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Conserved domains on  [gi|535478710|gb|EFG26461|]
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tRNA adenylyltransferase [Scardovia inopinata F0304]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
tRNA_CCA_actino super family cl31237
tRNA adenylyltransferase; The enzyme tRNA adenylyltransferase, also called ...
 19-478 0e+00

tRNA adenylyltransferase; The enzyme tRNA adenylyltransferase, also called tRNA-nucleotidyltransferase and CCA-adding enzyme, can add or repair the required CCA triplet at the 3'-end of tRNA molecules. Genes encoding tRNA include the CCA tail in some but not all bacteria, and this enzyme may be required for viability. Members of this family represent a distinct clade within the larger family pfam01743 (tRNA nucleotidyltransferase/poly(A) polymerase family protein). The example from Streptomyces coelicolor was shown to act as a CCA-adding enzyme and not as a poly(A) polymerase. [Protein synthesis, tRNA and rRNA base modification]


The actual alignment was detected with superfamily member TIGR02692:

Pssm-ID: 131739 [Multi-domain]  Cd Length: 466  Bit Score: 635.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710   19 PVAVELGHIFAEHGYELALVGGPVRDMILGRSAHDLDFCTSATPDQFEPLLKAWGDGFWDMGRKFGTLGTMKRLPQgeev 98
Cdd:TIGR02692  14 PLLAPLAAAFAAAGHELYLVGGSVRDALLGRLGHDLDFTTDARPEETLAILRPWADAVWDTGIAFGTVGAEKDGQQ---- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710   99 sIEITTYRTDAYQPNSRKPQVDYGSSLQGDLSRRDFTINSMAVRLP---SLDFVDPFGGMDDLSKRLLRTPVAAEQSFSD 175
Cdd:TIGR02692  90 -IEITTFRSDSYDGTSRKPEVTFGDTLEGDLIRRDFTVNAMAVRIPadgSLEFHDPVGGLDDLLAKVLDTPATPEQSFGD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  176 DPLRMMRAVRFVAQLDFRIALDTAEALSSMVDRIQIVSAERVRDELTKLLLSQHPRKGLESLVESGLADYVVPELPALHM 255
Cdd:TIGR02692 169 DPLRMLRAARFVSQLGFEVAPRVRAAMTEMADQIERISAERVRVELDKLLLGDHPRAGIDLMVETGLADRVLPEIPALRL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  256 DRDPNHHHKDVFDHTMKVLERAIALETSpdgpvpAPDLVLRLAALMHDIGKPRTRRFEPGGKVSFYHHDLVGAKMTRKRL 335
Cdd:TIGR02692 249 EIDEHHQHKDVYEHSLTVLRQAIDLEDD------GPDLVLRWAALLHDIGKPATRRFEPDGRVSFHHHEVVGAKMVRKRM 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  336 TSLRFDKHVVEDVSSLVELHLRFHGYVDEPWSDAAVRRYVKDSGHLYHRLNRLTRADATTQNRQKSLMFEQAMDELESRV 415
Cdd:TIGR02692 323 RALKYSKQMVEDVSRLVELHLRFHGYGDGQWTDSAVRRYVRDAGPLLPRLHKLVRADCTTRNKRKAARLQAAYDDLEERI 402

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535478710  416 NELKKKEDFEAIRPDLNGDQIMKILGLAPGPQVGHAYKHMLDFRLDNGPVDQDEAVAELQKWW 478
Cdd:TIGR02692 403 AELAAQEDLARVRPDLDGNEIMEILGIKPGPEVGQAWKYLKELRLERGPLEREEAIAELLAWW 465
 
Name Accession Description Interval E-value
tRNA_CCA_actino TIGR02692
tRNA adenylyltransferase; The enzyme tRNA adenylyltransferase, also called ...
 19-478 0e+00

tRNA adenylyltransferase; The enzyme tRNA adenylyltransferase, also called tRNA-nucleotidyltransferase and CCA-adding enzyme, can add or repair the required CCA triplet at the 3'-end of tRNA molecules. Genes encoding tRNA include the CCA tail in some but not all bacteria, and this enzyme may be required for viability. Members of this family represent a distinct clade within the larger family pfam01743 (tRNA nucleotidyltransferase/poly(A) polymerase family protein). The example from Streptomyces coelicolor was shown to act as a CCA-adding enzyme and not as a poly(A) polymerase. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 131739 [Multi-domain]  Cd Length: 466  Bit Score: 635.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710   19 PVAVELGHIFAEHGYELALVGGPVRDMILGRSAHDLDFCTSATPDQFEPLLKAWGDGFWDMGRKFGTLGTMKRLPQgeev 98
Cdd:TIGR02692  14 PLLAPLAAAFAAAGHELYLVGGSVRDALLGRLGHDLDFTTDARPEETLAILRPWADAVWDTGIAFGTVGAEKDGQQ---- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710   99 sIEITTYRTDAYQPNSRKPQVDYGSSLQGDLSRRDFTINSMAVRLP---SLDFVDPFGGMDDLSKRLLRTPVAAEQSFSD 175
Cdd:TIGR02692  90 -IEITTFRSDSYDGTSRKPEVTFGDTLEGDLIRRDFTVNAMAVRIPadgSLEFHDPVGGLDDLLAKVLDTPATPEQSFGD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  176 DPLRMMRAVRFVAQLDFRIALDTAEALSSMVDRIQIVSAERVRDELTKLLLSQHPRKGLESLVESGLADYVVPELPALHM 255
Cdd:TIGR02692 169 DPLRMLRAARFVSQLGFEVAPRVRAAMTEMADQIERISAERVRVELDKLLLGDHPRAGIDLMVETGLADRVLPEIPALRL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  256 DRDPNHHHKDVFDHTMKVLERAIALETSpdgpvpAPDLVLRLAALMHDIGKPRTRRFEPGGKVSFYHHDLVGAKMTRKRL 335
Cdd:TIGR02692 249 EIDEHHQHKDVYEHSLTVLRQAIDLEDD------GPDLVLRWAALLHDIGKPATRRFEPDGRVSFHHHEVVGAKMVRKRM 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  336 TSLRFDKHVVEDVSSLVELHLRFHGYVDEPWSDAAVRRYVKDSGHLYHRLNRLTRADATTQNRQKSLMFEQAMDELESRV 415
Cdd:TIGR02692 323 RALKYSKQMVEDVSRLVELHLRFHGYGDGQWTDSAVRRYVRDAGPLLPRLHKLVRADCTTRNKRKAARLQAAYDDLEERI 402

