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Conserved domains on  [gi|398366301|ref|NP_010545|]
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Yap6p [Saccharomyces cerevisiae S288C]

Protein Classification

bZIP transcription factor( domain architecture ID 10445711)

basic leucine zipper (bZIP) transcription factor binds to the promoter regions of genes to control their expression

CATH:  1.20.5.170
Gene Ontology:  GO:0046983|GO:0006355|GO:0003700|GO:0003677
PubMed:  23661758|7780801
SCOP:  4003836

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
 223-278 2.56e-09

bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper region.


:

Pssm-ID: 395118 [Multi-domain]  Cd Length: 60  Bit Score: 52.77  E-value: 2.56e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301  223 RNTRRAAQNRTAQKAFRQRKEKYIKNLEQKSKIFD----DLLAENNNFKSLNDSLRNDNN 278
Cdd:pfam00170   1 KREKRKQSNREAARRSRQRKQAYIEELERRVKALEgenkTLRSELEELKKEVEKLKSKNK 60
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 209-379 1.01e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301   209 DKDTQLISSSGKTLRNTRRAAQNRTAQkaFRQRKEKYIKNLEQKSKIFDDLLAENNNFKSLNDSLRNDNNILIAQHEAIR 288
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEE--LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301   289 NAITMLRSEYDVLCNENNMLKNENSIIKNEHNMSRNENENL---------KLENKRFH------AEYIRMIEDI----EN 349
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeieellkKLEEAELKelqaelEELEEELEELqeelER 458

                          170       180       190
                   ....*....|....*....|....*....|
gi 398366301   350 TKRKEQEQRDEIEQLKKKIRSLEEIVGRHS 379
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAERELAQLQ 488
 
Name Accession Description Interval E-value
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
 223-278 2.56e-09

bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper region.


Pssm-ID: 395118 [Multi-domain]  Cd Length: 60  Bit Score: 52.77  E-value: 2.56e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301  223 RNTRRAAQNRTAQKAFRQRKEKYIKNLEQKSKIFD----DLLAENNNFKSLNDSLRNDNN 278
Cdd:pfam00170   1 KREKRKQSNREAARRSRQRKQAYIEELERRVKALEgenkTLRSELEELKKEVEKLKSKNK 60
bZIP_YAP cd14688
Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a ...
 223-280 3.53e-09

Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed predominantly of AP-1-like transcription factors including Saccharomyces cerevisiae YAPs, Schizosaccharomyces pombe PAP1, and similar proteins. Members of this subfamily belong to the Basic leucine zipper (bZIP) family of transcription factors. The YAP subfamily is composed of eight members (YAP1-8) which may all be involved in stress responses. YAP1 is the major oxidative stress regulator and is also involved in iron metabolism (like YAP5) and detoxification of arsenic (like YAP8). YAP2 is involved in cadmium stress responses while YAP4 and YAP6 play roles in osmotic stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269836 [Multi-domain]  Cd Length: 63  Bit Score: 52.72  E-value: 3.53e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366301 223 RNTRRAAQNRTAQKAFRQRKEKYIKNLEQK----SKIFDDLLAENNNFKSLNDSLRNDNNIL 280
Cdd:cd14688    2 PKERRRAQNREAQRAFRERKKERIKELEQRvaelEEELAELEEELQELRAELRELESELQSL 63
BRLZ smart00338
basic region leucin zipper;
220-278 1.54e-05

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 42.17  E-value: 1.54e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366301   220 KTLRNTRRAAQNRTAQKAFRQRKEKYIKNLEQKSKIF----DDLLAENNNFKSLNDSLRNDNN 278
Cdd:smart00338   2 EDEKRRRRRERNREAARRSRERKKAEIEELERKVEQLeaenERLKKEIERLRRELEKLKSELE 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 209-379 1.01e-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: 44.66  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301   209 DKDTQLISSSGKTLRNTRRAAQNRTAQkaFRQRKEKYIKNLEQKSKIFDDLLAENNNFKSLNDSLRNDNNILIAQHEAIR 288
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEE--LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301   289 NAITMLRSEYDVLCNENNMLKNENSIIKNEHNMSRNENENL---------KLENKRFH------AEYIRMIEDI----EN 349
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeieellkKLEEAELKelqaelEELEEELEELqeelER 458

