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Conserved domains on  [gi|1002166894|ref|YP_009230336|]
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tRNA nucleotidyltransferase [Acidianus tailed spindle virus]

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 ...
 12-433 3.38e-81

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: 255.89  E-value: 3.38e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  12 EILEYIKKLGtNNVYLVGGTVRDILTGKKPKDLDFVVT-DFDKALKLAEEMNLPIHEdGIRFGVLRI---GDKYDFASLR 87
Cdd:COG0617     8 KVLEALEEAG-FEAYLVGGAVRDLLLGRPPKDIDIVTVaTPEEVAALFRKALRTVPV-GRDFGTVTVvfgGEKIEVATAR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  88 KERYDTVS-KPTVELGASLEEDARRRDFTINDLYgkivgIHGNKlvMEILDFNNGLEDLRNHTLRFVGNPQERIDEDPLR 166
Cdd:COG0617    86 TERYYGDGrRPFVEFGDTLEEDLARRDFTINALA-----YDLND--GELIDPFGGLADLEARVIRTVGDPEERFREDPLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 167 ILRGIRFIL-YGYKMSPDQLEIMKKNISKLDKLPIERIRDEILKILK-VNPAEGFKLLDEFGLLKYLYgehyealkntyh 244
Cdd:COG0617   159 ILRAVRFAArLGFTIEPETLAAIREMAGLLDRLSAERVWDELLKLLLsPHPSRGLELLRETGLLEVLA------------ 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 245 dnrgahhgedviehtyealkrLRnpdietiLAVIYHDVGKPYTRseKNGKIMFIGHAKKSAEIAKELMKRLKLPNNIIKD 324
Cdd:COG0617   227 ---------------------LR-------LAALLHDLGKPATR--EDGLPTFHGHEEAGAELAEALLKRLRLPNRERKL 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 325 VTNLIEMHMDF-NLAQNNEKNQAQLITKLMSLYY------WNPEKVREIYNKLVELSHADTgsenilnmsnRITEPIITG 397
Cdd:COG0617   277 VRELVELHLRFhGLGELRDSAVRRLLERGPEALEdllllrENGLEYPELQERLAELLEAAW----------RRFQPPVDG 346

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1002166894 398 EEIANTFGVSGNILKHLKERAYTLQLLGY---DKDEIMK 433
Cdd:COG0617   347 EDLMALGLKPGPEIGEILRALREAVLDGGipnRREEALL 385
 
Name Accession Description Interval E-value
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
 12-433 3.38e-81

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: 255.89  E-value: 3.38e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  12 EILEYIKKLGtNNVYLVGGTVRDILTGKKPKDLDFVVT-DFDKALKLAEEMNLPIHEdGIRFGVLRI---GDKYDFASLR 87
Cdd:COG0617     8 KVLEALEEAG-FEAYLVGGAVRDLLLGRPPKDIDIVTVaTPEEVAALFRKALRTVPV-GRDFGTVTVvfgGEKIEVATAR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  88 KERYDTVS-KPTVELGASLEEDARRRDFTINDLYgkivgIHGNKlvMEILDFNNGLEDLRNHTLRFVGNPQERIDEDPLR 166
Cdd:COG0617    86 TERYYGDGrRPFVEFGDTLEEDLARRDFTINALA-----YDLND--GELIDPFGGLADLEARVIRTVGDPEERFREDPLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 167 ILRGIRFIL-YGYKMSPDQLEIMKKNISKLDKLPIERIRDEILKILK-VNPAEGFKLLDEFGLLKYLYgehyealkntyh 244
Cdd:COG0617   159 ILRAVRFAArLGFTIEPETLAAIREMAGLLDRLSAERVWDELLKLLLsPHPSRGLELLRETGLLEVLA------------ 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 245 dnrgahhgedviehtyealkrLRnpdietiLAVIYHDVGKPYTRseKNGKIMFIGHAKKSAEIAKELMKRLKLPNNIIKD 324
Cdd:COG0617   227 ---------------------LR-------LAALLHDLGKPATR--EDGLPTFHGHEEAGAELAEALLKRLRLPNRERKL 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 325 VTNLIEMHMDF-NLAQNNEKNQAQLITKLMSLYY------WNPEKVREIYNKLVELSHADTgsenilnmsnRITEPIITG 397
Cdd:COG0617   277 VRELVELHLRFhGLGELRDSAVRRLLERGPEALEdllllrENGLEYPELQERLAELLEAAW----------RRFQPPVDG 346

