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Conserved domains on  [gi|16416451|dbj|BAB70662|]
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tRNA-nucleotidyltransferase [Homo sapiens]

Protein Classification

CCA tRNA nucleotidyltransferase( domain architecture ID 11427658)

[cytidine(C)-cytidine(C)-adenosine (A)] tRNA nucleotidyltransferase adds the CCA sequence one nucleotide at a time onto the 3' end of tRNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
43-428 2.26e-91

tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and biogenesis]; tRNA nucleotidyltransferase/poly(A) polymerase is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 440382 [Multi-domain]  Cd Length: 391  Bit Score: 281.70  E-value: 2.26e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  43 EGLKSLTELFVKENHELRIAGGAVRDLLNGVKPQDIDFATTATPTQMKEMFQSAgirmINNR--GEKHGTITARLHEENF 120
Cdd:COG0617   4 PNALKVLEALEEAGFEAYLVGGAVRDLLLGRPPKDIDIVTVATPEEVAALFRKA----LRTVpvGRDFGTVTVVFGGEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451 121 EITTLRIDV-TTDGRHAEVEFTTDWQKDAERRDLTINSMFLG-FDGTLFDYFNGYEDLKNKKVRFVGHAKQRIQEDYLRI 198
Cdd:COG0617  80 EVATARTERyYGDGRRPFVEFGDTLEEDLARRDFTINALAYDlNDGELIDPFGGLADLEARVIRTVGDPEERFREDPLRI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451 199 LRYFRFYGR----IvdkpgdhDPETLEAIAENAKGLAGISGERIWVELKKILVGNHVNHLIHLIYDLDVAPYIG------ 268
Cdd:COG0617 160 LRAVRFAARlgftI-------EPETLAAIREMAGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVLAlrlaal 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451 269 LPANASLEEFDKVSKNVDGFSPKPVTLLASLFKvqddvtkldlRLKIAKEEKNLGLFIVKNRKDLIKATDSSDplKPYQD 348
Cdd:COG0617 233 LHDLGKPATREDGLPTFHGHEEAGAELAEALLK----------RLRLPNRERKLVRELVELHLRFHGLGELRD--SAVRR 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451 349 FIIDSRE--PDATTRVCELLKYQGEHCLLKEM--QQWSIPPFPVSGHDIRKVGISSGKEIGALLQQLREQWKKSGYQMEK 424
Cdd:COG0617 301 LLERGPEalEDLLLLRENGLEYPELQERLAELleAAWRRFQPPVDGEDLMALGLKPGPEIGEILRALREAVLDGGIPNRR 380

                ....
gi 16416451 425 DELL 428
Cdd:COG0617 381 EEAL 384
 
Name Accession Description Interval E-value
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
43-428 2.26e-91

tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and biogenesis]; tRNA nucleotidyltransferase/poly(A) polymerase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440382 [Multi-domain]  Cd Length: 391  Bit Score: 281.70  E-value: 2.26e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  43 EGLKSLTELFVKENHELRIAGGAVRDLLNGVKPQDIDFATTATPTQMKEMFQSAgirmINNR--GEKHGTITARLHEENF 120
Cdd:COG0617   4 PNALKVLEALEEAGFEAYLVGGAVRDLLLGRPPKDIDIVTVATPEEVAALFRKA----LRTVpvGRDFGTVTVVFGGEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451 121 EITTLRIDV-TTDGRHAEVEFTTDWQKDAERRDLTINSMFLG-FDGTLFDYFNGYEDLKNKKVRFVGHAKQRIQEDYLRI 198
Cdd:COG0617  80 EVATARTERyYGDGRRPFVEFGDTLEEDLARRDFTINALAYDlNDGELIDPFGGLADLEARVIRTVGDPEERFREDPLRI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451 199 LRYFRFYGR----IvdkpgdhDPETLEAIAENAKGLAGISGERIWVELKKILVGNHVNHLIHLIYDLDVAPYIG------ 268
Cdd:COG0617 160 LRAVRFAARlgftI-------EPETLAAIREMAGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVLAlrlaal 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451 269 LPANASLEEFDKVSKNVDGFSPKPVTLLASLFKvqddvtkldlRLKIAKEEKNLGLFIVKNRKDLIKATDSSDplKPYQD 348
Cdd:COG0617 233 LHDLGKPATREDGLPTFHGHEEAGAELAEALLK----------RLRLPNRERKLVRELVELHLRFHGLGELRD--SAVRR 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451 349 FIIDSRE--PDATTRVCELLKYQGEHCLLKEM--QQWSIPPFPVSGHDIRKVGISSGKEIGALLQQLREQWKKSGYQMEK 424
Cdd:COG0617 301 LLERGPEalEDLLLLRENGLEYPELQERLAELleAAWRRFQPPVDGEDLMALGLKPGPEIGEILRALREAVLDGGIPNRR 380

