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Conserved domains on  [gi|322710269|gb|EFZ01844|]
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Cytidine deaminase [Metarhizium robertsii ARSEF 23]

Protein Classification

cytidine/deoxycytidylate deaminase family protein( domain architecture ID 10788416)

cytidine/deoxycytidylate deaminase family protein similar to deoxycytidylate deaminase that catalyzes the deamination of dCMP to dUMP, providing the nucleotide substrate for thymidylate synthase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
221-369 1.89e-59

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


:

Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 189.28  E-value: 1.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 221 RPGWDTYFMALASLAAQRSNCMKRRVGCVLVgRERRVISTGYNGTPRGIRNCADGGCPRCNEGNSSGVGLATCLCIHAEE 300
Cdd:COG2131    5 RPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVGCLREKLGIPSGERGECCRTVHAEQ 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 301 NALLEAGRERIR-DGSVLYCDTCPCLTCSIKICQVGIGEVVYAHGYsMDKEAAAVFSQAGVKLRQFIPPP 369
Cdd:COG2131   84 NAILQAARHGVStEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDY-PDELAKELLKEAGVEVRQLELEE 152
CoaE super family cl30785
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 1-23 6.15e-04

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


The actual alignment was detected with superfamily member COG0237:

Pssm-ID: 440007  Cd Length: 193  Bit Score: 40.44  E-value: 6.15e-04
                         10        20
                 ....*....|....*....|...
gi 322710269   1 MLIGICGGICSGKKTVAQYLVEH 23
Cdd:COG0237    2 LIIGLTGGIGSGKSTVARMFAEL 24
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
221-369 1.89e-59

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 189.28  E-value: 1.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 221 RPGWDTYFMALASLAAQRSNCMKRRVGCVLVgRERRVISTGYNGTPRGIRNCADGGCPRCNEGNSSGVGLATCLCIHAEE 300
Cdd:COG2131    5 RPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVGCLREKLGIPSGERGECCRTVHAEQ 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 301 NALLEAGRERIR-DGSVLYCDTCPCLTCSIKICQVGIGEVVYAHGYsMDKEAAAVFSQAGVKLRQFIPPP 369
Cdd:COG2131   84 NAILQAARHGVStEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDY-PDELAKELLKEAGVEVRQLELEE 152
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 225-355 9.51e-56

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: 179.01  E-value: 9.51e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 225 DTYFMALASLAAQRSNCMKRRVGCVLVgRERRVISTGYNGTPRGIRNCADGGCPRCNEgnSSGVGLATCLCIHAEENALL 304
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIV-KDKRIISTGYNGSPSGLPHCAEVGCERDDL--PSGEDQKCCRTVHAEQNAIL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 322710269 305 EAGRERIR-DGSVLYCDTCPCLTCSIKICQVGIGEVVYAHGYSMDKEAAAVF 355
Cdd:cd01286   78 QAARHGVSlEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDDPAAAEL 129
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
224-342 5.14e-26

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 100.45  E-value: 5.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269  224 WDTYFMALASLAAQRS-NCMKRRVGCVLVGRERRVISTGYNGTPRGIRNcadggcprcnegnssgvglatclCIHAEENA 302
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAGYDP-----------------------TIHAERNA 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 322710269  303 LLEAGRERIR---DGSVLYCDTCPCLTCSIKICQVGIGEVVYA 342
Cdd:pfam00383  58 IRQAGKRGEGvrlEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 225-372 3.12e-22

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 92.13  E-value: 3.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 225 DTYFMALASLAAQRSNCMKRRVGCVLVgRERRVISTGYNGTPRGIRNCADggcpRCNEG---NSSGVGLA---------- 291
Cdd:PHA02588   3 DSTYLQIAYLVSQESKCVSWKVGAVIE-KNGRIISTGYNGTPAGGVNCCD----HANEQgwlDDEGKLKKehrpehsaws 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 292 TCLCIHAEENALLEAGRERIR-DGSVLYCDTCPCLTCSIKICQVGIGEVVYAHGYSMDK-EAAAVFSQAGVKLRQFipPP 369
Cdd:PHA02588  78 SKNEIHAELNAILFAARNGISiEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYDRNGpGWDDILRKSGIEVIQI--PK 155


