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Conserved domains on  [gi|19076024|ref|NP_588524|]
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cytosine deaminase [Schizosaccharomyces pombe]

Protein Classification

nucleoside deaminase( domain architecture ID 10101196)

nucleoside deaminase (such as as adenosine, guanine, or cytosine deaminase) is a Zn-dependent enzyme which catalyzes the deamination of nucleosides

CATH:  3.40.140.10
EC:  3.5.4.-
Gene Ontology:  GO:0019239|GO:0009116|GO:0008270|GO:0001882
PubMed:  7599282|7599282|12637534
SCOP:  3001838|3001838

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 14-111 1.85e-41

Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. 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 functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.


:

Pssm-ID: 238612 [Multi-domain]  Cd Length: 109  Bit Score: 134.28  E-value: 1.85e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024  14 LREAIKVSQQARDEGQHPFGCIIVDENDNVIMSAGNRV-PDGDVTQHAETRAVGLITKTRRD--LEKCTLYTSTEPCAMC 90
Cdd:cd01285   1 MRLAIELARKALAEGEVPFGAVIVDDDGKVIARGHNRVeQDGDPTAHAEIVAIRNAARRLGSylLSGCTLYTTLEPCPMC 80

                        90       100
                ....*....|....*....|.
gi 19076024  91 SGAIFWSGIRRMIFGLSNENL 111
Cdd:cd01285  81 AGALLWARIKRVVYGASDPKL 101
 
Name Accession Description Interval E-value
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 14-111 1.85e-41

Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. 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 functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.


Pssm-ID: 238612 [Multi-domain]  Cd Length: 109  Bit Score: 134.28  E-value: 1.85e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024  14 LREAIKVSQQARDEGQHPFGCIIVDENDNVIMSAGNRV-PDGDVTQHAETRAVGLITKTRRD--LEKCTLYTSTEPCAMC 90
Cdd:cd01285   1 MRLAIELARKALAEGEVPFGAVIVDDDGKVIARGHNRVeQDGDPTAHAEIVAIRNAARRLGSylLSGCTLYTTLEPCPMC 80

                        90       100
                ....*....|....*....|.
gi 19076024  91 SGAIFWSGIRRMIFGLSNENL 111
Cdd:cd01285  81 AGALLWARIKRVVYGASDPKL 101
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 8-158 2.11e-40

tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification


Pssm-ID: 440355 [Multi-domain]  Cd Length: 148  Bit Score: 132.93  E-value: 2.11e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024   8 EKDLAYLREAIKVSQQARDEGQHPFGCIIVDeNDNVIMSAGNRV-PDGDVTQHAETRAvglITK-----TRRDLEKCTLY 81
Cdd:COG0590   2 EDDEEFMRRALELARKAVAEGEVPVGAVLVK-DGEIIARGHNRVeTLNDPTAHAEILA---IRAaarklGNWRLSGCTLY 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076024  82 TSTEPCAMCSGAIFWSGIRRMIFGLSNEnlikltqKSGECPPLYINSRDilGAASHPIEVVGPYIEDEAIIPHKGFW 158
Cdd:COG0590  78 VTLEPCPMCAGAIVWARIGRVVYGASDP-------KAGAAGSIYDLLAD--PRLNHRVEVVGGVLAEECAALLRDFF 145
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
9-105 5.97e-33

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 112.40  E-value: 5.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024     9 KDLAYLREAIKVSQQARDEGQHPFGCIIVDENDNVIMSAGNRVPDG-DVTQHAETRAVGLITKT--RRDLEKCTLYTSTE 85
Cdd:pfam00383   1 WDEYFMRLALKAAKRAYPYSNFPVGAVIVKKDGEIIATGYNGENAGyDPTIHAERNAIRQAGKRgeGVRLEGATLYVTLE 80

                          90       100
                  ....*....|....*....|
gi 19076024    86 PCAMCSGAIFWSGIRRMIFG 105
Cdd:pfam00383  81 PCGMCAQAIIESGIKRVVFG 100
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 1-149 8.26e-18

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 75.61  E-value: 8.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024    1 MSSTELSekDLAYLREAIKVSQQARDEGQHPFGCIIVdENDNVIMSAGNR-VPDGDVTQHAETRAV---GLITKTRRdLE 76
Cdd:PRK10860   6 LSEVEFS--HEYWMRHALTLAKRAWDEREVPVGAVLV-HNNRVIGEGWNRpIGRHDPTAHAEIMALrqgGLVLQNYR-LL 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19076024   77 KCTLYTSTEPCAMCSGAIFWSGIRRMIFGLSNEnlikltqKSGECPPLYinsrDILG--AASHPIEVVGPYIEDE 149
Cdd:PRK10860  82 DATLYVTLEPCVMCAGAMVHSRIGRLVFGARDA-------KTGAAGSLM----DVLHhpGMNHRVEITEGVLADE 145
 
Name Accession Description Interval E-value
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 14-111 1.85e-41

Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. 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 functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.


