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Conserved domains on  [gi|2560235997|gb|WLJ60565|]
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sxtB protein [Alexandrium pacificum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09027 super family cl30403
cytidine deaminase; Provisional
 45-286 1.31e-57

cytidine deaminase; Provisional


The actual alignment was detected with superfamily member PRK09027:

Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 187.73  E-value: 1.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  45 GILGKPEVEHLRLQTGLGDDAILQKLLPHAKDMALPQASGYQVGAAALGASGRIYLGFNLELSGLPPQLCVHAEQAAVYL 124
Cdd:PRK09027   31 AMLTAEQVSQLKSASGLDDDALALALLPLAAACAVTPISHFNVGAIARGVSGNFYFGANMEFAGAALQQTVHAEQSAISH 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 125 AVDAGEEKVVTLATSATPCGHCRQFMLEMYGAPELRVVCPEQAPASLKELVPDPFGPHHLDVPAVLLQAHSHKLKLARqp 204
Cdd:PRK09027  111 AWLRGEKAIADITVNYTPCGHCRQFMNELNSASDLRIHLPGRQAHTLHDYLPDAFGPKDLNITTLLMDPQDHGLALDT-- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 205 qaSDTLTTLALAAACRSYAPL-GSPAGMALRMRDGTLSDGFAVWSVAFNPGLTtagPLQGALVKLIAQGYrDFQEIEAAV 283
Cdd:PRK09027  189 --GDPLIQAALDAANRSHAPYsQSYSGVALETKDGRIYTGRYAENAAFNPSLP---PLQGALNLLNLSGE-DFSDIQRAV 262


                  ...
gi 2560235997 284 LVE 286
Cdd:PRK09027  263 LVE 265
 
Name Accession Description Interval E-value
PRK09027 PRK09027
cytidine deaminase; Provisional
 45-286 1.31e-57

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 187.73  E-value: 1.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  45 GILGKPEVEHLRLQTGLGDDAILQKLLPHAKDMALPQASGYQVGAAALGASGRIYLGFNLELSGLPPQLCVHAEQAAVYL 124
Cdd:PRK09027   31 AMLTAEQVSQLKSASGLDDDALALALLPLAAACAVTPISHFNVGAIARGVSGNFYFGANMEFAGAALQQTVHAEQSAISH 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 125 AVDAGEEKVVTLATSATPCGHCRQFMLEMYGAPELRVVCPEQAPASLKELVPDPFGPHHLDVPAVLLQAHSHKLKLARqp 204
Cdd:PRK09027  111 AWLRGEKAIADITVNYTPCGHCRQFMNELNSASDLRIHLPGRQAHTLHDYLPDAFGPKDLNITTLLMDPQDHGLALDT-- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 205 qaSDTLTTLALAAACRSYAPL-GSPAGMALRMRDGTLSDGFAVWSVAFNPGLTtagPLQGALVKLIAQGYrDFQEIEAAV 283
Cdd:PRK09027  189 --GDPLIQAALDAANRSHAPYsQSYSGVALETKDGRIYTGRYAENAAFNPSLP---PLQGALNLLNLSGE-DFSDIQRAV 262


                  ...
gi 2560235997 284 LVE 286
Cdd:PRK09027  263 LVE 265
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 51-313 1.29e-51

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: 171.94  E-value: 1.29e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  51 EVEHLRLQTGLGDDAILQKLLPHAKDMALPQASGYQVGAAALGASGRIYLGFNLELSGLPPQLCVHAEQAAVYLAVDAGE 130
Cdd:TIGR01355   9 QAQSLGTLSGLTDPKLLPKLIPKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLHHSIHAEQFLISHLALNGE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 131 EKVVTLATSATPCGHCRQFMLEMYGAPELRVVCP---EQAPASLKELVPDPFGPHHLDV--PAVLLQAHSHKLKL----- 200
Cdd:TIGR01355  89 RGLNDLAVSFAPCGHCRQFLNEIRNASSIKILLPdphNKRDMSLQSYLPDRFGPDDLLIksAPLLLEERHNCLALidpds 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 201 ARQPQASDTLTTLALAAACRSYAPLG-SPAGMALRMRDGTLSDGFAVWSVAFNPGLttaGPLQGALVKLIAQGY-RDFQE 278
Cdd:TIGR01355 169 IRNSDICSDLKQQALKAANRSYAPYSkSPSGVALKDREGKVYRGWYIESAAFNPSL---GPLQAALVDFMANGGgKGFED 245