                ....
gi 16416451 425 DELL 428
Cdd:COG0617 381 EEAL 384
PRK13299 PRK13299
tRNA CCA-pyrophosphorylase; Provisional
38-251 1.68e-48

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237339 [Multi-domain]  Cd Length: 394  Bit Score: 170.02  E-value: 1.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451   38 QSLFTEGLKSLTELfvKEN-HELRIAGGAVRDLLNGVKPQDIDFATTATPTQMKEMFQSA---GIrminnrgeKHGTITA 113
Cdd:PRK13299   3 PSEFQKALPILEKI--KEAgFEAYFVGGSVRDYLLGRPIHDVDIATSAYPEEVKAIFPRTvdvGI--------EHGTVLV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  114 RLHEENFEITTLRI-DVTTDGRH-AEVEFTTDWQKDAERRDLTINSMFLGFDGTLFDYFNGYEDLKNKKVRFVGHAKQRI 191
Cdd:PRK13299  73 LENGEEYEVTTFRTeSEYVDYRRpSEVTFVRSLEEDLKRRDFTINAIAMDENGEIIDLFDGLEDLKNRLIRAVGNAEERF 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16416451  192 QEDYLRILRYFRFygriVDKPG-DHDPETLEAIAENAKGLAGISGERIWVELKKILVGNHV 251
Cdd:PRK13299 153 QEDALRMMRAVRF----ASQLGfDLETETFEAMKTQAPLLEKISVERIFVEFEKLLLGPFW 209
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
42-178 5.03e-48

Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This Class II group is comprised mainly of eubacterial and eukaryotic enzymes and includes Bacillus stearothermophilus CCAase, Escherichia coli poly(A) polymerase I, human mitochondrial CCAase, and Saccharomyces cerevisiae CCAase (CCA1). CCA-adding enzymes have a single catalytic pocket, which recognizes both ATP and CTP substrates. Included in this subgroup are CC- and A-adding enzymes from various ancient species of bacteria such as Aquifex aeolicus; these enzymes collaborate to add CCA to tRNAs. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are fairly well conserved in this family. Escherichia coli CCAase is related to this group but has not been included in this alignment as this enzyme lacks the N-terminal helix conserved in the remainder of the NT superfamily.


Pssm-ID: 143388 [Multi-domain]  Cd Length: 139  Bit Score: 160.84  E-value: 5.03e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  42 TEGLKSLTELFVKE-NHELRIAGGAVRDLLNGVKPQDIDFATTA-TPTQMKEMFQSAGIRMInNRGEKHGTITARLHEEN 119
Cdd:cd05398   1 TPELLKLLRELKKAlGYEAYLVGGAVRDLLLGRPPKDIDIATDAdGPEFAEALFKKIGGRVV-GLGEEFGTATVVINGLT 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16416451 120 FEITTLRIDVTTD--GRHAEVEFTTDwqKDAERRDLTINSMFLG-FDGTLFDYFNGYEDLKN 178
Cdd:cd05398  80 IDVATLRTETYTDpgRRPPVVGFTIE--EDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
59-182 1.04e-39

Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, such as Poly(A) polymerase, which adds the poly (A) tail to mRNA EC:2.7.7.19. This family also includes the tRNA nucleotidyltransferase that adds the CCA to the 3' of the tRNA EC:2.7.7.25. This family is part of the nucleotidyltransferase superfamily.


