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Conserved domains on  [gi|119629222|gb|EAX08817|]
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cytidine and dCMP deaminase domain containing 1, isoform CRA_c [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 ...
 319-454 3.98e-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: 138.56  E-value: 3.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222 319 ARHCMVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGAMYFVGCGYNAFPVGSEYADFPhmddkqkDREIRKFRYIIH 398
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVH 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629222 399 AEQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 454
Cdd:cd01286   71 AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
cytidine_deaminase-like super family cl00269
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 79-151 7.18e-10

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: 56.90  E-value: 7.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222  79 STD-KRQVkrtGLVVVKNMKIVGL----------HCSSED-----------------LHAGQIALI---KHGSRLKNCDL 127
Cdd:cd01286   15 STCpRRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRHGVSLEGATL 91

                         90       100
                 ....*....|....*....|....
gi 119629222 128 YFSRKPCSACLKMIVNAGVNRISY 151
Cdd:cd01286   92 YVTLFPCIECAKLIIQAGIKKVVY 115
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 319-454 3.98e-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: 138.56  E-value: 3.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222 319 ARHCMVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGAMYFVGCGYNAFPVGSEYADFPhmddkqkDREIRKFRYIIH 398
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVH 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629222 399 AEQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 454
Cdd:cd01286   71 AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
323-442 3.40e-11

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 61.40  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222 323 MVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGamyfvgcgYNAFPVGSEYADFP-HMDDKQKDREIR--KFRYIIHA 399
Cdd:COG2131   13 MEIAKLVALRSTCLRRQVGAVIVKDKRILA---TG--------YNGAPSGLPHCDEVgCLREKLGIPSGErgECCRTVHA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 119629222 400 EQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIY 442
Cdd:COG2131   82 EQNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVV 124
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 79-151 7.18e-10

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: 56.90  E-value: 7.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222  79 STD-KRQVkrtGLVVVKNMKIVGL----------HCSSED-----------------LHAGQIALI---KHGSRLKNCDL 127
Cdd:cd01286   15 STCpRRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRHGVSLEGATL 91

                         90       100
                 ....*....|....*....|....
gi 119629222 128 YFSRKPCSACLKMIVNAGVNRISY 151
Cdd:cd01286   92 YVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
79-164 3.14e-09

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 55.62  E-value: 3.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222  79 STD-KRQVkrtGLVVVKNMKIV---------GL-HC-------------SSED------LHAGQIALI---KHGSRLKNC 125
Cdd:COG2131   23 STClRRQV---GAVIVKDKRILatgyngapsGLpHCdevgclreklgipSGERgeccrtVHAEQNAILqaaRHGVSTEGA 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 119629222 126 DLYFSRKPCSACLKMIVNAGVNRISY---WPADPEISLLTEA 164
Cdd:COG2131  100 TLYVTHFPCLECAKMIIQAGIKRVVYledYPDELAKELLKEA 141
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
323-444 8.57e-07

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 47.30  E-value: 8.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222  323 MVQARLLAYRTEDHKTG-VGAVIWAEGKSRscdgtgamyfVGCGYNafpvgseyadfphmddkqkdREIRKFRYIIHAEQ 401
Cdd:pfam00383   6 MRLALKAAKRAYPYSNFpVGAVIVKKDGEI----------IATGYN--------------------GENAGYDPTIHAER 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 119629222  402 NALTFRCQEIK--PEERSMIFVTKCPCDECVPLIKGAGIKQIYAG 444
Cdd:pfam00383  56 NAIRQAGKRGEgvRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 340-445 7.58e-06

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 46.29  E-value: 7.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222 340 VGAVIWAEGKsrscdgtgamyFVGCGYNAFPVGS----EYADFP-HMDDKQKDREIRKFRY-------IIHAEQNALTFR 407
Cdd:PHA02588  24 VGAVIEKNGR-----------IISTGYNGTPAGGvnccDHANEQgWLDDEGKLKKEHRPEHsawssknEIHAELNAILFA 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 119629222 408 CQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAGD 445
Cdd:PHA02588  93 ARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCE 130
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
89-151 2.70e-05

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 43.06  E-value: 2.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119629222   89 GLVVVK-NMKIVGLHCSSED------LHAGQIALIK-----HGSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY 151
Cdd:pfam00383  25 GAVIVKkDGEIIATGYNGENagydptIHAERNAIRQagkrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 319-454 3.98e-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: 138.56  E-value: 3.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222 319 ARHCMVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGAMYFVGCGYNAFPVGSEYADFPhmddkqkDREIRKFRYIIH 398
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVH 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119629222 399 AEQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 454
Cdd:cd01286   71 AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
323-442 3.40e-11

