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Conserved domains on  [gi|767978122|ref|XP_011533553|]
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cytidine and dCMP deaminase domain-containing protein 1 isoform X5 [Homo sapiens]

Protein Classification

cytidine deaminase( domain architecture ID 10217272)

cytidine deaminase catalyzes the deamination of cytidine to uridine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 274-409 7.66e-39

Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.


:

Pssm-ID: 238613 [Multi-domain]  Cd Length: 131  Bit Score: 137.02  E-value: 7.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122 274 ARHCMVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGAMYFVGCGYNAFPVGSEYADFPhmddkqkDREIRKFRYIIH 353
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVH 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767978122 354 AEQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 409
Cdd:cd01286   71 AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
cytidine_deaminase-like super family cl00269
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 34-106 1.23e-09

Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine deaminases, nucleoside deaminases, deoxycytidylate deaminases and riboflavin deaminases. Also included are the apoBec family of mRNA editing enzymes. All members are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate.


The actual alignment was detected with superfamily member cd01286:

Pssm-ID: 444801 [Multi-domain]  Cd Length: 131  Bit Score: 56.13  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122  34 STD-KRQVkrtGLVVVKNMKIVGL----------HCSSED-----------------LHAGQIALI---KHGSRLKNCDL 82
Cdd:cd01286   15 STCpRRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRHGVSLEGATL 91

                         90       100
                 ....*....|....*....|....
gi 767978122  83 YFSRKPCSACLKMIVNAGVNRISY 106
Cdd:cd01286   92 YVTLFPCIECAKLIIQAGIKKVVY 115
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 274-409 7.66e-39

Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.


Pssm-ID: 238613 [Multi-domain]  Cd Length: 131  Bit Score: 137.02  E-value: 7.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122 274 ARHCMVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGAMYFVGCGYNAFPVGSEYADFPhmddkqkDREIRKFRYIIH 353
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVH 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767978122 354 AEQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 409
Cdd:cd01286   71 AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
278-397 5.25e-11

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 60.62  E-value: 5.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122 278 MVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGamyfvgcgYNAFPVGSEYADFP-HMDDKQKDREIR--KFRYIIHA 354
Cdd:COG2131   13 MEIAKLVALRSTCLRRQVGAVIVKDKRILA---TG--------YNGAPSGLPHCDEVgCLREKLGIPSGErgECCRTVHA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767978122 355 EQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIY 397
Cdd:COG2131   82 EQNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVV 124
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 34-106 1.23e-09

Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.


Pssm-ID: 238613 [Multi-domain]  Cd Length: 131  Bit Score: 56.13  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122  34 STD-KRQVkrtGLVVVKNMKIVGL----------HCSSED-----------------LHAGQIALI---KHGSRLKNCDL 82
Cdd:cd01286   15 STCpRRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRHGVSLEGATL 91

                         90       100
                 ....*....|....*....|....
gi 767978122  83 YFSRKPCSACLKMIVNAGVNRISY 106
Cdd:cd01286   92 YVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
34-119 5.09e-09

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 54.85  E-value: 5.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122  34 STD-KRQVkrtGLVVVKNMKIV---------GL-HC-------------SSED------LHAGQIALI---KHGSRLKNC 80
Cdd:COG2131   23 STClRRQV---GAVIVKDKRILatgyngapsGLpHCdevgclreklgipSGERgeccrtVHAEQNAILqaaRHGVSTEGA 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767978122  81 DLYFSRKPCSACLKMIVNAGVNRISY---WPADPEISLLTEA 119
Cdd:COG2131  100 TLYVTHFPCLECAKMIIQAGIKRVVYledYPDELAKELLKEA 141
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
278-399 1.21e-06

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 46.91  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122  278 MVQARLLAYRTEDHKTG-VGAVIWAEGKSRscdgtgamyfVGCGYNafpvgseyadfphmddkqkdREIRKFRYIIHAEQ 356
Cdd:pfam00383   6 MRLALKAAKRAYPYSNFpVGAVIVKKDGEI----------IATGYN--------------------GENAGYDPTIHAER 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767978122  357 NALTFRCQEIK--PEERSMIFVTKCPCDECVPLIKGAGIKQIYAG 399
Cdd:pfam00383  56 NAIRQAGKRGEgvRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 295-400 7.73e-06

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 45.90  E-value: 7.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122 295 VGAVIWAEGKsrscdgtgamyFVGCGYNAFPVGS----EYADFP-HMDDKQKDREIRKFRY-------IIHAEQNALTFR 362
Cdd:PHA02588  24 VGAVIEKNGR-----------IISTGYNGTPAGGvnccDHANEQgWLDDEGKLKKEHRPEHsawssknEIHAELNAILFA 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767978122 363 CQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAGD 400
Cdd:PHA02588  93 ARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCE 130
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
44-106 3.60e-05

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 42.67  E-value: 3.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767978122   44 GLVVVK-NMKIVGLHCSSED------LHAGQIALIK-----HGSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY 106
Cdd:pfam00383  25 GAVIVKkDGEIIATGYNGENagydptIHAERNAIRQagkrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 274-409 7.66e-39

Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.