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2560235997 279 IEAAVLVEQEGEPVAFAEFWSAALQKIAPKAQLDV 313
Cdd:TIGR01355 246 IVRAVLVEKADAKVSHEATARALLETIAPSCELKV 280
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 63-184 1.41e-29

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: 109.47  E-value: 1.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  63 DDAILQKLLPHAKDMALPQASGYQVGAAALGASGRIYLGFNLELSGLPpqLCVHAEQAAVYLAVDAGEEKVVTLATSA-- 140
Cdd:COG0295     2 DDEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYG--LTLCAERTAIFAAVAAGEREIKAIAVVAdt 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2560235997 141 ----TPCGHCRQFMLEmYGAPELRVVCP----EQAPASLKELVPDPFGPHHL 184
Cdd:COG0295    80 gepvSPCGACRQVLAE-FAGPDLEVILPngdgEVKTVTLSELLPDAFGPEDL 130
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
171-292 1.73e-21

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 87.97  E-value: 1.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 171 LKELVPDPFGPHHLDVPAVLLQAHSHKLKLArqpqASDTLTTLALAAACRSYAP-LGSPAGMALRMRDGTLSDGFAVWSV 249
Cdd:pfam08211   1 LSSYLPDAFGPKDLLIDDLLLDPQDNGLTLD----DDDPLKQAALAAANRSYAPySKCPSGVALQDGDGRVYRGRYAENA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2560235997 250 AFNPGLttaGPLQGALVKLIAQGYrDFQEIEAAVLVEQEGEPV 292
Cdd:pfam08211  77 AFNPSL---PPLQAALVDFVAGGK-DFEDIVRAVLVEKEDAKV 115
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 69-165 6.44e-19

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: 80.85  E-value: 6.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  69 KLLPHAKDMALPQASGYQVGAAALGASGRIYLGFNLELSGLPpqLCVHAEQAAVYLAVDAGEEKV-VTLATS-----ATP 142
Cdd:cd01283     2 EAALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYG--LTLCAERTAIGKAVSEGLRRYlVTWAVSdeggvWSP 79

                          90       100
                  ....*....|....*....|...
gi 2560235997 143 CGHCRQFMLEmYGAPELRVVCPE 165
Cdd:cd01283    80 CGACRQVLAE-FLPSRLYIIIDN 101
 
Name Accession Description Interval E-value
PRK09027 PRK09027
cytidine deaminase; Provisional
 45-286 1.31e-57

cytidine deaminase; Provisional


Pssm-ID: 181614 [Multi-domain]  Cd Length: 295  Bit Score: 187.73  E-value: 1.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  45 GILGKPEVEHLRLQTGLGDDAILQKLLPHAKDMALPQASGYQVGAAALGASGRIYLGFNLELSGLPPQLCVHAEQAAVYL 124
Cdd:PRK09027   31 AMLTAEQVSQLKSASGLDDDALALALLPLAAACAVTPISHFNVGAIARGVSGNFYFGANMEFAGAALQQTVHAEQSAISH 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 125 AVDAGEEKVVTLATSATPCGHCRQFMLEMYGAPELRVVCPEQAPASLKELVPDPFGPHHLDVPAVLLQAHSHKLKLARqp 204
Cdd:PRK09027  111 AWLRGEKAIADITVNYTPCGHCRQFMNELNSASDLRIHLPGRQAHTLHDYLPDAFGPKDLNITTLLMDPQDHGLALDT-- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 205 qaSDTLTTLALAAACRSYAPL-GSPAGMALRMRDGTLSDGFAVWSVAFNPGLTtagPLQGALVKLIAQGYrDFQEIEAAV 283
Cdd:PRK09027  189 --GDPLIQAALDAANRSHAPYsQSYSGVALETKDGRIYTGRYAENAAFNPSLP---PLQGALNLLNLSGE-DFSDIQRAV 262


