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Conserved domains on  [gi|1227914501|ref|XP_021893607|]
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heat stress transcription factor A-1d [Carica papaya]

Protein Classification

heat shock factor family protein( domain architecture ID 10648050)

heat shock factor (HSF) family protein may act as a transcriptional factor

CATH:  1.10.10.10
Gene Ontology:  GO:0043565|GO:0003700
PubMed:  22044151|20945528|22033015|8689565|11344080
SCOP:  4000226

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HSF smart00415
heat shock factor;
38-130 1.70e-52

heat shock factor;


:

Pssm-ID: 214654  Cd Length: 105  Bit Score: 173.24  E-value: 1.70e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501   38 PPPFLSKTYDMVDDPATDGIVSWSSTNNSFVVWKPPEFARDLLPKHFKHNNFSSFVRQLNTYGFRKVDP----------- 106
Cdd:smart00415   2 PPPFLTKLYLLVEDPSTDKIISWSPSGKSFVIWDPEEFAKNLLPRYFKHNNFSSFVRQLNMYGFRKVDPefqgilynfts 81

                           90       100
                   ....*....|....*....|....
gi 1227914501  107 DRWEFANEGFLRGQKHLLRSITRR 130
Cdd:smart00415  82 DQWEFANPDFVRGQPELLRNIKRK 105
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 162-280 7.33e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 7.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501  162 LEEEVERLKRDKNVLMQELVRLRQQQQATDNQLQTMAQRLQGMEQRQQQMMSFLAKAVQSPGFLAQFVQQQnesNRRITE 241
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL---SKELTE 758

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1227914501  242 ANKKRRLKQEGIIEN-EHASAPDGQIVKYQPLMNEAAKAM 280
Cdd:TIGR02168  759 LEAEIEELEERLEEAeEELAEAEAEIEELEAQIEQLKEEL 798
 
Name Accession Description Interval E-value
HSF smart00415
heat shock factor;
38-130 1.70e-52

heat shock factor;


Pssm-ID: 214654  Cd Length: 105  Bit Score: 173.24  E-value: 1.70e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501   38 PPPFLSKTYDMVDDPATDGIVSWSSTNNSFVVWKPPEFARDLLPKHFKHNNFSSFVRQLNTYGFRKVDP----------- 106
Cdd:smart00415   2 PPPFLTKLYLLVEDPSTDKIISWSPSGKSFVIWDPEEFAKNLLPRYFKHNNFSSFVRQLNMYGFRKVDPefqgilynfts 81

                           90       100
                   ....*....|....*....|....
gi 1227914501  107 DRWEFANEGFLRGQKHLLRSITRR 130
Cdd:smart00415  82 DQWEFANPDFVRGQPELLRNIKRK 105
HSF_DNA-bind pfam00447
HSF-type DNA-binding;
41-130 4.13e-46

HSF-type DNA-binding;


Pssm-ID: 459813  Cd Length: 98  Bit Score: 156.19  E-value: 4.13e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501  41 FLSKTYDMVDDPATDGIVSWSSTNNSFVVWKPPEFARDLLPKHFKHNNFSSFVRQLNTYGFRKVDP--------DRWEFA 112
Cdd:pfam00447   1 FLRKLYRMLEDPETDDIISWSDDGDSFVILDPEEFAKEVLPKYFKHSNFSSFVRQLNMYGFHKVKDlsssksmgDSWEFR 80

                          90
                  ....*....|....*...
gi 1227914501 113 NEGFLRGQKHLLRSITRR 130
Cdd:pfam00447  81 HPNFRRGRPDLLKNIKRK 98
HSF1 COG5169
Heat shock transcription factor [Transcription];
30-131 3.67e-30

Heat shock transcription factor [Transcription];


