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Conserved domains on  [gi|429836851|ref|NP_001258863|]
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thymidine kinase 2 isoform 5 [Homo sapiens]

Protein Classification

deoxynucleoside kinase( domain architecture ID 10484182)

deoxynucleoside kinase catalyzes the phosphorylation of deoxyribonucleosides to yield the corresponding monophosphates

CATH:  3.40.50.300
EC:  2.7.1.-
Gene Ontology:  GO:0019136|GO:0005524
SCOP:  4004030

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
4-211 1.81e-82

Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2.7.1.74, guanosine EC:2.7.1.113, adenosine EC:2.7.1.76 and thymidine kinase EC:2.7.1.21 (which also phosphorylates deoxyuridine and deoxycytosine.) These enzymes catalyze the production of deoxynucleotide 5'-monophosphate from a deoxynucleoside. Using ATP and yielding ADP in the process.


:

Pssm-ID: 396326  Cd Length: 201  Bit Score: 243.76  E-value: 1.81e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851    4 ICVEGNIASGKTTCLEFFSNATDVEVLTEPVSKWRNvrghNPLGLMYHDASRWGLTLQTYVQLTMLDRHTRP-QVSSVRL 82
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEPVDRWTN----PYLDKFYKDPSRWSFALQTYFLNSRFKQQLEAfFTGQVVI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851   83 MERSIHSARYIFVENLYRSGKMPEVDYVVLSEWFDWILRNMDvSVDLIVYLRTNPETCYQRLKKRCREEEKVIPLEYLEA 162
Cdd:pfam01712  77 LERSIYSDRYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFP-KPDLIIYLKTSPETCLERIKKRGRTEEQNISLDYLER 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 429836851  163 IHHLHEEWLIKGSLFpmaaPVLVIEADhhmERMLELFEQNRDRILTPEN 211
Cdd:pfam01712 156 LHEKYEAWLKKLNLS----PVLVIDGD---ELDFVFFEEDREDVMNEVN 197
 
Name Accession Description Interval E-value
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
4-211 1.81e-82

Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2.7.1.74, guanosine EC:2.7.1.113, adenosine EC:2.7.1.76 and thymidine kinase EC:2.7.1.21 (which also phosphorylates deoxyuridine and deoxycytosine.) These enzymes catalyze the production of deoxynucleotide 5'-monophosphate from a deoxynucleoside. Using ATP and yielding ADP in the process.


Pssm-ID: 396326  Cd Length: 201  Bit Score: 243.76  E-value: 1.81e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851    4 ICVEGNIASGKTTCLEFFSNATDVEVLTEPVSKWRNvrghNPLGLMYHDASRWGLTLQTYVQLTMLDRHTRP-QVSSVRL 82
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEPVDRWTN----PYLDKFYKDPSRWSFALQTYFLNSRFKQQLEAfFTGQVVI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851   83 MERSIHSARYIFVENLYRSGKMPEVDYVVLSEWFDWILRNMDvSVDLIVYLRTNPETCYQRLKKRCREEEKVIPLEYLEA 162
Cdd:pfam01712  77 LERSIYSDRYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFP-KPDLIIYLKTSPETCLERIKKRGRTEEQNISLDYLER 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 429836851  163 IHHLHEEWLIKGSLFpmaaPVLVIEADhhmERMLELFEQNRDRILTPEN 211
Cdd:pfam01712 156 LHEKYEAWLKKLNLS----PVLVIDGD---ELDFVFFEEDREDVMNEVN 197
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
4-190 7.23e-67

Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to yield corresponding monophosphates (dNMPs). This family consists of various deoxynucleoside kinases including deoxyribo- cytidine (EC 2.7.1.74), guanosine (EC 2.7.1.113), adenosine (EC 2.7.1.76), and thymidine (EC 2.7.1.21) kinases. They are key enzymes in the salvage of deoxyribonucleosides originating from extra- or intracellular breakdown of DNA.


