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Conserved domains on  [gi|281182408|ref|NP_001162154|]
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gamma-taxilin isoform 2 [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 ...
35-312 5.28e-86

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: 263.35  E-value: 5.28e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   35 LEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENMQQAREEEERRKEATAHFQI 114
Cdd:pfam09728  31 LEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKLKEESKKLAKEEEEKRKELSEKFQS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408  115 TLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTqlikEADEKHQRER 194
Cdd:pfam09728 111 TLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTKELEVQLAEAKLQQAT----EEEEKKAQEK 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408  195 EflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRTKWENN 274
Cdd:pfam09728 187 E--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKS 264
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 281182408  275 NKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTE 312
Cdd:pfam09728 265 NKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
35-312 5.28e-86

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: 263.35  E-value: 5.28e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   35 LEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENMQQAREEEERRKEATAHFQI 114
Cdd:pfam09728  31 LEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKLKEESKKLAKEEEEKRKELSEKFQS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408  115 TLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTqlikEADEKHQRER 194
Cdd:pfam09728 111 TLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTKELEVQLAEAKLQQAT----EEEEKKAQEK 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408  195 EflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRTKWENN 274
Cdd:pfam09728 187 E--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKS 264
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 281182408  275 NKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTE 312
Cdd:pfam09728 265 NKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
39-326 2.21e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408    39 RSVQKQMKIL--QKKQAQIVKEKVHLQSEHSKAILARSkLESLCRELQRHNKTLKEENMQQAREEEERRKEATAHFQI-- 114
Cdd:TIGR02168  196 NELERQLKSLerQAEKAERYKELKAELRELELALLVLR-LEELREELEELQEELKEAEEELEELTAELQELEEKLEELrl 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   115 -------TLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEAD 187
Cdd:TIGR02168  275 evseleeEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   188 ------EKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLE 261
Cdd:TIGR02168  355 sleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281182408   262 KETIiwRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQ 326
Cdd:TIGR02168  435 LKEL--QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
106-341 3.01e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408 106 KEATAHFqitLNEIQAQLEqhdihnaKLRQENIELGEKLKKLIEQYALREEHIDKV-FKHKELQQQLvdAKLQQTTQLIK 184
Cdd:COG1196  227 AELLLLK---LRELEAELE-------ELEAELEELEAELEELEAELAELEAELEELrLELEELELEL--EEAQAEEYELL 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408 185 EADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKET 264
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281182408 265 IIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKV-EVLKEQVSIKAAIKAANRDLA 341
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALaELEEEEEEEEEALEEAAEEEA 452
46 PHA02562
endonuclease subunit; Provisional
157-336 4.92e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.31  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408 157 HIDKVFKHK--ELQQQL--VDAKLQQTTQLIKeADEKHQREREFLLKEA-TESRHKYEQMKQQEVQLKQQLSLYMDKFEE 231
Cdd:PHA02562 167 EMDKLNKDKirELNQQIqtLDMKIDHIQQQIK-TYNKNIEEQRKKNGENiARKQNKYDELVEEAKTIKAEIEELTDELLN 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408 232 FQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRT---------KWENNNKALLQMAEEKTVRDKEYKALQIKLERL 302
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 281182408 303 EKLC---RALQTERNELNEKVEVLKEQVS--------IKAAIKAA 336
Cdd:PHA02562 326 EEIMdefNEQSKKLLELKNKISTNKQSLItlvdkakkVKAAIEEL 370
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
35-312 5.28e-86