                          170       180       190
                   ....*....|....*....|....*....|
gi 398366301   350 TKRKEQEQRDEIEQLKKKIRSLEEIVGRHS 379
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAERELAQLQ 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 232-375 1.16e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301 232 RTAQKAFRQRKEKYIKNLEQKSKIFDDLLAENNNFKSLNDSLRNDNNILIAQHEAIRNAITMLRSEYDVLCNENNMLKNE 311
Cdd:COG1196  210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366301 312 NSIIKNEHNMSRNENENLKLENKRFHAEYIRMIEDIENTKRKEQEQRDEIEQLKKKIRSLEEIV 375
Cdd:COG1196  290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-374 2.05e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301 236 KAFRQRKEKYIKNLEQKSKIfDDLLAENNnfKSLNDSLRNDNNILIAQHEaIRNAITMLRSEYDVLcnennmlknensii 315
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENI-EELIKEKE--KELEEVLREINEISSELPE-LREELEKLEKEVKEL-------------- 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366301 316 kNEHnmsRNENENLKLENKRFHAEYIRMIEDIENTKRKEQEQRDEIEQLKKKIRSLEEI 374
Cdd:PRK03918 234 -EEL---KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL 288
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 258-373 2.14e-03

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: 39.55  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301  258 DLLAENNNFKSLNDSLRNDNNILIA---QHEAIRNAITMLRSEYDVLCNE----NNMLKNENSiiknehNMSRNENENLK 330
Cdd:pfam09728  29 ELLEEMKRLQKDLKKLKKKQDQLQKekdQLQSELSKAILAKSKLEKLCRElqkqNKKLKEESK------KLAKEEEEKRK 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 398366301  331 LENKRFHAeyirMIEDIENT----KRKEQEQRDEIEQLKKKIRSLEE 373
Cdd:pfam09728 103 ELSEKFQS----TLKDIQDKmeekSEKNNKLREENEELREKLKSLIE 145
 
Name Accession Description Interval E-value
bZIP_1 pfam00170
bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper ...
 223-278 2.56e-09

bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper region.


Pssm-ID: 395118 [Multi-domain]  Cd Length: 60  Bit Score: 52.77  E-value: 2.56e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301  223 RNTRRAAQNRTAQKAFRQRKEKYIKNLEQKSKIFD----DLLAENNNFKSLNDSLRNDNN 278
Cdd:pfam00170   1 KREKRKQSNREAARRSRQRKQAYIEELERRVKALEgenkTLRSELEELKKEVEKLKSKNK 60
bZIP_YAP cd14688
Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a ...
 223-280 3.53e-09

Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed predominantly of AP-1-like transcription factors including Saccharomyces cerevisiae YAPs, Schizosaccharomyces pombe PAP1, and similar proteins. Members of this subfamily belong to the Basic leucine zipper (bZIP) family of transcription factors. The YAP subfamily is composed of eight members (YAP1-8) which may all be involved in stress responses. YAP1 is the major oxidative stress regulator and is also involved in iron metabolism (like YAP5) and detoxification of arsenic (like YAP8). YAP2 is involved in cadmium stress responses while YAP4 and YAP6 play roles in osmotic stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269836 [Multi-domain]  Cd Length: 63  Bit Score: 52.72  E-value: 3.53e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366301 223 RNTRRAAQNRTAQKAFRQRKEKYIKNLEQK----SKIFDDLLAENNNFKSLNDSLRNDNNIL 280
Cdd:cd14688    2 PKERRRAQNREAQRAFRERKKERIKELEQRvaelEEELAELEEELQELRAELRELESELQSL 63
BRLZ smart00338
basic region leucin zipper;
220-278 1.54e-05

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 42.17  E-value: 1.54e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366301   220 KTLRNTRRAAQNRTAQKAFRQRKEKYIKNLEQKSKIF----DDLLAENNNFKSLNDSLRNDNN 278
Cdd:smart00338   2 EDEKRRRRRERNREAARRSRERKKAEIEELERKVEQLeaenERLKKEIERLRRELEKLKSELE 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 209-379 1.01e-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: 44.66  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301   209 DKDTQLISSSGKTLRNTRRAAQNRTAQkaFRQRKEKYIKNLEQKSKIFDDLLAENNNFKSLNDSLRNDNNILIAQHEAIR 288
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEE--LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301   289 NAITMLRSEYDVLCNENNMLKNENSIIKNEHNMSRNENENL---------KLENKRFH------AEYIRMIEDI----EN 349
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeieellkKLEEAELKelqaelEELEEELEELqeelER 458