Pssm-ID: 238612 [Multi-domain]  Cd Length: 109  Bit Score: 134.28  E-value: 1.85e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024  14 LREAIKVSQQARDEGQHPFGCIIVDENDNVIMSAGNRV-PDGDVTQHAETRAVGLITKTRRD--LEKCTLYTSTEPCAMC 90
Cdd:cd01285   1 MRLAIELARKALAEGEVPFGAVIVDDDGKVIARGHNRVeQDGDPTAHAEIVAIRNAARRLGSylLSGCTLYTTLEPCPMC 80

                        90       100
                ....*....|....*....|.
gi 19076024  91 SGAIFWSGIRRMIFGLSNENL 111
Cdd:cd01285  81 AGALLWARIKRVVYGASDPKL 101
TadA COG0590
tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA ...
 8-158 2.11e-40

tRNA(Arg) A34 adenosine deaminase TadA [Translation, ribosomal structure and biogenesis]; tRNA(Arg) A34 adenosine deaminase TadA is part of the Pathway/BioSystem: Pyrimidine salvagetRNA modification


Pssm-ID: 440355 [Multi-domain]  Cd Length: 148  Bit Score: 132.93  E-value: 2.11e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024   8 EKDLAYLREAIKVSQQARDEGQHPFGCIIVDeNDNVIMSAGNRV-PDGDVTQHAETRAvglITK-----TRRDLEKCTLY 81
Cdd:COG0590   2 EDDEEFMRRALELARKAVAEGEVPVGAVLVK-DGEIIARGHNRVeTLNDPTAHAEILA---IRAaarklGNWRLSGCTLY 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076024  82 TSTEPCAMCSGAIFWSGIRRMIFGLSNEnlikltqKSGECPPLYINSRDilGAASHPIEVVGPYIEDEAIIPHKGFW 158
Cdd:COG0590  78 VTLEPCPMCAGAIVWARIGRVVYGASDP-------KAGAAGSIYDLLAD--PRLNHRVEVVGGVLAEECAALLRDFF 145
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
9-105 5.97e-33

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 112.40  E-value: 5.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024     9 KDLAYLREAIKVSQQARDEGQHPFGCIIVDENDNVIMSAGNRVPDG-DVTQHAETRAVGLITKT--RRDLEKCTLYTSTE 85
Cdd:pfam00383   1 WDEYFMRLALKAAKRAYPYSNFPVGAVIVKKDGEIIATGYNGENAGyDPTIHAERNAIRQAGKRgeGVRLEGATLYVTLE 80

                          90       100
                  ....*....|....*....|
gi 19076024    86 PCAMCSGAIFWSGIRRMIFG 105
Cdd:pfam00383  81 PCGMCAQAIIESGIKRVVFG 100
PRK10860 PRK10860
tRNA-specific adenosine deaminase; Provisional
 1-149 8.26e-18

tRNA-specific adenosine deaminase; Provisional


Pssm-ID: 182786 [Multi-domain]  Cd Length: 172  Bit Score: 75.61  E-value: 8.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024    1 MSSTELSekDLAYLREAIKVSQQARDEGQHPFGCIIVdENDNVIMSAGNR-VPDGDVTQHAETRAV---GLITKTRRdLE 76
Cdd:PRK10860   6 LSEVEFS--HEYWMRHALTLAKRAWDEREVPVGAVLV-HNNRVIGEGWNRpIGRHDPTAHAEIMALrqgGLVLQNYR-LL 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19076024   77 KCTLYTSTEPCAMCSGAIFWSGIRRMIFGLSNEnlikltqKSGECPPLYinsrDILG--AASHPIEVVGPYIEDE 149
Cdd:PRK10860  82 DATLYVTLEPCVMCAGAMVHSRIGRLVFGARDA-------KTGAAGSLM----DVLHhpGMNHRVEITEGVLADE 145
MafB19-deam pfam14437
MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily ...
 8-109 2.98e-16

MafB19-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Neisseria MafB19. Members of this family are present in a wide phyletic range of bacteria and are predicted to function as toxins in bacterial polymorphic toxin systems.


