELREKLAQLelrlEGLEVRIDNLQERLSeEYSLTLEEAEAL 959
                          250       260
                   ....*....|....*....|....*
gi 2169827764  371 MAKSNELFTTFRQEMEKMTKKIKKL 395
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKIKEL 984
PRK11281 PRK11281
mechanosensitive channel MscK;
100-459 1.32e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.90  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  100 SSVFCTQETREEIPGREartgppDGQQDSEcSRNKEKTLGKEVLLLMQALN-TLST------PEEKLAALCKKYADLLEE 172
Cdd:PRK11281    23 SSAFARAASNGDLPTEA------DVQAQLD-ALNKQKLLEAEDKLVQQDLEqTLALldkidrQKEETEQLKQQLAQAPAK 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  173 SRNVQKQMKILQKKQAQIVKEkvhlqsEHSKAILAR--SKLESLCRELQRHNKTLKEENMQQAREEEerrkeATAHFQIT 250
Cdd:PRK11281    96 LRQAQAELEALKDDNDEETRE------TLSTLSLRQleSRLAQTLDQLQNAQNDLAEYNSQLVSLQT-----QPERAQAA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  251 LNEIQAQLEQhdIHNaklrqenielgeKLKKL-IEQYALREEHIDKVfkhkELQQQLVDAKLQQTTQLIKEADekhqrer 329
Cdd:PRK11281   165 LYANSQRLQQ--IRN------------LLKGGkVGGKALRPSQRVLL----QAEQALLNAQNDLQRKSLEGNT------- 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  330 efLLKEATESRHKYEQMK----QQEVQLKQQ------LSLYMDKFEEFQ----TTMAKSNELFttfRQEMEKMTKKIKKL 395
Cdd:PRK11281   220 --QLQDLLQKQRDYLTARiqrlEHQLQLLQEainskrLTLSEKTVQEAQsqdeAARIQANPLV---AQELEINLQLSQRL 294
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2169827764  396 EKETiiwrtkwENNNkALLQmaeeKTVRDKEYkafqiklerlekLCRALQTERNeLNEKVEVLK 459
Cdd:PRK11281   295 LKAT-------EKLN-TLTQ----QNLRVKNW------------LDRLTQSERN-IKEQISVLK 333
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
300-461 4.96e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 4.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  300 KELQQQLVDAK--LQQTTQLIKEADEKHQRereflLKEATESRHKYEQMKQQEVQLkqQLSLYMDKFEEFQTTMAKSNEL 377
Cdd:TIGR02168  175 KETERKLERTRenLDRLEDILNELERQLKS-----LERQAEKAERYKELKAELREL--ELALLVLRLEELREELEELQEE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  378 FTTFRQEMEKMTKKIKKLEketiiwrTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEV 457
Cdd:TIGR02168  248 LKEAEEELEELTAELQELE-------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                   ....
gi 2169827764  458 LKEQ 461
Cdd:TIGR02168  321 LEAQ 324
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
309-463 6.80e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.63  E-value: 6.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  309 AKLQQTTQLIKEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMD----KFEEFQTTMAKSNELFTTFRQE 384
Cdd:COG3096    509 ALAQRLQQLRAQLAELEQRLRQ--QQNAERLLEEFCQRIGQQLDAAEELEELLAeleaQLEELEEQAAEAVEQRSELRQQ 586
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2169827764  385 MEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLeklcRALQTERNELNEKVEVLKEQVS 463
Cdd:COG3096    587 LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERE----REATVERDELAARKQALESQIE 661
46 PHA02562
endonuclease subunit; Provisional
292-463 1.08e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 292 HIDKVFKHK--ELQQQL--VDAKLQQTTQLIKeADEKHQREREFLLKEA-TESRHKYEQMKQQEVQLKQQLSLYMDKFEE 366
Cdd:PHA02562  167 EMDKLNKDKirELNQQIqtLDMKIDHIQQQIK-TYNKNIEEQRKKNGENiARKQNKYDELVEEAKTIKAEIEELTDELLN 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 367 FQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRT---------KWENNNKALLQMAEEKTVRDKEYKAFQIKLERL 437
Cdd:PHA02562  246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325
                         170       180
                  ....*....|....*....|....*....
