|
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: 822.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 1 MKIYLVGGAIRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTDFTCYAAP 80
Cdd:PRK10885 1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 81 DVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLTLM 160
Cdd:PRK10885 81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 161 REMTHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVPAPARWHPEIDTGIHTLMTLSMAA 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 241 MLSPQVDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIHTFPMLNPKTIV 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 321 KLFDSIDAWRKPQRVEQLALTSEADVRGRTGFESADYPQGRWLREAWEVAQSVPTKAVVEAGFKGVEIREELTRRRIAAV 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400
|
....*....
gi 1414818703 401 ASWKEQRCP 409
Cdd:PRK10885 401 AAWKEQRCP 409
|
|
| PcnB |
COG0617 |
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ... |
1-403 |
7.94e-125 |
|
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: 366.45 E-value: 7.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 1 MKIYLVGGAIRDALLGLPVKDRDWVVVGsTPQEMLDAG-----YQQVGRDFPVFLHP--QTHEEYALARTERKSGSGYTD 73
Cdd:COG0617 18 FEAYLVGGAVRDLLLGRPPKDIDIVTVA-TPEEVAALFrkalrTVPVGRDFGTVTVVfgGEKIEVATARTERYYGDGRRP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 74 FTCYAApdvTLEDDLKRRDLTINALAQDDN-GEIIDPYNGLGDLQNRLLRHVS---PAFGEDPLRVLRVARFAARyahLG 149
Cdd:COG0617 97 FVEFGD---TLEEDLARRDFTINALAYDLNdGELIDPFGGLADLEARVIRTVGdpeERFREDPLRILRAVRFAAR---LG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 150 FRIADETLTLMREMthAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLfpeidalfgvpaparwhpeidtg 229
Cdd:COG0617 171 FTIEPETLAAIREM--AGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVL----------------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 230 ihtlmtlsmaamlspqvDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIH 309
Cdd:COG0617 226 -----------------ALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 310 TFPMLNPKTIVKLFDsidawRKPQRVEQLALTSEAdvrgrtGFESADYPQ--GRWLREAWEVAQ-SVPTKAVVEAGFK-G 385
Cdd:COG0617 289 GLGELRDSAVRRLLE-----RGPEALEDLLLLREN------GLEYPELQErlAELLEAAWRRFQpPVDGEDLMALGLKpG 357
|
410
....*....|....*...
gi 1414818703 386 VEIREELTRRRIAAVASW 403
Cdd:COG0617 358 PEIGEILRALREAVLDGG 375
|
|
| NT_ClassII-CCAase |
cd05398 |
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ... |
1-118 |
9.82e-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: 114.61 E-value: 9.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 1 MKIYLVGGAIRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHE--------EYALARTERKsgsgYT 72
Cdd:cd05398 17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEALFKKIGGRVVGLGEEFGTATvvingltiDVATLRTETY----TD 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1414818703 73 DFTCYAAPDVTLEDDLKRRDLTINALAQD-DNGEIIDPYNGLGDLQN 118
Cdd:cd05398 93 PGRRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
|
|
| PolyA_pol |
pfam01743 |
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ... |
3-122 |
2.70e-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: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 3 IYLVGGAIRDALLGLPVKDRDwVVVGSTPQEMLDAGYQQVGRDFPVFLHPQT------HEEYALARTerKSGSGYTDFtc 76
Cdd:pfam01743 1 LYIVGGAVRDLLLGKTPKDVD-IATDATPEQVATLFRRRRIVHLLSGIEFGTihvifgNQILEVATF--RIEFDESDF-- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1414818703 77 yAAPDV-----TLEDDLKRRDLTINALAQD-DNGEIIDPYNGLGDLQNRLLR 122
Cdd:pfam01743 76 -RNPRSeeytgTLEEDAKRRDFTINALAYNpNSGEVIDYFGGIKDLKSGVIR 126
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
228-328 |
1.68e-05 |
|
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: 43.82 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 228 TGIHTLMTLSMAAMLSPQVD------VRFATLCHDLGKGLTPPELWPR---HHGHGPAGVKLVEQlcqrLRVPNEIRDLA 298
Cdd:smart00471 5 VFEHSLRVAQLAAALAEELGlldielLLLAALLHDIGKPGTPDSFLVKtsvLEDHHFIGAEILLE----EEEPRILEEIL 80
|
90 100 110
....*....|....*....|....*....|....
