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Conserved domains on  [gi|42573650|ref|NP_974921|]
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alpha-taxilin-like protein [Arabidopsis thaliana]

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 ...
93-390 4.03e-68

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: 217.90  E-value: 4.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650    93 PISQTLSEGSTQNSTLSKEMDSLKpKKQQEVVESKRKGSKNMFKSEKEFLEFMLKYQQVLSERDSAITVRDKLESLCREL 172
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALC-KKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCREL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650   173 QRQNKMLMEECKRVSTEGQTLRSDLSTKFQDAIMDVSIKLDEQKNESLTQLKENEMLRTKLKHLADQFMLSEQQHEQRLK 252
Cdd:pfam09728  80 QKQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650   253 QKTLELQISALKIKQ---HEEKLIHEQSQ--MKVYADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQE 327
Cdd:pfam09728 160 TKELEVQLAEAKLQQateEEEKKAQEKEVakARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKE 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42573650   328 IDKMSKAIKELRKENAFLKNKTEKSDITLIELVEERERLKKLLEKTKKQKDKLESLCRSLQAE 390
Cdd:pfam09728 240 MEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
93-390 4.03e-68

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: 217.90  E-value: 4.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650    93 PISQTLSEGSTQNSTLSKEMDSLKpKKQQEVVESKRKGSKNMFKSEKEFLEFMLKYQQVLSERDSAITVRDKLESLCREL 172
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALC-KKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCREL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650   173 QRQNKMLMEECKRVSTEGQTLRSDLSTKFQDAIMDVSIKLDEQKNESLTQLKENEMLRTKLKHLADQFMLSEQQHEQRLK 252
Cdd:pfam09728  80 QKQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650   253 QKTLELQISALKIKQ---HEEKLIHEQSQ--MKVYADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQE 327
Cdd:pfam09728 160 TKELEVQLAEAKLQQateEEEKKAQEKEVakARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKE 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42573650   328 IDKMSKAIKELRKENAFLKNKTEKSDITLIELVEERERLKKLLEKTKKQKDKLESLCRSLQAE 390
Cdd:pfam09728 240 MEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
211-395 1.95e-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: 46.97  E-value: 1.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650    211 KLDEQKNESLTQLKENEM-----------LRTKLKHLADQFMLSEQQHEQRLKQKTLELQISALKIKQHEEKLIHEQSQM 279
Cdd:TIGR02168  169 KYKERRKETERKLERTREnldrledilneLERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650    280 KVYADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQEIDKMSKAIKELRKENAFLKNKTEKSDITLIEL 359
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 42573650    360 VEERERLKKLLEKTKKQKDKLESLCRSLQAERKQKE 395
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
202-400 1.96e-05

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: 46.30  E-value: 1.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650 202 QDAIMDVSIKLDEQKNESLTQLKENEMLRTKLKHLADQfmlsEQQHEQRLKQKTLELQISALKIKQHEEKLiheQSQMKV 281
Cdd:COG4942  33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARR----IRALEQELAALEAELAELEKEIAELRAEL---EAQKEE 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650 282 YADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQEIDKMSKAIKELRKENAFLKNKTEKSDITLIELVE 361
Cdd:COG4942 106 LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42573650 362 ERERLKKLLEKTKKQKDKLESLCRSLQAERKQKETNSTD 400
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
149-270 8.67e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 38.63  E-value: 8.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650   149 QQVLSERDSAITVRDKLESLCRELQRQN---KMLMEECKRVSTEGQTLRSDLSTKFQDAiMDVSIKLDEQKN--ESLTQL 223
Cdd:PRK10246  537 KEVKKLGEEGAALRGQLDALTKQLQRDEseaQSLRQEEQALTQQWQAVCASLNITLQPQ-DDIQPWLDAQEEheRQLRLL 615
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 42573650   224 KENEMLRTKLKHLADQFMLSEQQHEQRlkQKTLELQISALKIKQHEE 270
Cdd:PRK10246  616 SQRHELQGQIAAHNQQIIQYQQQIEQR--QQQLLTALAGYALTLPQE 660
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
93-390 4.03e-68

