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Conserved domains on  [gi|281182404|ref|NP_060830|]
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gamma-taxilin isoform 1 [Homo sapiens]

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 ...
 137-444 1.58e-108

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: 325.75  E-value: 1.58e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  137 KEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQ 216
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  217 RHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKH 296
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  297 KELQQQLVDAKLQQTTqlikEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFT 376
Cdd:pfam09728 161 KELEVQLAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281182404  377 TFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTE 444
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 ...
 137-444 1.58e-108

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: 325.75  E-value: 1.58e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  137 KEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQ 216
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  217 RHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKH 296
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  297 KELQQQLVDAKLQQTTqlikEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFT 376
Cdd:pfam09728 161 KELEVQLAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281182404  377 TFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTE 444
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-458 6.26e-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: 55.45  E-value: 6.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   165 DLLEEsrsVQKQMKIL--QKKQAQIVKEKVHLQSEHSKAILARSkLESLCRELQRHNKTLKEENMQQAREEEERRKEATA 242
Cdd:TIGR02168  193 DILNE---LERQLKSLerQAEKAERYKELKAELRELELALLVLR-LEELREELEELQEELKEAEEELEELTAELQELEEK 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   243 HFQI---------TLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQ 313
Cdd:TIGR02168  269 LEELrlevseleeEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   314 LIKEAD------EKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTK 387
Cdd:TIGR02168  349 LKEELEsleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281182404   388 KIKKLEKETIiwRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQ 458
Cdd:TIGR02168  429 KLEEAELKEL--QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 161-476 3.15e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 161 KKYADLLEESRSVQKQMKIL-----QKKQAQIVKEKVHLQSEHSKAILARSKLESLCREL--QRHNKTLKEENMQQAREE 233
Cdd:COG1196  213 ERYRELKEELKELEAELLLLklrelEAELEELEAELEELEAELEELEAELAELEAELEELrlELEELELELEEAQAEEYE 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 234 EERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQ 313
Cdd:COG1196  293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 314 LIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLslymdkfeefqttmaksnelfttfrQEMEKMTKKIKKLE 393
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL-------------------------ERLERLEEELEELE 427

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 394 KETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQVSIKAAIKAANRDLA 473
Cdd:COG1196  428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507


                 ...
gi 281182404 474 TPV 476
Cdd:COG1196  508 EGV 510
PRK11281 PRK11281
mechanosensitive channel MscK;
130-456 1.28e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.90  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  130 NKEKTLGKEVLLLMQALN-TLST------PEEKLAALCKKYADLLEESRSVQKQMKILQKKQAQIVKEkvhlqsEHSKAI 202
Cdd:PRK11281   49 NKQKLLEAEDKLVQQDLEqTLALldkidrQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE------TLSTLS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  203 LAR--SKLESLCRELQRHNKTLKEENMQQAREEEerrkeATAHFQITLNEIQAQLEQhdIHNaklrqenielgeKLKKL- 279
Cdd:PRK11281  123 LRQleSRLAQTLDQLQNAQNDLAEYNSQLVSLQT-----QPERAQAALYANSQRLQQ--IRN------------LLKGGk 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  280 IEQYALREEHIDKVfkhkELQQQLVDAKLQQTTQLIKEADekhqrerefLLKEATESRHKYEQMK----QQEVQLKQQ-- 353
Cdd:PRK11281  184 VGGKALRPSQRVLL----QAEQALLNAQNDLQRKSLEGNT---------QLQDLLQKQRDYLTARiqrlEHQLQLLQEai 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  354 ----LSLYMDKFEEFQ----TTMAKSNELFttfRQEMEKMTKKIKKLEKETiiwrtkwENNNkALLQmaeektvrdkeyK 425
Cdd:PRK11281  251 nskrLTLSEKTVQEAQsqdeAARIQANPLV---AQELEINLQLSQRLLKAT-------EKLN-TLTQ------------Q 307

                         330       340       350
                  ....*....|....*....|....*....|.
gi 281182404  426 ALQIKlerlEKLCRALQTERNeLNEKVEVLK 456
Cdd:PRK11281  308 NLRVK----NWLDRLTQSERN-IKEQISVLK 333
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 137-444 1.58e-108

