|
Name |
Accession |
Description |
Interval |
E-value |
| cca |
PRK10885 |
multifunctional CCA addition/repair protein; |
1-409 |
0e+00 |
|
multifunctional CCA addition/repair protein;
Pssm-ID: 182810 [Multi-domain] Cd Length: 409 Bit Score: 784.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 1 MKIYKVGGAVRDRLLGIEVTDIDRVVVGATAEEMLAKGYKPVGADFPVFLDPKNGDEYALARTERKNGRGYGGFIFHASP 80
Cdd:PRK10885 1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 81 DVTLEEDLIRRDLTINAMAEDDEGNLTDPYQGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARYAPLGFTVAPETLELM 160
Cdd:PRK10885 81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 161 RQLSESGELEALTPERSWKEISRALMEDQPQVFIQVLRDCDALKTLMPEVDALFGVPQPAAHHPEIDTGLHTLSVLQQAA 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 241 LHKQPLSVRWACLLHDLGKGLTPVDKLPQHIAHEHRGLKLIKAVNERFKVPRDCQELALLVGQYHTHGHRALELKASTLL 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 321 ELLQSFDVYRRPQRFEEFVAACEMDARGREGFEQRSYPQADYLRGAAKVAREVPVAPLLEKGFKGPELGEALKRERLKAL 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400
|
....*....
gi 518653987 401 KAYKEQQKP 409
Cdd:PRK10885 401 AAWKEQRCP 409
|
|
| PcnB |
COG0617 |
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ... |
1-400 |
9.10e-107 |
|
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: 320.22 E-value: 9.10e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 1 MKIYKVGGAVRDRLLGIEVTDIDrVVVGATAEEMLAKG-----YKPVGADFPVFLDPKNGD--EYALARTERKNGRGYGG 73
Cdd:COG0617 18 FEAYLVGGAVRDLLLGRPPKDID-IVTVATPEEVAALFrkalrTVPVGRDFGTVTVVFGGEkiEVATARTERYYGDGRRP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 74 FiFHASPdvTLEEDLIRRDLTINAMAED-DEGNLTDPYQGQRDLEARLLRHVS---PAFAEDPLRVLRVARFAARyapLG 149
Cdd:COG0617 97 F-VEFGD--TLEEDLARRDFTINALAYDlNDGELIDPFGGLADLEARVIRTVGdpeERFREDPLRILRAVRFAAR---LG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 150 FTVAPETLELMRQLSesGELEALTPERSWKEISRALMEDQPQVFIQVLRDCDALKtlmpevdalfgvpqpaahhpeidtg 229
Cdd:COG0617 171 FTIEPETLAAIREMA--GLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLE------------------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 230 lhtlsvlqqaalhkqPLSVRWACLLHDLGKGLTPVDKLPQHIAHEHRGLKLIKAVNERFKVPRDCQELALLVGQYHTHGH 309
Cdd:COG0617 224 ---------------VLALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 310 RALELKASTLLELLqsfdvYRRPQRFEEFVAACEmdaRGREGFEQRSYPQADYLRGAAKVAREVPVAPLLEKGFK-GPEL 388
Cdd:COG0617 289 GLGELRDSAVRRLL-----ERGPEALEDLLLLRE---NGLEYPELQERLAELLEAAWRRFQPPVDGEDLMALGLKpGPEI 360
|
410
....*....|..