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535478710  416 NELKKKEDFEAIRPDLNGDQIMKILGLAPGPQVGHAYKHMLDFRLDNGPVDQDEAVAELQKWW 478
Cdd:TIGR02692 403 AELAAQEDLARVRPDLDGNEIMEILGIKPGPEVGQAWKYLKELRLERGPLEREEAIAELLAWW 465
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
 17-481 2.54e-138

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: 403.43  E-value: 2.54e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  17 VPPVAVELGHIFAEHGYELALVGGPVRDMILGRSAHDLDFCTSATPDQFEPLLKAWgDGFWDMGRKFGTLGtmkrLPQGE 96
Cdd:COG0617    2 LSPNALKVLEALEEAGFEAYLVGGAVRDLLLGRPPKDIDIVTVATPEEVAALFRKA-LRTVPVGRDFGTVT----VVFGG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  97 EVsIEITTYRTDAYQPNSRKPQVDYGSSLQGDLSRRDFTINSMAVRLPSLDFVDPFGGMDDLSKRLLRTPVAAEQSFSDD 176
Cdd:COG0617   77 EK-IEVATARTERYYGDGRRPFVEFGDTLEEDLARRDFTINALAYDLNDGELIDPFGGLADLEARVIRTVGDPEERFRED 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 177 PLRMMRAVRFVAQLDFRIALDTAEALSSMVDRIQIVSAERVRDELTKLLLSQHPRKGLESLVESGLADYvvpelpalhmd 256
Cdd:COG0617  156 PLRILRAVRFAARLGFTIEPETLAAIREMAGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEV----------- 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 257 rdpnhhhkdvfdhtmkvleraialetspdgpvpapdLVLRLAALMHDIGKPRTRrfePGGKVSFYHHDLVGAKMTRKRLT 336
Cdd:COG0617  225 ------------------------------------LALRLAALLHDLGKPATR---EDGLPTFHGHEEAGAELAEALLK 265

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 337 SLRFDKHVVEDVSSLVELHLRFHGYVDepWSDAAVRRYVKDSGHLYHRLNRLTRAdattqnrqkslmfEQAMDELESRVN 416
Cdd:COG0617  266 RLRLPNRERKLVRELVELHLRFHGLGE--LRDSAVRRLLERGPEALEDLLLLREN-------------GLEYPELQERLA 330

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535478710 417 ELKKKeDFEAIRPDLNGDQIMKiLGLAPGPQVGHAYKHMLDFRLDNGPVDQDEavAELQKWWRSQ 481
Cdd:COG0617  331 ELLEA-AWRRFQPPVDGEDLMA-LGLKPGPEIGEILRALREAVLDGGIPNRRE--EALLRWLRRL 391
PRK13299 PRK13299
tRNA CCA-pyrophosphorylase; Provisional
 30-258 1.21e-60

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237339 [Multi-domain]  Cd Length: 394  Bit Score: 203.53  E-value: 1.21e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  30 EHGYELALVGGPVRDMILGRSAHDLDFCTSATPDQFEPLlkawgdgF---WDMGRKFGTLGTmkrLPQGEEvsIEITTYR 106
Cdd:PRK13299  18 EAGFEAYFVGGSVRDYLLGRPIHDVDIATSAYPEEVKAI-------FprtVDVGIEHGTVLV---LENGEE--YEVTTFR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 107 T-DAYQPNSRKPQVDYGSSLQGDLSRRDFTINSMAvrlpsLDF----VDPFGGMDDLSKRLLRTPVAAEQSFSDDPLRMM 181
Cdd:PRK13299  86 TeSEYVDYRRPSEVTFVRSLEEDLKRRDFTINAIA-----MDEngeiIDLFDGLEDLKNRLIRAVGNAEERFQEDALRMM 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535478710 182 RAVRFVAQLDFRIALDTAEALSSMVDRIQIVSAERVRDELTKLLLSQHPRKGLESLVESGLADYvvpeLPALHMDRD 258
Cdd:PRK13299 161 RAVRFASQLGFDLETETFEAMKTQAPLLEKISVERIFVEFEKLLLGPFWRKGLKLLIETGLYNY----LPGLKGKEE 233
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
 24-158 6.81e-38