Pssm-ID: 396348 [Multi-domain]  Cd Length: 126  Bit Score: 138.57  E-value: 1.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451    59 LRIAGGAVRDLLNGVKPQDIDFATTATPTQMKEMFQSAGIRMInNRGEKHGTITARLHEENFEITTLRID-VTTDGRHA- 136
Cdd:pfam01743   1 LYIVGGAVRDLLLGKTPKDVDIATDATPEQVATLFRRRRIVHL-LSGIEFGTIHVIFGNQILEVATFRIEfDESDFRNPr 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 16416451   137 EVEFTTDWQKDAERRDLTINSMFLG-FDGTLFDYFNGYEDLKNKKVR 182
Cdd:pfam01743  80 SEEYTGTLEEDAKRRDFTINALAYNpNSGEVIDYFGGIKDLKSGVIR 126
 
Name Accession Description Interval E-value
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
43-428 2.26e-91

tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and biogenesis]; tRNA nucleotidyltransferase/poly(A) polymerase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440382 [Multi-domain]  Cd Length: 391  Bit Score: 281.70  E-value: 2.26e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  43 EGLKSLTELFVKENHELRIAGGAVRDLLNGVKPQDIDFATTATPTQMKEMFQSAgirmINNR--GEKHGTITARLHEENF 120
Cdd:COG0617   4 PNALKVLEALEEAGFEAYLVGGAVRDLLLGRPPKDIDIVTVATPEEVAALFRKA----LRTVpvGRDFGTVTVVFGGEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451 121 EITTLRIDV-TTDGRHAEVEFTTDWQKDAERRDLTINSMFLG-FDGTLFDYFNGYEDLKNKKVRFVGHAKQRIQEDYLRI 198
Cdd:COG0617  80 EVATARTERyYGDGRRPFVEFGDTLEEDLARRDFTINALAYDlNDGELIDPFGGLADLEARVIRTVGDPEERFREDPLRI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451 199 LRYFRFYGR----IvdkpgdhDPETLEAIAENAKGLAGISGERIWVELKKILVGNHVNHLIHLIYDLDVAPYIG------ 268
Cdd:COG0617 160 LRAVRFAARlgftI-------EPETLAAIREMAGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVLAlrlaal 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451 269 LPANASLEEFDKVSKNVDGFSPKPVTLLASLFKvqddvtkldlRLKIAKEEKNLGLFIVKNRKDLIKATDSSDplKPYQD 348
Cdd:COG0617 233 LHDLGKPATREDGLPTFHGHEEAGAELAEALLK----------RLRLPNRERKLVRELVELHLRFHGLGELRD--SAVRR 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451 349 FIIDSRE--PDATTRVCELLKYQGEHCLLKEM--QQWSIPPFPVSGHDIRKVGISSGKEIGALLQQLREQWKKSGYQMEK 424
Cdd:COG0617 301 LLERGPEalEDLLLLRENGLEYPELQERLAELleAAWRRFQPPVDGEDLMALGLKPGPEIGEILRALREAVLDGGIPNRR 380

                ....
gi 16416451 425 DELL 428
Cdd:COG0617 381 EEAL 384
PRK13299 PRK13299
tRNA CCA-pyrophosphorylase; Provisional
38-251 1.68e-48

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237339 [Multi-domain]  Cd Length: 394  Bit Score: 170.02  E-value: 1.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451   38 QSLFTEGLKSLTELfvKEN-HELRIAGGAVRDLLNGVKPQDIDFATTATPTQMKEMFQSA---GIrminnrgeKHGTITA 113
Cdd:PRK13299   3 PSEFQKALPILEKI--KEAgFEAYFVGGSVRDYLLGRPIHDVDIATSAYPEEVKAIFPRTvdvGI--------EHGTVLV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  114 RLHEENFEITTLRI-DVTTDGRH-AEVEFTTDWQKDAERRDLTINSMFLGFDGTLFDYFNGYEDLKNKKVRFVGHAKQRI 191
Cdd:PRK13299  73 LENGEEYEVTTFRTeSEYVDYRRpSEVTFVRSLEEDLKRRDFTINAIAMDENGEIIDLFDGLEDLKNRLIRAVGNAEERF 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16416451  192 QEDYLRILRYFRFygriVDKPG-DHDPETLEAIAENAKGLAGISGERIWVELKKILVGNHV 251
Cdd:PRK13299 153 QEDALRMMRAVRF----ASQLGfDLETETFEAMKTQAPLLEKISVERIFVEFEKLLLGPFW 209
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
42-178 5.03e-48

Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This Class II group is comprised mainly of eubacterial and eukaryotic enzymes and includes Bacillus stearothermophilus CCAase, Escherichia coli poly(A) polymerase I, human mitochondrial CCAase, and Saccharomyces cerevisiae CCAase (CCA1). CCA-adding enzymes have a single catalytic pocket, which recognizes both ATP and CTP substrates. Included in this subgroup are CC- and A-adding enzymes from various ancient species of bacteria such as Aquifex aeolicus; these enzymes collaborate to add CCA to tRNAs. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are fairly well conserved in this family. Escherichia coli CCAase is related to this group but has not been included in this alignment as this enzyme lacks the N-terminal helix conserved in the remainder of the NT superfamily.


Pssm-ID: 143388 [Multi-domain]  Cd Length: 139  Bit Score: 160.84  E-value: 5.03e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  42 TEGLKSLTELFVKE-NHELRIAGGAVRDLLNGVKPQDIDFATTA-TPTQMKEMFQSAGIRMInNRGEKHGTITARLHEEN 119
Cdd:cd05398   1 TPELLKLLRELKKAlGYEAYLVGGAVRDLLLGRPPKDIDIATDAdGPEFAEALFKKIGGRVV-GLGEEFGTATVVINGLT 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16416451 120 FEITTLRIDVTTD--GRHAEVEFTTDwqKDAERRDLTINSMFLG-FDGTLFDYFNGYEDLKN 178
Cdd:cd05398  80 IDVATLRTETYTDpgRRPPVVGFTIE--EDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
59-182 1.04e-39

Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, such as Poly(A) polymerase, which adds the poly (A) tail to mRNA EC:2.7.7.19. This family also includes the tRNA nucleotidyltransferase that adds the CCA to the 3' of the tRNA EC:2.7.7.25. This family is part of the nucleotidyltransferase superfamily.


Pssm-ID: 396348 [Multi-domain]  Cd Length: 126  Bit Score: 138.57  E-value: 1.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451    59 LRIAGGAVRDLLNGVKPQDIDFATTATPTQMKEMFQSAGIRMInNRGEKHGTITARLHEENFEITTLRID-VTTDGRHA- 136
Cdd:pfam01743   1 LYIVGGAVRDLLLGKTPKDVDIATDATPEQVATLFRRRRIVHL-LSGIEFGTIHVIFGNQILEVATFRIEfDESDFRNPr 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 16416451   137 EVEFTTDWQKDAERRDLTINSMFLG-FDGTLFDYFNGYEDLKNKKVR 182
Cdd:pfam01743  80 SEEYTGTLEEDAKRRDFTINALAYNpNSGEVIDYFGGIKDLKSGVIR 126
pcnB PRK11623
poly(A) polymerase I; Provisional
54-246 3.06e-20

