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Conserved domains on  [gi|1777375997|ref|NP_001363787|]
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alpha-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 ...
1-302 3.31e-103

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: 306.49  E-value: 3.31e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997   1 MQTLNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSL 80
Cdd:pfam09728   7 MQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  81 KEEGVQRAREEEEKRKEVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQ 160
Cdd:pfam09728  87 KEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTKELEVQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 161 LVDAKLQQAQemlkEAEERHQREKDflLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEM 240
Cdd:pfam09728 167 LAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEM 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777375997 241 EKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTE 302
Cdd:pfam09728 241 EKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
1-302 3.31e-103

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: 306.49  E-value: 3.31e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997   1 MQTLNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSL 80
Cdd:pfam09728   7 MQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  81 KEEGVQRAREEEEKRKEVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQ 160
Cdd:pfam09728  87 KEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTKELEVQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 161 LVDAKLQQAQemlkEAEERHQREKDflLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEM 240
Cdd:pfam09728 167 LAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEM 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777375997 241 EKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTE 302
Cdd:pfam09728 241 EKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
111-312 4.30e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 4.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  111 LQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHID-KVFKHKDLQQQLVDAK-----LQQAQEMLKEAEERHQREK 184
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEeLRLEVSELEEEIEELQkelyaLANEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  185 DFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKEttmyrsrWESS 264
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETL 384
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1777375997  265 NKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQD 312
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
19-315 7.03e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 7.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  19 KKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLAR--SKLESLCRELQRHNRSLKEEGvQRAREEEEKRK 96
Cdd:COG1196   213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEleAELAELEAELEELRLELEELE-LELEEAQAEEY 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  97 EVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEhidkvfkhKDLQQQLVDAKLQQAQEMLKEA 176
Cdd:COG1196   292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE--------LEEELEEAEEELEEAEAELAEA 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 177 EERhqrekdflLKEAVESQRmcELMKQQETHLKQQLALYTEKfEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTM 256
Cdd:COG1196   364 EEA--------LLEAEAELA--EAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1777375997 257 YRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLSA 315
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
46 PHA02562
endonuclease subunit; Provisional
128-315 1.79e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.46  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 128 MEL--AERlKKLIEqyELRE----EHIDKVFKHK--DLQQQL--VDAKLQQAQEMLKeAEERHQREKDFLLKEAV-ESQR 196
Cdd:PHA02562  145 MQLsaPAR-RKLVE--DLLDisvlSEMDKLNKDKirELNQQIqtLDMKIDHIQQQIK-TYNKNIEEQRKKNGENIaRKQN 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 197 MCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYR---------SRWESSNKA 267
Cdd:PHA02562  221 KYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDR 300
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1777375997 268 LLEMAEEKTVRDKELEGLQVKIQRLEK-------LCRALQTERNDLNKRVQDLSA 315
Cdd:PHA02562  301 ITKIKDKLKELQHSLEKLDTAIDELEEimdefneQSKKLLELKNKISTNKQSLIT 355
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
1-302 3.31e-103