Pssm-ID: 238836  Cd Length: 193  Bit Score: 204.00  E-value: 7.23e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851   4 ICVEGNIASGKTTCLEFFSNATDVEVLTEPVSkwRNVRGHNPLGLMYHDASRWGLTLQTYVQLTMLDRHTRPQVSS---- 79
Cdd:cd01673    2 IVVEGNIGAGKSTLAKELAEHLGYEVVPEPVE--PDVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDALEHLstgq 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851  80 VRLMERSIHSARYIFVENLYRSGKMPeVDYVVLSEWFDWILRNmDVSVDLIVYLRTNPETCYQRLKKRCREEEKVIPLEY 159
Cdd:cd01673   80 GVILERSIFSDRVFAEANLKEGGIMK-TEYDLYNELFDNLIPE-LLPPDLVIYLDASPETCLKRIKKRGRPEEQGIPLDY 157
                        170       180       190
                 ....*....|....*....|....*....|.
gi 429836851 160 LEAIHHLHEEWLIKgsLFPMAAPVLVIEADH 190
Cdd:cd01673  158 LEDLHEAYEKWFLP--QMYEKAPVLIIDANE 186
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
4-190 7.25e-39

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 132.99  E-value: 7.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851   4 ICVEGNIASGKTTCLEFFSNATDVEVLTEPVSkwrnvrgHNP-LGLMYHDASRWGLTLQTY------VQLTMLDRHTRPQ 76
Cdd:COG1428    6 IAVEGNIGAGKTTLARLLAEHLGAELLLEPVE-------DNPfLEDFYEDPKRWAFPLQLFfllsrfKQLKDLRQFGGNV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851  77 VSsvrlmERSIHSARyIFVENLYRSGKMPEVDYVVLSEWFDWILRNMdVSVDLIVYLRTNPETCYQRLKKRCREEEKVIP 156
Cdd:COG1428   79 VS-----DRSIYKDA-IFAKLLHEMGTLSDREFDLYRQLFDNLTEDL-PKPDLVIYLQASVDTLLERIKKRGRDYEQNID 151
                        170       180       190
                 ....*....|....*....|....*....|....
gi 429836851 157 LEYLEAIHHLHEEWLIKgslFPmAAPVLVIEADH 190
Cdd:COG1428  152 LDYLERLNEAYEEWFEH---YD-ASPVLIIDTDE 181
PHA03132 PHA03132
thymidine kinase; Provisional
2-164 8.22e-08

thymidine kinase; Provisional


Pssm-ID: 222997 [Multi-domain]  Cd Length: 580  Bit Score: 51.69  E-value: 8.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851   2 TSICVEGNIASGKTTCLEFFSNATDVEVLT--EPVSKWRNVRgHNPLGLMYHDASRWG---------------------L 58
Cdd:PHA03132 258 CFLFLEGVMGVGKTTLLNHMRGILGDNVLVfpEPMRYWTEVY-SNCLKEIYKLVKPGKhgktstsakllacqmkfatpfR 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851  59 TLQTYVQLTMLDRHTRPQVSSVR---LMERSIHSARYIFVENLYRSGkmpevdyvVLS-EWFDWILRNMDVSV-DLIVYL 133
Cdd:PHA03132 337 ALATRTRRLVQPESVRRPVAPLDnwvLFDRHLLSATVVFPLMHLRNG--------MLSfSHFIQLLSTFRAHEgDVIVLL 408
                        170       180       190
                 ....*....|....*....|....*....|.
gi 429836851 134 RTNPETCYQRLKKRCREEEKVIPLEYLEAIH 164
Cdd:PHA03132 409 KLNSEENLRRVKKRGRKEEKGINLTYLKELN 439
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
4-189 2.12e-03

dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 161676  Cd Length: 195  Bit Score: 37.73  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851    4 ICVEGNIASGKTTCLEFF-----SNATDVEVLTEPvskwrnvrGHNPLG-------LMYHDASrwgLTLQTYVQLTMLDR 71
Cdd:TIGR00041   6 IVIEGIDGAGKTTQANLLkkllqENGYDVLFTREP--------GGTPIGekirellLNENDEP---LTDKAEALLFAADR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851   72 --HTRPQVSSVRLMERSIHSARYIFVENLYRSGKmPEVDYVVLSEWFDWILRNMDvsvDLIVYLRTNPETCYQRLKKrcR 149
Cdd:TIGR00041  75 heHLEDKIKPALAEGKLVISDRYVFSSIAYQGGA-RGIDEDLVLELNEDALGDMP---DLTIYLDIDPEVALERLRK--R 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 429836851  150 EEEKVIPLEYLEAIHHLHEEWLikgSLFPMAAPVLVIEAD 189
Cdd:TIGR00041 149 GELDREEFEKLDFFEKVRQRYL---ELADKEKSIHVIDAT 185
 
Name Accession Description Interval E-value
dNK pfam01712
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ...
4-211 1.81e-82

Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2.7.1.74, guanosine EC:2.7.1.113, adenosine EC:2.7.1.76 and thymidine kinase EC:2.7.1.21 (which also phosphorylates deoxyuridine and deoxycytosine.) These enzymes catalyze the production of deoxynucleotide 5'-monophosphate from a deoxynucleoside. Using ATP and yielding ADP in the process.


