|
Name |
Accession |
Description |
Interval |
E-value |
| cyt_deam_dimer |
TIGR01355 |
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ... |
2-287 |
8.29e-148 |
|
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: 415.77 E-value: 8.29e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 2 KFVYTPSEAAEEGVR-GPSD---LPKLIDKAMSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPLHHTIHAEQFLVT 77
Cdd:TIGR01355 2 KFVFTAEQAQSLGTLsGLTDpklLPKLIPKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLHHSIHAEQFLIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 78 NLALNSMKKLTHIAVSvtgtifGAPCGHCRQFYQEMRNAPEIEILIKRPKDGIDefMSLKSLMPERFGPDSILPEDASLL 157
Cdd:TIGR01355 82 HLALNGERGLNDLAVS------FAPCGHCRQFLNEIRNASSIKILLPDPHNKRD--MSLQSYLPDRFGPDDLLIKSAPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 158 LEQRDNSLVLSDPEEICsDPEDCSHTKCRALAAANKSYAPYSKCPSGVALIC-GGEVYKGWYIESVAYNPSLGPVEAALV 236
Cdd:TIGR01355 154 LEERHNCLALIDPDSIR-NSDICSDLKQQALKAANRSYAPYSKSPSGVALKDrEGKVYRGWYIESAAFNPSLGPLQAALV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15233626 237 DFVARGGGKEFNEITEVVLVEMKDVKVSQEATARTFLDKIAPKCDFKVLHC 287
Cdd:TIGR01355 233 DFMANGGGKGFEDIVRAVLVEKADAKVSHEATARALLETIAPSCELKVFHC 283
|
|
| PLN02402 |
PLN02402 |
cytidine deaminase |
8-288 |
3.06e-118 |
|
cytidine deaminase
Pssm-ID: 178024 [Multi-domain] Cd Length: 303 Bit Score: 341.46 E-value: 3.06e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 8 SEAAEEGVRGPSDLPKLIDKAMSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPLHHTIHAEQFLVTNLALNSMKKL 87
Cdd:PLN02402 15 SMAKQSGLTVLQLLPSLVKSAQSLARPPISKYHVGAVGLGSSGRIFLGVNLEFPGLPLHHSVHAEQFLITNLTLNAEPHL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 88 THIAVSvtgtifGAPCGHCRQFYQEMRNAPEIEILIKRPKDG----------IDEFMSLKSLMPERFGPDSILPEDASLL 157
Cdd:PLN02402 95 KYVAVS------AAPCGHCRQFFQEIRDAPDIKILITGDSNSndsyknsladSQQFEPLSCLLPHRFGPDDLLDKDVPLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 158 LEQRDNSLVLSDPEEICSDPEDCSHT-KCRALAAANKSYAPYSKCPSGVALI-CGGEVYKGWYIESVAYNPSLGPVEAAL 235
Cdd:PLN02402 169 LEPHHNHLSFVGDDKLPNGISASSDDlKNEALEAANKSHAPYSNCPSGVALMdCEGKVYRGSYMESAAYNPSMGPVQAAL 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15233626 236 VDFVARGGGKEFNEITEVVLVEMKDVKVSQEATARTFLDKIAPKCDFKVLHCY 288
Cdd:PLN02402 249 VAYVAGGRGGGYERIVAAVLVEKEGAVVRQEQTARLLLKEISPKCEFKVFHCS 301
|
|
| dCMP_cyt_deam_2 |
pfam08211 |
Cytidine and deoxycytidylate deaminase zinc-binding region; |
136-270 |
2.04e-67 |
|
Cytidine and deoxycytidylate deaminase zinc-binding region;
Pssm-ID: 429867 [Multi-domain] Cd Length: 122 Bit Score: 205.84 E-value: 2.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 136 LKSLMPERFGPDSILPEDasLLLEQRDNSLVLsdpeeicsdpEDCSHTKCRALAAANKSYAPYSKCPSGVAL-ICGGEVY 214
Cdd:pfam08211 1 LSSYLPDAFGPKDLLIDD--LLLDPQDNGLTL----------DDDDPLKQAALAAANRSYAPYSKCPSGVALqDGDGRVY 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15233626 215 KGWYIESVAYNPSLGPVEAALVDFVArgGGKEFNEITEVVLVEMKDVKVSQEATAR 270
Cdd:pfam08211 69 RGRYAENAAFNPSLPPLQAALVDFVA--GGKDFEDIVRAVLVEKEDAKVSQEATAR 122
|
|
| Cdd |
COG0295 |
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ... |
20-147 |
