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Conserved domains on  [gi|2462538143|ref|XP_054231027|]
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cytidine and dCMP deaminase domain-containing protein 1 isoform X1 [Homo sapiens]

Protein Classification

deoxycytidylate_deaminase domain-containing protein( domain architecture ID 10217272)

deoxycytidylate_deaminase domain-containing protein

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 ...
 333-468 1.47e-38

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: 137.41  E-value: 1.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143 333 ARHCMVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGAMYFVGCGYNAFPVGSEYADFPhmddkqkDREIRKFRYIIH 412
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVH 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462538143 413 AEQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 468
Cdd:cd01286    71 AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
cytidine_deaminase-like super family cl00269
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 93-165 1.29e-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: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143  93 STD-KRQVkrtGLVVVKNMKIVGL----------HCSSED-----------------LHAGQIALI---KHGSRLKNCDL 141
Cdd:cd01286    15 STCpRRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRHGVSLEGATL 91

                          90       100
                  ....*....|....*....|....
gi 2462538143 142 YFSRKPCSACLKMIVNAGVNRISY 165
Cdd:cd01286    92 YVTLFPCIECAKLIIQAGIKKVVY 115
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 333-468 1.47e-38

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: 137.41  E-value: 1.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143 333 ARHCMVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGAMYFVGCGYNAFPVGSEYADFPhmddkqkDREIRKFRYIIH 412
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVH 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462538143 413 AEQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 468
Cdd:cd01286    71 AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
337-456 5.26e-11

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 61.01  E-value: 5.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143 337 MVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGamyfvgcgYNAFPVGSEYADFP-HMDDKQKDREIR--KFRYIIHA 413
Cdd:COG2131    13 MEIAKLVALRSTCLRRQVGAVIVKDKRILA---TG--------YNGAPSGLPHCDEVgCLREKLGIPSGErgECCRTVHA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462538143 414 EQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIY 456
Cdd:COG2131    82 EQNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVV 124
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 93-165 1.29e-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: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143  93 STD-KRQVkrtGLVVVKNMKIVGL----------HCSSED-----------------LHAGQIALI---KHGSRLKNCDL 141
Cdd:cd01286    15 STCpRRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRHGVSLEGATL 91

                          90       100
                  ....*....|....*....|....
gi 2462538143 142 YFSRKPCSACLKMIVNAGVNRISY 165
Cdd:cd01286    92 YVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
93-178 4.91e-09

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 55.23  E-value: 4.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143  93 STD-KRQVkrtGLVVVKNMKIV---------GL-HC-------------SSED------LHAGQIALI---KHGSRLKNC 139
Cdd:COG2131    23 STClRRQV---GAVIVKDKRILatgyngapsGLpHCdevgclreklgipSGERgeccrtVHAEQNAILqaaRHGVSTEGA 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462538143 140 DLYFSRKPCSACLKMIVNAGVNRISY---WPADPEISLLTEA 178
Cdd:COG2131   100 TLYVTHFPCLECAKMIIQAGIKRVVYledYPDELAKELLKEA 141
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
337-458 1.58e-06

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 46.53  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143 337 MVQARLLAYRTEDHKTG-VGAVIWAEGKSRscdgtgamyfVGCGYNafpvgseyadfphmddkqkdREIRKFRYIIHAEQ 415
Cdd:pfam00383   6 MRLALKAAKRAYPYSNFpVGAVIVKKDGEI----------IATGYN--------------------GENAGYDPTIHAER 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462538143 416 NALTFRCQEIK--PEERSMIFVTKCPCDECVPLIKGAGIKQIYAG 458
Cdd:pfam00383  56 NAIRQAGKRGEgvRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 354-459 6.42e-06

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 46.67  E-value: 6.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143 354 VGAVIWAEGKsrscdgtgamyFVGCGYNAFPVGS----EYADFP-HMDDKQKDREIRKFRY-------IIHAEQNALTFR 421
Cdd:PHA02588   24 VGAVIEKNGR-----------IISTGYNGTPAGGvnccDHANEQgWLDDEGKLKKEHRPEHsawssknEIHAELNAILFA 92

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462538143 422 CQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAGD 459
Cdd:PHA02588   93 ARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCE 130
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
103-165 4.43e-05

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 42.29  E-value: 4.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462538143 103 GLVVVK-NMKIVGLHCSSED------LHAGQIALIK-----HGSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY 165
Cdd:pfam00383  25 GAVIVKkDGEIIATGYNGENagydptIHAERNAIRQagkrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
 
Name Accession Description Interval E-value
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 333-468 1.47e-38

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: 137.41  E-value: 1.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143 333 ARHCMVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGAMYFVGCGYNAFPVGSEYADFPhmddkqkDREIRKFRYIIH 412
Cdd:cd01286     1 DEYFMAIARLAALRSTCPRRQVGAVIVKDKRIIS---TGYNGSPSGLPHCAEVGCERDDLP-------SGEDQKCCRTVH 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462538143 413 AEQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIK-QIYAGDVDVGKKKAD 468
Cdd:cd01286    71 AEQNAILQAARHGVSLEGATLYVTLFPCIECAKLIIQAGIKkVVYAEPYDDDDPAAA 127
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
337-456 5.26e-11