poly(A) polymerase I; Provisional


Pssm-ID: 236939 [Multi-domain]  Cd Length: 472  Bit Score: 92.51  E-value: 3.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451   54 KENHELRIAGGAVRDLLNGVKPQDIDFATTATPTQMKEMFQSAgiRMINNRgekhgtitARLHE-----ENFEITTLRid 128
Cdd:PRK11623  64 KAGYEAYLVGGGVRDLLLGKKPKDFDVTTNATPEQVRKLFRNC--RLVGRR--------FRLAHvmfgpEIIEVATFR-- 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  129 vttdGRHAEVEFTTDW------------------QKDAERRDLTINSMFLGF-DGTLFDYFNGYEDLKNKKVRFVGHAKQ 189
Cdd:PRK11623 132 ----GHHEGNESDRNTsqrgqngmllrdnifgsiEEDAQRRDFTINSLYYSVaDFTVRDYVGGMKDLKEGVIRLIGNPET 207
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16416451  190 RIQEDYLRILRYFRFYGRIVDKPgdhDPETLEAIAENAKGLAGISGERIWVELKKIL 246
Cdd:PRK11623 208 RYREDPVRMLRAVRFAAKLDMRI---SPETAEPIPRLATLLNDIPPARLFEESLKLL 261
PRK13296 PRK13296
CCA tRNA nucleotidyltransferase;
58-246 7.52e-15

CCA tRNA nucleotidyltransferase;


Pssm-ID: 106256 [Multi-domain]  Cd Length: 360  Bit Score: 75.41  E-value: 7.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451   58 ELRIAGGAVRDLLNGVKPQDIDFATT-ATPTQMkemFQSAGIRMINNrgekhgtITARLHEENFEITTL--RIDVTTDGR 134
Cdd:PRK13296   2 KFYLVGGAVRDMLLGITPKDKDWVVVgATEDEM---LANGFIKIAAN-------FPVFIHPQTKQEYALarSEKKTASGY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  135 HA-EVEFTTD--WQKDAERRDLTINSMFLGFDGTLFDYFNGYEDLKNKKVRfvgHAKQRIQEDYLRILRYFRFYGRIVDK 211
Cdd:PRK13296  72 HGfEVNFSKYitLEDDLKRRDLTINSIAIDQNNKVIDPFNGQADLQNRILR---HTSIAFIEDPLRVVRLARFKAQLSNF 148
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 16416451  212 PGDHDPETLEAIAENAKG--LAGISGERIWVELKKIL 246
Cdd:PRK13296 149 NFSIAQEMLALIKELVKTgeLNHLTRERLHIEFVKAL 185
cca PRK10885
multifunctional CCA addition/repair protein;
63-246 9.11e-14

multifunctional CCA addition/repair protein;


Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 72.58  E-value: 9.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451   63 GGAVRDLLNGVKPQDIDFATT-ATPTQMkemfQSAGIRMINNrgekhgTITARLHEENFEITTL-RIDVTTdGR------ 134
Cdd:PRK10885   7 GGAVRDALLGLPVKDRDWVVVgATPEEM----LAQGYQQVGK------DFPVFLHPKTHEEYALaRTERKS-GRgytgft 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  135 -HAEVEFTTdwQKDAERRDLTINSMFLGFDGTLFDYFNGYEDLKNKKVRFVGHAkqrIQEDYLRILRYFRFYGRIVDKPG 213
Cdd:PRK10885  76 cYAAPDVTL--EEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPA---FAEDPLRVLRVARFAARFAHLGF 150
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 16416451  214 DHDPETLE---AIAENAKgLAGISGERIWVELKKIL 246
Cdd:PRK10885 151 RIAPETLAlmrEMVASGE-LDALTPERVWKETERAL 185
PRK13297 PRK13297
tRNA CCA-pyrophosphorylase; Provisional
61-286 5.43e-13

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 139469 [Multi-domain]  Cd Length: 364  Bit Score: 70.02  E-value: 5.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451   61 IAGGAVRDLLNGVKPQDIDFATT-ATPTQM-KEMFQSAGirminnrgekhGTITARLHEENFEITTLRIDVTTDGR-HAE 137
Cdd:PRK13297  16 IVGGAVRDALLGLPAGDRDWVVVgATPEDMaRRGFIPVG-----------GDFPVFLHPRTKEEYALARTERKSGRgYKG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  138 VEFTT----DWQKDAERRDLTINSMFLGFDGTLFDYFNGYEDLKNKKVRFVGHAkqrIQEDYLRILRYFRFYGRIvdkpG 213
Cdd:PRK13297  85 FTFYTgadvTLEQDLQRRDLTVNAIARTPQGELVDPLDGVADVRARVLRHVGEA---FAEDPVRILRLGRFAARF----G 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  214 DHD--PETLE---AIAENAKGLAGISgERIWVELKKILVGNHVNHLihliydLDVAPYIGLPANA--SLEEFDKVSKNVD 286
Cdd:PRK13297 158 DFSiaPETMQlcrRMVEAGEADALVP-ERVWKEVSRGLMAQAPSRM------LDVLARAGALARVmpELHDDAAVRAEID 230
PRK13298 PRK13298
tRNA CCA-pyrophosphorylase; Provisional
63-246 5.96e-13

