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Conserved domains on  [gi|765553876|gb|KJE94497|]
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TATA box binding protein (TBP)-associated factor [Capsaspora owczarzaki ATCC 30864]

Protein Classification

AAA family ATPase( domain architecture ID 10591166)

AAA family ATPase similar to Bacillus subtilis tunicamycin resistance protein (TmrB), an ATP-binding membrane protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAA_18 pfam13238
AAA domain;
7-121 3.75e-33

AAA domain;


:

Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 114.06  E-value: 3.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765553876    7 ILITGTPGVGKTTLCELVSAATGYpHYNVSQMAKDGNMLDGWDEEYQTH----------LLDELEP---LVHPGGAIVDY 73
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGF-GDNVRDLALENGLVLGDDPETRESkrldedkldrLLDLLEEnaaLEEGGNLIIDG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 765553876   74 HGCELFPKRWFDLV-VVLCADNTVLYDRLSARGYTGKKLSDNVESEIMQ 121
Cdd:pfam13238  80 HLAELEPERAKDLVgIVLRASPEELLERLEKRGYEEAKIKENEEAEILG 128
 
Name Accession Description Interval E-value
AAA_18 pfam13238
AAA domain;
7-121 3.75e-33

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 114.06  E-value: 3.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765553876    7 ILITGTPGVGKTTLCELVSAATGYpHYNVSQMAKDGNMLDGWDEEYQTH----------LLDELEP---LVHPGGAIVDY 73
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGF-GDNVRDLALENGLVLGDDPETRESkrldedkldrLLDLLEEnaaLEEGGNLIIDG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 765553876   74 HGCELFPKRWFDLV-VVLCADNTVLYDRLSARGYTGKKLSDNVESEIMQ 121
Cdd:pfam13238  80 HLAELEPERAKDLVgIVLRASPEELLERLEKRGYEEAKIKENEEAEILG 128
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
7-158 1.63e-31

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


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 111.06  E-value: 1.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765553876   7 ILITGTPGVGKTTLCELVSAATGYPHYNVSQMAKDGNMLDGWDEEYQTHLLD------ELEPLVhPGGAIVDYHGCELFP 80
Cdd:COG1936    3 IAITGTPGTGKTTVAKLLAERLGLEVIHLNDLVKEEGLYTEVDEERDSLVVDedalaeELEELK-EGDVIIEGHLAHLVD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 765553876  81 krwFDLVVVLCADNTVLYDRLSARGYTGKKLSDNVESEIMQVILQEAHESYDAEIILHLenDTTEQ-MEQNVQTISEWI 158
Cdd:COG1936   82 ---VDRVIVLRCNPEVLEERLEERGYSEEKIRENVEAEALDVILSEAVERFGEEKVYEI--DTTGRtPEEVADEILAII 155
PRK03839 PRK03839
putative kinase; Provisional
 7-151 1.86e-19

putative kinase; Provisional


Pssm-ID: 179660  Cd Length: 180  Bit Score: 80.53  E-value: 1.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765553876   7 ILITGTPGVGKTTLCELVSAATGYPHYNVSQMAKDGNMLDGWDEEYQTHLlDELEPLVHP----GGAIVDYHGCELFPKr 82
Cdd:PRK03839   3 IAITGTPGVGKTTVSKLLAEKLGYEYVDLTEFALKKGIGEEKDDEMEIDF-DKLAYFIEEefkeKNVVLDGHLSHLLPV- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 765553876  83 wfDLVVVLCADNTVLYDRLSARGYTGKKLSDNVESEIMQVILQEAHESYDAEIilhlENDTTEQMEQNV 151
Cdd:PRK03839  81 --DYVIVLRAHPKIIKERLKERGYSKKKILENVEAELVDVCLCEALEEKEKVI----EVDTTGKTPEEV 143
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 2-35 4.79e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 38.67  E-value: 4.79e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 765553876   2 RSQPSILITGTPGVGKTTLCELVSAATGYPHYNV 35
Cdd:cd00009   17 PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPF 50
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 3-35 3.14e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.20  E-value: 3.14e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 765553876     3 SQPSILITGTPGVGKTTLCELVSAATGYPHYNV 35
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV 33
 
Name Accession Description Interval E-value
AAA_18 pfam13238
AAA domain;
7-121 3.75e-33

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 114.06  E-value: 3.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765553876    7 ILITGTPGVGKTTLCELVSAATGYpHYNVSQMAKDGNMLDGWDEEYQTH----------LLDELEP---LVHPGGAIVDY 73
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGF-GDNVRDLALENGLVLGDDPETRESkrldedkldrLLDLLEEnaaLEEGGNLIIDG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 765553876   74 HGCELFPKRWFDLV-VVLCADNTVLYDRLSARGYTGKKLSDNVESEIMQ 121
Cdd:pfam13238  80 HLAELEPERAKDLVgIVLRASPEELLERLEKRGYEEAKIKENEEAEILG 128
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
7-158 1.63e-31