                          170       180       190
                   ....*....|....*....|....*....|
gi 398366301   350 TKRKEQEQRDEIEQLKKKIRSLEEIVGRHS 379
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAERELAQLQ 488
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 226-277 1.07e-04

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 39.45  E-value: 1.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 398366301 226 RRAAQNRTAQKAFRQRKEKYIKNLEQKskiFDDLLAENNNFKSLNDSLRNDN 277
Cdd:cd14686    3 RRRERNREAARRSRERKKERIEELEEE---VEELEEENEELKAELEELRAEV 51
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 222-374 3.13e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301   222 LRNTRRAAQNRTAQKAFRQR----KEKYIKNLEQKSKIFDDLLAENN-NFKSLNDSLRN---DNNILIAQHEAIRNAITM 293
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERriaaTERRLEDLEEQIEELSEDIESLAaEIEELEELIEElesELEALLNERASLEEALAL 891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301   294 LRSEYDVLCNENNMLKNENSIIKNEHNMSRNENENLKLE-----------NKRFHAEYIRMIEDIENTKRK----EQEQR 358
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRleglevridnlQERLSEEYSLTLEEAEALENKieddEEEAR 971

                          170
                   ....*....|....*.
gi 398366301   359 DEIEQLKKKIRSLEEI 374
Cdd:TIGR02168  972 RRLKRLENKIKELGPV 987
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 232-375 1.16e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301 232 RTAQKAFRQRKEKYIKNLEQKSKIFDDLLAENNNFKSLNDSLRNDNNILIAQHEAIRNAITMLRSEYDVLCNENNMLKNE 311
Cdd:COG1196  210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366301 312 NSIIKNEHNMSRNENENLKLENKRFHAEYIRMIEDIENTKRKEQEQRDEIEQLKKKIRSLEEIV 375
Cdd:COG1196  290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 244-373 1.57e-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: 40.77  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301  244 KYIKNLEQKSKIFDDLLAENNNFKSLNDSLRNDNNILIAQHEAIRNAITMLRSE-----------------YDVLCNENN 306
Cdd:TIGR04523 142 KFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKllklelllsnlkkkiqkNKSLESQIS 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366301  307 MLKNENSIIKNEHNMSRNENENLKLENKRFHAEYIRMIEDIENTKRKEQEQRDEIEQLKKKIRSLEE 373
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK 288
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 271-373 1.71e-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: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301   271 DSLRNDNNILIAQHEAIRNAITMLRSEYDVLCNENNMLKNENSIIKNEHNMSRNENENLKlenkrfhaEYIRMIED-IEN 349
Cdd:TIGR02169  684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE--------EDLSSLEQeIEN 755

                           90       100
                   ....*....|....*....|....
gi 398366301   350 TKRKEQEQRDEIEQLKKKIRSLEE 373
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEE 779
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-374 2.05e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301 236 KAFRQRKEKYIKNLEQKSKIfDDLLAENNnfKSLNDSLRNDNNILIAQHEaIRNAITMLRSEYDVLcnennmlknensii 315
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENI-EELIKEKE--KELEEVLREINEISSELPE-LREELEKLEKEVKEL-------------- 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366301 316 kNEHnmsRNENENLKLENKRFHAEYIRMIEDIENTKRKEQEQRDEIEQLKKKIRSLEEI 374
Cdd:PRK03918 234 -EEL---KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL 288
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 258-373 2.14e-03

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: 39.55  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301  258 DLLAENNNFKSLNDSLRNDNNILIA---QHEAIRNAITMLRSEYDVLCNE----NNMLKNENSiiknehNMSRNENENLK 330
Cdd:pfam09728  29 ELLEEMKRLQKDLKKLKKKQDQLQKekdQLQSELSKAILAKSKLEKLCRElqkqNKKLKEESK------KLAKEEEEKRK 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 398366301  331 LENKRFHAeyirMIEDIENT----KRKEQEQRDEIEQLKKKIRSLEE 373
Cdd:pfam09728 103 ELSEKFQS----TLKDIQDKmeekSEKNNKLREENEELREKLKSLIE 145
bZIP_HY5-like cd14704
Basic leucine zipper (bZIP) domain of Plant Elongated/Long Hypocotyl5 (HY5)-like transcription ...
 226-277 4.95e-03