gi 518653987 389 GEALKRERLKAL 400
Cdd:COG0617 361 GEILRALREAVL 372
|
|
| tRNA_CCA_actino |
TIGR02692 |
tRNA adenylyltransferase; The enzyme tRNA adenylyltransferase, also called ... |
3-259 |
5.93e-35 |
|
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: 134.47 E-value: 5.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 3 IYKVGGAVRDRLLGIEVTDIDrVVVGATAEEMLA--KGYKPV----GADFPVFLDPKNGDEY--------ALARTERKNG 68
Cdd:TIGR02692 30 LYLVGGSVRDALLGRLGHDLD-FTTDARPEETLAilRPWADAvwdtGIAFGTVGAEKDGQQIeittfrsdSYDGTSRKPE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 69 RGYGGfifhaspdvTLEEDLIRRDLTINAMA----EDDEGNLTDPYQGQRDLEARLLRHVSP---AFAEDPLRVLRVARF 141
Cdd:TIGR02692 109 VTFGD---------TLEGDLIRRDFTVNAMAvripADGSLEFHDPVGGLDDLLAKVLDTPATpeqSFGDDPLRMLRAARF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 142 AARyapLGFTVAPETLELMRQLseSGELEALTPERSWKEISRALMEDQPQVFIQVLRDCDALKTLMPEVDALfgVPQPAA 221
Cdd:TIGR02692 180 VSQ---LGFEVAPRVRAAMTEM--ADQIERISAERVRVELDKLLLGDHPRAGIDLMVETGLADRVLPEIPAL--RLEIDE 252
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 518653987 222 HHPEIDTGLHTLSVLQQA---ALHKQPLSVRWACLLHDLGK 259
Cdd:TIGR02692 253 HHQHKDVYEHSLTVLRQAidlEDDGPDLVLRWAALLHDIGK 293
|
|
| NT_ClassII-CCAase |
cd05398 |
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ... |
1-118 |
1.43e-26 |
|
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: 103.44 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 1 MKIYKVGGAVRDRLLGIEVTDIDRVVVGATAEEM--LAKGYK----PVGADFPV--FLDPKNGDEYALARTERKngrgYG 72
Cdd:cd05398 17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAeaLFKKIGgrvvGLGEEFGTatVVINGLTIDVATLRTETY----TD 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 518653987 73 GFIFHASPDVTLEEDLIRRDLTINAMAED-DEGNLTDPYQGQRDLEA 118
Cdd:cd05398 93 PGRRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
|
|
| PolyA_pol |
pfam01743 |
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ... |
3-122 |
3.58e-22 |
|
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: 91.19 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 3 IYKVGGAVRDRLLGIEVTDIDrVVVGATAEEMLA------KGYKPVGADFPVFLDPKNGDEYALARTerkngRGYGGFIF 76
Cdd:pfam01743 1 LYIVGGAVRDLLLGKTPKDVD-IATDATPEQVATlfrrrrIVHLLSGIEFGTIHVIFGNQILEVATF-----RIEFDESD 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 518653987 77 HASPDV-----TLEEDLIRRDLTINAMAED-DEGNLTDPYQGQRDLEARLLR 122
Cdd:pfam01743 75 FRNPRSeeytgTLEEDAKRRDFTINALAYNpNSGEVIDYFGGIKDLKSGVIR 126
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
231-323 |
2.37e-04 |
|
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: 40.74 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 231 HTLSVLQQAAL------HKQPLSVRWACLLHDLGKGLTP---VDKLPQHIAHEHRGLKLIKavneRFKVPRDCQELALLV 301
Cdd:smart00471 8 HSLRVAQLAAAlaeelgLLDIELLLLAALLHDIGKPGTPdsfLVKTSVLEDHHFIGAEILL----EEEEPRILEEILRTA 83
|
90 100
....*....|....*....|..
gi 518653987 302 GQYHTHGHRALELKASTLLELL 323
Cdd:smart00471 84 ILSHHERPDGLRGEPITLEARI 105
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| cca |
PRK10885 |
multifunctional CCA addition/repair protein; |
1-409 |
0e+00 |
|
multifunctional CCA addition/repair protein;
Pssm-ID: 182810 [Multi-domain] Cd Length: 409 Bit Score: 784.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 1 MKIYKVGGAVRDRLLGIEVTDIDRVVVGATAEEMLAKGYKPVGADFPVFLDPKNGDEYALARTERKNGRGYGGFIFHASP 80
Cdd:PRK10885 1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 81 DVTLEEDLIRRDLTINAMAEDDEGNLTDPYQGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARYAPLGFTVAPETLELM 160
Cdd:PRK10885 81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 161 RQLSESGELEALTPERSWKEISRALMEDQPQVFIQVLRDCDALKTLMPEVDALFGVPQPAAHHPEIDTGLHTLSVLQQAA 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 241 LHKQPLSVRWACLLHDLGKGLTPVDKLPQHIAHEHRGLKLIKAVNERFKVPRDCQELALLVGQYHTHGHRALELKASTLL 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 321 ELLQSFDVYRRPQRFEEFVAACEMDARGREGFEQRSYPQADYLRGAAKVAREVPVAPLLEKGFKGPELGEALKRERLKAL 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400
|
....*....