                 ...
gi 322710269 370 NGL 372
Cdd:PHA02588 156 EEL 158
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 1-23 6.15e-04

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440007  Cd Length: 193  Bit Score: 40.44  E-value: 6.15e-04
                         10        20
                 ....*....|....*....|...
gi 322710269   1 MLIGICGGICSGKKTVAQYLVEH 23
Cdd:COG0237    2 LIIGLTGGIGSGKSTVARMFAEL 24
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 2-24 4.84e-03

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 37.50  E-value: 4.84e-03
                         10        20
                 ....*....|....*....|...
gi 322710269   2 LIGICGGICSGKKTVAQYLVEHH 24
Cdd:cd02022    1 IIGLTGGIGSGKSTVAKLLKELG 23
 
Name Accession Description Interval E-value
ComEB COG2131
Deoxycytidylate deaminase [Nucleotide transport and metabolism];
221-369 1.89e-59

Deoxycytidylate deaminase [Nucleotide transport and metabolism];


Pssm-ID: 441734 [Multi-domain]  Cd Length: 154  Bit Score: 189.28  E-value: 1.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 221 RPGWDTYFMALASLAAQRSNCMKRRVGCVLVgRERRVISTGYNGTPRGIRNCADGGCPRCNEGNSSGVGLATCLCIHAEE 300
Cdd:COG2131    5 RPSWDEYFMEIAKLVALRSTCLRRQVGAVIV-KDKRILATGYNGAPSGLPHCDEVGCLREKLGIPSGERGECCRTVHAEQ 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 301 NALLEAGRERIR-DGSVLYCDTCPCLTCSIKICQVGIGEVVYAHGYsMDKEAAAVFSQAGVKLRQFIPPP 369
Cdd:COG2131   84 NAILQAARHGVStEGATLYVTHFPCLECAKMIIQAGIKRVVYLEDY-PDELAKELLKEAGVEVRQLELEE 152
deoxycytidylate_deaminase cd01286
Deoxycytidylate deaminase domain. Deoxycytidylate deaminase catalyzes the deamination of dCMP ...
 225-355 9.51e-56

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: 179.01  E-value: 9.51e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 225 DTYFMALASLAAQRSNCMKRRVGCVLVgRERRVISTGYNGTPRGIRNCADGGCPRCNEgnSSGVGLATCLCIHAEENALL 304
Cdd:cd01286    1 DEYFMAIARLAALRSTCPRRQVGAVIV-KDKRIISTGYNGSPSGLPHCAEVGCERDDL--PSGEDQKCCRTVHAEQNAIL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 322710269 305 EAGRERIR-DGSVLYCDTCPCLTCSIKICQVGIGEVVYAHGYSMDKEAAAVF 355
Cdd:cd01286   78 QAARHGVSlEGATLYVTLFPCIECAKLIIQAGIKKVVYAEPYDDDDPAAAEL 129
dCMP_cyt_deam_1 pfam00383
Cytidine and deoxycytidylate deaminase zinc-binding region;
224-342 5.14e-26

Cytidine and deoxycytidylate deaminase zinc-binding region;


Pssm-ID: 395307 [Multi-domain]  Cd Length: 100  Bit Score: 100.45  E-value: 5.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269  224 WDTYFMALASLAAQRS-NCMKRRVGCVLVGRERRVISTGYNGTPRGIRNcadggcprcnegnssgvglatclCIHAEENA 302
Cdd:pfam00383   1 WDEYFMRLALKAAKRAyPYSNFPVGAVIVKKDGEIIATGYNGENAGYDP-----------------------TIHAERNA 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 322710269  303 LLEAGRERIR---DGSVLYCDTCPCLTCSIKICQVGIGEVVYA 342
Cdd:pfam00383  58 IRQAGKRGEGvrlEGATLYVTLEPCGMCAQAIIESGIKRVVFG 100
cd PHA02588
deoxycytidylate deaminase; Provisional
 225-372 3.12e-22