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 61.40  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222 323 MVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGamyfvgcgYNAFPVGSEYADFP-HMDDKQKDREIR--KFRYIIHA 399
Cdd:COG2131   13 MEIAKLVALRSTCLRRQVGAVIVKDKRILA---TG--------YNGAPSGLPHCDEVgCLREKLGIPSGErgECCRTVHA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 119629222 400 EQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIY 442
Cdd:COG2131   82 EQNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVV 124
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 79-151 7.18e-10

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: 56.90  E-value: 7.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222  79 STD-KRQVkrtGLVVVKNMKIVGL----------HCSSED-----------------LHAGQIALI---KHGSRLKNCDL 127
Cdd:cd01286   15 STCpRRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRHGVSLEGATL 91

                         90       100
                 ....*....|....*....|....
gi 119629222 128 YFSRKPCSACLKMIVNAGVNRISY 151
Cdd:cd01286   92 YVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
79-164 3.14e-09

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 55.62  E-value: 3.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222  79 STD-KRQVkrtGLVVVKNMKIV---------GL-HC-------------SSED------LHAGQIALI---KHGSRLKNC 125
Cdd:COG2131   23 STClRRQV---GAVIVKDKRILatgyngapsGLpHCdevgclreklgipSGERgeccrtVHAEQNAILqaaRHGVSTEGA 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 119629222 126 DLYFSRKPCSACLKMIVNAGVNRISY---WPADPEISLLTEA 164
Cdd:COG2131  100 TLYVTHFPCLECAKMIIQAGIKRVVYledYPDELAKELLKEA 141
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
323-444 8.57e-07

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 47.30  E-value: 8.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222  323 MVQARLLAYRTEDHKTG-VGAVIWAEGKSRscdgtgamyfVGCGYNafpvgseyadfphmddkqkdREIRKFRYIIHAEQ 401
Cdd:pfam00383   6 MRLALKAAKRAYPYSNFpVGAVIVKKDGEI----------IATGYN--------------------GENAGYDPTIHAER 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 119629222  402 NALTFRCQEIK--PEERSMIFVTKCPCDECVPLIKGAGIKQIYAG 444
Cdd:pfam00383  56 NAIRQAGKRGEgvRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 340-445 7.58e-06

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 46.29  E-value: 7.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222 340 VGAVIWAEGKsrscdgtgamyFVGCGYNAFPVGS----EYADFP-HMDDKQKDREIRKFRY-------IIHAEQNALTFR 407
Cdd:PHA02588  24 VGAVIEKNGR-----------IISTGYNGTPAGGvnccDHANEQgWLDDEGKLKKEHRPEHsawssknEIHAELNAILFA 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 119629222 408 CQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAGD 445
Cdd:PHA02588  93 ARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCE 130
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
89-151 2.70e-05

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 43.06  E-value: 2.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119629222   89 GLVVVK-NMKIVGLHCSSED------LHAGQIALIK-----HGSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY 151
Cdd:pfam00383  25 GAVIVKkDGEIIATGYNGENagydptIHAERNAIRQagkrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 389-441 2.67e-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: 40.23  E-value: 2.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119629222 389 EIRKFRYIIHAEQNALtFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQI 441
Cdd:cd00786   40 ENAAYSMCNHAERTAL-FNAGSEGDTKGQMLYVALSPCGACAQLIIELGIKDV 91
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 89-149 1.77e-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: 37.91  E-value: 1.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119629222  89 GLVVVKNMK--IVGLHCS------SEDLHAGQIALIKHGS--RLKNCDLYFSRKPCSACLKMIVNAGVNRI 149
Cdd:cd00786   21 GACLVNKKDggKVGRGCNienaaySMCNHAERTALFNAGSegDTKGQMLYVALSPCGACAQLIIELGIKDV 91
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 89-183 1.86e-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: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119629222  89 GLVVVKNM-KIVGL--HCSSEDLHAGQIALIKHG-SRLKNCDLYFSRKPCS------ACLKMIVNAGVNRISYWPADPei 158
Cdd:cd01284   22 GCVIVDDDgEIVGEgyHRKAGGPHAEVNALASAGeKLARGATLYVTLEPCShhgktpPCVDAIIEAGIKRVVVGVRDP-- 99

                         90       100
                 ....*....|....*....|....*
gi 119629222 159 sllteassseDAKLDAKAVERLKSN 183
Cdd:cd01284  100 ----------NPLVAGKGAERLRAA 114
 
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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