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: 325.75  E-value: 1.58e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  137 KEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQ 216
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  217 RHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKH 296
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  297 KELQQQLVDAKLQQTTqlikEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFT 376
Cdd:pfam09728 161 KELEVQLAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281182404  377 TFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTE 444
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-458 6.26e-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: 55.45  E-value: 6.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   165 DLLEEsrsVQKQMKIL--QKKQAQIVKEKVHLQSEHSKAILARSkLESLCRELQRHNKTLKEENMQQAREEEERRKEATA 242
Cdd:TIGR02168  193 DILNE---LERQLKSLerQAEKAERYKELKAELRELELALLVLR-LEELREELEELQEELKEAEEELEELTAELQELEEK 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   243 HFQI---------TLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQ 313
Cdd:TIGR02168  269 LEELrlevseleeEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   314 LIKEAD------EKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTK 387
Cdd:TIGR02168  349 LKEELEsleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281182404   388 KIKKLEKETIiwRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQ 458
Cdd:TIGR02168  429 KLEEAELKEL--QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 189-453 7.31e-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: 52.37  E-value: 7.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   189 KEKVHLQSEHSKAILARskLESLCRELQRHNKTLKeenmQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQE 268
Cdd:TIGR02168  174 RKETERKLERTRENLDR--LEDILNELERQLKSLE----RQAEKAERYKELKAELRELELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   269 NIELGEKLKKLIEQYALREEHID-KVFKHKELQQQLVDA--KLQQTTQLIKEAD---EKHQREREFLLKEATESRHKYEQ 342
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEeLRLEVSELEEEIEELqkELYALANEISRLEqqkQILRERLANLERQLEELEAQLEE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   343 MKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKEtiiwrtkWENNNKALLQMAEEKTVRDK 422
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLELQIASLNN 400

                          250       260       270
                   ....*....|....*....|....*....|.
gi 281182404   423 EYKALQIKLERLEKLCRALQTERNELNEKVE 453
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLE 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 207-459 1.01e-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: 51.60  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   207 KLESLCRELQRHNKTLKEENMQ------QAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLI 280
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEEleeeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   281 EQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEADEKHQREREfLLKEATESRHKYEQMKQQEVQLKQQLSLYMDK 360
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   361 FEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETiiwrtkwENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRA 440
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNER-------ASLEEALALLRSELEELSEELRELESKRSELRRELEE 919

                          250
                   ....*....|....*....
gi 281182404   441 LQTERNELNEKVEVLKEQV 459
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRI 938
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 161-476 3.15e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 161 KKYADLLEESRSVQKQMKIL-----QKKQAQIVKEKVHLQSEHSKAILARSKLESLCREL--QRHNKTLKEENMQQAREE 233
Cdd:COG1196  213 ERYRELKEELKELEAELLLLklrelEAELEELEAELEELEAELEELEAELAELEAELEELrlELEELELELEEAQAEEYE 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 234 EERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQ 313
Cdd:COG1196  293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 314 LIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLslymdkfeefqttmaksnelfttfrQEMEKMTKKIKKLE 393
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL-------------------------ERLERLEEELEELE 427

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 394 KETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQVSIKAAIKAANRDLA 473
Cdd:COG1196  428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507


                 ...
gi 281182404 474 TPV 476
Cdd:COG1196  508 EGV 510
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 153-459 1.34e-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: 48.14  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   153 EEKLAALckKYADLLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILAR--SKLESLCRELQRHNKTLKEENMQqa 230
Cdd:TIGR02169  205 REREKAE--RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKltEEISELEKRLEEIEQLLEELNKK-- 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   231 reEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAklqq 310
Cdd:TIGR02169  281 --IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK---- 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   311 ttqlIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIK 390
Cdd:TIGR02169  355 ----LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281182404   391 -------KLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQV 459
Cdd:TIGR02169  431 gieakinELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
COG5022 COG5022
Myosin heavy chain [General function prediction only];
161-469 3.81e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 46.61  E-value: 3.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  161 KKYADLLEESRSVQKqmKILQKKQAQIVKEKVHlqsEHSKAILarskLESLCRELQRHNKTL---KEENMQQAREEEERR 237
Cdd:COG5022   810 KEYRSYLACIIKLQK--TIKREKKLRETEEVEF---SLKAEVL----IQKFGRSLKAKKRFSllkKETIYLQSAQRVELA 880