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: 135.03  E-value: 6.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  24 LGHIFAEHGYELALVGGPVRDMILGRSAHDLDFCTSA-TPDQFEPLLKAWGDGFWDMGRKFGTLGTMKRlpqgeEVSIEI 102
Cdd:cd05398    8 LRELKKALGYEAYLVGGAVRDLLLGRPPKDIDIATDAdGPEFAEALFKKIGGRVVGLGEEFGTATVVIN-----GLTIDV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 535478710 103 TTYRTDAYQPNSRKPqVDYGSSLQGDLSRRDFTINSMAVRLPSLDFVDPFGGMDDL 158
Cdd:cd05398   83 ATLRTETYTDPGRRP-PVVGFTIEEDLLRRDFTINAMAYDLDDGELIDPFGGLKDL 137
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
 37-164 9.68e-35

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: 126.24  E-value: 9.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710   37 LVGGPVRDMILGRSAHDLDFCTSATPDQFEPLLKAWGDGFWDMGRKFGTLGTMKRLPqgeevSIEITTYRTDAYQPNSRK 116
Cdd:pfam01743   3 IVGGAVRDLLLGKTPKDVDIATDATPEQVATLFRRRRIVHLLSGIEFGTIHVIFGNQ-----ILEVATFRIEFDESDFRN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 535478710  117 P-QVDYGSSLQGDLSRRDFTINSMAVRLPSLDFVDPFGGMDDLSKRLLR 164
Cdd:pfam01743  78 PrSEEYTGTLEEDAKRRDFTINALAYNPNSGEVIDYFGGIKDLKSGVIR 126
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 262-372 1.89e-07

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: 49.99  E-value: 1.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710   262 HHKDVFDHTMKVLEraIALETSPDGPVPAPDLvLRLAALMHDIGKPRTRRFEPGGKVSFYHHDLVGAKMtrkrLTSLRFD 341
Cdd:smart00471   1 SDYHVFEHSLRVAQ--LAAALAEELGLLDIEL-LLLAALLHDIGKPGTPDSFLVKTSVLEDHHFIGAEI----LLEEEEP 73

                           90       100       110
                   ....*....|....*....|....*....|.
gi 535478710   342 KHVVEDVSSLVELHLRFHGYVDEPWSDAAVR 372
Cdd:smart00471  74 RILEEILRTAILSHHERPDGLRGEPITLEAR 104
 
Name Accession Description Interval E-value
tRNA_CCA_actino TIGR02692
tRNA adenylyltransferase; The enzyme tRNA adenylyltransferase, also called ...
 19-478 0e+00

tRNA adenylyltransferase; The enzyme tRNA adenylyltransferase, also called tRNA-nucleotidyltransferase and CCA-adding enzyme, can add or repair the required CCA triplet at the 3'-end of tRNA molecules. Genes encoding tRNA include the CCA tail in some but not all bacteria, and this enzyme may be required for viability. Members of this family represent a distinct clade within the larger family pfam01743 (tRNA nucleotidyltransferase/poly(A) polymerase family protein). The example from Streptomyces coelicolor was shown to act as a CCA-adding enzyme and not as a poly(A) polymerase. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 131739 [Multi-domain]  Cd Length: 466  Bit Score: 635.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710   19 PVAVELGHIFAEHGYELALVGGPVRDMILGRSAHDLDFCTSATPDQFEPLLKAWGDGFWDMGRKFGTLGTMKRLPQgeev 98
Cdd:TIGR02692  14 PLLAPLAAAFAAAGHELYLVGGSVRDALLGRLGHDLDFTTDARPEETLAILRPWADAVWDTGIAFGTVGAEKDGQQ---- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710   99 sIEITTYRTDAYQPNSRKPQVDYGSSLQGDLSRRDFTINSMAVRLP---SLDFVDPFGGMDDLSKRLLRTPVAAEQSFSD 175
Cdd:TIGR02692  90 -IEITTFRSDSYDGTSRKPEVTFGDTLEGDLIRRDFTVNAMAVRIPadgSLEFHDPVGGLDDLLAKVLDTPATPEQSFGD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  176 DPLRMMRAVRFVAQLDFRIALDTAEALSSMVDRIQIVSAERVRDELTKLLLSQHPRKGLESLVESGLADYVVPELPALHM 255
Cdd:TIGR02692 169 DPLRMLRAARFVSQLGFEVAPRVRAAMTEMADQIERISAERVRVELDKLLLGDHPRAGIDLMVETGLADRVLPEIPALRL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  256 DRDPNHHHKDVFDHTMKVLERAIALETSpdgpvpAPDLVLRLAALMHDIGKPRTRRFEPGGKVSFYHHDLVGAKMTRKRL 335
Cdd:TIGR02692 249 EIDEHHQHKDVYEHSLTVLRQAIDLEDD------GPDLVLRWAALLHDIGKPATRRFEPDGRVSFHHHEVVGAKMVRKRM 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  336 TSLRFDKHVVEDVSSLVELHLRFHGYVDEPWSDAAVRRYVKDSGHLYHRLNRLTRADATTQNRQKSLMFEQAMDELESRV 415
Cdd:TIGR02692 323 RALKYSKQMVEDVSRLVELHLRFHGYGDGQWTDSAVRRYVRDAGPLLPRLHKLVRADCTTRNKRKAARLQAAYDDLEERI 402

