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Conserved domains on  [gi|31711880|gb|AAP68296|]
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At5g50840 [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 ...
93-389 1.01e-69

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: 221.75  E-value: 1.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880    93 PISQTLSEGSTQNSTLSKEMDSLKPKKQEVVESKRKGSKNMFKSEKEFLEFMLKYQQVLSERDSAITVRDKLESLCRELQ 172
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880   173 RQNKMLMEECKRVSTEGQTLRSDLSTKFQDAIMDVSIKLDEQKNESLTQLKENEMLRTKLKHLADQFMLSEQQHEQRLKQ 252
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880   253 KTLELQISALKIKQ---HEEKLIHEQSQ--MKVYADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQEI 327
Cdd:pfam09728 161 KELEVQLAEAKLQQateEEEKKAQEKEVakARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEM 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31711880   328 DKMSKAIKELRKENAFLKNKTEKSDITLIELVEERERLKKLLEKTKKQKDKLESLCRSLQAE 389
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 ...
93-389 1.01e-69

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: 221.75  E-value: 1.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880    93 PISQTLSEGSTQNSTLSKEMDSLKPKKQEVVESKRKGSKNMFKSEKEFLEFMLKYQQVLSERDSAITVRDKLESLCRELQ 172
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880   173 RQNKMLMEECKRVSTEGQTLRSDLSTKFQDAIMDVSIKLDEQKNESLTQLKENEMLRTKLKHLADQFMLSEQQHEQRLKQ 252
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880   253 KTLELQISALKIKQ---HEEKLIHEQSQ--MKVYADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQEI 327
Cdd:pfam09728 161 KELEVQLAEAKLQQateEEEKKAQEKEVakARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEM 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31711880   328 DKMSKAIKELRKENAFLKNKTEKSDITLIELVEERERLKKLLEKTKKQKDKLESLCRSLQAE 389
Cdd:pfam09728 241 EKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
201-399 1.90e-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: 1.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880 201 QDAIMDVSIKLDEQKNESLTQLKENEMLRTKLKHLADQfmlsEQQHEQRLKQKTLELQISALKIKQHEEKLiheQSQMKV 280
Cdd:COG4942  33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARR----IRALEQELAALEAELAELEKEIAELRAEL---EAQKEE 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880 281 YADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQEIDKMSKAIKELRKENAFLKNKTEKSDITLIELVE 360
Cdd:COG4942 106 LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 31711880 361 ERERLKKLLEKTKKQKDKLESLCRSLQAERKQKETNSTD 399
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
210-394 1.92e-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: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880    210 KLDEQKNESLTQLKENEM-----------LRTKLKHLADQFMLSEQQHEQRLKQKTLELQISALKIKQHEEKLIHEQSQM 278
Cdd:TIGR02168  169 KYKERRKETERKLERTREnldrledilneLERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880    279 KVYADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQEIDKMSKAIKELRKENAFLKNKTEKSDITLIEL 358
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 31711880    359 VEERERLKKLLEKTKKQKDKLESLCRSLQAERKQKE 394
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
148-269 7.33e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 38.63  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880   148 QQVLSERDSAITVRDKLESLCRELQRQN---KMLMEECKRVSTEGQTLRSDLSTKFQDAiMDVSIKLDEQKN--ESLTQL 222
Cdd:PRK10246  537 KEVKKLGEEGAALRGQLDALTKQLQRDEseaQSLRQEEQALTQQWQAVCASLNITLQPQ-DDIQPWLDAQEEheRQLRLL 615
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 31711880   223 KENEMLRTKLKHLADQFMLSEQQHEQRlkQKTLELQISALKIKQHEE 269
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 ...
93-389 1.01e-69

