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Conserved domains on  [gi|17551074|ref|NP_509384|]
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Cytidine deaminase [Caenorhabditis elegans]

Protein Classification

cytidine deaminase family protein( domain architecture ID 11416731)

cytidine deaminase family protein catalyzes the deamination of cytidine or deoxycytidine, converting them into uridine or deoxyuridine, and play essential roles in nucleotide metabolism, RNA editing, and immune responses

CATH:  3.40.140.10
EC:  3.5.4.5
Gene Ontology:  GO:0009972|GO:0008270|GO:0004126
PubMed:  16720547
SCOP:  3001838

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 12-138 8.24e-58

Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the Pathway/BioSystem: Pyrimidine salvage


:

Pssm-ID: 440064 [Multi-domain]  Cd Length: 130  Bit Score: 176.49  E-value: 8.24e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074  12 EQQLVDKAIGAMENAYCKYSNFKVGAALVCDDGEIIIGANHENASYGATICAERSAIVTALTKGHRKFKYIVVATELEAP 91
Cdd:COG0295   3 DEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVADTGEP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 17551074  92 CSPCGVCRQVLIEFG--DYKVILGSStSDQIIETTTYELLPYAFTPKSL 138
Cdd:COG0295  83 VSPCGACRQVLAEFAgpDLEVILPNG-DGEVKTVTLSELLPDAFGPEDL 130
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 12-138 8.24e-58

Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440064 [Multi-domain]  Cd Length: 130  Bit Score: 176.49  E-value: 8.24e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074  12 EQQLVDKAIGAMENAYCKYSNFKVGAALVCDDGEIIIGANHENASYGATICAERSAIVTALTKGHRKFKYIVVATELEAP 91
Cdd:COG0295   3 DEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVADTGEP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 17551074  92 CSPCGVCRQVLIEFG--DYKVILGSStSDQIIETTTYELLPYAFTPKSL 138
Cdd:COG0295  83 VSPCGACRQVLAEFAgpDLEVILPNG-DGEVKTVTLSELLPDAFGPEDL 130
PRK05578 PRK05578
cytidine deaminase; Validated
 14-139 4.52e-52

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 162.00  E-value: 4.52e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074   14 QLVDKAIGAMENAYCKYSNFKVGAALVCDDGEIIIGANHENASYGATICAERSAIVTALTKGHRKFKYIVVATELEAPCS 93
Cdd:PRK05578   5 ELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACVGETGEPLS 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 17551074   94 PCGVCRQVLIEFG--DYKVILGSSTSDQiIETTTYELLPYAFTPKSLD 139
Cdd:PRK05578  85 PCGRCRQVLAEFGgpDLLVTLVAKDGPT-GEMTLGELLPYAFTPDDLG 131
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 13-138 1.99e-50

cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in humans and most bacteria. A related, homodimeric form with a much larger subunit is found in E. coli and in Arabidopsis. Both types may act on deoxycytidine as well as cytidine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273572 [Multi-domain]  Cd Length: 127  Bit Score: 157.43  E-value: 1.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074    13 QQLVDKAIGAMENAYCKYSNFKVGAALVCDDGEIIIGANHENASYGATICAERSAIVTALTKGHRKFKYIVVATELEAPC 92
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSADDPV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 17551074    93 SPCGVCRQVLIEFG--DYKVILGSSTSDqIIETTTYELLPYAFTPKSL 138
Cdd:TIGR01354  81 SPCGACRQVLAEFAgpDTPIYMTNNDGT-YKVYTVGELLPFGFGPSDL 127
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 18-127 3.79e-43

Cytidine deaminase zinc-binding domain. These enzymes 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. Cytidine deaminases catalyze the deamination of cytidine to uridine and are important in the pyrimadine salvage pathway in many cell types, from bacteria to humans. This family also includes the apoBec proteins, which are a mammal specific expansion of RNA editing enzymes, and the closely related phorbolins, and the AID (activation-induced) enzymes.