                  ...
gi 2560235997 284 LVE 286
Cdd:PRK09027  263 LVE 265
cyt_deam_dimer TIGR01355
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ...
 51-313 1.29e-51

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: 171.94  E-value: 1.29e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  51 EVEHLRLQTGLGDDAILQKLLPHAKDMALPQASGYQVGAAALGASGRIYLGFNLELSGLPPQLCVHAEQAAVYLAVDAGE 130
Cdd:TIGR01355   9 QAQSLGTLSGLTDPKLLPKLIPKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLHHSIHAEQFLISHLALNGE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 131 EKVVTLATSATPCGHCRQFMLEMYGAPELRVVCP---EQAPASLKELVPDPFGPHHLDV--PAVLLQAHSHKLKL----- 200
Cdd:TIGR01355  89 RGLNDLAVSFAPCGHCRQFLNEIRNASSIKILLPdphNKRDMSLQSYLPDRFGPDDLLIksAPLLLEERHNCLALidpds 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 201 ARQPQASDTLTTLALAAACRSYAPLG-SPAGMALRMRDGTLSDGFAVWSVAFNPGLttaGPLQGALVKLIAQGY-RDFQE 278
Cdd:TIGR01355 169 IRNSDICSDLKQQALKAANRSYAPYSkSPSGVALKDREGKVYRGWYIESAAFNPSL---GPLQAALVDFMANGGgKGFED 245

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2560235997 279 IEAAVLVEQEGEPVAFAEFWSAALQKIAPKAQLDV 313
Cdd:TIGR01355 246 IVRAVLVEKADAKVSHEATARALLETIAPSCELKV 280
PLN02402 PLN02402
cytidine deaminase
 51-315 3.74e-41

cytidine deaminase


Pssm-ID: 178024 [Multi-domain]  Cd Length: 303  Bit Score: 145.39  E-value: 3.74e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  51 EVEHLRLQTGLGDDAILQKLLPHAKDMALPQASGYQVGAAALGASGRIYLGFNLELSGLPPQLCVHAEQAAVYLAVDAGE 130
Cdd:PLN02402   12 EAESMAKQSGLTVLQLLPSLVKSAQSLARPPISKYHVGAVGLGSSGRIFLGVNLEFPGLPLHHSVHAEQFLITNLTLNAE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 131 EKVVTLATSATPCGHCRQFMLEMYGAPELRVV---------------CPEQAPASLKELVPDPFGPHHL---DVPaVLLQ 192
Cdd:PLN02402   92 PHLKYVAVSAAPCGHCRQFFQEIRDAPDIKILitgdsnsndsyknslADSQQFEPLSCLLPHRFGPDDLldkDVP-LLLE 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 193 AHSHKLKLARQPQ-------ASDTLTTLALAAACRSYAPL-GSPAGMALRMRDGTLSDGFAVWSVAFNPGLttaGPLQGA 264
Cdd:PLN02402  171 PHHNHLSFVGDDKlpngisaSSDDLKNEALEAANKSHAPYsNCPSGVALMDCEGKVYRGSYMESAAYNPSM---GPVQAA 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2560235997 265 LVKLIAQGYRD-FQEIEAAVLVEQEGEPVAFAEFWSAALQKIAPKAQLDVVY 315
Cdd:PLN02402  248 LVAYVAGGRGGgYERIVAAVLVEKEGAVVRQEQTARLLLKEISPKCEFKVFH 299
Cdd COG0295
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ...
 63-184 1.41e-29