gi 1414818703 299 RLVAEFHDLIHTF----PMLNPKTIVKLFDSIDA 328
Cdd:smart00471 81 RTAILSHHERPDGlrgePITLEARIVKVADRLDA 114
|
|
| HDIG |
TIGR00277 |
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ... |
231-296 |
1.27e-03 |
|
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: 37.32 E-value: 1.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1414818703 231 HTLMT----LSMAAMLSPQVD-VRFATLCHDLGKGLTPpeLWPRHHGHGPAGVKLVEQLCQRLRVPNEIRD 296
Cdd:TIGR00277 8 HSLEVaklaEALARELGLDVElARRGALLHDIGKPITR--EGVIFESHVVVGAEIARKYGEPLEVIDIIAE 76
|
|
| |
|
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: 822.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 1 MKIYLVGGAIRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTDFTCYAAP 80
Cdd:PRK10885 1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 81 DVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLTLM 160
Cdd:PRK10885 81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 161 REMTHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVPAPARWHPEIDTGIHTLMTLSMAA 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 241 MLSPQVDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIHTFPMLNPKTIV 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 321 KLFDSIDAWRKPQRVEQLALTSEADVRGRTGFESADYPQGRWLREAWEVAQSVPTKAVVEAGFKGVEIREELTRRRIAAV 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400
|
....*....
gi 1414818703 401 ASWKEQRCP 409
Cdd:PRK10885 401 AAWKEQRCP 409
|
|
| PRK13298 |
PRK13298 |
tRNA CCA-pyrophosphorylase; Provisional |
1-406 |
0e+00 |
|
tRNA CCA-pyrophosphorylase; Provisional
Pssm-ID: 237338 [Multi-domain] Cd Length: 417 Bit Score: 540.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 1 MKIYLVGGAIRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTDFTCYAAP 80
Cdd:PRK13298 1 MKIYLVGGAVRDSLLNLPVKDKDWVVVGGTPKILLSINFQQVGKDFPVFLHPETHEEYALARTERKSGVGYTGFITDTSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 81 DVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLTLM 160
Cdd:PRK13298 81 DVTLEEDLIRRDLTINAIAQDENGNYIDPFQGKKDIQLRLLRHVSESFIEDPLRVLRVARFAALLVHLGFKIAKETMILM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 161 REMTHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVPAPARWH-PEIDTGIHTLMTLSMA 239
Cdd:PRK13298 161 CIMVKKHELLYLTPERIWNETEKALKTDNPHVYFQVLYECNALKFLFPEIDFLYEKPYFLNSFfKKFNLGNYILMGLSKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 240 AMLSPQVDVRFATLCHDLGKGLTPPELWP--RHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIHTFPMLNPK 317
Cdd:PRK13298 241 SKLTKDIDIRFSYLCQFLGSMIPINQIKRnyKKIFFDKYAASLIKNLCKRFKIPSYIRNIAVLNTGFYFFLYNIHYQSSK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 318 TIVKLFDSIDAWRKPQRVEQLALTSEADVRGRTGFESADYPQGRWLREAWEVAQSVPTKAVVEAGFKGVEIREELTRRRI 397
Cdd:PRK13298 321 NIITLFSKIDAWRKPDRIKKLIFLSNFNLLRNKKSINFLIKQGNFLKKAFSVTKKISIKDILKKGFKGYEIKQELYRLRI 400
|
....*....