Pssm-ID: 227497 [Multi-domain]  Cd Length: 282  Bit Score: 119.07  E-value: 3.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501  30 MAMQGANAPPP-FLSKTYDMVDDPATDGIVSWSSTNNSFVVWKPPEFARDLLPKHFKHNNFSSFVRQLNTYGFRKV---- 104
Cdd:COG5169     1 MSMSSRWSQPKeFVHKLYQILEEPEYYKLIQWSPDGRSFVILDPEEFTKVILPRYFKHGNFASFVRQLNKYGFHKVshks 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1227914501 105 ------DPDRWEFANEGFLRGQKHLLRSITRRK 131
Cdd:COG5169    81 gqrsyyNENVWEFGNKNFQLGMIELLKKIKRKK 113
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 162-280 7.33e-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: 45.82  E-value: 7.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501  162 LEEEVERLKRDKNVLMQELVRLRQQQQATDNQLQTMAQRLQGMEQRQQQMMSFLAKAVQSPGFLAQFVQQQnesNRRITE 241
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL---SKELTE 758

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1227914501  242 ANKKRRLKQEGIIEN-EHASAPDGQIVKYQPLMNEAAKAM 280
Cdd:TIGR02168  759 LEAEIEELEERLEEAeEELAEAEAEIEELEAQIEQLKEEL 798
DUF4175 pfam13779
Domain of unknown function (DUF4175);
163-280 7.09e-04

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 42.28  E-value: 7.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501 163 EEEVERLkrdknvlMQELvrlrqqQQATDNQLQTMAQRLQGMEQRQQQMMSFLAKAVqSPGFLAQFVQQQNESNRRITEA 242
Cdd:pfam13779 508 DEEIAKL-------MQEL------REALDDYMQALAEQAQQNPQDLQQPDDPNAQEM-TQQDLQRMLDRIEELARSGRRA 573

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1227914501 243 NKKRRLKQ-EGIIENEHASAPDGQivkYQPLMNEAAKAM 280
Cdd:pfam13779 574 EAQQMLSQlQQMLENLQAGQPQQQ---QQQGQSEMQQAM 609
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
162-245 1.56e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501 162 LEEEVERLKRDKNV---------LMQELVRLRQQQQATDNQLQTMAQRLQGMEQRQQQMMSFLAKAVQSPGfLAQFVQQQ 232
Cdd:COG3206   194 AEAALEEFRQKNGLvdlseeaklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQL 272

                          90
                  ....*....|...
gi 1227914501 233 NESNRRITEANKK 245
Cdd:COG3206   273 AELEAELAELSAR 285
bZIP_NFE2-like cd14720
Basic leucine zipper (bZIP) domain of Nuclear Factor, Erythroid-derived 2 (NFE2) and similar ...
 160-204 2.12e-03

Basic leucine zipper (bZIP) domain of Nuclear Factor, Erythroid-derived 2 (NFE2) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed of NFE2 and NFE2-like proteins including NFE2-like 1 or NFE2-related factor 1 (NFE2L1 or Nrf1), NFE2L2 (or Nrf2), and NFE2L3 (or Nrf3). These are Cap'n'Collar (CNC) Basic leucine zipper (bZIP) transcription factors that are defined by a conserved 43-amino acid region (called the CNC domain) located N-terminal to the bZIP DNA-binding domain. NFE2 functions in development; it is required for the proper development of platelets. The three Nrfs function in stress responses. Nrf2, the most extensively studied member of this subfamily, acts as a xenobiotic-activated receptor that regulates the adaptive response to oxidants and electrophiles. As the master regulator of the antioxidant defense pathway, it plays roles in the biology of inflammation, obesity, and cancer. Nrf1 is an essential protein that binds to the antioxidant response element (ARE) and is also involved in regulating oxidative stress. In addition, it also regulates genes involved in cell and tissue differentiation, inflammation, and hepatocyte homeostasis. 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: 269868 [Multi-domain]  Cd Length: 68  Bit Score: 36.90  E-value: 2.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1227914501 160 FGLEEEVERLKRDKNVLMQElvrlrqqQQATDNQLQTMAQRLQGM 204
Cdd:cd14720    30 VGLEDEVEQLQRQREKLLRE-------KAENAKSLREMKQKLNDL 67
 
