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Conserved domains on  [gi|55583934|sp|Q8BHN1|]
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RecName: Full=Gamma-taxilin; AltName: Full=Factor inhibiting ATF4-mediated transcription; Short=FIAT; AltName: Full=Lipopolysaccharide-responsive gene protein

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 1.93e-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: 325.37  E-value: 1.93e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   137 KEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQ 216
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   217 RHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKH 296
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   297 KELQQQLVDAKLQQTTqlikEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFT 376
Cdd:pfam09728 161 KELEVQLAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55583934   377 TFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTE 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 1.93e-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: 325.37  E-value: 1.93e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   137 KEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQ 216
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   217 RHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKH 296
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   297 KELQQQLVDAKLQQTTqlikEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFT 376
Cdd:pfam09728 161 KELEVQLAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55583934   377 TFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTE 444
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-451 7.53e-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: 7.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    165 DLLEEsrnVQKQMKIL--QKKQAQIVKEKVHLQSEHSKAILARSkLESLCRELQRHNKTLKEENMQQAREEEERRKEATA 242
Cdd:TIGR02168  193 DILNE---LERQLKSLerQAEKAERYKELKAELRELELALLVLR-LEELREELEELQEELKEAEEELEELTAELQELEEK 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    243 HFQI---------TLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQ 313
Cdd:TIGR02168  269 LEELrlevseleeEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    314 LIKEAD------EKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTK 387
Cdd:TIGR02168  349 LKEELEsleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55583934    388 KIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEykafqIKLERLEKLCRALQTERNELNEK 451
Cdd:TIGR02168  429 KLEEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALDAAERELAQL 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 238-458 1.41e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 238 KEATAHFqitLNEIQAQLEqhdihnaKLRQENIELGEKLKKLIEQYALREEHIDKV-FKHKELQQQLvdAKLQQTTQLIK 316
Cdd:COG1196 227 AELLLLK---LRELEAELE-------ELEAELEELEAELEELEAELAELEAELEELrLELEELELEL--EEAQAEEYELL 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 317 EADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKET 396
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55583934 397 IIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEVLKEQ 458
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
PRK11281 PRK11281
mechanosensitive channel MscK;
130-456 1.95e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   130 NKEKTLGKEVLLLMQALN-TLST------PEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEkvhlqsEHSKAI 202
Cdd:PRK11281   49 NKQKLLEAEDKLVQQDLEqTLALldkidrQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE------TLSTLS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   203 LAR--SKLESLCRELQRHNKTLKEENMQQareeeerrkeatahfqITLneiQAQLE--QHDIHNAKLRQEniELGEKLKK 278
Cdd:PRK11281  123 LRQleSRLAQTLDQLQNAQNDLAEYNSQL----------------VSL---QTQPEraQAALYANSQRLQ--QIRNLLKG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   279 L-IEQYALREEHIDKVfkhkELQQQLVDAKLQQTTQLIKEADekhqrerefLLKEATESRHKYEQMK----QQEVQLKQQ 353
Cdd:PRK11281  182 GkVGGKALRPSQRVLL----QAEQALLNAQNDLQRKSLEGNT---------QLQDLLQKQRDYLTARiqrlEHQLQLLQE 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   354 ------LSLYMDKFEEFQ----TTMAKSNELFttfRQEMEKMTKKIKKLEKETiiwrtkwENNNkALLQmaeeKTVRDKE 423
Cdd:PRK11281  249 ainskrLTLSEKTVQEAQsqdeAARIQANPLV---AQELEINLQLSQRLLKAT-------EKLN-TLTQ----QNLRVKN 313

