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Conserved domains on  [gi|74217146|dbj|BAC39238|]
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unnamed protein product, partial [Mus musculus]

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 ...
146-453 2.99e-92

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: 281.84  E-value: 2.99e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146   146 KEANLLMQNLNKLQAPEEKLDFLFKKYTELLDEHRTEQKKLKLLLKQQAQTQREKDQLQSEHNRAVLARSKLESLCRELQ 225
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146   226 RHNKTLKEETLQRAREEEEKRKEITSHFQTTLTDIQTQIEQQSERNMKLCQENTELAEKLKSIIDQYELREEHLDKIFKH 305
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146   306 RELQQKLAYAKLEEAqelmQEAEERHRREKEYllNQAAEWKLQAKVLKEQETVLQAQLTLYSGRFEEFQSTLTKSNEVFA 385
Cdd:pfam09728 161 KELEVQLAEAKLQQA----TEEEEKKAQEKEV--AKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74217146   386 TFKQEMDKTTKKMKKLEKDTATWKARFENCNKALLDMIEEKALRAKEYECFVMKIQRLENLCRALQEE 453
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 ...
146-453 2.99e-92

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: 281.84  E-value: 2.99e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146   146 KEANLLMQNLNKLQAPEEKLDFLFKKYTELLDEHRTEQKKLKLLLKQQAQTQREKDQLQSEHNRAVLARSKLESLCRELQ 225
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146   226 RHNKTLKEETLQRAREEEEKRKEITSHFQTTLTDIQTQIEQQSERNMKLCQENTELAEKLKSIIDQYELREEHLDKIFKH 305
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146   306 RELQQKLAYAKLEEAqelmQEAEERHRREKEYllNQAAEWKLQAKVLKEQETVLQAQLTLYSGRFEEFQSTLTKSNEVFA 385
Cdd:pfam09728 161 KELEVQLAEAKLQQA----TEEEEKKAQEKEV--AKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74217146   386 TFKQEMDKTTKKMKKLEKDTATWKARFENCNKALLDMIEEKALRAKEYECFVMKIQRLENLCRALQEE 453
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
196-459 4.50e-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: 46.20  E-value: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    196 TQREKDQLQSEHNRAVLARSKLESLCRELQRHNKTLKEEtLQRAREEEEKRKEITSHFQTTLTDIQTQIEQQSERNMKLC 275
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKD-LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    276 QENTELAEKLKSIIDQYELREEHLDkifkhrelQQKLAYAKLEEAQELMQEAEERHRREKEYLLNQAAEWKLQAKVLKEQ 355
Cdd:TIGR02168  775 EELAEAEAEIEELEAQIEQLKEELK--------ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    356 ETVLQAQLTLYSGRFEEFQSTLTKSNEVFATFKQEMDKTTKKMKKLEKDTATWKARFENCNKALLDMIEEKALRAKEYEC 435
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
                          250       260
                   ....*....|....*....|....
gi 74217146    436 FVMKIQRLENLCRALQEERKELYK 459
Cdd:TIGR02168  927 LELRLEGLEVRIDNLQERLSEEYS 950
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-363 1.14e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146  251 SHFQTtLTDIQTQIEQQSERnmklcqentelAEKLKSIIDQYELREEHLDKIFKHRELQQKLAYAKLEEAQELMQEAEER 330
Cdd:COG4913  232 EHFDD-LERAHEALEDAREQ-----------IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
                         90       100       110
                 ....*....|....*....|....*....|...
gi 74217146  331 HRREKEYLLNQAAEWKLQAKVLKEQETVLQAQL 363
Cdd:COG4913  300 LRAELARLEAELERLEARLDALREELDELEAQI 332
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
146-453 2.99e-92