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: 263.35  E-value: 5.28e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   35 LEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENMQQAREEEERRKEATAHFQI 114
Cdd:pfam09728  31 LEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKLKEESKKLAKEEEEKRKELSEKFQS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408  115 TLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTqlikEADEKHQRER 194
Cdd:pfam09728 111 TLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTKELEVQLAEAKLQQAT----EEEEKKAQEK 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408  195 EflLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRTKWENN 274
Cdd:pfam09728 187 E--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKS 264
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 281182408  275 NKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTE 312
Cdd:pfam09728 265 NKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
39-326 2.21e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408    39 RSVQKQMKIL--QKKQAQIVKEKVHLQSEHSKAILARSkLESLCRELQRHNKTLKEENMQQAREEEERRKEATAHFQI-- 114
Cdd:TIGR02168  196 NELERQLKSLerQAEKAERYKELKAELRELELALLVLR-LEELREELEELQEELKEAEEELEELTAELQELEEKLEELrl 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   115 -------TLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEAD 187
Cdd:TIGR02168  275 evseleeEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   188 ------EKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLE 261
Cdd:TIGR02168  355 sleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281182408   262 KETIiwRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQ 326
Cdd:TIGR02168  435 LKEL--QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
57-321 9.26e-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: 47.74  E-value: 9.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408    57 KEKVHLQSEHSKAILARskLESLCRELQRHNKTLKeenmQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQE 136
Cdd:TIGR02168  174 RKETERKLERTRENLDR--LEDILNELERQLKSLE----RQAEKAERYKELKAELRELELALLVLRLEELREELEELQEE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   137 NIELGEKLKKLIEQYALREEHID-KVFKHKELQQQLVDA--KLQQTTQLIKEAD---EKHQREREFLLKEATESRHKYEQ 210
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEeLRLEVSELEEEIEELqkELYALANEISRLEqqkQILRERLANLERQLEELEAQLEE 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   211 MKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKEtiiwrtkWENNNKALLQMAEEKTVRDK 290
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLELQIASLNN 400
                          250       260       270
                   ....*....|....*....|....*....|.
gi 281182408   291 EYKALQIKLERLEKLCRALQTERNELNEKVE 321
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLE 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
75-327 9.58e-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: 47.74  E-value: 9.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408    75 KLESLCRELQRHNKTLKEENMQ------QAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLI 148
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEEleeeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   149 EQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEADEKHQREREfLLKEATESRHKYEQMKQQEVQLKQQLSLYMDK 228
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   229 FEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETiiwrtkwENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRA 308
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNER-------ASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
                          250
                   ....*....|....*....
gi 281182408   309 LQTERNELNEKVEVLKEQV 327
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRI 938
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
106-341 3.01e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408 106 KEATAHFqitLNEIQAQLEqhdihnaKLRQENIELGEKLKKLIEQYALREEHIDKV-FKHKELQQQLvdAKLQQTTQLIK 184
Cdd:COG1196  227 AELLLLK---LRELEAELE-------ELEAELEELEAELEELEAELAELEAELEELrLELEELELEL--EEAQAEEYELL 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408 185 EADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKET 264
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281182408 265 IIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKV-EVLKEQVSIKAAIKAANRDLA 341
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALaELEEEEEEEEEALEEAAEEEA 452
COG5022 COG5022
Myosin heavy chain [General function prediction only];
30-337 1.00e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   30 SPRQKLEESRSVQKQMKILQK--KQAQIVKEKVHLQSEHSKAILarskLESLCRELQRHNKTL---KEENMQQAREEEER 104
Cdd:COG5022   804 SLLGSRKEYRSYLACIIKLQKtiKREKKLRETEEVEFSLKAEVL----IQKFGRSLKAKKRFSllkKETIYLQSAQRVEL 879
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408  105 RKEATAHFQITLNEIQAQLEQhdihNAKLRQENIELGEKLKK-LIEQYALREEHIDKVFKH-----------KELQQQLV 172
Cdd:COG5022   880 AERQLQELKIDVKSISSLKLV----NLELESEIIELKKSLSSdLIENLEFKTELIARLKKLlnnidleegpsIEYVKLPE 955
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408  173 DAKLQQTTQLIKEAdekhQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFrQEMEK 252
Cdd:COG5022   956 LNKLHEVESKLKET----SEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV-AELQS 1030
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408  253 MTKKIKKlEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEkVEVLKEQVSIKAA 332
Cdd:COG5022  1031 ASKIISS-ESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKT-INVKDLEVTNRNL 1108