Pssm-ID: 396326  Cd Length: 201  Bit Score: 243.76  E-value: 1.81e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851    4 ICVEGNIASGKTTCLEFFSNATDVEVLTEPVSKWRNvrghNPLGLMYHDASRWGLTLQTYVQLTMLDRHTRP-QVSSVRL 82
Cdd:pfam01712   1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEPVDRWTN----PYLDKFYKDPSRWSFALQTYFLNSRFKQQLEAfFTGQVVI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851   83 MERSIHSARYIFVENLYRSGKMPEVDYVVLSEWFDWILRNMDvSVDLIVYLRTNPETCYQRLKKRCREEEKVIPLEYLEA 162
Cdd:pfam01712  77 LERSIYSDRYIFAKMLYDKGTMSDEEYKTYKDLYDNMLLEFP-KPDLIIYLKTSPETCLERIKKRGRTEEQNISLDYLER 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 429836851  163 IHHLHEEWLIKGSLFpmaaPVLVIEADhhmERMLELFEQNRDRILTPEN 211
Cdd:pfam01712 156 LHEKYEAWLKKLNLS----PVLVIDGD---ELDFVFFEEDREDVMNEVN 197
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
4-190 7.23e-67

Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to yield corresponding monophosphates (dNMPs). This family consists of various deoxynucleoside kinases including deoxyribo- cytidine (EC 2.7.1.74), guanosine (EC 2.7.1.113), adenosine (EC 2.7.1.76), and thymidine (EC 2.7.1.21) kinases. They are key enzymes in the salvage of deoxyribonucleosides originating from extra- or intracellular breakdown of DNA.


Pssm-ID: 238836  Cd Length: 193  Bit Score: 204.00  E-value: 7.23e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851   4 ICVEGNIASGKTTCLEFFSNATDVEVLTEPVSkwRNVRGHNPLGLMYHDASRWGLTLQTYVQLTMLDRHTRPQVSS---- 79
Cdd:cd01673    2 IVVEGNIGAGKSTLAKELAEHLGYEVVPEPVE--PDVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDALEHLstgq 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851  80 VRLMERSIHSARYIFVENLYRSGKMPeVDYVVLSEWFDWILRNmDVSVDLIVYLRTNPETCYQRLKKRCREEEKVIPLEY 159
Cdd:cd01673   80 GVILERSIFSDRVFAEANLKEGGIMK-TEYDLYNELFDNLIPE-LLPPDLVIYLDASPETCLKRIKKRGRPEEQGIPLDY 157
                        170       180       190
                 ....*....|....*....|....*....|.
gi 429836851 160 LEAIHHLHEEWLIKgsLFPMAAPVLVIEADH 190
Cdd:cd01673  158 LEDLHEAYEKWFLP--QMYEKAPVLIIDANE 186
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
4-190 7.25e-39

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 132.99  E-value: 7.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851   4 ICVEGNIASGKTTCLEFFSNATDVEVLTEPVSkwrnvrgHNP-LGLMYHDASRWGLTLQTY------VQLTMLDRHTRPQ 76
Cdd:COG1428    6 IAVEGNIGAGKTTLARLLAEHLGAELLLEPVE-------DNPfLEDFYEDPKRWAFPLQLFfllsrfKQLKDLRQFGGNV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851  77 VSsvrlmERSIHSARyIFVENLYRSGKMPEVDYVVLSEWFDWILRNMdVSVDLIVYLRTNPETCYQRLKKRCREEEKVIP 156
Cdd:COG1428   79 VS-----DRSIYKDA-IFAKLLHEMGTLSDREFDLYRQLFDNLTEDL-PKPDLVIYLQASVDTLLERIKKRGRDYEQNID 151
                        170       180       190
                 ....*....|....*....|....*....|....
gi 429836851 157 LEYLEAIHHLHEEWLIKgslFPmAAPVLVIEADH 190
Cdd:COG1428  152 LDYLERLNEAYEEWFEH---YD-ASPVLIIDTDE 181
PHA03132 PHA03132
thymidine kinase; Provisional
2-164 8.22e-08