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1002166894 398 EEIANTFGVSGNILKHLKERAYTLQLLGY---DKDEIMK 433
Cdd:COG0617   347 EDLMALGLKPGPEIGEILRALREAVLDGGipnRREEALL 385
PRK13299 PRK13299
tRNA CCA-pyrophosphorylase; Provisional
 13-370 1.76e-37

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237339 [Multi-domain]  Cd Length: 394  Bit Score: 140.75  E-value: 1.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  13 ILEYIKKLGTNnVYLVGGTVRDILTGKKPKDLDfVVTD---------FDKALklaeemnlPIhedGIRFG---VLRIGDK 80
Cdd:PRK13299   12 ILEKIKEAGFE-AYFVGGSVRDYLLGRPIHDVD-IATSaypeevkaiFPRTV--------DV---GIEHGtvlVLENGEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  81 YDFASLRKE-RYDTVSKPT-VELGASLEEDARRRDFTIN----DLYGkivgihgnklvmEILDFNNGLEDLRNHTLRFVG 154
Cdd:PRK13299   79 YEVTTFRTEsEYVDYRRPSeVTFVRSLEEDLKRRDFTINaiamDENG------------EIIDLFDGLEDLKNRLIRAVG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 155 NPQERIDEDPLRILRGIRFI--LyGYKMSPDQLEIMKKNISKLDKLPIERIRDEILKILK-VNPAEGFKLLDEFGLLKYL 231
Cdd:PRK13299  147 NAEERFQEDALRMMRAVRFAsqL-GFDLETETFEAMKTQAPLLEKISVERIFVEFEKLLLgPFWRKGLKLLIETGLYNYL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 232 YGehyealkntyhdnrgahhgedvIEHTYEALKRL------RNPDIETILAVIYHDVGKpytrsekngkimfighakksa 305
Cdd:PRK13299  226 PG----------------------LKGKEENLLKLtqllwfSFETSEQAWAALLISLKI--------------------- 262

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002166894 306 EIAKELMKRLKLPNNIIKDVTNLIEMhmdFNLAQNNEKNQAQL-------------ITKLMSLYYwNPEKVREIYNKL 370
Cdd:PRK13299  263 ENIKSFLKAWKLSNKFIKDVVKLLAL---YALRSERSWEKLDLyqygkeiallaedLRQAQGLSV-DEEAIQELYQAL 336
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
 13-240 1.02e-32

poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as plasmid copy number protein). These enzymes sequentially add adenosine nucleotides to the 3' end of RNAs, targeting them for degradation by the cell. This was originally described for anti-sense RNAs, but was later demonstrated for mRNAs as well. Members of this family are as yet limited to the gamma- and beta-proteobacteria, with putative members in the Chlamydiacae and spirochetes. This family has homology to tRNA nucleotidyltransferase (cca).


Pssm-ID: 130997 [Multi-domain]  Cd Length: 410  Bit Score: 127.99  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  13 ILEYIKKLGTNnVYLVGGTVRDILTGKKPKDLDfVVTD---------FDKALKLAEEMNLpIHedgIRFGVlRIGDKYDF 83
Cdd:TIGR01942  21 VVERLKGAGYQ-AYIVGGAVRDLLLGIEPKDFD-VVTSatpeevrklFRNSRIVGRRFRL-VH---VSFGR-QIIEVATF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  84 ASLRKERYDTVSKPTVE-LGASLEEDARRRDFTINDLYGKIVGihgnklvMEILDFNNGLEDLRNHTLRFVGNPQERIDE 162
Cdd:TIGR01942  94 RSGHKSSVNAEGRILKDnVYGTLEEDAWRRDFTVNALYYDPSR-------EVIIDYVGGMEDLKNRRLRLIGDPRSRYQE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 163 DPLRILRGIRF-ILYGYKMSPDQLEIMKKNISKLDKLPIERIRDEILKILKV-NPAEGFKLLDEFGLLKYLYGEHYEALK 240
Cdd:TIGR01942 167 DPVRMLRALRFsVKLEFTIDESTARPIRESAPLLKGIPPARLFEEILKLLFSgRSAALFRMLCGYQLLEPLFPSVAYALR 246
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
 11-147 7.18e-31