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  238 KEATAHFQITLNEIQAQLEQhdihNAKLRQENIELGEKLKK-LIEQYALREEHIDKVFKH-----------KELQQQLVD 305
Cdd:COG5022   881 ERQLQELKIDVKSISSLKLV----NLELESEIIELKKSLSSdLIENLEFKTELIARLKKLlnnidleegpsIEYVKLPEL 956

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  306 AKLQQTTQLIKEAdekhQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFrQEMEKM 385
Cdd:COG5022   957 NKLHEVESKLKET----SEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV-AELQSA 1031

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  386 TKKIKKlEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEkVEVLKEQVSIKAAI 465
Cdd:COG5022  1032 SKIISS-ESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKT-INVKDLEVTNRNLV 1109


                  ....
gi 281182404  466 KAAN 469
Cdd:COG5022  1110 KPAN 1113
PRK11281 PRK11281
mechanosensitive channel MscK;
130-456 1.28e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.90  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  130 NKEKTLGKEVLLLMQALN-TLST------PEEKLAALCKKYADLLEESRSVQKQMKILQKKQAQIVKEkvhlqsEHSKAI 202
Cdd:PRK11281   49 NKQKLLEAEDKLVQQDLEqTLALldkidrQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE------TLSTLS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  203 LAR--SKLESLCRELQRHNKTLKEENMQQAREEEerrkeATAHFQITLNEIQAQLEQhdIHNaklrqenielgeKLKKL- 279
Cdd:PRK11281  123 LRQleSRLAQTLDQLQNAQNDLAEYNSQLVSLQT-----QPERAQAALYANSQRLQQ--IRN------------LLKGGk 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  280 IEQYALREEHIDKVfkhkELQQQLVDAKLQQTTQLIKEADekhqrerefLLKEATESRHKYEQMK----QQEVQLKQQ-- 353
Cdd:PRK11281  184 VGGKALRPSQRVLL----QAEQALLNAQNDLQRKSLEGNT---------QLQDLLQKQRDYLTARiqrlEHQLQLLQEai 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  354 ----LSLYMDKFEEFQ----TTMAKSNELFttfRQEMEKMTKKIKKLEKETiiwrtkwENNNkALLQmaeektvrdkeyK 425
Cdd:PRK11281  251 nskrLTLSEKTVQEAQsqdeAARIQANPLV---AQELEINLQLSQRLLKAT-------EKLN-TLTQ------------Q 307

                         330       340       350
                  ....*....|....*....|....*....|.
gi 281182404  426 ALQIKlerlEKLCRALQTERNeLNEKVEVLK 456
Cdd:PRK11281  308 NLRVK----NWLDRLTQSERN-IKEQISVLK 333
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 153-392 1.54e-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: 44.66  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   153 EEKLAALCKKYADLLEESRSVQKQMKILQK----KQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLK----- 223
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrea 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   224 -----------EENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYalreEHIDK 292
Cdd:TIGR02168  805 ldelraeltllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EALLN 880

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   293 VFKHKELQQQLVDAKLQQTTQLIKEADEKHQREREfLLKEATESRHKY----EQMKQQEVQLKQQLS-LYMDKFEEFQTT 367
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRR-ELEELREKLAQLelrlEGLEVRIDNLQERLSeEYSLTLEEAEAL 959