deoxycytidylate deaminase; Provisional


Pssm-ID: 222894 [Multi-domain]  Cd Length: 168  Bit Score: 92.13  E-value: 3.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 225 DTYFMALASLAAQRSNCMKRRVGCVLVgRERRVISTGYNGTPRGIRNCADggcpRCNEG---NSSGVGLA---------- 291
Cdd:PHA02588   3 DSTYLQIAYLVSQESKCVSWKVGAVIE-KNGRIISTGYNGTPAGGVNCCD----HANEQgwlDDEGKLKKehrpehsaws 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 292 TCLCIHAEENALLEAGRERIR-DGSVLYCDTCPCLTCSIKICQVGIGEVVYAHGYSMDK-EAAAVFSQAGVKLRQFipPP 369
Cdd:PHA02588  78 SKNEIHAELNAILFAARNGISiEGATMYVTASPCPDCAKAIAQSGIKKLVYCEKYDRNGpGWDDILRKSGIEVIQI--PK 155


                 ...
gi 322710269 370 NGL 372
Cdd:PHA02588 156 EEL 158
nucleoside_deaminase cd01285
Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn ...
 229-343 1.36e-07

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: 49.54  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 229 MALASLAAQRSNCMKRR-VGCVLVGRERRVISTGYNGTPRgirncadggcprcnEGNSSGvglatclciHAEENALLEAG 307
Cdd:cd01285    1 MRLAIELARKALAEGEVpFGAVIVDDDGKVIARGHNRVEQ--------------DGDPTA---------HAEIVAIRNAA 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 322710269 308 RER---IRDGSVLYCdTC-PCLTCSIKICQVGIGEVVYAH 343
Cdd:cd01285   58 RRLgsyLLSGCTLYT-TLePCPMCAGALLWARIKRVVYGA 96
cytidine_deaminase-like cd00786
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ...
 226-342 2.33e-07

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: 48.32  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 226 TYFMALASLAAQRSNcmKRRVGCVLVGRErrvistGYNGTPRGirncadggcprCNEGNSSGVGlatclCIHAEENALLE 305
Cdd:cd00786    2 TEALKAADLGYAKES--NFQVGACLVNKK------DGGKVGRG-----------CNIENAAYSM-----CNHAERTALFN 57

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 322710269 306 AGRERIRDGSVLYCDTCPCLTCSIKICQVGIGEVVYA 342
Cdd:cd00786   58 AGSEGDTKGQMLYVALSPCGACAQLIIELGIKDVIVV 94
Riboflavin_deaminase-reductase cd01284
Riboflavin-specific deaminase. Riboflavin biosynthesis protein RibD ...
 246-343 5.45e-06

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: 44.92  E-value: 5.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322710269 246 VGCVLVGRERRVISTGYngtprgirncadggcprcnegnSSGVGLAtclciHAEENALLEAGRERIRdGSVLYCDTCPCL 325
Cdd:cd01284   21 VGCVIVDDDGEIVGEGY----------------------HRKAGGP-----HAEVNALASAGEKLAR-GATLYVTLEPCS 72

                         90       100
                 ....*....|....*....|....
gi 322710269 326 ------TCSIKICQVGIGEVVYAH 343
Cdd:cd01284   73 hhgktpPCVDAIIEAGIKRVVVGV 96
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 1-23 6.15e-04

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440007  Cd Length: 193  Bit Score: 40.44  E-value: 6.15e-04
                         10        20
                 ....*....|....*....|...
gi 322710269   1 MLIGICGGICSGKKTVAQYLVEH 23
Cdd:COG0237    2 LIIGLTGGIGSGKSTVARMFAEL 24
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 2-24 4.84e-03

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 37.50  E-value: 4.84e-03
                         10        20
                 ....*....|....*....|...
gi 322710269   2 LIGICGGICSGKKTVAQYLVEHH 24
Cdd:cd02022    1 IIGLTGGIGSGKSTVAKLLKELG 23
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 2-22 6.95e-03

Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK), catalyzes the reversible phosphoryl transfer from ATP to uridine or cytidine to yield UMP or CMP. In the primidine nucleotide-salvage pathway, this enzyme combined with nucleoside diphosphate kinases further phosphorylates UMP and CMP to form UTP and CTP. This kinase also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs such as 5-flurrouridine and cyclopentenyl-cytidine.


Pssm-ID: 238981 [Multi-domain]  Cd Length: 198  Bit Score: 37.53  E-value: 6.95e-03
                         10        20
                 ....*....|....*....|.
gi 322710269   2 LIGICGGICSGKKTVAQYLVE 22
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIE 21
 
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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