Basic leucine zipper (bZIP) domain of Plant Elongated/Long Hypocotyl5 (HY5)-like transcription factors and similar proteins: a DNA-binding and dimerization domain; This subfamily is predominantly composed of plant Basic leucine zipper (bZIP) transcription factors with similarity to Solanum lycopersicum and Arabidopsis thaliana HY5. Also included are the Dictyostelium discoideum bZIP transcription factors E and F. HY5 plays an important role in seedling development and is a positive regulator of photomorphogenesis. Plants with decreased levels of HY5 show defects in light responses including inhibited photomorphogenesis, loss of alkaloid organization, and reduced carotenoid accumulation. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269852 [Multi-domain]  Cd Length: 52  Bit Score: 34.86  E-value: 4.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 398366301 226 RRAAQNRTAQKAFRQRKEKYIKNLEQKSKifdDLLAENNNFKSLNDSLRNDN 277
Cdd:cd14704    3 RRLLRNRESAQLSRQRKKEYLSELEAKCR---ELEAENAELEARVELLQAEN 51
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
 231-275 5.09e-03

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar proteins: a DNA-binding and dimerization domain; ATF-2 is a sequence-specific DNA-binding protein that belongs to the Basic leucine zipper (bZIP) family of transcription factors. In response to stress, it activates a variety of genes including cyclin A, cyclin D, and c-Jun. ATF-2 also plays a role in the DNA damage response that is independent of its transcriptional activity. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269835 [Multi-domain]  Cd Length: 61  Bit Score: 35.20  E-value: 5.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 398366301 231 NRTAQKAFRQRKEKYIKNLEQKskiFDDLLAENNNFKSLNDSLRN 275
Cdd:cd14687    9 NRIAASKCRQRKKQWVQQLEEK---VRKLESENKALKAEVDKLRE 50
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
239-377 5.60e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 5.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301 239 RQRKEKYIK---NLEQKSKIFDDLLAENNNFKSLNDSLRNdnniLIAQHEAIRNAITMLRSEYDVLCNENNMLKNENSII 315
Cdd:PRK03918 144 DESREKVVRqilGLDDYENAYKNLGEVIKEIKRRIERLEK----FIKRTENIEELIKEKEKELEEVLREINEISSELPEL 219

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366301 316 KNEHNMSRNENENLKlENKRFHAEYIRMIEDIENTKRKEQEQ----RDEIEQLKKKIRSLEEIVGR 377
Cdd:PRK03918 220 REELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKirelEERIEELKKEIEELEEKVKE 284
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
240-374 8.41e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 8.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301 240 QRKEKYIKNLEQK-SKIFDDLLAENNNFkslndslrndnniliaqhEAIRNAITMLRSEYDVLCNENnmLKNENSIIKNE 318
Cdd:PRK03918 615 EREEKELKKLEEElDKAFEELAETEKRL------------------EELRKELEELEKKYSEEEYEE--LREEYLELSRE 674

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 398366301 319 HNMSRNENEnlKLENKRfhAEYIRMIEDIENTKRKEQEQRDEIEQLKKKIRSLEEI 374
Cdd:PRK03918 675 LAGLRAELE--ELEKRR--EEIKKTLEKLKEELEEREKAKKELEKLEKALERVEEL 726
46 PHA02562
endonuclease subunit; Provisional
 243-371 9.02e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.07  E-value: 9.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366301 243 EKYIKNLEQKSK--------IFDDLLAENNNFKSLNDSLRNDNNILIAQHEAIRNAITMLRSEYdvlcnenNMLKNENSI 314
Cdd:PHA02562 201 NKNIEEQRKKNGeniarkqnKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA-------AKIKSKIEQ 273

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366301 315 IKNEHNMSRN------------ENENLKLENKRFHAEYIRMIEDIENTKRKEQEQRDEIEQLKKKIRSL 371
Cdd:PHA02562 274 FQKVIKMYEKggvcptctqqisEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLEL 342
 
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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