gi 518653987 401 KAYKEQQKP 409
Cdd:PRK10885 401 AAWKEQRCP 409
|
|
| PRK13298 |
PRK13298 |
tRNA CCA-pyrophosphorylase; Provisional |
1-408 |
1.02e-150 |
|
tRNA CCA-pyrophosphorylase; Provisional
Pssm-ID: 237338 [Multi-domain] Cd Length: 417 Bit Score: 433.00 E-value: 1.02e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 1 MKIYKVGGAVRDRLLGIEVTDIDRVVVGATAEEMLAKGYKPVGADFPVFLDPKNGDEYALARTERKNGRGYGGFIFHASP 80
Cdd:PRK13298 1 MKIYLVGGAVRDSLLNLPVKDKDWVVVGGTPKILLSINFQQVGKDFPVFLHPETHEEYALARTERKSGVGYTGFITDTSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 81 DVTLEEDLIRRDLTINAMAEDDEGNLTDPYQGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARYAPLGFTVAPETLELM 160
Cdd:PRK13298 81 DVTLEEDLIRRDLTINAIAQDENGNYIDPFQGKKDIQLRLLRHVSESFIEDPLRVLRVARFAALLVHLGFKIAKETMILM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 161 RQLSESGELEALTPERSWKEISRALMEDQPQVFIQVLRDCDALKTLMPEVDALFGVPQPAAHH-PEIDTGLHTLSVLQQA 239
Cdd:PRK13298 161 CIMVKKHELLYLTPERIWNETEKALKTDNPHVYFQVLYECNALKFLFPEIDFLYEKPYFLNSFfKKFNLGNYILMGLSKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 240 ALHKQPLSVRWACLLHDLGKG--LTPVDKLPQHIAHEHRGLKLIKAVNERFKVPRDCQELALLVGQYHTHGHRALELKAS 317
Cdd:PRK13298 241 SKLTKDIDIRFSYLCQFLGSMipINQIKRNYKKIFFDKYAASLIKNLCKRFKIPSYIRNIAVLNTGFYFFLYNIHYQSSK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 318 TLLELLQSFDVYRRPQRFEEFVAACEMDARGREGFEQRSYPQADYLRGAAKVAREVPVAPLLEKGFKGPELGEALKRERL 397
Cdd:PRK13298 321 NIITLFSKIDAWRKPDRIKKLIFLSNFNLLRNKKSINFLIKQGNFLKKAFSVTKKISIKDILKKGFKGYEIKQELYRLRI 400
|
410
....*....|.