6.90e-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: 107.16 E-value: 6.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 20 DLPKLIDKA---MSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPLhhTIHAEQFLVTNLALNSMKKLTHIAVSVTG 96
Cdd:COG0295 2 DDEELIEAAreaRENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGL--TLCAERTAIFAAVAAGEREIKAIAVVADT 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15233626 97 TIFGAPCGHCRQFYQEMrNAPEIEILIKRPkDGIDEFMSLKSLMPERFGPD 147
Cdd:COG0295 80 GEPVSPCGACRQVLAEF-AGPDLEVILPNG-DGEVKTVTLSELLPDAFGPE 128
|
|
| cytidine_deaminase |
cd01283 |
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ... |
27-137 |
8.33e-22 |
|
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: 87.78 E-value: 8.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 27 KAMSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPlhHTIHAEQFLVTNLALNSMKKLTHIAVSVTGTIFGAPCGHC 106
Cdd:cd01283 6 AAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYG--LTLCAERTAIGKAVSEGLRRYLVTWAVSDEGGVWSPCGAC 83
|
90 100 110
....*....|....*....|....*....|.
gi 15233626 107 RQFYQEMrNAPEIEILIKrPKDGIDEFMSLK 137
Cdd:cd01283 84 RQVLAEF-LPSRLYIIID-NPKGEEFAYTLS 112
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| cyt_deam_dimer |
TIGR01355 |
cytidine deaminase, homodimeric; This homodimeric zinc metalloprotein is found in Arabidopis ... |
2-287 |
8.29e-148 |
|
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: 415.77 E-value: 8.29e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 2 KFVYTPSEAAEEGVR-GPSD---LPKLIDKAMSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPLHHTIHAEQFLVT 77
Cdd:TIGR01355 2 KFVFTAEQAQSLGTLsGLTDpklLPKLIPKAASYARAPISKFNVGAVGRGSSGRFYLGVNVEFPGLPLHHSIHAEQFLIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 78 NLALNSMKKLTHIAVSvtgtifGAPCGHCRQFYQEMRNAPEIEILIKRPKDGIDefMSLKSLMPERFGPDSILPEDASLL 157
Cdd:TIGR01355 82 HLALNGERGLNDLAVS------FAPCGHCRQFLNEIRNASSIKILLPDPHNKRD--MSLQSYLPDRFGPDDLLIKSAPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 158 LEQRDNSLVLSDPEEICsDPEDCSHTKCRALAAANKSYAPYSKCPSGVALIC-GGEVYKGWYIESVAYNPSLGPVEAALV 236
Cdd:TIGR01355 154 LEERHNCLALIDPDSIR-NSDICSDLKQQALKAANRSYAPYSKSPSGVALKDrEGKVYRGWYIESAAFNPSLGPLQAALV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15233626 237 DFVARGGGKEFNEITEVVLVEMKDVKVSQEATARTFLDKIAPKCDFKVLHC 287
Cdd:TIGR01355 233 DFMANGGGKGFEDIVRAVLVEKADAKVSHEATARALLETIAPSCELKVFHC 283
|
|
| PLN02402 |
PLN02402 |
cytidine deaminase |
8-288 |
3.06e-118 |
|
cytidine deaminase
Pssm-ID: 178024 [Multi-domain] Cd Length: 303 Bit Score: 341.46 E-value: 3.06e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 8 SEAAEEGVRGPSDLPKLIDKAMSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPLHHTIHAEQFLVTNLALNSMKKL 87
Cdd:PLN02402 15 SMAKQSGLTVLQLLPSLVKSAQSLARPPISKYHVGAVGLGSSGRIFLGVNLEFPGLPLHHSVHAEQFLITNLTLNAEPHL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 88 THIAVSvtgtifGAPCGHCRQFYQEMRNAPEIEILIKRPKDG----------IDEFMSLKSLMPERFGPDSILPEDASLL 157
Cdd:PLN02402 95 KYVAVS------AAPCGHCRQFFQEIRDAPDIKILITGDSNSndsyknsladSQQFEPLSCLLPHRFGPDDLLDKDVPLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 158 LEQRDNSLVLSDPEEICSDPEDCSHT-KCRALAAANKSYAPYSKCPSGVALI-CGGEVYKGWYIESVAYNPSLGPVEAAL 235