                         330       340       350
                  ....*....|....*....|....*....|...
gi 55583934   424 YkafqiklerlekLCRALQTERNeLNEKVEVLK 456
Cdd:PRK11281  314 W------------LDRLTQSERN-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 1.93e-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: 325.37  E-value: 1.93e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   137 KEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQ 216
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   217 RHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKH 296
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   297 KELQQQLVDAKLQQTTqlikEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFT 376
Cdd:pfam09728 161 KELEVQLAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55583934   377 TFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTE 444
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-451 7.53e-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: 7.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    165 DLLEEsrnVQKQMKIL--QKKQAQIVKEKVHLQSEHSKAILARSkLESLCRELQRHNKTLKEENMQQAREEEERRKEATA 242
Cdd:TIGR02168  193 DILNE---LERQLKSLerQAEKAERYKELKAELRELELALLVLR-LEELREELEELQEELKEAEEELEELTAELQELEEK 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    243 HFQI---------TLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQ 313
Cdd:TIGR02168  269 LEELrlevseleeEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    314 LIKEAD------EKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTK 387
Cdd:TIGR02168  349 LKEELEsleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55583934    388 KIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEykafqIKLERLEKLCRALQTERNELNEK 451
Cdd:TIGR02168  429 KLEEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALDAAERELAQL 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 189-453 1.63e-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: 51.21  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    189 KEKVHLQSEHSKAILARskLESLCRELQRHNKTLKeenmQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQE 268
Cdd:TIGR02168  174 RKETERKLERTRENLDR--LEDILNELERQLKSLE----RQAEKAERYKELKAELRELELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    269 NIELGEKLKKLIEQYALREEHID-KVFKHKELQQQLVDA--KLQQTTQLIKEAD---EKHQREREFLLKEATESRHKYEQ 342
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEeLRLEVSELEEEIEELqkELYALANEISRLEqqkQILRERLANLERQLEELEAQLEE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    343 MKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKEtiiwrtkWENNNKALLQMAEEKTVRDK 422
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLELQIASLNN 400

                          250       260       270
                   ....*....|....*....|....*....|.
gi 55583934    423 EYKAFQIKLERLEKLCRALQTERNELNEKVE 453
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLE 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 207-459 8.26e-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: 48.90  E-value: 8.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    207 KLESLCRELQRHNKTLKEENMQ------QAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLI 280
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEEleeeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    281 EQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEADEKHQREREfLLKEATESRHKYEQMKQQEVQLKQQLSLYMDK 360
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    361 FEEFQTTMAKSNElfttfrqEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRA 440
Cdd:TIGR02168  847 IEELSEDIESLAA-------EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919

                          250
                   ....*....|....*....
gi 55583934    441 LQTERNELNEKVEVLKEQV 459
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRI 938
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 238-458 1.41e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 238 KEATAHFqitLNEIQAQLEqhdihnaKLRQENIELGEKLKKLIEQYALREEHIDKV-FKHKELQQQLvdAKLQQTTQLIK 316
Cdd:COG1196 227 AELLLLK---LRELEAELE-------ELEAELEELEAELEELEAELAELEAELEELrLELEELELEL--EEAQAEEYELL 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 317 EADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKET 396
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55583934 397 IIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEVLKEQ 458
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
COG5022 COG5022
Myosin heavy chain [General function prediction only];
161-472 1.93e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 47.77  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934  161 KKYADLLEESRNVQKqmKILQKKQAQIVKEKVHlqsEHSKAILarskLESLCRELQRHNKTL---KEENMQQAREEEERR 237
Cdd:COG5022  810 KEYRSYLACIIKLQK--TIKREKKLRETEEVEF---SLKAEVL----IQKFGRSLKAKKRFSllkKETIYLQSAQRVELA 880

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934  238 KEATAHFQITLNEIQAQLEQhdihNAKLRQENIELGEKLKK-LIEQYALREEHIDKVFKH-----------KELQQQLVD 305
Cdd:COG5022  881 ERQLQELKIDVKSISSLKLV----NLELESEIIELKKSLSSdLIENLEFKTELIARLKKLlnnidleegpsIEYVKLPEL 956

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934  306 AKLQQTTQLIKEAdekhQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFrQEMEKM 385
Cdd:COG5022  957 NKLHEVESKLKET----SEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV-AELQSA 1031

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934  386 TKKIKKlEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEkVEVLKEQVSikaaD 465
Cdd:COG5022 1032 SKIISS-ESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKT-INVKDLEVT----N 1105