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: 306.49  E-value: 3.31e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997   1 MQTLNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSL 80
Cdd:pfam09728   7 MQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  81 KEEGVQRAREEEEKRKEVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQ 160
Cdd:pfam09728  87 KEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTKELEVQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 161 LVDAKLQQAQemlkEAEERHQREKDflLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEM 240
Cdd:pfam09728 167 LAEAKLQQAT----EEEEKKAQEKE--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEM 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777375997 241 EKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTE 302
Cdd:pfam09728 241 EKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
111-312 4.30e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 4.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  111 LQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHID-KVFKHKDLQQQLVDAK-----LQQAQEMLKEAEERHQREK 184
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEeLRLEVSELEEEIEELQkelyaLANEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  185 DFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKEttmyrsrWESS 264
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETL 384
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1777375997  265 NKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQD 312
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
19-315 7.03e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 7.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  19 KKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLAR--SKLESLCRELQRHNRSLKEEGvQRAREEEEKRK 96
Cdd:COG1196   213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEleAELAELEAELEELRLELEELE-LELEEAQAEEY 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  97 EVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEhidkvfkhKDLQQQLVDAKLQQAQEMLKEA 176
Cdd:COG1196   292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE--------LEEELEEAEEELEEAEAELAEA 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 177 EERhqrekdflLKEAVESQRmcELMKQQETHLKQQLALYTEKfEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTM 256
Cdd:COG1196   364 EEA--------LLEAEAELA--EAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1777375997 257 YRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLSA 315
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
11-286 1.28e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  11 EEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRARE 90
Cdd:COG1196   245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  91 EEEkrkevtshfqvtlndIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQ 170
Cdd:COG1196   325 LAE---------------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 171 EMLKEAEERHQREKDFLLKEAVESQRMCELMKQQETHLKQQLALyTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKL 250
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL-EEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1777375997 251 EKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQ 286
Cdd:COG1196   469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
103-313 6.94e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 6.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  103 QVTLNDIQLQMEQHNERNSKLRQENMELAERLKKL---IEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEEr 179
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA- 782
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  180 hqrEKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRS 259
Cdd:TIGR02168  783 ---EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1777375997  260 RWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDL 313
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
46 PHA02562
endonuclease subunit; Provisional
128-315 1.79e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.46  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 128 MEL--AERlKKLIEqyELRE----EHIDKVFKHK--DLQQQL--VDAKLQQAQEMLKeAEERHQREKDFLLKEAV-ESQR 196
Cdd:PHA02562  145 MQLsaPAR-RKLVE--DLLDisvlSEMDKLNKDKirELNQQIqtLDMKIDHIQQQIK-TYNKNIEEQRKKNGENIaRKQN 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 197 MCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYR---------SRWESSNKA 267
Cdd:PHA02562  221 KYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDR 300
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1777375997 268 LLEMAEEKTVRDKELEGLQVKIQRLEK-------LCRALQTERNDLNKRVQDLSA 315
Cdd:PHA02562  301 ITKIKDKLKELQHSLEKLDTAIDELEEimdefneQSKKLLELKNKISTNKQSLIT 355
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-239 4.57e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 4.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997   11 EEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGeHSKAVLARSKLESLCRELQRhnrslkeegvqrare 90
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAEREIAE--------------- 672
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997   91 eeekrkevtshfqvtlndIQLQMEQHNERNSKLRqenmELAERLKKLIEQY-ELREEHIDKVFKHKDLQQQLVDAK--LQ 167
Cdd:COG4913    673 ------------------LEAELERLDASSDDLA----ALEEQLEELEAELeELEEELDELKGEIGRLEKELEQAEeeLD 730
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777375997  168 QAQEMLKEAEERHQREKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKsseVFTTFKQE 239
Cdd:COG4913    731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELER---AMRAFNRE 799
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
106-315 4.73e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 106 LNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVfkhkDLQQQLVDAKLQQAQEMLKEAEERHQREKD 185
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAELRAELEAQKE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 186 FLLKEAVESQRMcelmkqqETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSN 265
Cdd:COG4942   105 ELAELLRALYRL-------GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1777375997 266 KALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLSA 315
Cdd:COG4942   178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
7-252 6.87e-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: 6.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997    7 LSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEGVQ 86
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997   87 RAREEEEKRKEVTShFQVTLNDIQLQMEQHNERNSKLRQEnmelAERLKKLIEQYELREEHIDKvfkhkdlQQQLVDAKL 166
Cdd:TIGR02168  342 LEEKLEELKEELES-LEAELEELEAELEELESRLEELEEQ----LETLRSKVAQLELQIASLNN-------EIERLEARL 409
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  167 QQAQEML-KEAEERHQREKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTK 245
Cdd:TIGR02168  410 ERLEDRReRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489

                   ....*..
gi 1777375997  246 KIKKLEK 252
Cdd:TIGR02168  490 RLDSLER 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
7-319 6.92e-04