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


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 111.06  E-value: 1.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765553876   7 ILITGTPGVGKTTLCELVSAATGYPHYNVSQMAKDGNMLDGWDEEYQTHLLD------ELEPLVhPGGAIVDYHGCELFP 80
Cdd:COG1936    3 IAITGTPGTGKTTVAKLLAERLGLEVIHLNDLVKEEGLYTEVDEERDSLVVDedalaeELEELK-EGDVIIEGHLAHLVD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 765553876  81 krwFDLVVVLCADNTVLYDRLSARGYTGKKLSDNVESEIMQVILQEAHESYDAEIILHLenDTTEQ-MEQNVQTISEWI 158
Cdd:COG1936   82 ---VDRVIVLRCNPEVLEERLEERGYSEEKIRENVEAEALDVILSEAVERFGEEKVYEI--DTTGRtPEEVADEILAII 155
PRK03839 PRK03839
putative kinase; Provisional
 7-151 1.86e-19

putative kinase; Provisional


Pssm-ID: 179660  Cd Length: 180  Bit Score: 80.53  E-value: 1.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765553876   7 ILITGTPGVGKTTLCELVSAATGYPHYNVSQMAKDGNMLDGWDEEYQTHLlDELEPLVHP----GGAIVDYHGCELFPKr 82
Cdd:PRK03839   3 IAITGTPGVGKTTVSKLLAEKLGYEYVDLTEFALKKGIGEEKDDEMEIDF-DKLAYFIEEefkeKNVVLDGHLSHLLPV- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 765553876  83 wfDLVVVLCADNTVLYDRLSARGYTGKKLSDNVESEIMQVILQEAHESYDAEIilhlENDTTEQMEQNV 151
Cdd:PRK03839  81 --DYVIVLRAHPKIIKERLKERGYSKKKILENVEAELVDVCLCEALEEKEKVI----EVDTTGKTPEEV 143
AAA_17 pfam13207
AAA domain;
10-105 1.99e-07

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 47.62  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765553876   10 TGTPGVGKTTLCELVSAATGYPHYNVS----QMAKDGNMLDGWDE------EYQTHLLDELEPLV----HPGGAIVDYHG 75
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFPHISAGdllrEEAKERGLVEDRDEmrklplEPQKELQKLAAERIaeeaGEGGVIVDGHP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 765553876   76 C--------ELFPKRWF-----DLVVVL-CADNTVLYDRLSARG 105
Cdd:pfam13207  81 RiktpagylPGLPVEVLrelkpDAIILLeADPEEILERRLKDRT 124
PRK04182 PRK04182
cytidylate kinase; Provisional
 7-44 3.52e-05

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 42.10  E-value: 3.52e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 765553876   7 ILITGTPGVGKTTLCELVSAATGYPHYNVS----QMAKDGNM 44
Cdd:PRK04182   3 ITISGPPGSGKTTVARLLAEKLGLKHVSAGeifrELAKERGM 44
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 7-36 2.42e-04

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 39.11  E-value: 2.42e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 765553876    7 ILITGTPGVGKTTLCELVSAATGYPHYNVS 36
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEIS 30
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 5-36 2.86e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 40.07  E-value: 2.86e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 765553876   5 PSILITGTPGVGKTTLCELVSAATGYPHYNVS 36
Cdd:PRK13342  37 SSMILWGPPGTGKTTLARIIAGATDAPFEALS 68
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 2-35 4.79e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 38.67  E-value: 4.79e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 765553876   2 RSQPSILITGTPGVGKTTLCELVSAATGYPHYNV 35
Cdd:cd00009   17 PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPF 50
PRK06217 PRK06217
hypothetical protein; Validated
 7-104 8.34e-04

hypothetical protein; Validated


Pssm-ID: 168472  Cd Length: 183  Bit Score: 38.11  E-value: 8.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765553876   7 ILITGTPGVGKTTLCELVSAATGYPHYNVSQ---MAKDGNMLDGWDEEYQTHLLdeLEPLVHPGGAIV----DYHGCELF 79
Cdd:PRK06217   4 IHITGASGSGTTTLGAALAERLDIPHLDTDDyfwLPTDPPFTTKRPPEERLRLL--LEDLRPREGWVLsgsaLGWGDPLE 81

                         90       100
                 ....*....|....*....|....*
gi 765553876  80 PKrwFDLVVVLCADNTVLYDRLSAR 104
Cdd:PRK06217  82 PL--FDLVVFLTIPPELRLERLRLR 104
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 7-107 9.68e-04