gi 1414818703 398 AAVASWKEQ 406
Cdd:PRK13298 401 HKLKFWRNK 409
|
|
| PcnB |
COG0617 |
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ... |
1-403 |
7.94e-125 |
|
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: 366.45 E-value: 7.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 1 MKIYLVGGAIRDALLGLPVKDRDWVVVGsTPQEMLDAG-----YQQVGRDFPVFLHP--QTHEEYALARTERKSGSGYTD 73
Cdd:COG0617 18 FEAYLVGGAVRDLLLGRPPKDIDIVTVA-TPEEVAALFrkalrTVPVGRDFGTVTVVfgGEKIEVATARTERYYGDGRRP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 74 FTCYAApdvTLEDDLKRRDLTINALAQDDN-GEIIDPYNGLGDLQNRLLRHVS---PAFGEDPLRVLRVARFAARyahLG 149
Cdd:COG0617 97 FVEFGD---TLEEDLARRDFTINALAYDLNdGELIDPFGGLADLEARVIRTVGdpeERFREDPLRILRAVRFAAR---LG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 150 FRIADETLTLMREMthAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLfpeidalfgvpaparwhpeidtg 229
Cdd:COG0617 171 FTIEPETLAAIREM--AGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVL----------------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 230 ihtlmtlsmaamlspqvDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIH 309
Cdd:COG0617 226 -----------------ALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 310 TFPMLNPKTIVKLFDsidawRKPQRVEQLALTSEAdvrgrtGFESADYPQ--GRWLREAWEVAQ-SVPTKAVVEAGFK-G 385
Cdd:COG0617 289 GLGELRDSAVRRLLE-----RGPEALEDLLLLREN------GLEYPELQErlAELLEAAWRRFQpPVDGEDLMALGLKpG 357
|
410
....*....|....*...
gi 1414818703 386 VEIREELTRRRIAAVASW 403
Cdd:COG0617 358 PEIGEILRALREAVLDGG 375
|
|
| PRK13297 |
PRK13297 |
tRNA CCA-pyrophosphorylase; Provisional |
1-339 |
9.00e-94 |
|
tRNA CCA-pyrophosphorylase; Provisional
Pssm-ID: 139469 [Multi-domain] Cd Length: 364 Bit Score: 286.12 E-value: 9.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 1 MKIYLVGGAIRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTDFTCYAAP 80
Cdd:PRK13297 12 LQVYIVGGAVRDALLGLPAGDRDWVVVGATPEDMARRGFIPVGGDFPVFLHPRTKEEYALARTERKSGRGYKGFTFYTGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 81 DVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHlgFRIADETLTLM 160
Cdd:PRK13297 92 DVTLEQDLQRRDLTVNAIARTPQGELVDPLDGVADVRARVLRHVGEAFAEDPVRILRLGRFAARFGD--FSIAPETMQLC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 161 REMTHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVpaparwHPEIDTgihtlmtlsmAA 240
Cdd:PRK13297 170 RRMVEAGEADALVPERVWKEVSRGLMAQAPSRMLDVLARAGALARVMPELHDDAAV------RAEIDR----------AA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 241 MLSPQVDVRFATLCHdlgkgLTPPELwprhhghgpagvklveQLCQRLRVPNEIRDLARLVAEFHDLIHTFPMlnPKTIV 320
Cdd:PRK13297 234 AAGLPLAGRYALLCR-----HTPERD----------------ALGRRLRAPVECMDQARLLPLAVDALAASAT--PAAQL 290
|
330
....*....|....*....