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237338 [Multi-domain]  Cd Length: 417  Bit Score: 70.14  E-value: 5.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451   63 GGAVRDLLNGVKPQDIDFATT-ATPTQM-KEMFQSAGirminnrgekhGTITARLHEENFEITTL-----RIDVTTDGRH 135
Cdd:PRK13298   7 GGAVRDSLLNLPVKDKDWVVVgGTPKILlSINFQQVG-----------KDFPVFLHPETHEEYALarterKSGVGYTGFI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16416451  136 AEVEFTTDWQKDAERRDLTINSMFLGFDGTLFDYFNGYEDLKNKKVRFVGHAkqrIQEDYLRILRYFRFYGRIVDKPGDH 215
Cdd:PRK13298  76 TDTSSDVTLEEDLIRRDLTINAIAQDENGNYIDPFQGKKDIQLRLLRHVSES---FIEDPLRVLRVARFAALLVHLGFKI 152
                        170       180       190
                 ....*....|....*....|....*....|...
gi 16416451  216 DPETLE--AIAENAKGLAGISGERIWVELKKIL 246
Cdd:PRK13298 153 AKETMIlmCIMVKKHELLYLTPERIWNETEKAL 185
PolyA_pol_RNAbd pfam12627
Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA ...
216-270 1.66e-08

Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA and SrmB binding motifs on polymerase A.


Pssm-ID: 463648 [Multi-domain]  Cd Length: 64  Bit Score: 50.95  E-value: 1.66e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16416451   216 DPETLEAIAENAKGLAGISGERIWVELKKILVGNHVNHLIHLIYDLDVAPYIgLP 270
Cdd:pfam12627   5 EPETREAIRKLAPLLKKISPERIFEELLKLLLSGHPERGLELLRETGLLEYL-FP 58
PHA01806 PHA01806
hypothetical protein
61-97 1.78e-03

hypothetical protein


Pssm-ID: 222838  Cd Length: 200  Bit Score: 39.48  E-value: 1.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 16416451   61 IAGGAVRDLLNGVKPQDIDFATTA-TPTQMKEMFQSAG 97
Cdd:PHA01806  40 LAGGAARDLMHGAEPKDIDIALYGmDDRQAELLIGCIL 77
NT_Pol-beta-like cd05397
Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins; This ...
42-83 4.82e-03

Nucleotidyltransferase (NT) domain of DNA polymerase beta and similar proteins; This superfamily includes the NT domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of Class I and Class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, and Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. The Escherichia coli CCA-adding enzyme belongs to this superfamily but is not included as this enzyme lacks the N-terminal helix conserved in the remainder of the superfamily. In the majority of the Pol beta-like superfamily NTs, two carboxylates, Dx[D/E], together with a third more distal carboxylate coordinate two divalent metal cations that are essential for catalysis. These divalent metal ions are involved in a two-metal ion mechanism of nucleotide addition. Two of the three catalytic carboxylates are found in Rel-Spo enzymes, with the second carboxylate of the DXD motif missing. Evidence supports a single-cation synthetase mechanism for Rel-Spo enzymes.


Pssm-ID: 143387 [Multi-domain]  Cd Length: 49  Bit Score: 34.99  E-value: 4.82e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 16416451  42 TEGLKSLTELFVKE--NHELRIAGGAVRDLLngVKPQDIDFATT 83
Cdd:cd05397   1 EELLDIIKERLKKLvpGYEIVVYGSLVRGLL--KKSSDIDLACV 42
 
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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