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: 221.75  E-value: 1.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880    93 PISQTLSEGSTQNSTLSKEMDSLKPKKQEVVESKRKGSKNMFKSEKEFLEFMLKYQQVLSERDSAITVRDKLESLCRELQ 172
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880   173 RQNKMLMEECKRVSTEGQTLRSDLSTKFQDAIMDVSIKLDEQKNESLTQLKENEMLRTKLKHLADQFMLSEQQHEQRLKQ 252
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880   253 KTLELQISALKIKQ---HEEKLIHEQSQ--MKVYADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQEI 327
Cdd:pfam09728 161 KELEVQLAEAKLQQateEEEKKAQEKEVakARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEM 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31711880   328 DKMSKAIKELRKENAFLKNKTEKSDITLIELVEERERLKKLLEKTKKQKDKLESLCRSLQAE 389
Cdd:pfam09728 241 EKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
201-399 1.90e-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: 1.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880 201 QDAIMDVSIKLDEQKNESLTQLKENEMLRTKLKHLADQfmlsEQQHEQRLKQKTLELQISALKIKQHEEKLiheQSQMKV 280
Cdd:COG4942  33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARR----IRALEQELAALEAELAELEKEIAELRAEL---EAQKEE 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880 281 YADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQEIDKMSKAIKELRKENAFLKNKTEKSDITLIELVE 360
Cdd:COG4942 106 LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 31711880 361 ERERLKKLLEKTKKQKDKLESLCRSLQAERKQKETNSTD 399
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
210-394 1.92e-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: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880    210 KLDEQKNESLTQLKENEM-----------LRTKLKHLADQFMLSEQQHEQRLKQKTLELQISALKIKQHEEKLIHEQSQM 278
Cdd:TIGR02168  169 KYKERRKETERKLERTREnldrledilneLERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880    279 KVYADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVFETFKQEIDKMSKAIKELRKENAFLKNKTEKSDITLIEL 358
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 31711880    359 VEERERLKKLLEKTKKQKDKLESLCRSLQAERKQKE 394
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
145-394 4.05e-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: 4.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880 145 LKYQQVLSERDSAITV--RDKLESLCRELQRQNKMLMEECKRVSTEGQTLRSDLSTKfQDAIMDVSIKLDEQKNESLTQL 222
Cdd:COG1196 216 RELKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELELEEAQAEEYELL 294
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880 223 KENEMLRTKLKHLADQfmlsEQQHEQRLKQKTLELQISALKIKQHEEKLIHEQSQMKVYADQVSQLLSTEKNLRLQLTSD 302
Cdd:COG1196 295 AELARLEQDIARLEER----RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880 303 GDKFQQFQDALVKSNEVFETFKQEIDKMSKAIKELRKENAFLKNKTEKSDITLIELVEERERLKKLLEKTKKQKDKLESL 382
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
                       250
                ....*....|..
gi 31711880 383 CRSLQAERKQKE 394
Cdd:COG1196 451 EAELEEEEEALL 462
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
81-396 2.58e-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: 40.34  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880     81 LEFEQKEKEASPPIsqtlsegSTQNSTLSKEMDSLKPKKQEVVESKRKGSKNMFKSEKEFLEFMLKYQQVLSERDSAITV 160
Cdd:pfam02463  166 RLKRKKKEALKKLI-------EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880    161 RDKLESLCRELQRQNKMLMEECKRVSTEGQTLRSDLSTKFQdAIMDVSIKLDEQKNESLTQLKENEMLRTKLKHLADQFM 240
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK-EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880    241 LSEQQHEQRLKQKTLELQISALKIKQHEEKLIHEQSQMKVYADQVSQLLSTEKNLRLQLTSDGDKFQQFQDALVKSNEVF 320
Cdd:pfam02463  318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31711880    321 ETFKQEIDKMSKAIKELRKENAFLKNKTEKSDITLIELVEERERLKKLLEKTKKQKDKLESLCRSLQAERKQKETN 396
Cdd:pfam02463  398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
148-269 7.33e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 38.63  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31711880   148 QQVLSERDSAITVRDKLESLCRELQRQN---KMLMEECKRVSTEGQTLRSDLSTKFQDAiMDVSIKLDEQKN--ESLTQL 222
Cdd:PRK10246  537 KEVKKLGEEGAALRGQLDALTKQLQRDEseaQSLRQEEQALTQQWQAVCASLNITLQPQ-DDIQPWLDAQEEheRQLRLL 615
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 31711880   223 KENEMLRTKLKHLADQFMLSEQQHEQRlkQKTLELQISALKIKQHEE 269
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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