gi 1414818703 321 KLFDSIDAWRKPQRVEQLA 339
Cdd:PRK13297 291 DLIERCDALRKPERFDALL 309
|
|
| PRK13296 |
PRK13296 |
CCA tRNA nucleotidyltransferase; |
1-217 |
4.52e-90 |
|
CCA tRNA nucleotidyltransferase;
Pssm-ID: 106256 [Multi-domain] Cd Length: 360 Bit Score: 276.48 E-value: 4.52e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 1 MKIYLVGGAIRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTDFTCYAAP 80
Cdd:PRK13296 1 MKFYLVGGAVRDMLLGITPKDKDWVVVGATEDEMLANGFIKIAANFPVFIHPQTKQEYALARSEKKTASGYHGFEVNFSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 81 DVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLTLM 160
Cdd:PRK13296 81 YITLEDDLKRRDLTINSIAIDQNNKVIDPFNGQADLQNRILRHTSIAFIEDPLRVVRLARFKAQLSNFNFSIAQEMLALI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1414818703 161 REMTHAGELEHLTPERVWKETESALttRNPQVFFQVLRDCGALRVLFPEID-ALFGVP 217
Cdd:PRK13296 161 KELVKTGELNHLTRERLHIEFVKAL--NNPKIFFTTLKELEALKIIFPNIScILPLIP 216
|
|
| PRK13299 |
PRK13299 |
tRNA CCA-pyrophosphorylase; Provisional |
4-238 |
9.16e-41 |
|
tRNA CCA-pyrophosphorylase; Provisional
Pssm-ID: 237339 [Multi-domain] Cd Length: 394 Bit Score: 148.83 E-value: 9.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 4 YLVGGAIRDALLGLPVKDRDwVVVGSTPQEMLDAgYQ---QVGRDFPVFLHPQTHEEYALA--RTErksgSGYTDftcYA 78
Cdd:PRK13299 24 YFVGGSVRDYLLGRPIHDVD-IATSAYPEEVKAI-FPrtvDVGIEHGTVLVLENGEEYEVTtfRTE----SEYVD---YR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 79 APD-VT----LEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHV-SPA--FGEDPLRVLRVARFAARyahLGF 150
Cdd:PRK13299 95 RPSeVTfvrsLEEDLKRRDFTINAIAMDENGEIIDLFDGLEDLKNRLIRAVgNAEerFQEDALRMMRAVRFASQ---LGF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 151 RIADETLTLMREmtHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGalrvLFPEI-------DALFGVPAPARWH 223
Cdd:PRK13299 172 DLETETFEAMKT--QAPLLEKISVERIFVEFEKLLLGPFWRKGLKLLIETG----LYNYLpglkgkeENLLKLTQLLWFS 245
|
250
....*....|....*
gi 1414818703 224 PEIDTGIHTLMTLSM 238
Cdd:PRK13299 246 FETSEQAWAALLISL 260
|
|
| NT_ClassII-CCAase |
cd05398 |
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ... |
1-118 |
9.82e-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: 114.61 E-value: 9.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 1 MKIYLVGGAIRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHE--------EYALARTERKsgsgYT 72
Cdd:cd05398 17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEALFKKIGGRVVGLGEEFGTATvvingltiDVATLRTETY----TD 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1414818703 73 DFTCYAAPDVTLEDDLKRRDLTINALAQD-DNGEIIDPYNGLGDLQN 118
Cdd:cd05398 93 PGRRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
|
|
| PolyA_pol |
pfam01743 |
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ... |
3-122 |
2.70e-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: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 3 IYLVGGAIRDALLGLPVKDRDwVVVGSTPQEMLDAGYQQVGRDFPVFLHPQT------HEEYALARTerKSGSGYTDFtc 76
Cdd:pfam01743 1 LYIVGGAVRDLLLGKTPKDVD-IATDATPEQVATLFRRRRIVHLLSGIEFGTihvifgNQILEVATF--RIEFDESDF-- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1414818703 77 yAAPDV-----TLEDDLKRRDLTINALAQD-DNGEIIDPYNGLGDLQNRLLR 122
Cdd:pfam01743 76 -RNPRSeeytgTLEEDAKRRDFTINALAYNpNSGEVIDYFGGIKDLKSGVIR 126
|
|
| pcnB |
PRK11623 |
poly(A) polymerase I; Provisional |
4-214 |
8.15e-14 |
|
poly(A) polymerase I; Provisional