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: 115.77  E-value: 7.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  11 PEILEYIKKLGTN---NVYLVGGTVRDILTGKKPKDLDFVVTD--FDKALKLAEEMNLPIHEDGIRFGVLRI---GDKYD 82
Cdd:cd05398     2 PELLKLLRELKKAlgyEAYLVGGAVRDLLLGRPPKDIDIATDAdgPEFAEALFKKIGGRVVGLGEEFGTATVvinGLTID 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002166894  83 FASLRKERYDTVSKPTVELGASLEEDARRRDFTINDLYgkiVGIHGNklvmEILDFNNGLEDLRN 147
Cdd:cd05398    82 VATLRTETYTDPGRRPPVVGFTIEEDLLRRDFTINAMA---YDLDDG----ELIDPFGGLKDLEN 139
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
 26-151 4.09e-20

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: 85.79  E-value: 4.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  26 YLVGGTVRDILTGKKPKDLDFVVTDFDKALKLAEEMNLPIH-EDGIRFG---VLRIGDKYDFASLRKERY--DTVSKPTV 99
Cdd:pfam01743   2 YIVGGAVRDLLLGKTPKDVDIATDATPEQVATLFRRRRIVHlLSGIEFGtihVIFGNQILEVATFRIEFDesDFRNPRSE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002166894 100 ELGASLEEDARRRDFTINDLYGKIVgiHGnklvmEILDFNNGLEDLRNHTLR 151
Cdd:pfam01743  82 EYTGTLEEDAKRRDFTINALAYNPN--SG-----EVIDYFGGIKDLKSGVIR 126
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 250-335 1.29e-03

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 38.82  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  250 HHGEDVIEHTYEALKRLRNPDIETIL-AVIYHDVGKPYTRSEKNGKIM-FIGHAKKSAEIAKElmkrLKLPNNIIKDVTN 327
Cdd:smart00471   7 EHSLRVAQLAAALAEELGLLDIELLLlAALLHDIGKPGTPDSFLVKTSvLEDHHFIGAEILLE----EEEPRILEEILRT 82


                   ....*...
gi 1002166894  328 LIEMHMDF 335
Cdd:smart00471  83 AILSHHER 90
 
Name Accession Description Interval E-value
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
 12-433 3.38e-81

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: 255.89  E-value: 3.38e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  12 EILEYIKKLGtNNVYLVGGTVRDILTGKKPKDLDFVVT-DFDKALKLAEEMNLPIHEdGIRFGVLRI---GDKYDFASLR 87
Cdd:COG0617     8 KVLEALEEAG-FEAYLVGGAVRDLLLGRPPKDIDIVTVaTPEEVAALFRKALRTVPV-GRDFGTVTVvfgGEKIEVATAR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  88 KERYDTVS-KPTVELGASLEEDARRRDFTINDLYgkivgIHGNKlvMEILDFNNGLEDLRNHTLRFVGNPQERIDEDPLR 166
Cdd:COG0617    86 TERYYGDGrRPFVEFGDTLEEDLARRDFTINALA-----YDLND--GELIDPFGGLADLEARVIRTVGDPEERFREDPLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 167 ILRGIRFIL-YGYKMSPDQLEIMKKNISKLDKLPIERIRDEILKILK-VNPAEGFKLLDEFGLLKYLYgehyealkntyh 244
Cdd:COG0617   159 ILRAVRFAArLGFTIEPETLAAIREMAGLLDRLSAERVWDELLKLLLsPHPSRGLELLRETGLLEVLA------------ 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 245 dnrgahhgedviehtyealkrLRnpdietiLAVIYHDVGKPYTRseKNGKIMFIGHAKKSAEIAKELMKRLKLPNNIIKD 324
Cdd:COG0617   227 ---------------------LR-------LAALLHDLGKPATR--EDGLPTFHGHEEAGAELAEALLKRLRLPNRERKL 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 325 VTNLIEMHMDF-NLAQNNEKNQAQLITKLMSLYY------WNPEKVREIYNKLVELSHADTgsenilnmsnRITEPIITG 397
Cdd:COG0617   277 VRELVELHLRFhGLGELRDSAVRRLLERGPEALEdllllrENGLEYPELQERLAELLEAAW----------RRFQPPVDG 346