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: 41.59  E-value: 6.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997    7 LSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVlaRSKLESLCRELQRHNRSL--KEEG 84
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV--KEKIGELEAEIASLERSIaeKERE 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997   85 VQRAREEEEKRkevtshfQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYE-LREEHIDKVFKHKDLQQQLVD 163
Cdd:TIGR02169  317 LEDAEERLAKL-------EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdLRAELEEVDKEFAETRDELKD 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  164 akLQQAQEMLKEAEERHQREKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKM 243
Cdd:TIGR02169  390 --YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777375997  244 TKKIKKLEKETTMYrsrwessnkallemaeektvrDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLSAGGQG 319
Cdd:TIGR02169  468 EQELYDLKEEYDRV---------------------EKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
155-315 2.08e-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: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  155 KDLQQQLVDAK--LQQAQEMLKEAEERHQRekdfLLKEAVESQRMCELmKQQETHLkqQLALYTEKFEEFQNTLSkssev 232
Cdd:TIGR02168  175 KETERKLERTRenLDRLEDILNELERQLKS----LERQAEKAERYKEL-KAELREL--ELALLVLRLEELREELE----- 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  233 ftTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQD 312
Cdd:TIGR02168  243 --ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                   ...
gi 1777375997  313 LSA 315
Cdd:TIGR02168  321 LEA 323
PRK12704 PRK12704
phosphodiesterase; Provisional
108-221 5.26e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997 108 DIQLQMEQ-HNERNSKL-RQEN--MELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQRE 183
Cdd:PRK12704   68 KLRNEFEKeLRERRNELqKLEKrlLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1777375997 184 KDFLLKEAVEsqrmcELMKQQETHLKQQLALYTEKFEE 221
Cdd:PRK12704  148 SGLTAEEAKE-----ILLEKVEEEARHEAAVLIKEIEE 180
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
14-228 6.44e-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: 38.21  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  14 LAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEE--GVQRAREE 91
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaELEKEIAE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  92 EEKRKEVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQY-ELREEHIDKVFKHKDLQQQLVdAKLQQAQ 170
Cdd:COG4942    95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAELAALR-AELEAER 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1777375997 171 EMLKEAEERHQREKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSK 228
Cdd:COG4942   174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
PTZ00121 PTZ00121
MAEBL; Provisional
26-303 8.42e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 8.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997   26 EEHRNSQKQMKLLQKKQSQLVQEKDHLR-GEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQV 104
Cdd:PTZ00121  1525 DEAKKAEEAKKADEAKKAEEKKKADELKkAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  105 TLNDIQlqmEQHNERNSKLRQENMELAERLKKLIEQYELREEHidkvfkhkdlqqqlvdaKLQQAQEMLKEAEERHQREK 184
Cdd:PTZ00121  1605 KKMKAE---EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-----------------EKKKAEELKKAEEENKIKAA 1664
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  185 DFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEefqntlSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESS 264
Cdd:PTZ00121  1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE------AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1777375997  265 NKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTER 303
Cdd:PTZ00121  1739 AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
10-327 9.54e-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: 38.03  E-value: 9.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997   10 PEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEK-DHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRA 88
Cdd:pfam02463  735 NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKeLAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA 814
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997   89 REEEEKRKEVTSHfqvtLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQ 168
Cdd:pfam02463  815 ELLEEEQLLIEQE----EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES 890
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  169 AQEMLKEAEERHQREKDFLLKEAvESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFT-TFKQEMEKMTKKI 247
Cdd:pfam02463  891 KEEKEKEEKKELEEESQKLNLLE-EKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKeEEEERNKRLLLAK 969
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375997  248 KKLEKETTMYRSRWESSNKA---LLEMAEEKTVRDKELEGLQVKI--QRLEKLCRALQTERNDLNKRVQDLSAGGQGSLT 322
Cdd:pfam02463  970 EELGKVNLMAIEEFEEKEERynkDELEKERLEEEKKKLIRAIIEEtcQRLKEFLELFVSINKGWNKVFFYLELGGSAELR 1049

                   ....*
gi 1777375997  323 DSGPE 327
Cdd:pfam02463 1050 LEDPD 1054
 
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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