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535478710  416 NELKKKEDFEAIRPDLNGDQIMKILGLAPGPQVGHAYKHMLDFRLDNGPVDQDEAVAELQKWW 478
Cdd:TIGR02692 403 AELAAQEDLARVRPDLDGNEIMEILGIKPGPEVGQAWKYLKELRLERGPLEREEAIAELLAWW 465
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
 17-481 2.54e-138

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: 403.43  E-value: 2.54e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  17 VPPVAVELGHIFAEHGYELALVGGPVRDMILGRSAHDLDFCTSATPDQFEPLLKAWgDGFWDMGRKFGTLGtmkrLPQGE 96
Cdd:COG0617    2 LSPNALKVLEALEEAGFEAYLVGGAVRDLLLGRPPKDIDIVTVATPEEVAALFRKA-LRTVPVGRDFGTVT----VVFGG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  97 EVsIEITTYRTDAYQPNSRKPQVDYGSSLQGDLSRRDFTINSMAVRLPSLDFVDPFGGMDDLSKRLLRTPVAAEQSFSDD 176
Cdd:COG0617   77 EK-IEVATARTERYYGDGRRPFVEFGDTLEEDLARRDFTINALAYDLNDGELIDPFGGLADLEARVIRTVGDPEERFRED 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 177 PLRMMRAVRFVAQLDFRIALDTAEALSSMVDRIQIVSAERVRDELTKLLLSQHPRKGLESLVESGLADYvvpelpalhmd 256
Cdd:COG0617  156 PLRILRAVRFAARLGFTIEPETLAAIREMAGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEV----------- 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 257 rdpnhhhkdvfdhtmkvleraialetspdgpvpapdLVLRLAALMHDIGKPRTRrfePGGKVSFYHHDLVGAKMTRKRLT 336
Cdd:COG0617  225 ------------------------------------LALRLAALLHDLGKPATR---EDGLPTFHGHEEAGAELAEALLK 265

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 337 SLRFDKHVVEDVSSLVELHLRFHGYVDepWSDAAVRRYVKDSGHLYHRLNRLTRAdattqnrqkslmfEQAMDELESRVN 416
Cdd:COG0617  266 RLRLPNRERKLVRELVELHLRFHGLGE--LRDSAVRRLLERGPEALEDLLLLREN-------------GLEYPELQERLA 330

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535478710 417 ELKKKeDFEAIRPDLNGDQIMKiLGLAPGPQVGHAYKHMLDFRLDNGPVDQDEavAELQKWWRSQ 481
Cdd:COG0617  331 ELLEA-AWRRFQPPVDGEDLMA-LGLKPGPEIGEILRALREAVLDGGIPNRRE--EALLRWLRRL 391
PRK13299 PRK13299
tRNA CCA-pyrophosphorylase; Provisional
 30-258 1.21e-60

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237339 [Multi-domain]  Cd Length: 394  Bit Score: 203.53  E-value: 1.21e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  30 EHGYELALVGGPVRDMILGRSAHDLDFCTSATPDQFEPLlkawgdgF---WDMGRKFGTLGTmkrLPQGEEvsIEITTYR 106
Cdd:PRK13299  18 EAGFEAYFVGGSVRDYLLGRPIHDVDIATSAYPEEVKAI-------FprtVDVGIEHGTVLV---LENGEE--YEVTTFR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 107 T-DAYQPNSRKPQVDYGSSLQGDLSRRDFTINSMAvrlpsLDF----VDPFGGMDDLSKRLLRTPVAAEQSFSDDPLRMM 181
Cdd:PRK13299  86 TeSEYVDYRRPSEVTFVRSLEEDLKRRDFTINAIA-----MDEngeiIDLFDGLEDLKNRLIRAVGNAEERFQEDALRMM 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535478710 182 RAVRFVAQLDFRIALDTAEALSSMVDRIQIVSAERVRDELTKLLLSQHPRKGLESLVESGLADYvvpeLPALHMDRD 258
Cdd:PRK13299 161 RAVRFASQLGFDLETETFEAMKTQAPLLEKISVERIFVEFEKLLLGPFWRKGLKLLIETGLYNY----LPGLKGKEE 233
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
 24-158 6.81e-38