Pssm-ID: 238610 [Multi-domain]  Cd Length: 112  Bit Score: 138.63  E-value: 3.79e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074  18 KAIGAMENAYCKYSNFKVGAALVCDDGEIIIGANHENASYGATICAERSAIVTALTKGHRKFKYIVVATELEAPCSPCGV 97
Cdd:cd01283   3 AALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSDEGGVWSPCGA 82

                        90       100       110
                ....*....|....*....|....*....|
gi 17551074  98 CRQVLIEFGDYKVILGSSTSDQIIETTTYE 127
Cdd:cd01283  83 CRQVLAEFLPSRLYIIIDNPKGEEFAYTLS 112
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
13-113 1.31e-27

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 98.91  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074    13 QQLVDKAIGAMENAYcKYSNFKVGAALVCDDGEIII-GANHENASYGATICAERSAIVTALTKGHR-KFKYIVVATelea 90
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEIIAtGYNGENAGYDPTIHAERNAIRQAGKRGEGvRLEGATLYV---- 77

                          90       100
                  ....*....|....*....|...
gi 17551074    91 PCSPCGVCRQVLIEFGDYKVILG 113
Cdd:pfam00383  78 TLEPCGMCAQAIIESGIKRVVFG 100
 
Name Accession Description Interval E-value
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 12-138 8.24e-58

Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440064 [Multi-domain]  Cd Length: 130  Bit Score: 176.49  E-value: 8.24e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074  12 EQQLVDKAIGAMENAYCKYSNFKVGAALVCDDGEIIIGANHENASYGATICAERSAIVTALTKGHRKFKYIVVATELEAP 91
Cdd:COG0295   3 DEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGLTLCAERTAIFAAVAAGEREIKAIAVVADTGEP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 17551074  92 CSPCGVCRQVLIEFG--DYKVILGSStSDQIIETTTYELLPYAFTPKSL 138
Cdd:COG0295  83 VSPCGACRQVLAEFAgpDLEVILPNG-DGEVKTVTLSELLPDAFGPEDL 130
PRK05578 PRK05578
cytidine deaminase; Validated
 14-139 4.52e-52

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 162.00  E-value: 4.52e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074   14 QLVDKAIGAMENAYCKYSNFKVGAALVCDDGEIIIGANHENASYGATICAERSAIVTALTKGHRKFKYIVVATELEAPCS 93
Cdd:PRK05578   5 ELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGRLVAIACVGETGEPLS 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 17551074   94 PCGVCRQVLIEFG--DYKVILGSSTSDQiIETTTYELLPYAFTPKSLD 139
Cdd:PRK05578  85 PCGRCRQVLAEFGgpDLLVTLVAKDGPT-GEMTLGELLPYAFTPDDLG 131
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 13-138 1.99e-50

cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in humans and most bacteria. A related, homodimeric form with a much larger subunit is found in E. coli and in Arabidopsis. Both types may act on deoxycytidine as well as cytidine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273572 [Multi-domain]  Cd Length: 127  Bit Score: 157.43  E-value: 1.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074    13 QQLVDKAIGAMENAYCKYSNFKVGAALVCDDGEIIIGANHENASYGATICAERSAIVTALTKGHRKFKYIVVATELEAPC 92
Cdd:TIGR01354   1 DKLFKAAQEARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPLTICAERSAIGKAISAGYRKFVAIAVADSADDPV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 17551074    93 SPCGVCRQVLIEFG--DYKVILGSSTSDqIIETTTYELLPYAFTPKSL 138
Cdd:TIGR01354  81 SPCGACRQVLAEFAgpDTPIYMTNNDGT-YKVYTVGELLPFGFGPSDL 127
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 18-127 3.79e-43

Cytidine deaminase zinc-binding domain. These enzymes 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. Cytidine deaminases catalyze the deamination of cytidine to uridine and are important in the pyrimadine salvage pathway in many cell types, from bacteria to humans. This family also includes the apoBec proteins, which are a mammal specific expansion of RNA editing enzymes, and the closely related phorbolins, and the AID (activation-induced) enzymes.