gi 518653987 398 KALKAYKEQQK 408
Cdd:PRK13298 401 HKLKFWRNKII 411
|
|
| PcnB |
COG0617 |
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ... |
1-400 |
9.10e-107 |
|
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: 320.22 E-value: 9.10e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 1 MKIYKVGGAVRDRLLGIEVTDIDrVVVGATAEEMLAKG-----YKPVGADFPVFLDPKNGD--EYALARTERKNGRGYGG 73
Cdd:COG0617 18 FEAYLVGGAVRDLLLGRPPKDID-IVTVATPEEVAALFrkalrTVPVGRDFGTVTVVFGGEkiEVATARTERYYGDGRRP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 74 FiFHASPdvTLEEDLIRRDLTINAMAED-DEGNLTDPYQGQRDLEARLLRHVS---PAFAEDPLRVLRVARFAARyapLG 149
Cdd:COG0617 97 F-VEFGD--TLEEDLARRDFTINALAYDlNDGELIDPFGGLADLEARVIRTVGdpeERFREDPLRILRAVRFAAR---LG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 150 FTVAPETLELMRQLSesGELEALTPERSWKEISRALMEDQPQVFIQVLRDCDALKtlmpevdalfgvpqpaahhpeidtg 229
Cdd:COG0617 171 FTIEPETLAAIREMA--GLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLE------------------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 230 lhtlsvlqqaalhkqPLSVRWACLLHDLGKGLTPVDKLPQHIAHEHRGLKLIKAVNERFKVPRDCQELALLVGQYHTHGH 309
Cdd:COG0617 224 ---------------VLALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 310 RALELKASTLLELLqsfdvYRRPQRFEEFVAACEmdaRGREGFEQRSYPQADYLRGAAKVAREVPVAPLLEKGFK-GPEL 388
Cdd:COG0617 289 GLGELRDSAVRRLL-----ERGPEALEDLLLLRE---NGLEYPELQERLAELLEAAWRRFQPPVDGEDLMALGLKpGPEI 360
|
410
....*....|..
gi 518653987 389 GEALKRERLKAL 400
Cdd:COG0617 361 GEILRALREAVL 372
|
|
| PRK13297 |
PRK13297 |
tRNA CCA-pyrophosphorylase; Provisional |
1-402 |
7.76e-91 |
|
tRNA CCA-pyrophosphorylase; Provisional
Pssm-ID: 139469 [Multi-domain] Cd Length: 364 Bit Score: 278.42 E-value: 7.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 1 MKIYKVGGAVRDRLLGIEVTDIDRVVVGATAEEMLAKGYKPVGADFPVFLDPKNGDEYALARTERKNGRGYGGFIFHASP 80
Cdd:PRK13297 12 LQVYIVGGAVRDALLGLPAGDRDWVVVGATPEDMARRGFIPVGGDFPVFLHPRTKEEYALARTERKSGRGYKGFTFYTGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 81 DVTLEEDLIRRDLTINAMAEDDEGNLTDPYQGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARYAplGFTVAPETLELM 160
Cdd:PRK13297 92 DVTLEQDLQRRDLTVNAIARTPQGELVDPLDGVADVRARVLRHVGEAFAEDPVRILRLGRFAARFG--DFSIAPETMQLC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 161 RQLSESGELEALTPERSWKEISRALMEDQPQVFIQVLRDCDALKTLMPEVDalfgvpQPAAHHPEIDtglhtlsvlqQAA 240
Cdd:PRK13297 170 RRMVEAGEADALVPERVWKEVSRGLMAQAPSRMLDVLARAGALARVMPELH------DDAAVRAEID----------RAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 241 LHKQPLSVRWACLLHdlgkgLTPVDklpqhiahehrglkliKAVNERFKVPRDCQELALLVGQYhthgHRALELKA--ST 318
Cdd:PRK13297 234 AAGLPLAGRYALLCR-----HTPER----------------DALGRRLRAPVECMDQARLLPLA----VDALAASAtpAA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 319 LLELLQSFDVYRRPQRFEEFVAACEMDARGREGFEQRsypQADYLRG--AAKVAREVPVAPllekgfkgPELGEALKRER 396
Cdd:PRK13297 289 QLDLIERCDALRKPERFDALLQAAAIVAPVDLSAWRA---RVQAVRAidAGAIARQCAGDP--------ARIKPALRQAR 357
|
....*.