                          250       260
                   ....*....|....*....|....*
gi 281182404   368 MAKSNELFTTFRQEMEKMTKKIKKL 392
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKIKEL 984
46 PHA02562
endonuclease subunit; Provisional
 289-468 1.58e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.23  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 289 HIDKVFKHK--ELQQQL--VDAKLQQTTQLIKeADEKHQREREFLLKEA-TESRHKYEQMKQQEVQLKQQLSLYMDKFEE 363
Cdd:PHA02562 167 EMDKLNKDKirELNQQIqtLDMKIDHIQQQIK-TYNKNIEEQRKKNGENiARKQNKYDELVEEAKTIKAEIEELTDELLN 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 364 FQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRT---------KWENNNKALLQMAEEKTVRDKEYKALQIKLERL 434
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 281182404 435 EKLC---RALQTERNELNEKVEVLKEQVS--------IKAAIKAA 468
Cdd:PHA02562 326 EEIMdefNEQSKKLLELKNKISTNKQSLItlvdkakkVKAAIEEL 370
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 297-458 2.11e-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: 44.28  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   297 KELQQQLVDAK--LQQTTQLIKEADEKHQRereflLKEATESRHKYEQMKQQEVQLkqQLSLYMDKFEEFQTTMAKSNEL 374
Cdd:TIGR02168  175 KETERKLERTRenLDRLEDILNELERQLKS-----LERQAEKAERYKELKAELREL--ELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   375 FTTFRQEMEKMTKKIKKLEketiiwrTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEV 454
Cdd:TIGR02168  248 LKEAEEELEELTAELQELE-------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320


                   ....
gi 281182404   455 LKEQ 458
Cdd:TIGR02168  321 LEAQ 324
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 306-460 3.63e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  306 AKLQQTTQLIKEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMD----KFEEFQTTMAKSNELFTTFRQE 381
Cdd:COG3096   509 ALAQRLQQLRAQLAELEQRLRQ--QQNAERLLEEFCQRIGQQLDAAEELEELLAeleaQLEELEEQAAEAVEQRSELRQQ 586

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281182404  382 MEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLeklcRALQTERNELNEKVEVLKEQVS 460
Cdd:COG3096   587 LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERE----REATVERDELAARKQALESQIE 661
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 153-356 6.84e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 6.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 153 EEKLAALCKKYADLLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKE---ENMQQ 229
Cdd:COG1196  266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleELEEE 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 230 AREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQ 309
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 281182404 310 QTTQLIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSL 356
Cdd:COG1196  426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 248-475 1.27e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 248 LNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVfkhkELQQQLVDAKLQQTTQLIKEAdEKHQRERE 327
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAEL-RAELEAQK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 328 FLLKEATESRHKYEQMKQQEVQLKQqlslymDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRTKWENNN 407
Cdd:COG4942  104 EELAELLRALYRLGRQPPLALLLSP------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 408 KALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQVS--IKAAIKAANRDLATP 475
Cdd:COG4942  178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIArlEAEAAAAAERTPAAG 247
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 129-466 1.81e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.26  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   129 RNKEKTLGKEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRSVQKQMKILQKKQAQIvkekvhlQSEHSKAILARSKL 208
Cdd:pfam15921  454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI-------EATNAEITKLRSRV 526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   209 ESLCRELQrHNKTlKEENMQQAREEEERRKEATAHFQITLNEIQAQLE-------QHDIHNAKLRQENIELGEKLK-KLI 280
Cdd:pfam15921  527 DLKLQELQ-HLKN-EGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgQHGRTAGAMQVEKAQLEKEINdRRL 604

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   281 EQYALREEHIDKVFKHKELQQQLVDAKLQQTtQLIKEADEKH------QREREFLLKEATESRHKYEQMKQQEVQLKQQl 354
Cdd:pfam15921  605 ELQEFKILKDKKDAKIRELEARVSDLELEKV-KLVNAGSERLravkdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRN- 682

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   355 slYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETiiwrtkwENNNKALLQMAEEKTVRDKEYKALQIKLERL 434
Cdd:pfam15921  683 --FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSD-------GHAMKVAMGMQKQITAKRGQIDALQSKIQFL 753

                          330       340       350
                   ....*....|....*....|....*....|..
gi 281182404   435 EKLCRALQTERNELNEKVEVLKEQVSIKAAIK 466
Cdd:pfam15921  754 EEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 128-451 1.82e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.11  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   128 NRNKEKTLGKEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRSvQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSK 207
Cdd:pfam02463  668 LSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL-KKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   208 LESLCRELQRHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQ-------------AQLEQHDIHNAKLRQENIE--- 271
Cdd:pfam02463  747 EEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEkeeklkaqeeelrALEEELKEEAELLEEEQLLieq 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   272 LGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLK 351
Cdd:pfam02463  827 EEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   352 QQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQ-----------MAEEKTVR 420
Cdd:pfam02463  907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLakeelgkvnlmAIEEFEEK 986