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1002166894 398 EEIANTFGVSGNILKHLKERAYTLQLLGY---DKDEIMK 433
Cdd:COG0617   347 EDLMALGLKPGPEIGEILRALREAVLDGGipnRREEALL 385
PRK13299 PRK13299
tRNA CCA-pyrophosphorylase; Provisional
 13-370 1.76e-37

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237339 [Multi-domain]  Cd Length: 394  Bit Score: 140.75  E-value: 1.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  13 ILEYIKKLGTNnVYLVGGTVRDILTGKKPKDLDfVVTD---------FDKALklaeemnlPIhedGIRFG---VLRIGDK 80
Cdd:PRK13299   12 ILEKIKEAGFE-AYFVGGSVRDYLLGRPIHDVD-IATSaypeevkaiFPRTV--------DV---GIEHGtvlVLENGEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  81 YDFASLRKE-RYDTVSKPT-VELGASLEEDARRRDFTIN----DLYGkivgihgnklvmEILDFNNGLEDLRNHTLRFVG 154
Cdd:PRK13299   79 YEVTTFRTEsEYVDYRRPSeVTFVRSLEEDLKRRDFTINaiamDENG------------EIIDLFDGLEDLKNRLIRAVG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 155 NPQERIDEDPLRILRGIRFI--LyGYKMSPDQLEIMKKNISKLDKLPIERIRDEILKILK-VNPAEGFKLLDEFGLLKYL 231
Cdd:PRK13299  147 NAEERFQEDALRMMRAVRFAsqL-GFDLETETFEAMKTQAPLLEKISVERIFVEFEKLLLgPFWRKGLKLLIETGLYNYL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 232 YGehyealkntyhdnrgahhgedvIEHTYEALKRL------RNPDIETILAVIYHDVGKpytrsekngkimfighakksa 305
Cdd:PRK13299  226 PG----------------------LKGKEENLLKLtqllwfSFETSEQAWAALLISLKI--------------------- 262

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002166894 306 EIAKELMKRLKLPNNIIKDVTNLIEMhmdFNLAQNNEKNQAQL-------------ITKLMSLYYwNPEKVREIYNKL 370
Cdd:PRK13299  263 ENIKSFLKAWKLSNKFIKDVVKLLAL---YALRSERSWEKLDLyqygkeiallaedLRQAQGLSV-DEEAIQELYQAL 336
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
 13-240 1.02e-32

poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as plasmid copy number protein). These enzymes sequentially add adenosine nucleotides to the 3' end of RNAs, targeting them for degradation by the cell. This was originally described for anti-sense RNAs, but was later demonstrated for mRNAs as well. Members of this family are as yet limited to the gamma- and beta-proteobacteria, with putative members in the Chlamydiacae and spirochetes. This family has homology to tRNA nucleotidyltransferase (cca).


Pssm-ID: 130997 [Multi-domain]  Cd Length: 410  Bit Score: 127.99  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  13 ILEYIKKLGTNnVYLVGGTVRDILTGKKPKDLDfVVTD---------FDKALKLAEEMNLpIHedgIRFGVlRIGDKYDF 83
Cdd:TIGR01942  21 VVERLKGAGYQ-AYIVGGAVRDLLLGIEPKDFD-VVTSatpeevrklFRNSRIVGRRFRL-VH---VSFGR-QIIEVATF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  84 ASLRKERYDTVSKPTVE-LGASLEEDARRRDFTINDLYGKIVGihgnklvMEILDFNNGLEDLRNHTLRFVGNPQERIDE 162
Cdd:TIGR01942  94 RSGHKSSVNAEGRILKDnVYGTLEEDAWRRDFTVNALYYDPSR-------EVIIDYVGGMEDLKNRRLRLIGDPRSRYQE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 163 DPLRILRGIRF-ILYGYKMSPDQLEIMKKNISKLDKLPIERIRDEILKILKV-NPAEGFKLLDEFGLLKYLYGEHYEALK 240
Cdd:TIGR01942 167 DPVRMLRALRFsVKLEFTIDESTARPIRESAPLLKGIPPARLFEEILKLLFSgRSAALFRMLCGYQLLEPLFPSVAYALR 246
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
 11-147 7.18e-31