                 ....*..
gi 55583934  466 GDLVSPA 472
Cdd:COG5022 1106 RNLVKPA 1112
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 153-459 2.74e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    153 EEKLAALckKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILAR--SKLESLCRELQRHNKTLKEENMQqa 230
Cdd:TIGR02169  205 REREKAE--RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKltEEISELEKRLEEIEQLLEELNKK-- 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    231 reEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAklqq 310
Cdd:TIGR02169  281 --IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK---- 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    311 ttqlIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIK 390
Cdd:TIGR02169  355 ----LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55583934    391 -------KLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEVLKEQV 459
Cdd:TIGR02169  431 gieakinELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 153-392 4.00e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 4.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    153 EEKLAALCKKYADLLEESRNVQKQMKILQK----KQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLK----- 223
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrea 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    224 -----------EENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYalreEHIDK 292
Cdd:TIGR02168  805 ldelraeltllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EALLN 880

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    293 VFKHKELQQQLVDAKLQQTTQLIKEADEKHQREREfLLKEATESRHKY----EQMKQQEVQLKQQLS-LYMDKFEEFQTT 367
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRR-ELEELREKLAQLelrlEGLEVRIDNLQERLSeEYSLTLEEAEAL 959

                          250       260
                   ....*....|....*....|....*
gi 55583934    368 MAKSNELFTTFRQEMEKMTKKIKKL 392
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKIKEL 984
PRK11281 PRK11281
mechanosensitive channel MscK;
130-456 1.95e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   130 NKEKTLGKEVLLLMQALN-TLST------PEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEkvhlqsEHSKAI 202
Cdd:PRK11281   49 NKQKLLEAEDKLVQQDLEqTLALldkidrQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE------TLSTLS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   203 LAR--SKLESLCRELQRHNKTLKEENMQQareeeerrkeatahfqITLneiQAQLE--QHDIHNAKLRQEniELGEKLKK 278
Cdd:PRK11281  123 LRQleSRLAQTLDQLQNAQNDLAEYNSQL----------------VSL---QTQPEraQAALYANSQRLQ--QIRNLLKG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   279 L-IEQYALREEHIDKVfkhkELQQQLVDAKLQQTTQLIKEADekhqrerefLLKEATESRHKYEQMK----QQEVQLKQQ 353
Cdd:PRK11281  182 GkVGGKALRPSQRVLL----QAEQALLNAQNDLQRKSLEGNT---------QLQDLLQKQRDYLTARiqrlEHQLQLLQE 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   354 ------LSLYMDKFEEFQ----TTMAKSNELFttfRQEMEKMTKKIKKLEKETiiwrtkwENNNkALLQmaeeKTVRDKE 423
Cdd:PRK11281  249 ainskrLTLSEKTVQEAQsqdeAARIQANPLV---AQELEINLQLSQRLLKAT-------EKLN-TLTQ----QNLRVKN 313

                         330       340       350
                  ....*....|....*....|....*....|...
gi 55583934   424 YkafqiklerlekLCRALQTERNeLNEKVEVLK 456
Cdd:PRK11281  314 W------------LDRLTQSERN-IKEQISVLK 333
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 297-458 2.55e-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: 43.89  E-value: 2.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    297 KELQQQLVDAK--LQQTTQLIKEADEKHQRereflLKEATESRHKYEQMKQQEVQLkqQLSLYMDKFEEFQTTMAKSNEL 374
Cdd:TIGR02168  175 KETERKLERTRenLDRLEDILNELERQLKS-----LERQAEKAERYKELKAELREL--ELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    375 FTTFRQEMEKMTKKIKKLEketiiwrTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEV 454
Cdd:TIGR02168  248 LKEAEEELEELTAELQELE-------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320


                   ....
gi 55583934    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 5.50e-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: 43.02  E-value: 5.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934  306 AKLQQTTQLIKEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMD----KFEEFQTTMAKSNELFTTFRQE 381
Cdd:COG3096  509 ALAQRLQQLRAQLAELEQRLRQ--QQNAERLLEEFCQRIGQQLDAAEELEELLAeleaQLEELEEQAAEAVEQRSELRQQ 586