gi 518653987 397 LKALKA 402
Cdd:PRK13297 358 LQALGG 363
|
|
| PRK13296 |
PRK13296 |
CCA tRNA nucleotidyltransferase; |
1-217 |
1.10e-73 |
|
CCA tRNA nucleotidyltransferase;
Pssm-ID: 106256 [Multi-domain] Cd Length: 360 Bit Score: 234.49 E-value: 1.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 1 MKIYKVGGAVRDRLLGIEVTDIDRVVVGATAEEMLAKGYKPVGADFPVFLDPKNGDEYALARTERKNGRGYGGFIFHASP 80
Cdd:PRK13296 1 MKFYLVGGAVRDMLLGITPKDKDWVVVGATEDEMLANGFIKIAANFPVFIHPQTKQEYALARSEKKTASGYHGFEVNFSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 81 DVTLEEDLIRRDLTINAMAEDDEGNLTDPYQGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARYAPLGFTVAPETLELM 160
Cdd:PRK13296 81 YITLEDDLKRRDLTINSIAIDQNNKVIDPFNGQADLQNRILRHTSIAFIEDPLRVVRLARFKAQLSNFNFSIAQEMLALI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518653987 161 RQLSESGELEALTPERSWKEISRALmeDQPQVFIQVLRDCDALKTLMPEVD-ALFGVP 217
Cdd:PRK13296 161 KELVKTGELNHLTRERLHIEFVKAL--NNPKIFFTTLKELEALKIIFPNIScILPLIP 216
|
|
| tRNA_CCA_actino |
TIGR02692 |
tRNA adenylyltransferase; The enzyme tRNA adenylyltransferase, also called ... |
3-259 |
5.93e-35 |
|
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: 134.47 E-value: 5.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 3 IYKVGGAVRDRLLGIEVTDIDrVVVGATAEEMLA--KGYKPV----GADFPVFLDPKNGDEY--------ALARTERKNG 68
Cdd:TIGR02692 30 LYLVGGSVRDALLGRLGHDLD-FTTDARPEETLAilRPWADAvwdtGIAFGTVGAEKDGQQIeittfrsdSYDGTSRKPE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 69 RGYGGfifhaspdvTLEEDLIRRDLTINAMA----EDDEGNLTDPYQGQRDLEARLLRHVSP---AFAEDPLRVLRVARF 141
Cdd:TIGR02692 109 VTFGD---------TLEGDLIRRDFTVNAMAvripADGSLEFHDPVGGLDDLLAKVLDTPATpeqSFGDDPLRMLRAARF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 142 AARyapLGFTVAPETLELMRQLseSGELEALTPERSWKEISRALMEDQPQVFIQVLRDCDALKTLMPEVDALfgVPQPAA 221
Cdd:TIGR02692 180 VSQ---LGFEVAPRVRAAMTEM--ADQIERISAERVRVELDKLLLGDHPRAGIDLMVETGLADRVLPEIPAL--RLEIDE 252
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 518653987 222 HHPEIDTGLHTLSVLQQA---ALHKQPLSVRWACLLHDLGK 259
Cdd:TIGR02692 253 HHQHKDVYEHSLTVLRQAidlEDDGPDLVLRWAALLHDIGK 293
|
|
| PRK13299 |
PRK13299 |
tRNA CCA-pyrophosphorylase; Provisional |
4-206 |
1.89e-30 |
|
tRNA CCA-pyrophosphorylase; Provisional
Pssm-ID: 237339 [Multi-domain] Cd Length: 394 Bit Score: 120.72 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 4 YKVGGAVRDRLLGIEVTDIDrVVVGATAEEMLA---KGYkPVGADFPVFLDPKNGDEYALA--RTErkngrgyGGFIFHA 78
Cdd:PRK13299 24 YFVGGSVRDYLLGRPIHDVD-IATSAYPEEVKAifpRTV-DVGIEHGTVLVLENGEEYEVTtfRTE-------SEYVDYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 79 SPD-VT----LEEDLIRRDLTINAMAEDDEGNLTDPYQGQRDLEARLLRHV-SPA--FAEDPLRVLRVARFAARyapLGF 150
Cdd:PRK13299 95 RPSeVTfvrsLEEDLKRRDFTINAIAMDENGEIIDLFDGLEDLKNRLIRAVgNAEerFQEDALRMMRAVRFASQ---LGF 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518653987 151 TVAPETLELMRQLSESgeLEALTPERSWKEISRALMEDQPQVFIQVLRDCDALKTL 206