Name Accession Description Interval E-value
HSF smart00415
heat shock factor;
38-130 1.70e-52

heat shock factor;


Pssm-ID: 214654  Cd Length: 105  Bit Score: 173.24  E-value: 1.70e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501   38 PPPFLSKTYDMVDDPATDGIVSWSSTNNSFVVWKPPEFARDLLPKHFKHNNFSSFVRQLNTYGFRKVDP----------- 106
Cdd:smart00415   2 PPPFLTKLYLLVEDPSTDKIISWSPSGKSFVIWDPEEFAKNLLPRYFKHNNFSSFVRQLNMYGFRKVDPefqgilynfts 81

                           90       100
                   ....*....|....*....|....
gi 1227914501  107 DRWEFANEGFLRGQKHLLRSITRR 130
Cdd:smart00415  82 DQWEFANPDFVRGQPELLRNIKRK 105
HSF_DNA-bind pfam00447
HSF-type DNA-binding;
41-130 4.13e-46

HSF-type DNA-binding;


Pssm-ID: 459813  Cd Length: 98  Bit Score: 156.19  E-value: 4.13e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501  41 FLSKTYDMVDDPATDGIVSWSSTNNSFVVWKPPEFARDLLPKHFKHNNFSSFVRQLNTYGFRKVDP--------DRWEFA 112
Cdd:pfam00447   1 FLRKLYRMLEDPETDDIISWSDDGDSFVILDPEEFAKEVLPKYFKHSNFSSFVRQLNMYGFHKVKDlsssksmgDSWEFR 80

                          90
                  ....*....|....*...
gi 1227914501 113 NEGFLRGQKHLLRSITRR 130
Cdd:pfam00447  81 HPNFRRGRPDLLKNIKRK 98
HSF1 COG5169
Heat shock transcription factor [Transcription];
30-131 3.67e-30

Heat shock transcription factor [Transcription];


Pssm-ID: 227497 [Multi-domain]  Cd Length: 282  Bit Score: 119.07  E-value: 3.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501  30 MAMQGANAPPP-FLSKTYDMVDDPATDGIVSWSSTNNSFVVWKPPEFARDLLPKHFKHNNFSSFVRQLNTYGFRKV---- 104
Cdd:COG5169     1 MSMSSRWSQPKeFVHKLYQILEEPEYYKLIQWSPDGRSFVILDPEEFTKVILPRYFKHGNFASFVRQLNKYGFHKVshks 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1227914501 105 ------DPDRWEFANEGFLRGQKHLLRSITRRK 131
Cdd:COG5169    81 gqrsyyNENVWEFGNKNFQLGMIELLKKIKRKK 113
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 162-280 7.33e-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: 45.82  E-value: 7.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501  162 LEEEVERLKRDKNVLMQELVRLRQQQQATDNQLQTMAQRLQGMEQRQQQMMSFLAKAVQSPGFLAQFVQQQnesNRRITE 241
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL---SKELTE 758

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1227914501  242 ANKKRRLKQEGIIEN-EHASAPDGQIVKYQPLMNEAAKAM 280
Cdd:TIGR02168  759 LEAEIEELEERLEEAeEELAEAEAEIEELEAQIEQLKEEL 798
DUF4175 pfam13779
Domain of unknown function (DUF4175);
163-280 7.09e-04

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 42.28  E-value: 7.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501 163 EEEVERLkrdknvlMQELvrlrqqQQATDNQLQTMAQRLQGMEQRQQQMMSFLAKAVqSPGFLAQFVQQQNESNRRITEA 242
Cdd:pfam13779 508 DEEIAKL-------MQEL------REALDDYMQALAEQAQQNPQDLQQPDDPNAQEM-TQQDLQRMLDRIEELARSGRRA 573