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55583934  382 MEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLeklcRALQTERNELNEKVEVLKEQVS 460
Cdd:COG3096  587 LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERE----REATVERDELAARKQALESQIE 661
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 153-356 7.06e-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: 7.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 153 EEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKE---ENMQQ 229
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleELEEE 345

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 230 AREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQ 309
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 55583934 310 QTTQLIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSL 356
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
46 PHA02562
endonuclease subunit; Provisional
 289-460 7.52e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.31  E-value: 7.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934  289 HIDKVFKHK--ELQQQL--VDAKLQQTTQLIKeADEKHQREREFLLKEA-TESRHKYEQMKQQEVQLKQQLSLYMDKFEE 363
Cdd:PHA02562 167 EMDKLNKDKirELNQQIqtLDMKIDHIQQQIK-TYNKNIEEQRKKNGENiARKQNKYDELVEEAKTIKAEIEELTDELLN 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934  364 FQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRT---------KWENNNKALLQMAEEKTVRDKEYKAFQIKLERL 434
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325

                        170       180
                 ....*....|....*....|....*....
gi 55583934  435 EKLC---RALQTERNELNEKVEVLKEQVS 460
Cdd:PHA02562 326 EEIMdefNEQSKKLLELKNKISTNKQSLI 354
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 154-366 8.37e-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: 42.35  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    154 EKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLkEENMQQAREE 233
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL-EEQLETLRSK 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    234 EERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLieqyalreehidkvfKHKELQQQLVDAKLQQTTQ 313
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA---------------ELKELQAELEELEEELEEL 452

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 55583934    314 liKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQT 366
Cdd:TIGR02168  453 --QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 295-460 8.97e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 8.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 295 KHKELQQQLVDAKLQQTTQLIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLkqqlslymdkfEEFQTTMAKSNEL 374
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL-----------EELRLELEELELE 282

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 375 FTTFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEV 454
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362


                ....*.
gi 55583934 455 LKEQVS 460
Cdd:COG1196 363 AEEALL 368
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 155-395 2.55e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 155 KLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEEnMQQAREEE 234
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-LARLEQDI 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 235 ERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKV--------------------- 293
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealleaeaelaeaeeeleel 384

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 294 -FKHKELQQQLVDAKLQQTTQLIKEADEKHQRER--EFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAK 370
Cdd:COG1196 385 aEELLEALRAAAELAAQLEELEEAEEALLERLERleEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464

                       250       260
                ....*....|....*....|....*
gi 55583934 371 SNELFTTFRQEMEKMTKKIKKLEKE 395
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEA 489
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 139-370 3.66e-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: 39.75  E-value: 3.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 139 VLLLMQALNTLSTPEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEkvhLQSEHSKAILARSKLESLCRELQRH 218
Cdd:COG4942   5 LLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAAL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 219 NKTLKEENMQQAREEEERRKEaTAHFQITLNEIQaQLEQHDIHNAKLRQENIELGEKLKKLIEQYA-LREEHIDKVFKHK 297
Cdd:COG4942  82 EAELAELEKEIAELRAELEAQ-KEELAELLRALY-RLGRQPPLALLLSPEDFLDAVRRLQYLKYLApARREQAEELRADL 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55583934 298 ELQQQLVDAKLQQTTQLIKEADEKhQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAK 370
Cdd:COG4942 160 AELAALRAELEAERAELEALLAEL-EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 129-465 5.13e-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: 39.72  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    129 RNKEKTLGKEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIvkekvhlQSEHSKAILARSKL 208
Cdd:pfam15921  454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI-------EATNAEITKLRSRV 526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    209 ESLCRELQrHNKTlKEENMQQAREEEERRKEATAHFQITLNEIQAQLE-------QHDIHNAKLRQENIELGEKLK-KLI 280
Cdd:pfam15921  527 DLKLQELQ-HLKN-EGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgQHGRTAGAMQVEKAQLEKEINdRRL 604