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: 135.03  E-value: 6.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  24 LGHIFAEHGYELALVGGPVRDMILGRSAHDLDFCTSA-TPDQFEPLLKAWGDGFWDMGRKFGTLGTMKRlpqgeEVSIEI 102
Cdd:cd05398    8 LRELKKALGYEAYLVGGAVRDLLLGRPPKDIDIATDAdGPEFAEALFKKIGGRVVGLGEEFGTATVVIN-----GLTIDV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 535478710 103 TTYRTDAYQPNSRKPqVDYGSSLQGDLSRRDFTINSMAVRLPSLDFVDPFGGMDDL 158
Cdd:cd05398   83 ATLRTETYTDPGRRP-PVVGFTIEEDLLRRDFTINAMAYDLDDGELIDPFGGLKDL 137
cca PRK10885
multifunctional CCA addition/repair protein;
37-362 2.88e-35

multifunctional CCA addition/repair protein;


Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 135.75  E-value: 2.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  37 LVGGPVRDMILGRSAHDLDF-CTSATPDQFEPLlkawgdGFWDMGRKFGTLgtmkrL-PQ-GEEVSIEittyRTDayqpn 113
Cdd:PRK10885   5 LVGGAVRDALLGLPVKDRDWvVVGATPEEMLAQ------GYQQVGKDFPVF-----LhPKtHEEYALA----RTE----- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 114 sRKPQVDYGS---------SLQGDLSRRDFTINSMAvRLPSLDFVDPFGGMDDLSKRLLRTPVAAeqsFSDDPLRMMRAV 184
Cdd:PRK10885  65 -RKSGRGYTGftcyaapdvTLEEDLIRRDLTINAMA-QDDDGELIDPYGGQRDLEARLLRHVSPA---FAEDPLRVLRVA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 185 RFVAQ---LDFRIALDTAEALSSMVDR--IQIVSAERVRDELTKLLLSQHPRKGLESLVESGLADYVVPELPALHMDRDP 259
Cdd:PRK10885 140 RFAARfahLGFRIAPETLALMREMVASgeLDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQP 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 260 NHHHK--DVFDHTMKVLERAIALetspdgpvpAPDLVLRLAALMHDIGKPRTRRFE-PggkvSFYHHDLVGAKMTRKRLT 336
Cdd:PRK10885 220 AKWHPeiDTGIHTLMVLDQAAKL---------SPSLDVRFAALCHDLGKGLTPPEEwP----RHHGHEPRGVKLVEQLCQ 286

                        330       340
                 ....*....|....*....|....*.
gi 535478710 337 SLRfdkhVVEDVSSLVELHLRFHGYV 362
Cdd:PRK10885 287 RLR----VPNECRDLALLVAEEHDNI 308
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
 37-164 9.68e-35

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: 126.24  E-value: 9.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710   37 LVGGPVRDMILGRSAHDLDFCTSATPDQFEPLLKAWGDGFWDMGRKFGTLGTMKRLPqgeevSIEITTYRTDAYQPNSRK 116
Cdd:pfam01743   3 IVGGAVRDLLLGKTPKDVDIATDATPEQVATLFRRRRIVHLLSGIEFGTIHVIFGNQ-----ILEVATFRIEFDESDFRN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 535478710  117 P-QVDYGSSLQGDLSRRDFTINSMAVRLPSLDFVDPFGGMDDLSKRLLR 164
Cdd:pfam01743  78 PrSEEYTGTLEEDAKRRDFTINALAYNPNSGEVIDYFGGIKDLKSGVIR 126
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
 32-258 7.72e-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: 126.07  E-value: 7.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710   32 GYELALVGGPVRDMILGRSAHDLDFCTSATPDQFEPLLKawgdGFWDMGRKFGTLGTMkrlpQGEEVsIEITTYRTDAYQ 111
Cdd:TIGR01942  29 GYQAYIVGGAVRDLLLGIEPKDFDVVTSATPEEVRKLFR----NSRIVGRRFRLVHVS----FGRQI-IEVATFRSGHKS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  112 PNSR-----KPQVdYGsSLQGDLSRRDFTINSMAVRLPSLDFVDPFGGMDDLSKRLLRTPVAAEQSFSDDPLRMMRAVRF 186
Cdd:TIGR01942 100 SVNAegrilKDNV-YG-TLEEDAWRRDFTVNALYYDPSREVIIDYVGGMEDLKNRRLRLIGDPRSRYQEDPVRMLRALRF 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 535478710  187 VAQLDFRIALDTAEALSSMVDRIQIVSAERVRDELTKLLLSQHPRKGLESLVESGLADYVVPELPALHMDRD 258
Cdd:TIGR01942 178 SVKLEFTIDESTARPIRESAPLLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLEPLFPSVAYALRESP 249
pcnB PRK11623
poly(A) polymerase I; Provisional
 32-229 1.81e-26

poly(A) polymerase I; Provisional


Pssm-ID: 236939 [Multi-domain]  Cd Length: 472  Bit Score: 111.77  E-value: 1.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  32 GYELALVGGPVRDMILGRSAHDLDFCTSATPDQFEPLLKawgdGFWDMGRKFgtlgtmkRLPQ---GEEVsIEITTYRTD 108
Cdd:PRK11623  66 GYEAYLVGGGVRDLLLGKKPKDFDVTTNATPEQVRKLFR----NCRLVGRRF-------RLAHvmfGPEI-IEVATFRGH 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 109 AYQPNSRKPQVDYGS-----------SLQGDLSRRDFTINSMAVRLPSLDFVDPFGGMDDLSKRLLRTPVAAEQSFSDDP 177
Cdd:PRK11623 134 HEGNESDRNTSQRGQngmllrdnifgSIEEDAQRRDFTINSLYYSVADFTVRDYVGGMKDLKEGVIRLIGNPETRYREDP 213

