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Conserved domains on  [gi|767902967|ref|XP_011539234|]
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alpha-taxilin isoform X2 [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 ...
40-317 1.99e-95

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: 287.23  E-value: 1.99e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   40 LEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQV 119
Cdd:pfam09728  31 LEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKLKEESKKLAKEEEEKRKELSEKFQS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  120 TLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQemlkEAEERHQREK 199
Cdd:pfam09728 111 TLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTKELEVQLAEAKLQQAT----EEEEKKAQEK 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  200 DflLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESS 279
Cdd:pfam09728 187 E--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKS 264
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767902967  280 NKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTE 317
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 ...
40-317 1.99e-95

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: 287.23  E-value: 1.99e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   40 LEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQV 119
Cdd:pfam09728  31 LEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKLKEESKKLAKEEEEKRKELSEKFQS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  120 TLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQemlkEAEERHQREK 199
Cdd:pfam09728 111 TLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTKELEVQLAEAKLQQAT----EEEEKKAQEK 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  200 DflLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESS 279
Cdd:pfam09728 187 E--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKS 264
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767902967  280 NKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTE 317
Cdd:pfam09728 265 NKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
126-327 3.48e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 3.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   126 LQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHID-KVFKHKDLQQQLVDAK-----LQQAQEMLKEAEERHQREK 199
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEeLRLEVSELEEEIEELQkelyaLANEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   200 DFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKEttmyrsrWESS 279
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETL 384
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 767902967   280 NKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQD 327
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
123-330 1.08e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 123 DIQLQMEQHNERNSKLRQENMELAErLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKDFL 202
Cdd:COG1196  240 ELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 203 LKEAvesqrmcelmkQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKA 282
Cdd:COG1196  319 EELE-----------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767902967 283 LLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLSA 330
Cdd:COG1196  388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
46 PHA02562
endonuclease subunit; Provisional
143-330 1.03e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.23  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 143 MEL--AERlKKLIEqyELRE----EHIDKVFKHK--DLQQQL--VDAKLQQAQEMLKeAEERHQREKDFLLKEAV-ESQR 211
Cdd:PHA02562 145 MQLsaPAR-RKLVE--DLLDisvlSEMDKLNKDKirELNQQIqtLDMKIDHIQQQIK-TYNKNIEEQRKKNGENIaRKQN 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 212 MCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYR---------SRWESSNKA 282
Cdd:PHA02562 221 KYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDR 300
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767902967 283 LLEMAEEKTVRDKELEGLQVKIQRLEK-------LCRALQTERNDLNKRVQDLSA 330
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 ...
40-317 1.99e-95