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 61.01  E-value: 5.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143 337 MVQARLLAYRTEDHKTGVGAVIWAEGKSRScdgTGamyfvgcgYNAFPVGSEYADFP-HMDDKQKDREIR--KFRYIIHA 413
Cdd:COG2131    13 MEIAKLVALRSTCLRRQVGAVIVKDKRILA---TG--------YNGAPSGLPHCDEVgCLREKLGIPSGErgECCRTVHA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462538143 414 EQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIY 456
Cdd:COG2131    82 EQNAILQAARHGVSTEGATLYVTHFPCLECAKMIIQAGIKRVV 124
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 93-165 1.29e-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: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143  93 STD-KRQVkrtGLVVVKNMKIVGL----------HCSSED-----------------LHAGQIALI---KHGSRLKNCDL 141
Cdd:cd01286    15 STCpRRQV---GAVIVKDKRIISTgyngspsglpHCAEVGcerddlpsgedqkccrtVHAEQNAILqaaRHGVSLEGATL 91

                          90       100
                  ....*....|....*....|....
gi 2462538143 142 YFSRKPCSACLKMIVNAGVNRISY 165
Cdd:cd01286    92 YVTLFPCIECAKLIIQAGIKKVVY 115
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
93-178 4.91e-09

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 55.23  E-value: 4.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143  93 STD-KRQVkrtGLVVVKNMKIV---------GL-HC-------------SSED------LHAGQIALI---KHGSRLKNC 139
Cdd:COG2131    23 STClRRQV---GAVIVKDKRILatgyngapsGLpHCdevgclreklgipSGERgeccrtVHAEQNAILqaaRHGVSTEGA 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462538143 140 DLYFSRKPCSACLKMIVNAGVNRISY---WPADPEISLLTEA 178
Cdd:COG2131   100 TLYVTHFPCLECAKMIIQAGIKRVVYledYPDELAKELLKEA 141
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
337-458 1.58e-06

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 46.53  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143 337 MVQARLLAYRTEDHKTG-VGAVIWAEGKSRscdgtgamyfVGCGYNafpvgseyadfphmddkqkdREIRKFRYIIHAEQ 415
Cdd:pfam00383   6 MRLALKAAKRAYPYSNFpVGAVIVKKDGEI----------IATGYN--------------------GENAGYDPTIHAER 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462538143 416 NALTFRCQEIK--PEERSMIFVTKCPCDECVPLIKGAGIKQIYAG 458
Cdd:pfam00383  56 NAIRQAGKRGEgvRLEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 354-459 6.42e-06

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 46.67  E-value: 6.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143 354 VGAVIWAEGKsrscdgtgamyFVGCGYNAFPVGS----EYADFP-HMDDKQKDREIRKFRY-------IIHAEQNALTFR 421
Cdd:PHA02588   24 VGAVIEKNGR-----------IISTGYNGTPAGGvnccDHANEQgWLDDEGKLKKEHRPEHsawssknEIHAELNAILFA 92

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462538143 422 CQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAGD 459
Cdd:PHA02588   93 ARNGISIEGATMYVTASPCPDCAKAIAQSGIKKLVYCE 130
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
103-165 4.43e-05

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 42.29  E-value: 4.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462538143 103 GLVVVK-NMKIVGLHCSSED------LHAGQIALIK-----HGSRLKNCDLYFSRKPCSACLKMIVNAGVNRISY 165
Cdd:pfam00383  25 GAVIVKkDGEIIATGYNGENagydptIHAERNAIRQagkrgEGVRLEGATLYVTLEPCGMCAQAIIESGIKRVVF 99
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 403-455 3.28e-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: 3.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462538143 403 EIRKFRYIIHAEQNALtFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQI 455
Cdd:cd00786    40 ENAAYSMCNHAERTAL-FNAGSEGDTKGQMLYVALSPCGACAQLIIELGIKDV 91
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 103-197 1.92e-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: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462538143 103 GLVVVKNM-KIVGL--HCSSEDLHAGQIALIKHG-SRLKNCDLYFSRKPCS------ACLKMIVNAGVNRISYWPADPei 172
Cdd:cd01284    22 GCVIVDDDgEIVGEgyHRKAGGPHAEVNALASAGeKLARGATLYVTLEPCShhgktpPCVDAIIEAGIKRVVVGVRDP-- 99

                          90       100
                  ....*....|....*....|....*
gi 2462538143 173 sllteassseDAKLDAKAVERLKSN 197
Cdd:cd01284   100 ----------NPLVAGKGAERLRAA 114
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 103-163 2.22e-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: 2.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462538143 103 GLVVVKNMK--IVGLHCS------SEDLHAGQIALIKHGS--RLKNCDLYFSRKPCSACLKMIVNAGVNRI 163
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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