Cdd:PLN02402 169 LEPHHNHLSFVGDDKLPNGISASSDDlKNEALEAANKSHAPYSNCPSGVALMdCEGKVYRGSYMESAAYNPSMGPVQAAL 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15233626 236 VDFVARGGGKEFNEITEVVLVEMKDVKVSQEATARTFLDKIAPKCDFKVLHCY 288
Cdd:PLN02402 249 VAYVAGGRGGGYERIVAAVLVEKEGAVVRQEQTARLLLKEISPKCEFKVFHCS 301
|
|
| PLN02182 |
PLN02182 |
cytidine deaminase |
2-287 |
9.65e-113 |
|
cytidine deaminase
Pssm-ID: 177837 Cd Length: 339 Bit Score: 328.94 E-value: 9.65e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 2 KFVYTPSEAAEEGVRGPSDLPKLIDKAMSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPLHHTIHAEQFLVTNLAL 81
Cdd:PLN02182 29 KFVFTANEAAAEGVTDPIRLPNLIRKAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLHHSIHAEQFLVTNLAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 82 NSMKKLTHIAV--SVTGTIFGAPCGHCRQFYQEMRNAPEIEILIKrPKDGIDEFMSLKSLMPerfgpdSILPEDASLLLE 159
Cdd:PLN02182 109 NSEKDLCELAVaiSTDGKEFGTPCGHCLQFLMEMSNALDIKILSK-PKHEAGSFSSLRHLLP------NVLPKGSPFLLE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 160 QRDNSLVLSDPE-EICSdpEDCSHTKCRALAAANKSYAPYSKCPSGVALICG-GEVYKGWYIESVAYNPSLGPVEAALVD 237
Cdd:PLN02182 182 KRDNCLTLSGPAgEICS--LDCSHLKCKALAAANNSFSPYTESPSGVALLDNdGKWYRGWYIESVASNPSFGPVQAALVD 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15233626 238 FVARGGGKEFNEITEVVLVEMKDVKVSQEATARTFLDKI-APKCDFKVLHC 287
Cdd:PLN02182 260 FVARSRGKMFNKIVQAVLVEKNNAIVSQERTAKIILDTIaAPNCDFKVFHC 310
|
|
| dCMP_cyt_deam_2 |
pfam08211 |
Cytidine and deoxycytidylate deaminase zinc-binding region; |
136-270 |
2.04e-67 |
|
Cytidine and deoxycytidylate deaminase zinc-binding region;
Pssm-ID: 429867 [Multi-domain] Cd Length: 122 Bit Score: 205.84 E-value: 2.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 136 LKSLMPERFGPDSILPEDasLLLEQRDNSLVLsdpeeicsdpEDCSHTKCRALAAANKSYAPYSKCPSGVAL-ICGGEVY 214
Cdd:pfam08211 1 LSSYLPDAFGPKDLLIDD--LLLDPQDNGLTL----------DDDDPLKQAALAAANRSYAPYSKCPSGVALqDGDGRVY 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15233626 215 KGWYIESVAYNPSLGPVEAALVDFVArgGGKEFNEITEVVLVEMKDVKVSQEATAR 270
Cdd:pfam08211 69 RGRYAENAAFNPSLPPLQAALVDFVA--GGKDFEDIVRAVLVEKEDAKVSQEATAR 122
|
|
| PRK09027 |
PRK09027 |
cytidine deaminase; Provisional |
24-273 |
3.14e-58 |
|
cytidine deaminase; Provisional
Pssm-ID: 181614 [Multi-domain] Cd Length: 295 Bit Score: 188.12 E-value: 3.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 24 LIDKAMSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPLHHTIHAEQFLVTNLALNSMKKLTHIAVSVTgtifgaPC 103
Cdd:PRK09027 56 LLPLAAACAVTPISHFNVGAIARGVSGNFYFGANMEFAGAALQQTVHAEQSAISHAWLRGEKAIADITVNYT------PC 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 104 GHCRQFYQEMRNAPEIEI-LIKRPKdgidefMSLKSLMPERFGpdsilPED---ASLLLEQRDNSLVL--SDPEEIcsdp 177
Cdd:PRK09027 130 GHCRQFMNELNSASDLRIhLPGRQA------HTLHDYLPDAFG-----PKDlniTTLLMDPQDHGLALdtGDPLIQ---- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 178 edcshtkcRALAAANKSYAPYSKCPSGVALICG-GEVYKGWYIESVAYNPSLGPVEAALVdfVARGGGKEFNEITEVVLV 256
Cdd:PRK09027 195 --------AALDAANRSHAPYSQSYSGVALETKdGRIYTGRYAENAAFNPSLPPLQGALN--LLNLSGEDFSDIQRAVLV 264
|
250
....*....|....*..