thymidine kinase; Provisional


Pssm-ID: 222997 [Multi-domain]  Cd Length: 580  Bit Score: 51.69  E-value: 8.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851   2 TSICVEGNIASGKTTCLEFFSNATDVEVLT--EPVSKWRNVRgHNPLGLMYHDASRWG---------------------L 58
Cdd:PHA03132 258 CFLFLEGVMGVGKTTLLNHMRGILGDNVLVfpEPMRYWTEVY-SNCLKEIYKLVKPGKhgktstsakllacqmkfatpfR 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851  59 TLQTYVQLTMLDRHTRPQVSSVR---LMERSIHSARYIFVENLYRSGkmpevdyvVLS-EWFDWILRNMDVSV-DLIVYL 133
Cdd:PHA03132 337 ALATRTRRLVQPESVRRPVAPLDnwvLFDRHLLSATVVFPLMHLRNG--------MLSfSHFIQLLSTFRAHEgDVIVLL 408
                        170       180       190
                 ....*....|....*....|....*....|.
gi 429836851 134 RTNPETCYQRLKKRCREEEKVIPLEYLEAIH 164
Cdd:PHA03132 409 KLNSEENLRRVKKRGRKEEKGINLTYLKELN 439
NDUO42 cd02030
NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar ...
4-178 1.19e-04

NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar to deoxyribonucleoside kinases (dNK). Members of this family have been identified as one of the subunits of NADH:Ubiquinone oxioreductase (complex I), a multi-protein complex located in the inner mitochondrial membrane. The main function of the complex is to transport electrons from NADH to ubiquinone, which is accompanied by the translocation of protons from the mitochondrial matrix to the inter membrane space.


Pssm-ID: 238988  Cd Length: 219  Bit Score: 41.57  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851   4 ICVEGNIASGKTTC---------LEFFSNAT--DVEVLTEPVSKWRNVRGHNP-LGLMYHDASRWG---LTLQTYVQLTM 68
Cdd:cd02030    2 ITVDGNIASGKGKLakelaeklgMKYFPEAGihYLDSTTGDGKPLDPAFNGNCsLEKFYDDPKSNDgnsYRLQSWMYSSR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851  69 LDR------HTRPQVSSVRLmERSIHSaRYIFVENLYRSGKMP--------EVDYVVLSEWFdwilrnmdvSVDLIVYLR 134
Cdd:cd02030   82 LLQysdaleHLLSTGQGVVL-ERSPFS-DFVFLEAMYKQGYIRkqcvdhynEVKGNTIPELL---------PPHLVIYLD 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 429836851 135 TNPETCYQRLKKRCREEEKVIPLEYLEAIhhlheEWLIKGSLFP 178
Cdd:cd02030  151 VPVPEVQKRIKKRGDPHEMKVTSAYLQDI-----ENAYKKTFLP 189
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
125-162 4.53e-04

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 39.41  E-value: 4.53e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 429836851 125 VSVDLIVYLRTNPETCYQRLKKRCREEEKVipLEYLEA 162
Cdd:COG1936   80 VDVDRVIVLRCNPEVLEERLEERGYSEEKI--RENVEA 115
DTMP_kinase TIGR00041
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ...
4-189 2.12e-03

dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 161676  Cd Length: 195  Bit Score: 37.73  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851    4 ICVEGNIASGKTTCLEFF-----SNATDVEVLTEPvskwrnvrGHNPLG-------LMYHDASrwgLTLQTYVQLTMLDR 71
Cdd:TIGR00041   6 IVIEGIDGAGKTTQANLLkkllqENGYDVLFTREP--------GGTPIGekirellLNENDEP---LTDKAEALLFAADR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429836851   72 --HTRPQVSSVRLMERSIHSARYIFVENLYRSGKmPEVDYVVLSEWFDWILRNMDvsvDLIVYLRTNPETCYQRLKKrcR 149
Cdd:TIGR00041  75 heHLEDKIKPALAEGKLVISDRYVFSSIAYQGGA-RGIDEDLVLELNEDALGDMP---DLTIYLDIDPEVALERLRK--R 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 429836851  150 EEEKVIPLEYLEAIHHLHEEWLikgSLFPMAAPVLVIEAD 189
Cdd:TIGR00041 149 GELDREEFEKLDFFEKVRQRYL---ELADKEKSIHVIDAT 185
 
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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