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: 115.77  E-value: 7.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  11 PEILEYIKKLGTN---NVYLVGGTVRDILTGKKPKDLDFVVTD--FDKALKLAEEMNLPIHEDGIRFGVLRI---GDKYD 82
Cdd:cd05398     2 PELLKLLRELKKAlgyEAYLVGGAVRDLLLGRPPKDIDIATDAdgPEFAEALFKKIGGRVVGLGEEFGTATVvinGLTID 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002166894  83 FASLRKERYDTVSKPTVELGASLEEDARRRDFTINDLYgkiVGIHGNklvmEILDFNNGLEDLRN 147
Cdd:cd05398    82 VATLRTETYTDPGRRPPVVGFTIEEDLLRRDFTINAMA---YDLDDG----ELIDPFGGLKDLEN 139
cca PRK10885
multifunctional CCA addition/repair protein;
24-319 1.62e-26

multifunctional CCA addition/repair protein;


Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 110.71  E-value: 1.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  24 NVYLVGGTVRDILTGKKPKDLDFVVTDFDkalklAEEM-NLPIHEDGIRFGVL---RIGDKYDFAslRKER--------- 90
Cdd:PRK10885    2 KIYLVGGAVRDALLGLPVKDRDWVVVGAT-----PEEMlAQGYQQVGKDFPVFlhpKTHEEYALA--RTERksgrgytgf 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  91 ---YDtvskPTVelgaSLEEDARRRDFTIN----DLYGKIVgihgnklvmeilDFNNGLEDLRNHTLRFVGnpqERIDED 163
Cdd:PRK10885   75 tcyAA----PDV----TLEEDLIRRDLTINamaqDDDGELI------------DPYGGQRDLEARLLRHVS---PAFAED 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 164 PLRILR----GIRFILYGYKMSPDQLEIMKKNIS--KLDKLPIERIRDEILKILK-VNPAEGFKLLDEFGLLKYLYGEhY 236
Cdd:PRK10885  132 PLRVLRvarfAARFAHLGFRIAPETLALMREMVAsgELDALTPERVWKETERALMeRNPQVFFQVLRDCGALAVLLPE-I 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 237 EALKNTyhDNRGAHHGE-DVIEHTYEALKR--LRNPDIETILAVIYHDVGKPYTRSEKNGKimFIGHAKKSAEIAKELMK 313
Cdd:PRK10885  211 DALFGV--PQPAKWHPEiDTGIHTLMVLDQaaKLSPSLDVRFAALCHDLGKGLTPPEEWPR--HHGHEPRGVKLVEQLCQ 286


                  ....*.
gi 1002166894 314 RLKLPN 319
Cdd:PRK10885  287 RLRVPN 292
pcnB PRK11623
poly(A) polymerase I; Provisional
 26-232 5.03e-23

poly(A) polymerase I; Provisional


Pssm-ID: 236939 [Multi-domain]  Cd Length: 472  Bit Score: 100.98  E-value: 5.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  26 YLVGGTVRDILTGKKPKDLDfVVTDF--DKALKLAEEMNLPihedGIRFGVLRI---GDKYDFASLRKERYDTVSKPTVE 100
Cdd:PRK11623   70 YLVGGGVRDLLLGKKPKDFD-VTTNAtpEQVRKLFRNCRLV----GRRFRLAHVmfgPEIIEVATFRGHHEGNESDRNTS 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 101 LGA------------SLEEDARRRDFTINDLYGKIVGihgnklvMEILDFNNGLEDLRNHTLRFVGNPQERIDEDPLRIL 168
Cdd:PRK11623  145 QRGqngmllrdnifgSIEEDAQRRDFTINSLYYSVAD-------FTVRDYVGGMKDLKEGVIRLIGNPETRYREDPVRML 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002166894 169 RGIRFIL-YGYKMSPDQLEIMKKNISKLDKLPIERIRDEILKILKV-NPAEGFKLLDEFGLLKYLY 232
Cdd:PRK11623  218 RAVRFAAkLDMRISPETAEPIPRLATLLNDIPPARLFEESLKLLQAgYGYETYKLLCEYHLFQPLF 283
PRK13298 PRK13298
tRNA CCA-pyrophosphorylase; Provisional
 25-335 2.45e-22