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 535478710 178 LRMMRAVRFVAQLDFRIALDTAEALSSMVDRIQIVSAERVRDELTKLLLSQH 229
Cdd:PRK11623 214 VRMLRAVRFAAKLDMRISPETAEPIPRLATLLNDIPPARLFEESLKLLQAGY 265
PRK13297 PRK13297
tRNA CCA-pyrophosphorylase; Provisional
 32-250 5.92e-22

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 139469 [Multi-domain]  Cd Length: 364  Bit Score: 96.99  E-value: 5.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  32 GYELALVGGPVRDMILGRSAHDLDF-CTSATPDQFEPllkawgDGFWDMGRKFGTLgtmkRLPQGEEvsiEITTYRTDAY 110
Cdd:PRK13297  11 GLQVYIVGGAVRDALLGLPAGDRDWvVVGATPEDMAR------RGFIPVGGDFPVF----LHPRTKE---EYALARTERK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 111 QPNSRKPQVDYGSS---LQGDLSRRDFTINSMAvRLPSLDFVDPFGGMDDLSKRLLRtpvAAEQSFSDDPLRMMRAVRFV 187
Cdd:PRK13297  78 SGRGYKGFTFYTGAdvtLEQDLQRRDLTVNAIA-RTPQGELVDPLDGVADVRARVLR---HVGEAFAEDPVRILRLGRFA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535478710 188 AQL-DFRIALDTAEALSSMVDR--IQIVSAERVRDELTKLLLSQHPRKGLESLVESGLADYVVPEL 250
Cdd:PRK13297 154 ARFgDFSIAPETMQLCRRMVEAgeADALVPERVWKEVSRGLMAQAPSRMLDVLARAGALARVMPEL 219
PRK13298 PRK13298
tRNA CCA-pyrophosphorylase; Provisional
 37-263 2.39e-19

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237338 [Multi-domain]  Cd Length: 417  Bit Score: 90.17  E-value: 2.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  37 LVGGPVRDMILGRSAHDLDFC-TSATPdqfEPLLKAwgdGFWDMGRKFGTLgtmkRLPQGEEvsiEITTYRTDayqpnsR 115
Cdd:PRK13298   5 LVGGAVRDSLLNLPVKDKDWVvVGGTP---KILLSI---NFQQVGKDFPVF----LHPETHE---EYALARTE------R 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 116 KPQV-------DYGSS--LQGDLSRRDFTINSMAvRLPSLDFVDPFGGMDDLSKRLLRtpvAAEQSFSDDPLRMMRAVRF 186
Cdd:PRK13298  66 KSGVgytgfitDTSSDvtLEEDLIRRDLTINAIA-QDENGNYIDPFQGKKDIQLRLLR---HVSESFIEDPLRVLRVARF 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 187 VA---QLDFRIALDTAEALSSMVDRIQI--VSAERVRDELTKLLLSQHPRKGLESLVESGLADYVVPELPALHMDRDPNH 261
Cdd:PRK13298 142 AAllvHLGFKIAKETMILMCIMVKKHELlyLTPERIWNETEKALKTDNPHVYFQVLYECNALKFLFPEIDFLYEKPYFLN 221


                 ..
gi 535478710 262 HH 263
Cdd:PRK13298 222 SF 223
PRK13296 PRK13296
CCA tRNA nucleotidyltransferase;
34-239 5.46e-19

CCA tRNA nucleotidyltransferase;


Pssm-ID: 106256 [Multi-domain]  Cd Length: 360  Bit Score: 88.12  E-value: 5.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  34 ELALVGGPVRDMILGRSAHDLDFCT-SATPDQfepLLKAwgdGFWDMGRKFGTLGTmkrlPQGEEvsiEITTYRTDAYQP 112
Cdd:PRK13296   2 KFYLVGGAVRDMLLGITPKDKDWVVvGATEDE---MLAN---GFIKIAANFPVFIH----PQTKQ---EYALARSEKKTA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 113 NSRKP-QVDYGS--SLQGDLSRRDFTINSMAVRLPSlDFVDPFGGMDDLSKRLLRtpvAAEQSFSDDPLRMMRAVRFVAQ 189
Cdd:PRK13296  69 SGYHGfEVNFSKyiTLEDDLKRRDLTINSIAIDQNN-KVIDPFNGQADLQNRILR---HTSIAFIEDPLRVVRLARFKAQ 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 535478710 190 L---DFRIALDTAEALSSMVD--RIQIVSAERVRDELTKLLlsQHPRKGLESLVE 239
Cdd:PRK13296 145 LsnfNFSIAQEMLALIKELVKtgELNHLTRERLHIEFVKAL--NNPKIFFTTLKE 197
PolyA_pol_RNAbd pfam12627
Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA ...
 191-250 9.95e-19