Cdd:PRK13299 172 DLETETFEAMKTQAPL--LEKISVERIFVEFEKLLLGPFWRKGLKLLIETGLYNYL 225
|
|
| NT_ClassII-CCAase |
cd05398 |
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ... |
1-118 |
1.43e-26 |
|
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: 103.44 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 1 MKIYKVGGAVRDRLLGIEVTDIDRVVVGATAEEM--LAKGYK----PVGADFPV--FLDPKNGDEYALARTERKngrgYG 72
Cdd:cd05398 17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAeaLFKKIGgrvvGLGEEFGTatVVINGLTIDVATLRTETY----TD 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 518653987 73 GFIFHASPDVTLEEDLIRRDLTINAMAED-DEGNLTDPYQGQRDLEA 118
Cdd:cd05398 93 PGRRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
|
|
| pcnB |
TIGR01942 |
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ... |
4-214 |
2.25e-23 |
|
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: 101.03 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 4 YKVGGAVRDRLLGIEVTDIDrVVVGATAEEM--LAKGYKPVGADFPV--FLDPKNGDEYALARTERKNGRGYGGFIFHAS 79
Cdd:TIGR01942 33 YIVGGAVRDLLLGIEPKDFD-VVTSATPEEVrkLFRNSRIVGRRFRLvhVSFGRQIIEVATFRSGHKSSVNAEGRILKDN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 80 PDVTLEEDLIRRDLTINAMAEDDEGN-LTDPYQGQRDLEARLLRHVSPA---FAEDPLRVLRVARFAARYaplGFTVAPE 155
Cdd:TIGR01942 112 VYGTLEEDAWRRDFTVNALYYDPSREvIIDYVGGMEDLKNRRLRLIGDPrsrYQEDPVRMLRALRFSVKL---EFTIDES 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518653987 156 TLELMRQLSEsgELEALTPERSWKEISRALMEDQPQVFIQVLRDCDALKTLMPEVDALF 214
Cdd:TIGR01942 189 TARPIRESAP--LLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLEPLFPSVAYAL 245
|
|
| PolyA_pol |
pfam01743 |
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ... |
3-122 |
3.58e-22 |
|
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: 91.19 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 3 IYKVGGAVRDRLLGIEVTDIDrVVVGATAEEMLA------KGYKPVGADFPVFLDPKNGDEYALARTerkngRGYGGFIF 76
Cdd:pfam01743 1 LYIVGGAVRDLLLGKTPKDVD-IATDATPEQVATlfrrrrIVHLLSGIEFGTIHVIFGNQILEVATF-----RIEFDESD 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 518653987 77 HASPDV-----TLEEDLIRRDLTINAMAED-DEGNLTDPYQGQRDLEARLLR 122
Cdd:pfam01743 75 FRNPRSeeytgTLEEDAKRRDFTINALAYNpNSGEVIDYFGGIKDLKSGVIR 126
|
|
| pcnB |
PRK11623 |
poly(A) polymerase I; Provisional |
4-164 |
1.59e-11 |
|
poly(A) polymerase I; Provisional
Pssm-ID: 236939 [Multi-domain] Cd Length: 472 Bit Score: 65.54 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 4 YKVGGAVRDRLLGIEVTDIDrVVVGATAEEM--LAKGYKPVGADFP---VFLDPK-------NGDEYALARTERKNGRGY 71
Cdd:PRK11623 70 YLVGGGVRDLLLGKKPKDFD-VTTNATPEQVrkLFRNCRLVGRRFRlahVMFGPEiievatfRGHHEGNESDRNTSQRGQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 72 GGFIFHASPDVTLEEDLIRRDLTINAMAED-DEGNLTDPYQGQRDLEA---RLLRHVSPAFAEDPLRVLRVARFAARyap 147
Cdd:PRK11623 149 NGMLLRDNIFGSIEEDAQRRDFTINSLYYSvADFTVRDYVGGMKDLKEgviRLIGNPETRYREDPVRMLRAVRFAAK--- 225
|
170
....*....|....*..