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: 217.90  E-value: 4.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650    93 PISQTLSEGSTQNSTLSKEMDSLKpKKQQEVVESKRKGSKNMFKSEKEFLEFMLKYQQVLSERDSAITVRDKLESLCREL 172
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALC-KKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCREL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650   173 QRQNKMLMEECKRVSTEGQTLRSDLSTKFQDAIMDVSIKLDEQKNESLTQLKENEMLRTKLKHLADQFMLSEQQHEQRLK 252
Cdd:pfam09728  80 QKQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650   253 QKTLELQISALKIKQ---HEEKLIHEQSQ--MKVYADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQE 327
Cdd:pfam09728 160 TKELEVQLAEAKLQQateEEEKKAQEKEVakARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKE 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42573650   328 IDKMSKAIKELRKENAFLKNKTEKSDITLIELVEERERLKKLLEKTKKQKDKLESLCRSLQAE 390
Cdd:pfam09728 240 MEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
211-395 1.95e-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: 46.97  E-value: 1.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650    211 KLDEQKNESLTQLKENEM-----------LRTKLKHLADQFMLSEQQHEQRLKQKTLELQISALKIKQHEEKLIHEQSQM 279
Cdd:TIGR02168  169 KYKERRKETERKLERTREnldrledilneLERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650    280 KVYADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQEIDKMSKAIKELRKENAFLKNKTEKSDITLIEL 359
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 42573650    360 VEERERLKKLLEKTKKQKDKLESLCRSLQAERKQKE 395
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
202-400 1.96e-05

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: 46.30  E-value: 1.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650 202 QDAIMDVSIKLDEQKNESLTQLKENEMLRTKLKHLADQfmlsEQQHEQRLKQKTLELQISALKIKQHEEKLiheQSQMKV 281
Cdd:COG4942  33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARR----IRALEQELAALEAELAELEKEIAELRAEL---EAQKEE 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650 282 YADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQEIDKMSKAIKELRKENAFLKNKTEKSDITLIELVE 361
Cdd:COG4942 106 LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42573650 362 ERERLKKLLEKTKKQKDKLESLCRSLQAERKQKETNSTD 400
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
146-395 4.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 4.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650 146 LKYQQVLSERDSAITV--RDKLESLCRELQRQNKMLMEECKRVSTEGQTLRSDLSTKfQDAIMDVSIKLDEQKNESLTQL 223
Cdd:COG1196 216 RELKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELELEEAQAEEYELL 294
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650 224 KENEMLRTKLKHLADQfmlsEQQHEQRLKQKTLELQISALKIKQHEEKLIHEQSQMKVYADQVSQLLSTEKNLRLQLTSD 303
Cdd:COG1196 295 AELARLEQDIARLEER----RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650 304 GDKFQQFQDALVKSNEVFETFKQEIDKMSKAIKELRKENAFLKNKTEKSDITLIELVEERERLKKLLEKTKKQKDKLESL 383
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
                       250
                ....*....|..
gi 42573650 384 CRSLQAERKQKE 395
Cdd:COG1196 451 EAELEEEEEALL 462
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
149-270 8.67e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 38.63  E-value: 8.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573650   149 QQVLSERDSAITVRDKLESLCRELQRQN---KMLMEECKRVSTEGQTLRSDLSTKFQDAiMDVSIKLDEQKN--ESLTQL 223
Cdd:PRK10246  537 KEVKKLGEEGAALRGQLDALTKQLQRDEseaQSLRQEEQALTQQWQAVCASLNITLQPQ-DDIQPWLDAQEEheRQLRLL 615
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 42573650   224 KENEMLRTKLKHLADQFMLSEQQHEQRlkQKTLELQISALKIKQHEE 270
Cdd:PRK10246  616 SQRHELQGQIAAHNQQIIQYQQQIEQR--QQQLLTALAGYALTLPQE 660
 
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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