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: 281.84  E-value: 2.99e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146   146 KEANLLMQNLNKLQAPEEKLDFLFKKYTELLDEHRTEQKKLKLLLKQQAQTQREKDQLQSEHNRAVLARSKLESLCRELQ 225
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146   226 RHNKTLKEETLQRAREEEEKRKEITSHFQTTLTDIQTQIEQQSERNMKLCQENTELAEKLKSIIDQYELREEHLDKIFKH 305
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146   306 RELQQKLAYAKLEEAqelmQEAEERHRREKEYllNQAAEWKLQAKVLKEQETVLQAQLTLYSGRFEEFQSTLTKSNEVFA 385
Cdd:pfam09728 161 KELEVQLAEAKLQQA----TEEEEKKAQEKEV--AKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74217146   386 TFKQEMDKTTKKMKKLEKDTATWKARFENCNKALLDMIEEKALRAKEYECFVMKIQRLENLCRALQEE 453
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
196-459 4.50e-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: 46.20  E-value: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    196 TQREKDQLQSEHNRAVLARSKLESLCRELQRHNKTLKEEtLQRAREEEEKRKEITSHFQTTLTDIQTQIEQQSERNMKLC 275
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKD-LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    276 QENTELAEKLKSIIDQYELREEHLDkifkhrelQQKLAYAKLEEAQELMQEAEERHRREKEYLLNQAAEWKLQAKVLKEQ 355
Cdd:TIGR02168  775 EELAEAEAEIEELEAQIEQLKEELK--------ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    356 ETVLQAQLTLYSGRFEEFQSTLTKSNEVFATFKQEMDKTTKKMKKLEKDTATWKARFENCNKALLDMIEEKALRAKEYEC 435
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
                          250       260
                   ....*....|....*....|....
gi 74217146    436 FVMKIQRLENLCRALQEERKELYK 459
Cdd:TIGR02168  927 LELRLEGLEVRIDNLQERLSEEYS 950
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
164-464 2.56e-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: 43.51  E-value: 2.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    164 KLDFLFKKYTELLDEHRTEQKKLKLLLKQQAQTQREKDQLQSEHNRAVLARSKLESLCRELQRHNKTLKEEtLQRAREEE 243
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-ISRLEQQK 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    244 EKRKEITSHFQTTLTDIQTQIEQQSERNMKLCQENTELAEKLKSIIDQYELREEHLDKifkhrelqqklAYAKLEEAQEL 323
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE-----------LEAELEELESR 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    324 MQEAEERHRREKeyllNQAAEWKLQAKVLKEQETVLQAQLTLYSGRFEEFQSTLTKSNEVFATF-KQEMDKTTKKMKKLE 402
Cdd:TIGR02168  374 LEELEEQLETLR----SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEEL 449
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74217146    403 KDTATWKARFENCNKALLDMIEEKALRAKEYECFVMKIQRLENLCRALQEERKELYKKIREA 464
Cdd:TIGR02168  450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-363 1.14e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146  251 SHFQTtLTDIQTQIEQQSERnmklcqentelAEKLKSIIDQYELREEHLDKIFKHRELQQKLAYAKLEEAQELMQEAEER 330
Cdd:COG4913  232 EHFDD-LERAHEALEDAREQ-----------IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
                         90       100       110
                 ....*....|....*....|....*....|...
gi 74217146  331 HRREKEYLLNQAAEWKLQAKVLKEQETVLQAQL 363
Cdd:COG4913  300 LRAELARLEAELERLEARLDALREELDELEAQI 332
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
106-362 1.78e-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: 40.81  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    106 EETTEEIDREPTAPEEPAAAKEPVSNKEQKLEKKILKGLGKEANLLMQNLNKLQAPEEKLDFLFKKYTELLDEHRTEQKK 185
Cdd:TIGR02168  690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    186 LKLLLKQQAQTQREKDQLQSEHNRAVLARSKLESLCRELQRHNKTLKEEtLQRAREEEEKRKEITSHFQTTLTDIQTQIE 265
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE-AANLRERLESLERRIAATERRLEDLEEQIE 848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    266 QQSERNMKLCQENTELAEKLKSIIDQYelreEHLDKIFKHRELQQKLAYAKLEEAQELMQEAEERhRREKEYLLNQAAEw 345
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESEL----EALLNERASLEEALALLRSELEELSEELRELESK-RSELRRELEELRE- 922
                          250
                   ....*....|....*..
gi 74217146    346 KLQAKVLKEQETVLQAQ 362
Cdd:TIGR02168  923 KLAQLELRLEGLEVRID 939
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
254-464 5.68e-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: 39.27  E-value: 5.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    254 QTTLTDIQTQIEQQSERNMKLCQENTELAEKLKSI---IDQYELREEHLDKIFKHRELQQKLAYAKLEEAQELMQEAEEr 330
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA- 782
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146    331 hrrEKEYLLNQAAEWKLQAKVLKEQETVLQAQLTLYSGRFEEFQSTLTKSNEVFATFKQEMDKTTKKMKKLEKDTATWKA 410
Cdd:TIGR02168  783 ---EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 74217146    411 RFENCNKALLDMIEEKALRAKEYECFVMKIQRLENLCRALQEERKELYKKIREA 464
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
252-464 7.52e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 7.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146 252 HFQTTLTDIQTQIEQQSERNMKLCQENTELAEKLKsiidqyELREEHLDKIFKHRELQQKL-----AYAKLEEAQELMQE 326
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELE------ELRLELEELELELEEAQAEEyellaELARLEQDIARLEE 309
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74217146 327 AEERHRREKEYLLNQAAEWKLQAKVLKEQETVLQAQLTLYSGRFEEFQSTLTKSNEVFATFKQEMDKTTKKMKKLEKDTA 406
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 74217146 407 TWKARFENCNKALLDMIEEKALRAKEYECFVMKIQRLENLCRALQEERKELYKKIREA 464
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
 
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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