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 37.99  E-value: 9.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765553876   7 ILITGTPGVGKTTLCELVSAATGYPHYNVsqmakdGNMLdgwDEE--YQTHLLDELEPLVHPGGAIVD------------ 72
Cdd:cd01428    2 ILLLGPPGSGKGTQAERLAKKYGLPHIST------GDLL---REEiaSGTELGKKAKEYIDSGKLVPDeivikllkerlk 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 765553876  73 ----YHGCEL--FP------KRWF---------DLVVVLCADNTVLYDRLSARGYT 107
Cdd:cd01428   73 kpdcKKGFILdgFPrtvdqaEALDelldegikpDKVIELDVPDEVLIERILGRRIC 128
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 7-104 1.23e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 37.23  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765553876   7 ILITGTPGVGKTTLCELVSAATGYPHY---------NVSQMAK----DGNMLDGWDEEYQTHLLDELepLVHPGGAIVDy 73
Cdd:cd02021    2 IVVMGVSGSGKSTVGKALAERLGAPFIdgddlhppaNIAKMAAgiplNDEDRWPWLQALTDALLAKL--ASAGEGVVVA- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 765553876  74 hgCELFPKRWFDLV-----------VVLCADNTVLYDRLSAR 104
Cdd:cd02021   79 --CSALKRIYRDILrggaanprvrfVHLDGPREVLAERLAAR 118
AAA_28 pfam13521
AAA domain;
7-32 1.24e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 37.24  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|....*.
gi 765553876    7 ILITGTPGVGKTTLCELVSAATGYPH 32
Cdd:pfam13521   2 IVITGGPSTGKTTLAEALAARFGYPV 27
RecA-like_Thep1 cd19482
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the ...
 7-24 2.26e-03

RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the THEP1 family ATPase domain. It includes nucleoside-triphosphatase THEP 1 from Aquifex aeolicus (aaTHEP1) a nucleoside-phosphatase, with activity towards ATP, GTP, CTP, TTP and UTP; and which may hydrolyze nucleoside diphosphates with lower efficiency. The catalytic function of aaTHEP1 remains unclear, it may be a DNA/RNA modifying enzyme. Human THEP1 (hsTHEP1) may have a general function in many human tissues, as it is widely expressed in most examined tissues (such as in brain, heart, lymph node, skin, pancreas); it is especially highly expressed in embryonic and various tumor tissues. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410890 [Multi-domain]  Cd Length: 164  Bit Score: 36.81  E-value: 2.26e-03
                         10
                 ....*....|....*...
gi 765553876   7 ILITGTPGVGKTTLCELV 24
Cdd:cd19482    1 IFITGPPGVGKTTLVLKV 18
COG3911 COG3911
Predicted ATPase [General function prediction only];
7-45 2.57e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443117  Cd Length: 180  Bit Score: 36.72  E-value: 2.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 765553876   7 ILITGTPGVGKTTLCELVSAAtGYPHYN-VS------QMAKDGNML 45
Cdd:COG3911    6 IVITGGPGSGKTTLLNALARR-GYACVPeAGreiireQQAIGGDAL 50
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 5-36 2.72e-03

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 37.34  E-value: 2.72e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 765553876   5 PSILITGTPGVGKTTLCELVSAATGYPHYNVS 36
Cdd:COG2256   50 SSMILWGPPGTGKTTLARLIANATDAEFVALS 81
NTPase_1 pfam03266
NTPase; This domain is found across all species from bacteria to human, and the function was ...
 7-27 3.12e-03

NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.


Pssm-ID: 460869  Cd Length: 168  Bit Score: 36.45  E-value: 3.12e-03
                          10        20
                  ....*....|....*....|.
gi 765553876    7 ILITGTPGVGKTTLCELVSAA 27
Cdd:pfam03266   2 IFITGPPGVGKTTLVLKVAEL 22
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 3-35 3.14e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.20  E-value: 3.14e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 765553876     3 SQPSILITGTPGVGKTTLCELVSAATGYPHYNV 35
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV 33
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
7-35 3.41e-03

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 36.42  E-value: 3.41e-03
                         10        20
                 ....*....|....*....|....*....
gi 765553876   7 ILITGTPGVGKTTLCELVSAATGYPHYNV 35
Cdd:COG1618    3 IFITGRPGVGKTTLLLKVVEELRDEGLRV 31
PRK13695 PRK13695
NTPase;
7-21 5.10e-03

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 35.66  E-value: 5.10e-03
                         10
                 ....*....|....*
gi 765553876   7 ILITGTPGVGKTTLC 21
Cdd:PRK13695   3 IGITGPPGVGKTTLV 17
 
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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