gi 2169827764 438 EKLC---RALQTERNELNEKVEVLKEQVS 463
Cdd:PHA02562  326 EEIMdefNEQSKKLLELKNKISTNKQSLI 354
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
156-359 1.08e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 156 EEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKE---ENMQQ 232
Cdd:COG1196   266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleELEEE 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 233 AREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQ 312
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2169827764 313 QTTQLIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSL 359
Cdd:COG1196   426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
157-369 1.48e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  157 EKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLkEENMQQAREE 236
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL-EEQLETLRSK 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  237 EERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLieqyalreehidkvfKHKELQQQLVDAKLQQTTQ 316
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA---------------ELKELQAELEELEEELEEL 452
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2169827764  317 liKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQT 369
Cdd:TIGR02168  453 --QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
158-398 5.19e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 158 KLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEEnMQQAREEE 237
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-LARLEQDI 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 238 ERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKV--------------------- 296
Cdd:COG1196   305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealleaeaelaeaeeeleel 384
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 297 -FKHKELQQQLVDAKLQQTTQLIKEADEKHQRER--EFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAK 373
Cdd:COG1196   385 aEELLEALRAAAELAAQLEELEEAEEALLERLERleEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
                         250       260
                  ....*....|....*....|....*
gi 2169827764 374 SNELFTTFRQEMEKMTKKIKKLEKE 398
Cdd:COG1196   465 LAELLEEAALLEAALAELLEELAEA 489
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
251-463 5.75e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 251 LNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVfkhkELQQQLVDAKLQQTTQLIKEAdEKHQRERE 330
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAEL-RAELEAQK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 331 FLLKEATESRHKYEQMKQQEVQLKQqlslymDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRTKWENNN 410
Cdd:COG4942   104 EELAELLRALYRLGRQPPLALLLSP------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2169827764 411 KALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEVLKEQVS 463
Cdd:COG4942   178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
142-373 6.39e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 142 VLLLMQALNTLSTPEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEkvhLQSEHSKAILARSKLESLCRELQRH 221
Cdd:COG4942     5 LLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764 222 NKTLKEENMQQAREEEERRKEaTAHFQITLNEIQaQLEQHDIHNAKLRQENIELGEKLKKLIEQYA-LREEHIDKVFKHK 300
Cdd:COG4942    82 EAELAELEKEIAELRAELEAQ-KEELAELLRALY-RLGRQPPLALLLSPEDFLDAVRRLQYLKYLApARREQAEELRADL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2169827764 301 ELQQQLVDAKLQQTTQLIKEADEKhQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAK 373
Cdd:COG4942   160 AELAALRAELEAERAELEALLAEL-EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
132-468 9.48e-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: 38.95  E-value: 9.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  132 RNKEKTLGKEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIvkekvhlQSEHSKAILARSKL 211
Cdd:pfam15921  454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI-------EATNAEITKLRSRV 526
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  212 ESLCRELQrHNKTlKEENMQQAREEEERRKEATAHFQITLNEIQAQLE-------QHDIHNAKLRQENIELGEKLK-KLI 283
Cdd:pfam15921  527 DLKLQELQ-HLKN-EGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgQHGRTAGAMQVEKAQLEKEINdRRL 604
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  284 EQYALREEHIDKVFKHKELQQQLVDAKLQQTtQLIKEADEKH------QREREFLLKEATESRHKYEQMKQQEVQLKQQl 357
Cdd:pfam15921  605 ELQEFKILKDKKDAKIRELEARVSDLELEKV-KLVNAGSERLravkdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRN- 682
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169827764  358 slYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETiiwrtkwENNNKALLQMAEEKTVRDKEYKAFQIKLERL 437
Cdd:pfam15921  683 --FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSD-------GHAMKVAMGMQKQITAKRGQIDALQSKIQFL 753
                          330       340       350
                   ....*....|....*....|....*....|.
gi 2169827764  438 EKLCRALQTERNELNEKVEVLKEQVSIKAAD 468
Cdd:pfam15921  754 EEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
 
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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