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: 109.47  E-value: 1.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  63 DDAILQKLLPHAKDMALPQASGYQVGAAALGASGRIYLGFNLELSGLPpqLCVHAEQAAVYLAVDAGEEKVVTLATSA-- 140
Cdd:COG0295     2 DDEELIEAAREARENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYG--LTLCAERTAIFAAVAAGEREIKAIAVVAdt 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2560235997 141 ----TPCGHCRQFMLEmYGAPELRVVCP----EQAPASLKELVPDPFGPHHL 184
Cdd:COG0295    80 gepvSPCGACRQVLAE-FAGPDLEVILPngdgEVKTVTLSELLPDAFGPEDL 130
PLN02182 PLN02182
cytidine deaminase
 60-293 1.20e-22

cytidine deaminase


Pssm-ID: 177837  Cd Length: 339  Bit Score: 96.28  E-value: 1.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  60 GLGDDAILQKLLPHAKDMALPQASGYQVGAAALGASGRIYLGFNLELSGLPPQLCVHAEQAAVYLAVDAGEEKVVTLATS 139
Cdd:PLN02182   41 GVTDPIRLPNLIRKAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLHHSIHAEQFLVTNLALNSEKDLCELAVA 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 140 --------ATPCGHCRQFMLEMYGAPELRVVCPEQAPA----SLKELVPD--PFGphhldvPAVLLQAHSHKLKLArqPQ 205
Cdd:PLN02182  121 istdgkefGTPCGHCLQFLMEMSNALDIKILSKPKHEAgsfsSLRHLLPNvlPKG------SPFLLEKRDNCLTLS--GP 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 206 ASDTLTTLALAAACR-------SYAPLG-SPAGMALRMRDGTLSDGFAVWSVAFNPGLttaGPLQGALVKLIAQGY-RDF 276
Cdd:PLN02182  193 AGEICSLDCSHLKCKalaaannSFSPYTeSPSGVALLDNDGKWYRGWYIESVASNPSF---GPVQAALVDFVARSRgKMF 269

                         250
                  ....*....|....*..
gi 2560235997 277 QEIEAAVLVEQEGEPVA 293
Cdd:PLN02182  270 NKIVQAVLVEKNNAIVS 286
dCMP_cyt_deam_2 pfam08211
Cytidine and deoxycytidylate deaminase zinc-binding region;
171-292 1.73e-21

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 429867 [Multi-domain]  Cd Length: 122  Bit Score: 87.97  E-value: 1.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997 171 LKELVPDPFGPHHLDVPAVLLQAHSHKLKLArqpqASDTLTTLALAAACRSYAP-LGSPAGMALRMRDGTLSDGFAVWSV 249
Cdd:pfam08211   1 LSSYLPDAFGPKDLLIDDLLLDPQDNGLTLD----DDDPLKQAALAAANRSYAPySKCPSGVALQDGDGRVYRGRYAENA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2560235997 250 AFNPGLttaGPLQGALVKLIAQGYrDFQEIEAAVLVEQEGEPV 292
Cdd:pfam08211  77 AFNPSL---PPLQAALVDFVAGGK-DFEDIVRAVLVEKEDAKV 115
cytidine_deaminase cd01283
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ...
 69-165 6.44e-19

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: 80.85  E-value: 6.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  69 KLLPHAKDMALPQASGYQVGAAALGASGRIYLGFNLELSGLPpqLCVHAEQAAVYLAVDAGEEKV-VTLATS-----ATP 142
Cdd:cd01283     2 EAALAAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYG--LTLCAERTAIGKAVSEGLRRYlVTWAVSdeggvWSP 79

                          90       100
                  ....*....|....*....|...
gi 2560235997 143 CGHCRQFMLEmYGAPELRVVCPE 165
Cdd:cd01283    80 CGACRQVLAE-FLPSRLYIIIDN 101
cyt_deam_tetra TIGR01354
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ...
 83-184 4.51e-18

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: 78.85  E-value: 4.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  83 SGYQVGAAALGASGRIYLGFNLELSGLPPQLCvhAEQAAVYLAVDAGEEKVVTLA------TSATPCGHCRQFMLEmYGA 156
Cdd:TIGR01354  19 SNFKVGAALLTKDGRIFTGVNVENASYPLTIC--AERSAIGKAISAGYRKFVAIAvadsadDPVSPCGACRQVLAE-FAG 95