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: 287.23  E-value: 1.99e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   40 LEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQV 119
Cdd:pfam09728  31 LEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKLKEESKKLAKEEEEKRKELSEKFQS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  120 TLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQemlkEAEERHQREK 199
Cdd:pfam09728 111 TLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTKELEVQLAEAKLQQAT----EEEEKKAQEK 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  200 DflLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESS 279
Cdd:pfam09728 187 E--VAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKS 264
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767902967  280 NKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTE 317
Cdd:pfam09728 265 NKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
126-327 3.48e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 3.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   126 LQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHID-KVFKHKDLQQQLVDAK-----LQQAQEMLKEAEERHQREK 199
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEeLRLEVSELEEEIEELQkelyaLANEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   200 DFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKEttmyrsrWESS 279
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETL 384
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 767902967   280 NKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQD 327
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
123-330 1.08e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 123 DIQLQMEQHNERNSKLRQENMELAErLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKDFL 202
Cdd:COG1196  240 ELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 203 LKEAvesqrmcelmkQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKA 282
Cdd:COG1196  319 EELE-----------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767902967 283 LLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLSA 330
Cdd:COG1196  388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
118-328 5.56e-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: 45.43  E-value: 5.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   118 QVTLNDIQLQMEQHNERNSKLRQENMELAERLKKL---IEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEEr 194
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA- 782
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   195 hqrEKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRS 274
Cdd:TIGR02168  783 ---EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767902967   275 RWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDL 328
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
46 PHA02562
endonuclease subunit; Provisional
143-330 1.03e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.23  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 143 MEL--AERlKKLIEqyELRE----EHIDKVFKHK--DLQQQL--VDAKLQQAQEMLKeAEERHQREKDFLLKEAV-ESQR 211
Cdd:PHA02562 145 MQLsaPAR-RKLVE--DLLDisvlSEMDKLNKDKirELNQQIqtLDMKIDHIQQQIK-TYNKNIEEQRKKNGENIaRKQN 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 212 MCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYR---------SRWESSNKA 282
Cdd:PHA02562 221 KYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDR 300
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767902967 283 LLEMAEEKTVRDKELEGLQVKIQRLEK-------LCRALQTERNDLNKRVQDLSA 330
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKLDTAIDELEEimdefneQSKKLLELKNKISTNKQSLIT 355
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
118-328 1.82e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 118 QVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYEL---REEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEER 194
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 195 ---HQREKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTM 271
Cdd:COG1196  332 leeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767902967 272 YRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDL 328
Cdd:COG1196  412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
41-301 1.91e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  41 EEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLK---EEGVQRAREEEEKRKEVTS-- 115
Cdd:COG1196  239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLaelARLEQDIARLEERRRELEErl 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 116 -HFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEER 194
Cdd:COG1196  319 eELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 195 HQREKDFLLKEAVESQRMCELMKQQETHLKQQLALyTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRS 274
Cdd:COG1196  399 AAQLEELEEAEEALLERLERLEEELEELEEALAEL-EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
                        250       260
                 ....*....|....*....|....*..
gi 767902967 275 RWESSNKALLEMAEEKTVRDKELEGLQ 301
Cdd:COG1196  478 ALAELLEELAEAAARLLLLLEAEADYE 504
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
121-330 4.87e-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: 42.06  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 121 LNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVfkhkDLQQQLVDAKLQQAQEMLKEAEERHQREKD 200
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAELRAELEAQKE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 201 FLLKEAVESQRMcelmkqqETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSN 280
Cdd:COG4942  105 ELAELLRALYRL-------GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767902967 281 KALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLSA 330
Cdd:COG4942  178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
170-330 1.53e-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: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   170 KDLQQQLVDAK--LQQAQEMLKEAEERHQRekdfLLKEAVESQRMCELmKQQETHLkqQLALYTEKFEEFQNTLSkssev 247
Cdd:TIGR02168  175 KETERKLERTRenLDRLEDILNELERQLKS----LERQAEKAERYKEL-KAELREL--ELALLVLRLEELREELE----- 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   248 ftTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQD 327
Cdd:TIGR02168  243 --ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                   ...
gi 767902967   328 LSA 330
Cdd:TIGR02168  321 LEA 323
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
21-334 2.20e-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: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967    21 RSETETIEGHRRRKKPRVWLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEhskavlarskLESLCRELQRHNRSLKEEGV 100
Cdd:TIGR02169  217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----------LEEIEQLLEELNKKIKDLGE 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   101 QRAREEEEKRKEVTSHF---QVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYE--------LREEHIDKVFKH 169
Cdd:TIGR02169  287 EEQLRVKEKIGELEAEIaslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrdkLTEEYAELKEEL 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   170 KDLQQQLVD------------AKLQQAQEMLKEAEERHQREKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEF 237
Cdd:TIGR02169  367 EDLRAELEEvdkefaetrdelKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   238 QNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYrsrwessnkallemaeektvrDKELEGLQVKIQRLEKLCRALQTE 317
Cdd:TIGR02169  447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV---------------------EKELSKLQRELAEAEAQARASEER 505
                          330
                   ....*....|....*..
gi 767902967   318 RNDLNKRVQDLSAGGQG 334
Cdd:TIGR02169  506 VRGGRAVEEVLKASIQG 522
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
129-308 4.59e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  129 EQHNERNSKLRQENMELAERLKKlIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKDFLLKEAVE 208
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQE-IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  209 SQRMCELMKQQET----------HLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWES 278
Cdd:TIGR04523 442 IKDLTNQDSVKELiiknldntreSLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
                         170       180       190
                  ....*....|....*....|....*....|
gi 767902967  279 SNKALLEMAEEKTVRDKELEGLQVKIQRLE 308
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDD 551
PRK12704 PRK12704
phosphodiesterase; Provisional
123-236 5.60e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 5.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967 123 DIQLQMEQ-HNERNSKL-RQEN--MELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQRE 198
Cdd:PRK12704  68 KLRNEFEKeLRERRNELqKLEKrlLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767902967 199 KDFLLKEAVEsqrmcELMKQQETHLKQQLALYTEKFEE 236
Cdd:PRK12704 148 SGLTAEEAKE-----ILLEKVEEEARHEAAVLIKEIEE 180
PRK11281 PRK11281
mechanosensitive channel MscK;
118-326 6.65e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  118 QVTLNDIQLQMEQHNER-----NSKLRQENMELAERLKKLIEQYELREEhidkvfkhkDLQQQLVDA--KLQQAQEMLke 190
Cdd:PRK11281   35 LPTEADVQAQLDALNKQklleaEDKLVQQDLEQTLALLDKIDRQKEETE---------QLKQQLAQApaKLRQAQAEL-- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  191 aeERHQREKDFLLKEAVESQRMCELMKQQETHLKQQlalytekfEEFQNTLSK-SSEVFTTFKQ---------EMEKMTK 260
Cdd:PRK11281  104 --EALKDDNDEETRETLSTLSLRQLESRLAQTLDQL--------QNAQNDLAEyNSQLVSLQTQperaqaalyANSQRLQ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  261 KIKKLEKETTMYRSRWESSNKALLEmAEEKTV------RDKELEG--------------LQVKIQRLEKLCRALQTERND 320
Cdd:PRK11281  174 QIRNLLKGGKVGGKALRPSQRVLLQ-AEQALLnaqndlQRKSLEGntqlqdllqkqrdyLTARIQRLEHQLQLLQEAINS 252

                  ....*.
gi 767902967  321 lnKRVQ 326
Cdd:PRK11281  253 --KRLT 256
PTZ00121 PTZ00121
MAEBL; Provisional
41-318 8.97e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 8.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967   41 EEHRNSQKQMKLLQKKQSQLVQEKDHLR-GEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQV 119
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKkAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  120 TLNDIQlqmEQHNERNSKLRQENMELAERLKKLIEQYELREEHidkvfkhkdlqqqlvdaKLQQAQEMLKEAEERHQREK 199
Cdd:PTZ00121 1605 KKMKAE---EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-----------------EKKKAEELKKAEEENKIKAA 1664
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902967  200 DFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEefqntlSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESS 279
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE------AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767902967  280 NKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTER 318
Cdd:PTZ00121 1739 AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
 
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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