Pssm-ID: 238610 [Multi-domain]  Cd Length: 112  Bit Score: 138.63  E-value: 3.79e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074  18 KAIGAMENAYCKYSNFKVGAALVCDDGEIIIGANHENASYGATICAERSAIVTALTKGHRKFKYIVVATELEAPCSPCGV 97
Cdd:cd01283   3 AALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSDEGGVWSPCGA 82

                        90       100       110
                ....*....|....*....|....*....|
gi 17551074  98 CRQVLIEFGDYKVILGSSTSDQIIETTTYE 127
Cdd:cd01283  83 CRQVLAEFLPSRLYIIIDNPKGEEFAYTLS 112
PRK12411 PRK12411
cytidine deaminase; Provisional
 13-140 7.14e-41

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 133.55  E-value: 7.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074   13 QQLVDKAIGAMENAYCKYSNFKVGAALVCDDGEIIIGANHENASYGATICAERSAIVTALTKGHRKFKYIVVATELEAPC 92
Cdd:PRK12411   4 KQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTKRPV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 17551074   93 SPCGVCRQVLIEF--GDYKVILGSSTSDqIIETTTYELLPYAFTPKSLDD 140
Cdd:PRK12411  84 PPCGACRQVMVELckQDTKVYLSNLHGD-VQETTVGELLPGAFLAEDLHE 132
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
13-113 1.31e-27

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 98.91  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074    13 QQLVDKAIGAMENAYcKYSNFKVGAALVCDDGEIII-GANHENASYGATICAERSAIVTALTKGHR-KFKYIVVATelea 90
Cdd:pfam00383   3 EYFMRLALKAAKRAY-PYSNFPVGAVIVKKDGEIIAtGYNGENAGYDPTIHAERNAIRQAGKRGEGvRLEGATLYV---- 77

                          90       100
                  ....*....|....*....|...
gi 17551074    91 PCSPCGVCRQVLIEFGDYKVILG 113
Cdd:pfam00383  78 TLEPCGMCAQAIIESGIKRVVFG 100
PRK06848 PRK06848
cytidine deaminase;
8-134 1.05e-13

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 63.99  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074    8 LTEFEQQLVDKAIGAMENAYcKYSNFKVGAALVCDDGEIIIGANHEnASYG-ATICAERSAIVTALTKGHRKFKYIVVAT 86
Cdd:PRK06848   3 LNSEDYELIKAAEKVIEKRY-RNDWHHVGAALRTKTGRIYAAVHLE-AYVGrITVCAEAIAIGKAISEGDHEIDTIVAVR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17551074   87 -----ELEAPC---SPCGVCRQVLIEFG-DYKVILgsSTSDQIIETTTYELLPYAFT 134
Cdd:PRK06848  81 hpkphEDDREIwvvSPCGACRELISDYGkNTNVIV--PYNDELVKVNIMELLPNKYT 135
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 16-111 3.19e-13

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: 61.80  E-value: 3.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074  16 VDKAIGAMENAYCKYSNFKVGAALVCDDGEIII--GANHENASYGATICAERSAIVTALTKGHRKFKYIVVATeleapcS 93
Cdd:cd00786   1 MTEALKAADLGYAKESNFQVGACLVNKKDGGKVgrGCNIENAAYSMCNHAERTALFNAGSEGDTKGQMLYVAL------S 74