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2560235997 157 PELRVVCPEQAPA----SLKELVPDPFGPHHL 184
Cdd:TIGR01354  96 PDTPIYMTNNDGTykvyTVGELLPFGFGPSDL 127
PRK05578 PRK05578
cytidine deaminase; Validated
 83-185 1.12e-15

cytidine deaminase; Validated


Pssm-ID: 180142 [Multi-domain]  Cd Length: 131  Bit Score: 72.25  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  83 SGYQVGAAALGASGRIYLGFNLELSGLPPQLCvhAEQAAVYLAVDAGEEKVVTLATSA------TPCGHCRQFMLEmYGA 156
Cdd:PRK05578   22 SKFPVGAALLTDDGRIYTGCNIENASYGLTNC--AERTAIFKAISEGGGRLVAIACVGetgeplSPCGRCRQVLAE-FGG 98

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2560235997 157 PELRVV-CPEQAPA---SLKELVPDPFGPHHLD 185
Cdd:PRK05578   99 PDLLVTlVAKDGPTgemTLGELLPYAFTPDDLG 131
PRK12411 PRK12411
cytidine deaminase; Provisional
 63-177 4.77e-12

cytidine deaminase; Provisional


Pssm-ID: 183511 [Multi-domain]  Cd Length: 132  Bit Score: 62.29  E-value: 4.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  63 DDAILQKLLPHAKDMALPQASGYQVGAAALGASGRIYLGFNLELSGLppQLCVHAEQAAVYLAVDAGEEKVVTLATSAT- 141
Cdd:PRK12411    2 NSKQLIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVENASY--GLCNCAERTALFKAVSEGDKEFVAIAIVADt 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2560235997 142 -----PCGHCRQFMLEMygapelrvvCPEQAPASLKELVPD 177
Cdd:PRK12411   80 krpvpPCGACRQVMVEL---------CKQDTKVYLSNLHGD 111
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
83-152 1.88e-10

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 56.93  E-value: 1.88e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2560235997  83 SGYQVGAAALGASGR-IYLGFNLELSGLPPqlCVHAEQAAVYLAVDAGE---EKVVTLATSATPCGHCRQFMLE 152
Cdd:pfam00383  20 SNFPVGAVIVKKDGEiIATGYNGENAGYDP--TIHAERNAIRQAGKRGEgvrLEGATLYVTLEPCGMCAQAIIE 91
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 74-162 2.37e-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: 51.01  E-value: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  74 AKDMALPQASGYQVGAAAL--GASGRIYLGFNLELsgLPPQLCVHAEQAAVYLAVDAGEEKVVTLATSATPCGHCRQFML 151
Cdd:cd00786     7 AADLGYAKESNFQVGACLVnkKDGGKVGRGCNIEN--AAYSMCNHAERTALFNAGSEGDTKGQMLYVALSPCGACAQLII 84

                          90
                  ....*....|.
gi 2560235997 152 eMYGAPELRVV 162
Cdd:cd00786    85 -ELGIKDVIVV 94
PRK06848 PRK06848
cytidine deaminase;
86-179 2.06e-03

cytidine deaminase;


Pssm-ID: 235875 [Multi-domain]  Cd Length: 139  Bit Score: 37.80  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560235997  86 QVGAAALGASGRIYLGFNLELSGLPPQLCvhAEQAAVYLAV---DAGEEKVVTLATSA-----------TPCGHCRQfML 151
Cdd:PRK06848   28 HVGAALRTKTGRIYAAVHLEAYVGRITVC--AEAIAIGKAIsegDHEIDTIVAVRHPKpheddreiwvvSPCGACRE-LI 104

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2560235997 152 EMYGaPELRVVCP-EQAPASLK--ELVPDPF 179
Cdd:PRK06848  105 SDYG-KNTNVIVPyNDELVKVNimELLPNKY 134
 
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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