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237338 [Multi-domain]  Cd Length: 417  Bit Score: 98.65  E-value: 2.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  25 VYLVGGTVRDILTGKKPKDLDFVVTDFDKalklaEEM-NLPIHEDGIRFGV-LRIGDKYDFASLRKER----------YD 92
Cdd:PRK13298    3 IYLVGGAVRDSLLNLPVKDKDWVVVGGTP-----KILlSINFQQVGKDFPVfLHPETHEEYALARTERksgvgytgfiTD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  93 TVSKPTvelgasLEEDARRRDFTIN----DLYGKivgihgnklvmeILDFNNGLEDLRNHTLRFVgnpQERIDEDPLRIL 168
Cdd:PRK13298   78 TSSDVT------LEEDLIRRDLTINaiaqDENGN------------YIDPFQGKKDIQLRLLRHV---SESFIEDPLRVL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 169 RGIRFIL----YGYKMSPDQLEIMKKNISK--LDKLPIERIRDEILKILKV-NPAEGFKLLDEFGLLKYLYGEHYEALKN 241
Cdd:PRK13298  137 RVARFAAllvhLGFKIAKETMILMCIMVKKheLLYLTPERIWNETEKALKTdNPHVYFQVLYECNALKFLFPEIDFLYEK 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 242 TYHDNRGAHHgedvIEHTYEALKRLRN-----PDIETILAVIYHDVGKPYTRSEKNGKIMFIGHAKKSAEIAKELMKRLK 316
Cdd:PRK13298  217 PYFLNSFFKK----FNLGNYILMGLSKiskltKDIDIRFSYLCQFLGSMIPINQIKRNYKKIFFDKYAASLIKNLCKRFK 292

                         330
                  ....*....|....*....
gi 1002166894 317 LPNNiIKDVTNLIEMHMDF 335
Cdd:PRK13298  293 IPSY-IRNIAVLNTGFYFF 310
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
 26-151 4.09e-20

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: 85.79  E-value: 4.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  26 YLVGGTVRDILTGKKPKDLDFVVTDFDKALKLAEEMNLPIH-EDGIRFG---VLRIGDKYDFASLRKERY--DTVSKPTV 99
Cdd:pfam01743   2 YIVGGAVRDLLLGKTPKDVDIATDATPEQVATLFRRRRIVHlLSGIEFGtihVIFGNQILEVATFRIEFDesDFRNPRSE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002166894 100 ELGASLEEDARRRDFTINDLYGKIVgiHGnklvmEILDFNNGLEDLRNHTLR 151
Cdd:pfam01743  82 EYTGTLEEDAKRRDFTINALAYNPN--SG-----EVIDYFGGIKDLKSGVIR 126
PRK13297 PRK13297
tRNA CCA-pyrophosphorylase; Provisional
 24-228 1.20e-15

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 139469 [Multi-domain]  Cd Length: 364  Bit Score: 78.11  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  24 NVYLVGGTVRDILTGKKPKDLDFVVTDfdkalKLAEEMN----LPIHEDGIRFGVLRIGDKYDFASLRKERYDTVSKPTV 99
Cdd:PRK13297   13 QVYIVGGAVRDALLGLPAGDRDWVVVG-----ATPEDMArrgfIPVGGDFPVFLHPRTKEEYALARTERKSGRGYKGFTF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 100 ELGA--SLEEDARRRDFTINDLYGKIVGihgnklvmEILDFNNGLEDLRNHTLRFVGnpqERIDEDPLRILRGIRFI--L 175
Cdd:PRK13297   88 YTGAdvTLEQDLQRRDLTVNAIARTPQG--------ELVDPLDGVADVRARVLRHVG---EAFAEDPVRILRLGRFAarF 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002166894 176 YGYKMSPDQLEIMKKNIS--KLDKLPIERIRDEILK-ILKVNPAEGFKLLDEFGLL 228
Cdd:PRK13297  157 GDFSIAPETMQLCRRMVEagEADALVPERVWKEVSRgLMAQAPSRMLDVLARAGAL 212
PRK13296 PRK13296
CCA tRNA nucleotidyltransferase;
26-232 1.27e-15

CCA tRNA nucleotidyltransferase;