                          330       340       350
                   ....*....|....*....|....*....|.
gi 281182404   421 DKEYKALQIKLERLEKLCRALQTERNELNEK 451
Cdd:pfam02463  987 EERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 154-366 3.21e-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: 40.43  E-value: 3.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   154 EKLAALCKKYADLLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLkEENMQQAREE 233
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL-EEQLETLRSK 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404   234 EERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLieqyalreehidkvfKHKELQQQLVDAKLQQTTQ 313
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA---------------ELKELQAELEELEEELEEL 452

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 281182404   314 liKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQT 366
Cdd:TIGR02168  453 --QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 249-457 3.59e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  249 NEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFK-HKELQQQLVDA-----KLQQTTQLIKEADEKH 322
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKlNQQKDEQIKKLqqekeLLEKEIERLKETIIKN 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  323 QREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRTK 402
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281182404  403 WENNNKALLQMAEEKTVRDKEYKALQIKLERL--EKLCRALQTERNELNEKVEVLKE 457
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQ 575
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 155-395 4.35e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 155 KLAALCKKYADLLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEEnMQQAREEE 234
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-LARLEQDI 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 235 ERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKV--------------------- 293
Cdd:COG1196  305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealleaeaelaeaeeeleel 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 294 -FKHKELQQQLVDAKLQQTTQLIKEADEKHQRER--EFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAK 370
Cdd:COG1196  385 aEELLEALRAAAELAAQLEELEEAEEALLERLERleEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464

                        250       260
                 ....*....|....*....|....*
gi 281182404 371 SNELFTTFRQEMEKMTKKIKKLEKE 395
Cdd:COG1196  465 LAELLEEAALLEAALAELLEELAEA 489
mukB PRK04863
chromosome partition protein MukB;
300-460 4.74e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  300 QQQLVDAKLQQTTQLIKEADEKH--QREREFLLKEATEsrhKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTT 377
Cdd:PRK04863  507 EQRHLAEQLQQLRMRLSELEQRLrqQQRAERLLAEFCK---RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMA 583

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404  378 FRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLeklcRALQTERNELNEKVEVLKE 457
Cdd:PRK04863  584 LRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERE----RELTVERDELAARKQALDE 659


                  ...
gi 281182404  458 QVS 460
Cdd:PRK04863  660 EIE 662
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 139-370 7.77e-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: 38.59  E-value: 7.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 139 VLLLMQALNTLSTPEEKLAALCKKYADLLEESRSVQKQMKILQKKQAQIVKEkvhLQSEHSKAILARSKLESLCRELQRH 218
Cdd:COG4942    5 LLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 219 NKTLKEENMQQAREEEERRKEaTAHFQITLNEIQaQLEQHDIHNAKLRQENIELGEKLKKLIEQYA-LREEHIDKVFKHK 297
Cdd:COG4942   82 EAELAELEKEIAELRAELEAQ-KEELAELLRALY-RLGRQPPLALLLSPEDFLDAVRRLQYLKYLApARREQAEELRADL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281182404 298 ELQQQLVDAKLQQTTQLIKEADEKhQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAK 370
Cdd:COG4942  160 AELAALRAELEAERAELEALLAEL-EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
161-466 9.69e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 9.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 161 KKYADLLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENMQQAREEEERRKea 240
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-- 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 241 tahFQITLNEIQAQLEqhdihnaKLRQENIELGEKLKKL--IEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEA 318
Cdd:PRK03918 257 ---LEEKIRELEERIE-------ELKKEIEELEEKVKELkeLKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182404 319 DEKhqrereflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELfttFRQEMEKMTKKIKKLEKETII 398
Cdd:PRK03918 327 EER--------IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL---ERLKKRLTGLTPEKLEKELEE 395

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281182404 399 WRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEK------LCRALQTERNELNEKVEVLKEQVSIKAAIK 466
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpVCGRELTEEHRKELLEEYTAELKRIEKELK 469
 
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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