                  ....*
gi 281182408  333 IKAAN 337
Cdd:COG5022  1109 VKPAN 1113
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
33-326 3.75e-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: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408  33 QKLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENmQQAREEEERRKEATAHF 112
Cdd:COG1196  219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE-LELEEAQAEEYELLAEL 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408 113 QITLNEIQAQLEQhdihNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEADEKHQR 192
Cdd:COG1196  298 ARLEQDIARLEER----RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408 193 EREFLLKEATESRHKYEQMKQQEVQLKQQLSLymdkfeefQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRTKWE 272
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEEL--------EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 281182408 273 NNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQ 326
Cdd:COG1196  446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
46 PHA02562
endonuclease subunit; Provisional
157-336 4.92e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.31  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408 157 HIDKVFKHK--ELQQQL--VDAKLQQTTQLIKeADEKHQREREFLLKEA-TESRHKYEQMKQQEVQLKQQLSLYMDKFEE 231
Cdd:PHA02562 167 EMDKLNKDKirELNQQIqtLDMKIDHIQQQIK-TYNKNIEEQRKKNGENiARKQNKYDELVEEAKTIKAEIEELTDELLN 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408 232 FQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRT---------KWENNNKALLQMAEEKTVRDKEYKALQIKLERL 302
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 281182408 303 EKLC---RALQTERNELNEKVEVLKEQVS--------IKAAIKAA 336
Cdd:PHA02562 326 EEIMdefNEQSKKLLELKNKISTNKQSLItlvdkakkVKAAIEEL 370
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
16-260 6.18e-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: 41.97  E-value: 6.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408    16 AEEATEAGRGGRRRSPRQKLEESRSVQKQMKI-LQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEEn 94
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE- 818
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408    95 MQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYalreEHIDKVFKHKELQQQLVDA 174
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EALLNERASLEEALALLRS 894
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   175 KLQQTTQLIKEADEKHQREREfLLKEATESRHKY----EQMKQQEVQLKQQLS-LYMDKFEEFQTTMAKSNELFTTFRQE 249
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRR-ELEELREKLAQLelrlEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRR 973
                          250
                   ....*....|.
gi 281182408   250 MEKMTKKIKKL 260
Cdd:TIGR02168  974 LKRLENKIKEL 984
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
174-328 1.14e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.09  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408  174 AKLQQTTQLIKEADEKHQREREflLKEATESRHKYEQMKQQEVQLKQQLSLYMD----KFEEFQTTMAKSNELFTTFRQE 249
Cdd:COG3096   509 ALAQRLQQLRAQLAELEQRLRQ--QQNAERLLEEFCQRIGQQLDAAEELEELLAeleaQLEELEEQAAEAVEQRSELRQQ 586
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281182408  250 MEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLeklcRALQTERNELNEKVEVLKEQVS 328
Cdd:COG3096   587 LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERE----REATVERDELAARKQALESQIE 661
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
163-341 1.34e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408 163 KHKELQQQLVDAKLQQTTQLIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLkqqlslymdkfEEFQTTMAKSNEL 242
Cdd:COG1196  214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL-----------EELRLELEELELE 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408 243 FTTFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEV 322
Cdd:COG1196  283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
                        170
                 ....*....|....*....
gi 281182408 323 LKEQVSIKAAIKAANRDLA 341
Cdd:COG1196  363 AEEALLEAEAELAEAEEEL 381
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
36-269 1.77e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408    36 EESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEEnMQQAREEEERRKEATAHFQIT 115
Cdd:TIGR02169  287 EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE-IEEERKRRDKLTEEYAELKEE 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   116 LNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQyalREEHIDKVFKHKELQQQLvDAKLQQTTQLIKEADEKHQRere 195
Cdd:TIGR02169  366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE---INELKRELDRLQEELQRL-SEELADLNAAIAGIEAKINE--- 438
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281182408   196 fLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNElfttfrqEMEKMTKKIKKLEKETIIWRT 269
Cdd:TIGR02169  439 -LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK-------ELSKLQRELAEAEAQARASEE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
165-326 1.95e-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: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   165 KELQQQLVDAK--LQQTTQLIKEADEKHQRereflLKEATESRHKYEQMKQQEVQLkqQLSLYMDKFEEFQTTMAKSNEL 242
Cdd:TIGR02168  175 KETERKLERTRenLDRLEDILNELERQLKS-----LERQAEKAERYKELKAELREL--ELALLVLRLEELREELEELQEE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   243 FTTFRQEMEKMTKKIKKLEketiiwrTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEV 322
Cdd:TIGR02168  248 LKEAEEELEELTAELQELE-------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                   ....
gi 281182408   323 LKEQ 326
Cdd:TIGR02168  321 LEAQ 324
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
34-327 2.30e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408    34 KLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENMQQareeeerrkeatahFQ 113
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR--------------VK 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   114 ITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAklqqttqlIKEADEKHQRE 193
Cdd:TIGR02169  294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK--------LTEEYAELKEE 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182408   194 REFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIK-------KLEKETII 266
Cdd:TIGR02169  366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAgieakinELEEEKED 445
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281182408   267 WRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQV 327
Cdd:TIGR02169  446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
 
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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