gi 15233626 257 EMKDVKVSQEATARTFL 273
Cdd:PRK09027 265 EKADAKLSQWDATQATL 281
|
|
| Cdd |
COG0295 |
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ... |
20-147 |
6.90e-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: 107.16 E-value: 6.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 20 DLPKLIDKA---MSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPLhhTIHAEQFLVTNLALNSMKKLTHIAVSVTG 96
Cdd:COG0295 2 DDEELIEAAreaRENAYAPYSKFPVGAALLTEDGRIYTGCNVENASYGL--TLCAERTAIFAAVAAGEREIKAIAVVADT 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15233626 97 TIFGAPCGHCRQFYQEMrNAPEIEILIKRPkDGIDEFMSLKSLMPERFGPD 147
Cdd:COG0295 80 GEPVSPCGACRQVLAEF-AGPDLEVILPNG-DGEVKTVTLSELLPDAFGPE 128
|
|
| cytidine_deaminase |
cd01283 |
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ... |
27-137 |
8.33e-22 |
|
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: 87.78 E-value: 8.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 27 KAMSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPlhHTIHAEQFLVTNLALNSMKKLTHIAVSVTGTIFGAPCGHC 106
Cdd:cd01283 6 AAAEFAYAPYSNFTVGAALLTKDGRIFTGVNVENASYG--LTLCAERTAIGKAVSEGLRRYLVTWAVSDEGGVWSPCGAC 83
|
90 100 110
....*....|....*....|....*....|.
gi 15233626 107 RQFYQEMrNAPEIEILIKrPKDGIDEFMSLK 137
Cdd:cd01283 84 RQVLAEF-LPSRLYIIID-NPKGEEFAYTLS 112
|
|
| cyt_deam_tetra |
TIGR01354 |
cytidine deaminase, homotetrameric; This small, homotetrameric zinc metalloprotein is found in ... |
27-147 |
4.34e-20 |
|
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: 83.86 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 27 KAMSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPLhhTIHAEQFLVTNLALNSMKKLTHIAVSVTGTIFGAPCGHC 106
Cdd:TIGR01354 9 EARKNAYAPYSNFKVGAALLTKDGRIFTGVNVENASYPL--TICAERSAIGKAISAGYRKFVAIAVADSADDPVSPCGAC 86
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15233626 107 RQFYQEMrNAPEIEILIKRPKDGIdEFMSLKSLMPERFGPD 147
Cdd:TIGR01354 87 RQVLAEF-AGPDTPIYMTNNDGTY-KVYTVGELLPFGFGPS 125
|
|
| PRK05578 |
PRK05578 |
cytidine deaminase; Validated |
20-147 |
3.08e-15 |
|
cytidine deaminase; Validated
Pssm-ID: 180142 [Multi-domain] Cd Length: 131 Bit Score: 70.71 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 20 DLPKLIDKAMSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPLhhTIHAEQFLVTNLALNSMKKLTHIA-VSVTGTI 98
Cdd:PRK05578 5 ELIEAAIEASEKAYAPYSKFPVGAALLTDDGRIYTGCNIENASYGL--TNCAERTAIFKAISEGGGRLVAIAcVGETGEP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15233626 99 FgAPCGHCRQFYQEMrNAPEIEILIKRpKDGIDEFMSLKSLMPERFGPD 147
Cdd:PRK05578 83 L-SPCGRCRQVLAEF-GGPDLLVTLVA-KDGPTGEMTLGELLPYAFTPD 128
|
|
| dCMP_cyt_deam_1 |
pfam00383 |
Cytidine and deoxycytidylate deaminase zinc-binding region; |
27-114 |
7.40e-10 |
|
Cytidine and deoxycytidylate deaminase zinc-binding region;
Pssm-ID: 395307 [Multi-domain] Cd Length: 100 Bit Score: 55.00 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 27 KAMSLARaPVSTFKVGAVGLTSSGEV-FLGVNVEFPNLPlhHTIHAEQFLVTNLALNSMK---KLTHIAVSVTgtifgaP 102
Cdd:pfam00383 11 KAAKRAY-PYSNFPVGAVIVKKDGEIiATGYNGENAGYD--PTIHAERNAIRQAGKRGEGvrlEGATLYVTLE------P 81
|
90
....*....|..