                        90
                ....*....|....*...
gi 17551074  94 PCGVCRQVLIEFGDYKVI 111
Cdd:cd00786  75 PCGACAQLIIELGIKDVI 92
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 22-152 8.23e-13

cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis and some Proteobacteria. A related, homotetrameric form with a much smaller subunit is found most bacteria and in animals. Both types may act on deoxycytidine as well as cytidine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273573 [Multi-domain]  Cd Length: 283  Bit Score: 64.08  E-value: 8.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074    22 AMENAYCKYSNFKVGAALVCDDGEIIIGANHE--NASYGATICAERSAIVTALTKGHRKFKYIVVATeleapcSPCGVCR 99
Cdd:TIGR01355  32 AASYARAPISKFNVGAVGRGSSGRFYLGVNVEfpGLPLHHSIHAEQFLISHLALNGERGLNDLAVSF------APCGHCR 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17551074   100 QVLIEFGD---YKVILGSSTSDQIIETTTYelLPYAFTPKSLDDHEKETEERKHHN 152
Cdd:TIGR01355 106 QFLNEIRNassIKILLPDPHNKRDMSLQSY--LPDRFGPDDLLIKSAPLLLEERHN 159
PRK09027 PRK09027
cytidine deaminase; Provisional
 31-142 1.78e-10

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 57.54  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074   31 SNFKVGAALVCDDGEIIIGANHE--NASYGATICAERSAIVTALTKGHRKFKYIVVAteleapCSPCGVCRQVLIEfgdy 108
Cdd:PRK09027  69 SHFNVGAIARGVSGNFYFGANMEfaGAALQQTVHAEQSAISHAWLRGEKAIADITVN------YTPCGHCRQFMNE---- 138

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 17551074  109 kviLGSSTSDQI-----IETTTYELLPYAFTPKSLDDHE 142
Cdd:PRK09027 139 ---LNSASDLRIhlpgrQAHTLHDYLPDAFGPKDLNITT 174
PRK08298 PRK08298
cytidine deaminase; Validated
 9-131 3.18e-10

cytidine deaminase; Validated


Pssm-ID: 236225 [Multi-domain]  Cd Length: 136  Bit Score: 54.80  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074    9 TEFEQQLVDKAIGAMENAYCkySNFKVGAALVCDDGEIIIGANHENASYGATICAERSAIVTALTKGHRKFKYIVVATEL 88
Cdd:PRK08298   1 MNIEQALYDVAKQLIEQRYP--NGWGGAAAMRVEDGTILTSVAPEVINASTELCMETGAICEAHKLQKRVTHSICVAREN 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 17551074   89 E-APC---SPCGVCRQVLIEFGDyKVILGSSTSDQ---IIETTTYELLPY 131
Cdd:PRK08298  79 EhSELkvlSPCGVCQERLFYWGP-DVMCAVTNADDptdIIFKPLKELQPY 127
PLN02402 PLN02402
cytidine deaminase
 31-152 2.19e-06

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 46.01  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551074   31 SNFKVGAALVCDDGEIIIGANHE--NASYGATICAERSAIVTALTKGHRKFKYIVVATeleapcSPCGVCRQVLIEFGDY 108
Cdd:PLN02402  44 SKYHVGAVGLGSSGRIFLGVNLEfpGLPLHHSVHAEQFLITNLTLNAEPHLKYVAVSA------APCGHCRQFFQEIRDA 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17551074  109 K----VILGSSTSDQIIET---------TTYELLPYAFTPKSLDDHEKETEERKHHN 152
Cdd:PLN02402 118 PdikiLITGDSNSNDSYKNsladsqqfePLSCLLPHRFGPDDLLDKDVPLLLEPHHN 174
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
15-85 4.28e-05

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 40.59  E-value: 4.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17551074    15 LVDKAIGAMENAYCKYSNFKVGAALVCDDGEIIIGANHENASYGATICAERSAIVTALTKGHrKFKYIVVA 85
Cdd:pfam08211  36 LKQAALAAANRSYAPYSKCPSGVALQDGDGRVYRGRYAENAAFNPSLPPLQAALVDFVAGGK-DFEDIVRA 105
 
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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