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: 79.84  E-value: 9.95e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  191 DFRIALDTAEALSSMVDRIQIVSAERVRDELTKLLLSQHPRKGLESLVESGLADYVVPEL 250
Cdd:pfam12627   1 GFTIEPETREAIRKLAPLLKKISPERIFEELLKLLLSGHPERGLELLRETGLLEYLFPEL 60
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 263-349 2.88e-11

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: 59.27  E-value: 2.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  263 HKDVFDHTMKVLERAIALETSpdgpVPAPDLVLRLAALMHDIGKPRTRRfepggKVSFYHHDLVGAKMTRKRLTSLRFDK 342
Cdd:TIGR00277   2 GQNVLQHSLEVAKLAEALARE----LGLDVELARRGALLHDIGKPITRE-----GVIFESHVVVGAEIARKYGEPLEVID 72


                  ....*..
gi 535478710  343 HVVEDVS 349
Cdd:TIGR00277  73 IIAEHHG 79
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 266-377 2.33e-09

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 54.93  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  266 VFDHTMKVLEraIALETSPDGPVPAPDLvLRLAALMHDIGKPRTRRfEPGGKVSFYHHDLVGAKMTRKRLTSLRFdkhvv 345
Cdd:pfam01966   1 RLEHSLRVAL--LARELAEELGELDREL-LLLAALLHDIGKGPFGD-EKPEFEIFLGHAVVGAEILRELEKRLGL----- 71

                          90       100       110
                  ....*....|....*....|....*....|..
gi 535478710  346 EDVSSLVELHLRFHGYVDEPWSDAAVRRYVKD 377
Cdd:pfam01966  72 EDVLKLILEHHESWEGAGYPEEISLEARIVKL 103
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 265-364 1.67e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 53.50  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 265 DVFDHTMKVLERAIALETSpDGPVPAPDLVLRLAALMHDIGKPRTRR-FEPGGKVSFYHHDLVGAKMTRK--RLTSLRFD 341
Cdd:cd00077    2 HRFEHSLRVAQLARRLAEE-LGLSEEDIELLRLAALLHDIGKPGTPDaITEEESELEKDHAIVGAEILREllLEEVIKLI 80

                         90       100
                 ....*....|....*....|...
gi 535478710 342 KHVVEDVSSLVELHLRFHGYVDE 364
Cdd:cd00077   81 DELILAVDASHHERLDGLGYPDG 103
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 262-372 1.89e-07

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: 49.99  E-value: 1.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710   262 HHKDVFDHTMKVLEraIALETSPDGPVPAPDLvLRLAALMHDIGKPRTRRFEPGGKVSFYHHDLVGAKMtrkrLTSLRFD 341
Cdd:smart00471   1 SDYHVFEHSLRVAQ--LAAALAEELGLLDIEL-LLLAALLHDIGKPGTPDSFLVKTSVLEDHHFIGAEI----LLEEEEP 73

                           90       100       110
                   ....*....|....*....|....*....|.
gi 535478710   342 KHVVEDVSSLVELHLRFHGYVDEPWSDAAVR 372
Cdd:smart00471  74 RILEEILRTAILSHHERPDGLRGEPITLEAR 104
glnD PRK00227
[protein-PII] uridylyltransferase;
227-393 2.02e-07

[protein-PII] uridylyltransferase;


Pssm-ID: 178937 [Multi-domain]  Cd Length: 693  Bit Score: 53.62  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 227 SQHPRKGLESLVESGLADYVVPELPALH--MDRDPNHHHKdVFDHTMKVLERAiALETSPdgpVPAPDLVLrLAALMHDI 304
Cdd:PRK00227 341 PVNSRRVIKQMDRHGLWERIVPEWDRIRglMPREPSHIHT-IDEHSLNTVANC-ALETVT---VARPDLLL-LGALYHDI 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 305 GKPRTRRfepggkvsfyhHDLVGAKMTRKRLTSLRFDKHVVEDVSSLVELH---LRFHGYVDePWSDAAVRRYVKDSGHL 381
Cdd:PRK00227 415 GKGYPRP-----------HEQVGAEMVARAARRMGLNLRDRAVVQTLVAEHttlARIAGRLD-PTSEEAVDKLLDAVRYD 482

                        170
                 ....*....|....*
gi 535478710 382 YHRLN---RLTRADA 393
Cdd:PRK00227 483 LLTLNlleVLTEADA 497
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 175-393 2.46e-07

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 53.46  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 175 DDPLRMMRAVRFVAQLDFRIALDTAEALSSMVDRIQIVSAERVRDELTKLLLSQHPRKG-LESLVESGLADYVVPELPAL 253
Cdd:PRK03381 328 RDPGLVLRVAAAAATTGLPIAAATLSRLAASAPPLPTPWPAEARDDLLVLLGAGPAAVAvIEALDRTGLWGRLLPEWEAV 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 254 HmDRDPNH--HHKDVFDHTMKVLERAIALETSpdgpVPAPDLVLrLAALMHDIGKPRtrrfePGgkvsfyHHDLVGAKMT 331
Cdd:PRK03381 408 R-DLPPRDpvHRWTVDRHLVETAVRAAALTRR----VARPDLLL-LGALLHDIGKGR-----GG------DHSVVGAELA 470