gi 518653987 148 LGFTVAPETLELMRQLS 164
Cdd:PRK11623 226 LDMRISPETAEPIPRLA 242
|
|
| PolyA_pol_RNAbd |
pfam12627 |
Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA ... |
149-214 |
2.51e-10 |
|
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: 55.95 E-value: 2.51e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518653987 149 GFTVAPETLELMRQLSEsgELEALTPERSWKEISRALMEDQPQVFIQVLRDCDALKTLMPEVDALF 214
Cdd:pfam12627 1 GFTIEPETREAIRKLAP--LLKKISPERIFEELLKLLLSGHPERGLELLRETGLLEYLFPELAAAL 64
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
231-323 |
7.66e-05 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 41.84 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 231 HTLSVLQQAALH------KQPLSVRWACLLHDLGKGLTPVDKLPQHIAHEH--RGLKLIKAVNERFKVpRDCQELALlvg 302
Cdd:pfam01966 4 HSLRVALLARELaeelgeLDRELLLLAALLHDIGKGPFGDEKPEFEIFLGHavVGAEILRELEKRLGL-EDVLKLIL--- 79
|
90 100
....*....|....*....|.
gi 518653987 303 qYHTHGHRALELKASTLLELL 323
Cdd:pfam01966 80 -EHHESWEGAGYPEEISLEAR 99
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
231-323 |
2.37e-04 |
|
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: 40.74 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 231 HTLSVLQQAAL------HKQPLSVRWACLLHDLGKGLTP---VDKLPQHIAHEHRGLKLIKavneRFKVPRDCQELALLV 301
Cdd:smart00471 8 HSLRVAQLAAAlaeelgLLDIELLLLAALLHDIGKPGTPdsfLVKTSVLEDHHFIGAEILL----EEEEPRILEEILRTA 83
|
90 100
....*....|....*....|..
gi 518653987 302 GQYHTHGHRALELKASTLLELL 323
Cdd:smart00471 84 ILSHHERPDGLRGEPITLEARI 105
|
|
| UTase_glnD |
TIGR01693 |
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ... |
127-301 |
4.34e-04 |
|
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase/uridylyl-removing enzyme for the nitrogen regulatory protein PII. Not all homologs of PII share the property of uridylyltransferase modification on the characteristic Tyr residue (see Prosite pattern PS00496 and document PDOC00439), but the modification site is preserved in the PII homolog of all species with a member of this family. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, Protein interactions]
Pssm-ID: 273761 [Multi-domain] Cd Length: 850 Bit Score: 42.40 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 127 AFAEDPLRVLRVARFAARYaplGFTVAPETLelmRQLSESGELeALTPERSWKEISRALME--DQPQVFIQVLR---DCD 201
Cdd:TIGR01693 331 VFERDPALLLRLFAIAAQR---GLPIHPAAL---RQLTASLPL-LPTPLREDPEARELFLEllTSGNGTVRALRamnRAG 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518653987 202 ALKTLMPEVDALFGVPQ-PAAHHPEIDTglHTLSVLQQAA------LHKQ-PLSVRW------------ACLLHDLGKGl 261
Cdd:TIGR01693 404 VLGRFLPEWGRIVGQMQfDLFHVYTVDE--HTLRTVVHLApfargrLAREhPLASELmpkiedpellylAALLHDIGKG- 480
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518653987 262 TPVDklpqhiaHEHRGLKLIKAVNERFKVPR-DCQELALLV 301
Cdd:TIGR01693 481 RGGD-------HSVLGAEDARDVCPRLGLDRpDTELVAWLV 514
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
231-284 |
9.77e-04 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 39.24 E-value: 9.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518653987 231 HTLSVLQQAAL--------HKQPLSVRWACLLHDLGKGLTP----VDKLPQHIAHEHRGLKLIKAV 284
Cdd:cd00077 6 HSLRVAQLARRlaeelglsEEDIELLRLAALLHDIGKPGTPdaitEEESELEKDHAIVGAEILREL 71
|
|
| |