Pssm-ID: 236939 [Multi-domain] Cd Length: 472 Bit Score: 72.86 E-value: 8.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 4 YLVGGAIRDALLGLPVKDRDwVVVGSTPQEM--LDAGYQQVGRDFP---VFLHPQT---------HEEYALARTER---K 66
Cdd:PRK11623 70 YLVGGGVRDLLLGKKPKDFD-VTTNATPEQVrkLFRNCRLVGRRFRlahVMFGPEIievatfrghHEGNESDRNTSqrgQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 67 SGSGYTD--FTcyaapdvTLEDDLKRRDLTINALAQD-DNGEIIDPYNGLGDLQN---RLLRHVSPAFGEDPLRVLRVAR 140
Cdd:PRK11623 149 NGMLLRDniFG-------SIEEDAQRRDFTINSLYYSvADFTVRDYVGGMKDLKEgviRLIGNPETRYREDPVRMLRAVR 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1414818703 141 FAARyahLGFRIADETLTLMREMthAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALF 214
Cdd:PRK11623 222 FAAK---LDMRISPETAEPIPRL--ATLLNDIPPARLFEESLKLLQAGYGYETYKLLCEYHLFQPLFPTITRYF 290
|
|
| PolyA_pol_RNAbd |
pfam12627 |
Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA ... |
149-214 |
2.60e-13 |
|
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: 64.43 E-value: 2.60e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1414818703 149 GFRIADETLTLMREMTHagELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALF 214
Cdd:pfam12627 1 GFTIEPETREAIRKLAP--LLKKISPERIFEELLKLLLSGHPERGLELLRETGLLEYLFPELAAAL 64
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
228-329 |
1.88e-10 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 57.63 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 228 TGIHTLMTLSMAAMLSPQVD------VRFATLCHDLGKGLTPPE--LWPRHHGHGPAGVKLVEQLCQRLRVpneiRDLAR 299
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGeldrelLLLAALLHDIGKGPFGDEkpEFEIFLGHAVVGAEILRELEKRLGL----EDVLK 76
|
90 100 110
....*....|....*....|....*....|....
gi 1414818703 300 LVAEFHDLIHTFPMLNPKT----IVKLFDSIDAW 329
Cdd:pfam01966 77 LILEHHESWEGAGYPEEISlearIVKLADRLDAL 110
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
227-343 |
7.27e-07 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 48.49 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 227 DTGIHTLMTLSMAAMLSPQVD--------VRFATLCHDLGKGLTP----PELWPRHHGHGPAGVKLVEQLcQRLRVPNEI 294
Cdd:cd00077 2 HRFEHSLRVAQLARRLAEELGlseedielLRLAALLHDIGKPGTPdaitEEESELEKDHAIVGAEILREL-LLEEVIKLI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1414818703 295 RDLARLVAEFH----------DLIHTFPMLNPKTIVKLFDSIDAWRKPQRVEQLALTSE 343
Cdd:cd00077 81 DELILAVDASHherldglgypDGLKGEEITLEARIVKLADRLDALRRDSREKRRRIAEE 139
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
228-328 |
1.68e-05 |
|
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: 43.82 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1414818703 228 TGIHTLMTLSMAAMLSPQVD------VRFATLCHDLGKGLTPPELWPR---HHGHGPAGVKLVEQlcqrLRVPNEIRDLA 298
Cdd:smart00471 5 VFEHSLRVAQLAAALAEELGlldielLLLAALLHDIGKPGTPDSFLVKtsvLEDHHFIGAEILLE----EEEPRILEEIL 80
|
90 100 110
....*....|....*....|....*....|....
gi 1414818703 299 RLVAEFHDLIHTF----PMLNPKTIVKLFDSIDA 328
Cdd:smart00471 81 RTAILSHHERPDGlrgePITLEARIVKVADRLDA 114
|
|
| HDIG |
TIGR00277 |
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ... |
231-296 |
1.27e-03 |
|
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: 37.32 E-value: 1.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1414818703 231 HTLMT----LSMAAMLSPQVD-VRFATLCHDLGKGLTPpeLWPRHHGHGPAGVKLVEQLCQRLRVPNEIRD 296
Cdd:TIGR00277 8 HSLEVaklaEALARELGLDVElARRGALLHDIGKPITR--EGVIFESHVVVGAEIARKYGEPLEVIDIIAE 76
|
|
| |