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1227914501 243 NKKRRLKQ-EGIIENEHASAPDGQivkYQPLMNEAAKAM 280
Cdd:pfam13779 574 EAQQMLSQlQQMLENLQAGQPQQQ---QQQGQSEMQQAM 609
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
162-245 1.56e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501 162 LEEEVERLKRDKNV---------LMQELVRLRQQQQATDNQLQTMAQRLQGMEQRQQQMMSFLAKAVQSPGfLAQFVQQQ 232
Cdd:COG3206   194 AEAALEEFRQKNGLvdlseeaklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQL 272

                          90
                  ....*....|...
gi 1227914501 233 NESNRRITEANKK 245
Cdd:COG3206   273 AELEAELAELSAR 285
bZIP_NFE2-like cd14720
Basic leucine zipper (bZIP) domain of Nuclear Factor, Erythroid-derived 2 (NFE2) and similar ...
 160-204 2.12e-03

Basic leucine zipper (bZIP) domain of Nuclear Factor, Erythroid-derived 2 (NFE2) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed of NFE2 and NFE2-like proteins including NFE2-like 1 or NFE2-related factor 1 (NFE2L1 or Nrf1), NFE2L2 (or Nrf2), and NFE2L3 (or Nrf3). These are Cap'n'Collar (CNC) Basic leucine zipper (bZIP) transcription factors that are defined by a conserved 43-amino acid region (called the CNC domain) located N-terminal to the bZIP DNA-binding domain. NFE2 functions in development; it is required for the proper development of platelets. The three Nrfs function in stress responses. Nrf2, the most extensively studied member of this subfamily, acts as a xenobiotic-activated receptor that regulates the adaptive response to oxidants and electrophiles. As the master regulator of the antioxidant defense pathway, it plays roles in the biology of inflammation, obesity, and cancer. Nrf1 is an essential protein that binds to the antioxidant response element (ARE) and is also involved in regulating oxidative stress. In addition, it also regulates genes involved in cell and tissue differentiation, inflammation, and hepatocyte homeostasis. 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: 269868 [Multi-domain]  Cd Length: 68  Bit Score: 36.90  E-value: 2.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1227914501 160 FGLEEEVERLKRDKNVLMQElvrlrqqQQATDNQLQTMAQRLQGM 204
Cdd:cd14720    30 VGLEDEVEQLQRQREKLLRE-------KAENAKSLREMKQKLNDL 67
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
162-251 2.91e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501 162 LEEEVERLKRDKNVLMQELVRLRQQQQATDNQLQTMAQRLQGMEQRQQQMMSFLAKAVQSpgfLAQFVQQQNESNRRITE 241
Cdd:COG4372    43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE---LESLQEEAEELQEELEE 119

                          90
                  ....*....|.
gi 1227914501 242 ANKKR-RLKQE 251
Cdd:COG4372   120 LQKERqDLEQQ 130
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
162-254 6.30e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 6.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501 162 LEEEVERLKRDKNVLMQELVRLRQQ-QQATDNQLQTMAQRLQGMEQRQQQMMSFLAKAVQSPGFLAqfvQQQNESNRRIT 240
Cdd:COG4717   161 LEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE---EELEQLENELE 237

                          90
                  ....*....|....
gi 1227914501 241 EANKKRRLKQEGII 254
Cdd:COG4717   238 AAALEERLKEARLL 251
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
162-251 9.58e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 9.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227914501  162 LEEEVERLKRDKNVLMQELVRLRQQQQATDNQLQTMAQRLQGMEQRQQQmMSFLAKAVQSPGFLAQFVQQQNESNRRITE 241
Cdd:COG4913    690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA-AEDLARLELRALLEERFAAALGDAVERELR 768

                           90
                   ....*....|
gi 1227914501  242 ANKKRRLKQE 251
Cdd:COG4913    769 ENLEERIDAL 778
 
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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