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    281 EQYALREEHIDKVFKHKELQQQLVDAKLQQTtQLIKEADEKH------QREREFLLKEATESRHKYEQMKQQEVQLKQQl 354
Cdd:pfam15921  605 ELQEFKILKDKKDAKIRELEARVSDLELEKV-KLVNAGSERLravkdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRN- 682

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    355 slYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETiiwrtkwENNNKALLQMAEEKTVRDKEYKAFQIKLERL 434
Cdd:pfam15921  683 --FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSD-------GHAMKVAMGMQKQITAKRGQIDALQSKIQFL 753

                          330       340       350
                   ....*....|....*....|....*....|.
gi 55583934    435 EKLCRALQTERNELNEKVEVLKEQVSIKAAD 465
Cdd:pfam15921  754 EEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 104-451 6.01e-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: 39.57  E-value: 6.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    104 EKREEIPGREARTGPPDGQQDSECSRN--KEKTLGKEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRNVQKQMKILQ 181
Cdd:pfam02463  641 AKAKESGLRKGVSLEEGLAEKSEVKASlsELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE 720

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    182 KKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQ--------- 252
Cdd:pfam02463  721 ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEkeeklkaqe 800

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    253 ----AQLEQHDIHNAKLRQENIE---LGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEADEKHQRE 325
Cdd:pfam02463  801 eelrALEEELKEEAELLEEEQLLieqEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELE 880

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934    326 REFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSN-----------ELFTTFRQEMEKMTKKIKKLEK 394
Cdd:pfam02463  881 EQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAeillkyeeepeELLLEEADEKEKEENNKEEEEE 960

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 55583934    395 ETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEK 451
Cdd:pfam02463  961 RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 248-473 6.40e-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: 6.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 248 LNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVfkhkELQQQLVDAKLQQTTQLIKEAdEKHQRERE 327
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAEL-RAELEAQK 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934 328 FLLKEATESRHKYEQMKQQEVQLKQQLSLYMDK-FEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRTKWENN 406
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55583934 407 NKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEVLKEQV----------SIKAADGDLVSPAT 473
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAaaaaertpaaGFAALKGKLPWPVS 260
mukB PRK04863
chromosome partition protein MukB;
300-460 7.83e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 7.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   300 QQQLVDAKLQQTTQLIKEADEKH--QREREFLLKEATEsrhKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTT 377
Cdd:PRK04863  507 EQRHLAEQLQQLRMRLSELEQRLrqQQRAERLLAEFCK---RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMA 583

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   378 FRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLeklcRALQTERNELNEKVEVLKE 457
Cdd:PRK04863  584 LRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERE----RELTVERDELAARKQALDE 659


                  ...
gi 55583934   458 QVS 460
Cdd:PRK04863  660 EIE 662
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
161-457 7.94e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 7.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934  161 KKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENMQQAREEEERRKea 240
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-- 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934  241 tahFQITLNEIQAQLEqhdihnaKLRQENIELGEKLKKL--IEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEA 318
Cdd:PRK03918 257 ---LEEKIRELEERIE-------ELKKEIEELEEKVKELkeLKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934  319 DEKhqrereflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNelfttfrqEMEKMTKKIKKLEKETIi 398
Cdd:PRK03918 327 EER--------IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE--------ELERLKKRLTGLTPEKL- 389

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 55583934  399 wrtkwennnKALLQMAEektvrdKEYKAFQIKLERLEKLCRALQTERNELNEKVEVLKE 457
Cdd:PRK03918 390 ---------EKELEELE------KAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 249-457 9.23e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   249 NEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFK-HKELQQQLVDA-----KLQQTTQLIKEADEKH 322
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKlNQQKDEQIKKLqqekeLLEKEIERLKETIIKN 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55583934   323 QREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRTK 402
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 55583934   403 WENNNKALLQMAEEKTVRDKEYKAFQIKLERL--EKLCRALQTERNELNEKVEVLKE 457
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQ 575
 
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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