Pssm-ID: 238613 [Multi-domain]  Cd Length: 131  Bit Score: 137.02  E-value: 7.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122 274 ARHCMVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGAMYFVGCGYNAFPVGSEYADFPhmddkqkDREIRKFRYIIH 353
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVH 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767978122 354 AEQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 409
Cdd:cd01286   71 AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
278-397 5.25e-11

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 60.62  E-value: 5.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122 278 MVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGamyfvgcgYNAFPVGSEYADFP-HMDDKQKDREIR--KFRYIIHA 354
Cdd:COG2131   13 MEIAKLVALRSTCLRRQVGAVIVKDKRILA---TG--------YNGAPSGLPHCDEVgCLREKLGIPSGErgECCRTVHA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767978122 355 EQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIY 397
Cdd:COG2131   82 EQNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVV 124
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 34-106 1.23e-09

Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase. The enzyme binds Zn++, which is required for catalytic activity. The activity of the enzyme is allosterically regulated by the ratio of dCTP to dTTP not only in eukaryotic cells but also in T-even phage-infected Escherichia coli, with dCTP acting as an activator and dTTP as an inhibitor.


Pssm-ID: 238613 [Multi-domain]  Cd Length: 131  Bit Score: 56.13  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122  34 STD-KRQVkrtGLVVVKNMKIVGL----------HCSSED-----------------LHAGQIALI---KHGSRLKNCDL 82
Cdd:cd01286   15 STCpRRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRHGVSLEGATL 91

                         90       100
                 ....*....|....*....|....
gi 767978122  83 YFSRKPCSACLKMIVNAGVNRISY 106
Cdd:cd01286   92 YVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
34-119 5.09e-09

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 54.85  E-value: 5.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122  34 STD-KRQVkrtGLVVVKNMKIV---------GL-HC-------------SSED------LHAGQIALI---KHGSRLKNC 80
Cdd:COG2131   23 STClRRQV---GAVIVKDKRILatgyngapsGLpHCdevgclreklgipSGERgeccrtVHAEQNAILqaaRHGVSTEGA 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767978122  81 DLYFSRKPCSACLKMIVNAGVNRISY---WPADPEISLLTEA 119
Cdd:COG2131  100 TLYVTHFPCLECAKMIIQAGIKRVVYledYPDELAKELLKEA 141
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
278-399 1.21e-06

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 46.91  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122  278 MVQARLLAYRTEDHKTG-VGAVIWAEGKSRscdgtgamyfVGCGYNafpvgseyadfphmddkqkdREIRKFRYIIHAEQ 356
Cdd:pfam00383   6 MRLALKAAKRAYPYSNFpVGAVIVKKDGEI----------IATGYN--------------------GENAGYDPTIHAER 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767978122  357 NALTFRCQEIK--PEERSMIFVTKCPCDECVPLIKGAGIKQIYAG 399
Cdd:pfam00383  56 NAIRQAGKRGEgvRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 295-400 7.73e-06

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 45.90  E-value: 7.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122 295 VGAVIWAEGKsrscdgtgamyFVGCGYNAFPVGS----EYADFP-HMDDKQKDREIRKFRY-------IIHAEQNALTFR 362
Cdd:PHA02588  24 VGAVIEKNGR-----------IISTGYNGTPAGGvnccDHANEQgWLDDEGKLKKEHRPEHsawssknEIHAELNAILFA 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767978122 363 CQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAGD 400
Cdd:PHA02588  93 ARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCE 130
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
44-106 3.60e-05

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 42.67  E-value: 3.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767978122   44 GLVVVK-NMKIVGLHCSSED------LHAGQIALIK-----HGSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY 106
Cdd:pfam00383  25 GAVIVKkDGEIIATGYNGENagydptIHAERNAIRQagkrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 344-396 2.91e-04

Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine deaminases, nucleoside deaminases, deoxycytidylate deaminases and riboflavin deaminases. Also included are the apoBec family of mRNA editing enzymes. All members are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate.


Pssm-ID: 238406 [Multi-domain]  Cd Length: 96  Bit Score: 39.84  E-value: 2.91e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767978122 344 EIRKFRYIIHAEQNALtFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQI 396
Cdd:cd00786   40 ENAAYSMCNHAERTAL-FNAGSEGDTKGQMLYVALSPCGACAQLIIELGIKDV 91
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 44-138 1.68e-03

Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD (Diaminohydroxyphosphoribosylaminopyrimidine deaminase) catalyzes the deamination of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, which is an intermediate step in the biosynthesis of riboflavin.The ribG gene of Bacillus subtilis and the ribD gene of E. coli are bifunctional and contain this deaminase domain and a reductase domain which catalyzes the subsequent reduction of the ribosyl side chain.


Pssm-ID: 238611 [Multi-domain]  Cd Length: 115  Bit Score: 37.98  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978122  44 GLVVVKNM-KIVGL--HCSSEDLHAGQIALIKHG-SRLKNCDLYFSRKPCS------ACLKMIVNAGVNRISYWPADPei 113
Cdd:cd01284   22 GCVIVDDDgEIVGEgyHRKAGGPHAEVNALASAGeKLARGATLYVTLEPCShhgktpPCVDAIIEAGIKRVVVGVRDP-- 99

                         90       100
                 ....*....|....*....|....*
gi 767978122 114 sllteassseDAKLDAKAVERLKSN 138
Cdd:cd01284  100 ----------NPLVAGKGAERLRAA 114
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 44-104 2.02e-03

Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine deaminases, nucleoside deaminases, deoxycytidylate deaminases and riboflavin deaminases. Also included are the apoBec family of mRNA editing enzymes. All members are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate.


Pssm-ID: 238406 [Multi-domain]  Cd Length: 96  Bit Score: 37.53  E-value: 2.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767978122  44 GLVVVKNMK--IVGLHCS------SEDLHAGQIALIKHGS--RLKNCDLYFSRKPCSACLKMIVNAGVNRI 104
Cdd:cd00786   21 GACLVNKKDggKVGRGCNienaaySMCNHAERTALFNAGSegDTKGQMLYVALSPCGACAQLIIELGIKDV 91
 
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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