Pssm-ID: 106256 [Multi-domain]  Cd Length: 360  Bit Score: 78.10  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  26 YLVGGTVRDILTGKKPKDLDFVV-----TDFDKA--LKLAEEMNLPIHEDgirfgvlrigDKYDFASLRKERYDTVSKPT 98
Cdd:PRK13296    4 YLVGGAVRDMLLGITPKDKDWVVvgateDEMLANgfIKIAANFPVFIHPQ----------TKQEYALARSEKKTASGYHG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  99 VELGAS----LEEDARRRDFTINDlygkiVGIHGNKlvmEILDFNNGLEDLRNHTLRfvgNPQERIDEDPLRILRGIRFI 174
Cdd:PRK13296   74 FEVNFSkyitLEDDLKRRDLTINS-----IAIDQNN---KVIDPFNGQADLQNRILR---HTSIAFIEDPLRVVRLARFK 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002166894 175 L----YGYKMSPDQLEIMKKNIS--KLDKLPIERIRDEILKILKvNPAEGFKLLDEFGLLKYLY 232
Cdd:PRK13296  143 AqlsnFNFSIAQEMLALIKELVKtgELNHLTRERLHIEFVKALN-NPKIFFTTLKELEALKIIF 205
PolyA_pol_RNAbd pfam12627
Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA ...
 177-239 1.03e-11

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: 59.81  E-value: 1.03e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002166894 177 GYKMSPDQLEIMKKNISKLDKLPIERIRDEILKILKV-NPAEGFKLLDEFGLLKYLYGEHYEAL 239
Cdd:pfam12627   1 GFTIEPETREAIRKLAPLLKKISPERIFEELLKLLLSgHPERGLELLRETGLLEYLFPELAAAL 64
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 255-335 9.69e-08

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 50.31  E-value: 9.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 255 VIEHTYEALK-------RLRNPDIETI-LAVIYHDVGKPYTRSEKNGKIMFIGHAKKSAEIAKELMKRLKLpnniiKDVT 326
Cdd:pfam01966   1 RLEHSLRVALlarelaeELGELDRELLlLAALLHDIGKGPFGDEKPEFEIFLGHAVVGAEILRELEKRLGL-----EDVL 75


                  ....*....
gi 1002166894 327 NLIEMHMDF 335
Cdd:pfam01966  76 KLILEHHES 84
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 252-325 2.20e-06

HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.


Pssm-ID: 272994 [Multi-domain]  Cd Length: 80  Bit Score: 45.40  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 252 GEDVIEHTYE------ALKRLRNPDIE-TILAVIYHDVGKPYTRseknGKIMFIGHAKKSAEIAKELMKRLKLPNNIIKD 324
Cdd:TIGR00277   2 GQNVLQHSLEvaklaeALARELGLDVElARRGALLHDIGKPITR----EGVIFESHVVVGAEIARKYGEPLEVIDIIAEH 77


                  .
gi 1002166894 325 V 325
Cdd:TIGR00277  78 H 78
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 268-334 2.33e-04

HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];


Pssm-ID: 441028 [Multi-domain]  Cd Length: 191  Bit Score: 42.19  E-value: 2.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002166894 268 NPDIeTILAVIYHDVGKPYTRSEKNGkimfigHAKKSAEIAKELMKRLKLPNNIIKDVTNLIEMHMD 334
Cdd:COG1418    40 DVEV-AKRAALLHDIGKAKDHEVEGS------HAEIGAELARKYLESLGFPEEEIEAVVHAIEAHSF 99
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 250-335 1.29e-03

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 38.82  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894  250 HHGEDVIEHTYEALKRLRNPDIETIL-AVIYHDVGKPYTRSEKNGKIM-FIGHAKKSAEIAKElmkrLKLPNNIIKDVTN 327
Cdd:smart00471   7 EHSLRVAQLAAALAEELGLLDIELLLlAALLHDIGKPGTPDSFLVKTSvLEDHHFIGAEILLE----EEEPRILEEILRT 82


                   ....*...
gi 1002166894  328 LIEMHMDF 335
Cdd:smart00471  83 AILSHHER 90
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 249-325 4.42e-03

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 37.70  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002166894 249 AHHGEDVIEHTYEALKRLRNPDIE---TILAVIYHDVGKPYTRSE--KNGKIMFIGHAKKSAEIAKELM--KRLKLPNNI 321
Cdd:cd00077     4 FEHSLRVAQLARRLAEELGLSEEDielLRLAALLHDIGKPGTPDAitEEESELEKDHAIVGAEILRELLleEVIKLIDEL 83


                  ....
gi 1002166894 322 IKDV 325
Cdd:cd00077    84 ILAV 87
 
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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