gi 15233626 103 CGHCRQFYQEMR 114
Cdd:pfam00383 82 CGMCAQAIIESG 93
|
|
| PRK12411 |
PRK12411 |
cytidine deaminase; Provisional |
21-144 |
8.83e-06 |
|
cytidine deaminase; Provisional
Pssm-ID: 183511 [Multi-domain] Cd Length: 132 Bit Score: 44.57 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 21 LPKLIDKAMSLARAPVSTFKVGAVGLTSSGEVFLGVNVEfpNLPLHHTIHAEQFLVTNLALNSMKKLTHIAVSVTGTIFG 100
Cdd:PRK12411 6 LIQEAIEARKQAYVPYSKFQVGAALLTQDGKVYRGCNVE--NASYGLCNCAERTALFKAVSEGDKEFVAIAIVADTKRPV 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15233626 101 APCGHCRQFYQEMrNAPEIEILIKRPKDGIDEfMSLKSLMPERF 144
Cdd:PRK12411 84 PPCGACRQVMVEL-CKQDTKVYLSNLHGDVQE-TTVGELLPGAF 125
|
|
| cytidine_deaminase |
cd01283 |
Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the ... |
186-247 |
1.79e-05 |
|
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: 43.10 E-value: 1.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233626 186 RALAAANKSYAPYSKCPSGVALIC-GGEVYKGWYIESVAYNPSLGPVEAALVDFVARGGGKEF 247
Cdd:cd01283 3 AALAAAEFAYAPYSNFTVGAALLTkDGRIFTGVNVENASYGLTLCAERTAIGKAVSEGLRRYL 65
|
|
| Cdd |
COG0295 |
Cytidine deaminase [Nucleotide transport and metabolism]; Cytidine deaminase is part of the ... |
186-256 |
4.07e-05 |
|
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: 42.44 E-value: 4.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233626 186 RALAAANKSYAPYSKCPSGVALICG-GEVYKGWYIESVAYNPSLGPVEAALVDFVARGGGkefnEITEVVLV 256
Cdd:COG0295 9 AAREARENAYAPYSKFPVGAALLTEdGRIYTGCNVENASYGLTLCAERTAIFAAVAAGER----EIKAIAVV 76
|
|
| PRK05578 |
PRK05578 |
cytidine deaminase; Validated |
187-251 |
5.94e-05 |
|
cytidine deaminase; Validated
Pssm-ID: 180142 [Multi-domain] Cd Length: 131 Bit Score: 41.82 E-value: 5.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233626 187 ALAAANKSYAPYSKCPSGVALICG-GEVYKGWYIESVAYNPSLGPVEAALVDFVARGGGKeFNEIT 251
Cdd:PRK05578 10 AIEASEKAYAPYSKFPVGAALLTDdGRIYTGCNIENASYGLTNCAERTAIFKAISEGGGR-LVAIA 74
|
|
| cytidine_deaminase-like |
cd00786 |
Cytidine and deoxycytidylate deaminase zinc-binding region. The family contains cytidine ... |
22-108 |
3.40e-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: 36.37 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233626 22 PKLIDKAMSLARAPVSTFKVGAVGLTSSGEVFLGVNVEFPNLPLHHTIHAEQFLVTNLALNSMKKLTHIAVSVTgtifga 101
Cdd:cd00786 1 MTEALKAADLGYAKESNFQVGACLVNKKDGGKVGRGCNIENAAYSMCNHAERTALFNAGSEGDTKGQMLYVALS------ 74
|
....*..
gi 15233626 102 PCGHCRQ 108
Cdd:cd00786 75 PCGACAQ 81
|
|
| |