Pssm-ID: 433953 [Multi-domain]  Cd Length: 144  Bit Score: 71.01  E-value: 2.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024     8 EKDLAYLREAIKVSQQARDEGQHPFGCIIVdENDNVIMSAGNRVP-DGDVTQHAET----RAVGLITKTRrdLEKCTLYT 82
Cdd:pfam14437   1 ENHEKWFRKALGLAEKAYDAGEVPIGAVIV-KDGKVIARGYNRKElNADTTAHAEIlaiqQAAKKLGSWR--LDDATLYV 77

                          90       100
                  ....*....|....*....|....*..
gi 19076024    83 STEPCAMCSGAIFWSGIRRMIFGLSNE 109
Cdd:pfam14437  78 TLEPCPMCAGAIVQAGLKSLVYGAGNP 104
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 16-104 1.30e-08

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: 49.86  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024  16 EAIKVSQQAR-DEGQHPFG-CIIVDENDNVI-MSAGNRVPDGDVTQHAETRAVGLITKTRrDLEKCTLYTSTEPCAMCSG 92
Cdd:cd00786   3 EALKAADLGYaKESNFQVGaCLVNKKDGGKVgRGCNIENAAYSMCNHAERTALFNAGSEG-DTKGQMLYVALSPCGACAQ 81

                        90
                ....*....|..
gi 19076024  93 AIFWSGIRRMIF 104
Cdd:cd00786  82 LIIELGIKDVIV 93
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 31-111 8.29e-08

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: 48.00  E-value: 8.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024  31 PFGCIIVDENDNVImSAGNRVPDGDVtqHAETRAvgLITKTRRDLEKCTLYTSTEPCAM------CSGAIFWSGIRRMIF 104
Cdd:cd01284  20 PVGCVIVDDDGEIV-GEGYHRKAGGP--HAEVNA--LASAGEKLARGATLYVTLEPCSHhgktppCVDAIIEAGIKRVVV 94


                ....*..
gi 19076024 105 GLSNENL 111
Cdd:cd01284  95 GVRDPNP 101
cd PHA02588
deoxycytidylate deaminase; Provisional
 9-119 4.72e-07

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 47.06  E-value: 4.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024    9 KDLAYLREAIKVSQQARDEgQHPFGCIIvdENDNVIMSAG-NRVPDGDVT------------------------------ 57
Cdd:PHA02588   2 KDSTYLQIAYLVSQESKCV-SWKVGAVI--EKNGRIISTGyNGTPAGGVNccdhaneqgwlddegklkkehrpehsawss 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19076024   58 ---QHAETRAVGLITKTRRDLEKCTLYTSTEPCAMCSGAIFWSGIRRMIFG----LSNENLIKLTQKSG 119
Cdd:PHA02588  79 kneIHAELNAILFAARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCekydRNGPGWDDILRKSG 147
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 59-104 1.04e-06

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: 45.34  E-value: 1.04e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 19076024  59 HAETRAVGLITKTRRDLEKCTLYTSTEPCAMCSGAIFWSGIRRMIF 104
Cdd:cd01286  70 HAEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
33-104 1.28e-06

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 45.60  E-value: 1.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024  33 GCIIVDenDNVIMSAG-NRVPDGDV------------------------TQHAETRAVGLITKTRRDLEKCTLYTSTEPC 87
Cdd:COG2131  31 GAVIVK--DKRILATGyNGAPSGLPhcdevgclreklgipsgergeccrTVHAEQNAILQAARHGVSTEGATLYVTHFPC 108

                        90
                ....*....|....*..
gi 19076024  88 AMCSGAIFWSGIRRMIF 104
Cdd:COG2131 109 LECAKMIIQAGIKRVVY 125
RibD1 COG0117
Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and ...
 12-106 9.14e-06

Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain [Coenzyme transport and metabolism]; Riboflavin biosynthesis protein RibD, pyrimidine deaminase domain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439887 [Multi-domain]  Cd Length: 311  Bit Score: 44.28  E-value: 9.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076024  12 AYLREAIKVSQQARdeGQH----PFGCIIVDenDNVIMSAGNRVPDGdvTQHAETRAvglITKTRRDLEKCTLYTSTEPC 87
Cdd:COG0117   2 RYMRRALELARRGL--GTTspnpLVGCVIVK--DGRIVGEGYHQRAG--GPHAEVNA---LAQAGEAARGATLYVTLEPC 72

                        90       100
                ....*....|....*....|....*
gi 19076024  88 AM------CSGAIFWSGIRRMIFGL 106
Cdd:COG0117  73 SHhgrtppCADALIEAGIKRVVIAM 97
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 30-95 3.91e-03

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: 35.39  E-value: 3.91e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19076024  30 HPFGCIIVdENDNVIMSAGNR-VPDGDVTQHAETRAVGLITKTRRDLEKCTLYTSTE-----PCAMCSGAIF 95
Cdd:cd01283  18 FTVGAALL-TKDGRIFTGVNVeNASYGLTLCAERTAIGKAVSEGLRRYLVTWAVSDEggvwsPCGACRQVLA 88
 
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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