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 332 RKRLTSLRFDKHVVEDVSSLVELHL--------RfhgYVDEPWSDAAVRRYVKDSGHLYHRLNRLTRADA 393
Cdd:PRK03381 471 RQIGARLGLSPADVALLSALVRHHLllpetatrR---DLDDPATIEAVAEALGGDPVLLELLHALTEADS 537
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 167-356 1.15e-06

UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 51.30  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 167 VAAEQSFSDDPLRMMRAVRFVAQLDF--RIALDTAEALSSMVDRIqivsAERVRD--ELTKLLLS--QHPR---KGLESL 237
Cdd:COG2844  335 VADPDVFERDPVALLRLFLLAAQHPEglGIHPDTLRLLRRALRLI----DDAFRRdpEARRLFLEilRQPRgitRALRRM 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 238 VESG-LADYvvpeLPAL-----HMDRDPNHHHKdVFDHTMKVLE--RAIAL-ETSPDGPVP---APDL----VLRLAALM 301
Cdd:COG2844  411 NEYGvLGRY----IPEFgrivgQMQFDLFHVYT-VDEHTLRVVRnlRRFERgELAEEFPLAselIAELpkpeLLYLAALF 485

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 535478710 302 HDIGKPRtrrfepGGkvsfyHHDLVGAKMTRKRLTSLRFDKHVVEDVSSLVELHL 356
Cdd:COG2844  486 HDIAKGR------GG-----DHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHL 529
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 266-355 1.45e-06

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: 48.74  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 266 VFDHTMKVLE--RAIALETSpdgpvpAPDLVLRLAALMHDIGKPRTRRFEPGgkvsfyhHDLVGAKMTRKRLTSLRFDKH 343
Cdd:COG1418   19 DLQHSLRVAKlaGLIAAEEG------ADVEVAKRAALLHDIGKAKDHEVEGS-------HAEIGAELARKYLESLGFPEE 85

                         90
                 ....*....|..
gi 535478710 344 VVEDVSSLVELH 355
Cdd:COG1418   86 EIEAVVHAIEAH 97
COG4339 COG4339
Predicted metal-dependent phosphohydrolase, HD superfamily [General function prediction only];
261-354 6.84e-06

Predicted metal-dependent phosphohydrolase, HD superfamily [General function prediction only];


Pssm-ID: 443480  Cd Length: 202  Bit Score: 46.81  E-value: 6.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 261 HHHKdvFDHTMKVLERAIALETSPDgpvpAPDLVlRLAALMHDIGkprtrrFEPGGKvsfyHHDLVGAKMTRKRLTSLRF 340
Cdd:COG4339   31 HYHN--LRHLQAVLAALDELAELAE----DPDAV-RLAAWFHDAV------YDTGAG----DNEERSAELAREFLTSLGV 93

                         90
                 ....*....|....
gi 535478710 341 DKHVVEDVSSLVEL 354
Cdd:COG4339   94 PEEVIERVARLILA 107
Cas3''_I cd09641
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short ...
 268-442 2.75e-04

CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; HD-like nuclease, specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs; signature gene for Type I


Pssm-ID: 193608 [Multi-domain]  Cd Length: 200  Bit Score: 42.26  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 268 DHTMKVLERAIALETS----PDGPVPAPDLVLRLAALMHDIGK---------PRTRRFEPGGKVSFYHHDLVGAKMTRKR 334
Cdd:cd09641   11 EHLLDVAAWDAELAEEfarkLGLELGLSRELLALAGLLHDLGKatpafqkylRGGKEALREGKRKEVRHSLLGALLLYEL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710 335 LTSLRFDKHVVEDVSSLVELHlrfHGYvdepWSDAAVRRYVKDSGHLYHRLNRLtradatTQNRQKSLMFEQAMDELESR 414
Cdd:cd09641   91 LKELGLDEELALLLAYAIAGH---HGG----LPDVLLLLDEDDESALKERLEEL------DEEKLLLELWEEELEELLDE 157

                        170       180
                 ....*....|....*....|....*...
gi 535478710 415 VNELKKKEDFEAIRPDLNGDQIMKILGL 442
Cdd:cd09641  158 LLKELLLLLLPELLSFELYLLLRLLFSL 185
cas3_HD TIGR01596
CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for ...
 268-365 4.80e-04

CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for host defense against invasive elements such as phage. In these systems, Cas3 designates one of the core proteins shared widely by multiple types of CRISPR/Cas system. This model represents an HD-like endonuclease that occurs either separately or as the N-terminal region of Cas3, the helicase-containing CRISPR-associated protein.


Pssm-ID: 273711 [Multi-domain]  Cd Length: 176  Bit Score: 41.03  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535478710  268 DHTMKVLERAIALET-----SPDGPVPAPDLvLRLAALMHDIGKpRTRRF-------EPGGKVSFYHHDLVGAKMTRKRL 335
Cdd:TIGR01596   3 EHLLDVAAVAEALPAlrprlAEKLGLELREL-LKLAGLLHDLGK-ASPAFqkklrkaEERGDRGEVRHSTLSAALLYDLL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 535478710  336 TSLRFDKHVVEDVSSLVELHlrfHGYVDEP 365
Cdd:TIGR01596  81 EELGLEEELALLLALAIAGH---HGGLIDD 107
 
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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