|
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: 755.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 1 MKVYLVGGAVRDQLLGLPISDRDYVVVGATPEAMLSQGFQQVGKDFPVFLHPKTHEEYALARTERKIGAGYTGFSCYSAP 80
Cdd:PRK10885 1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 81 DVTIEDDLLRRDLTINAIAQDESGEIIDPFHGVIDLDKRILRHVSDAFSEDPLRVLRVARFAARYFEHGFTIAPETLALM 160
Cdd:PRK10885 81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 161 QTMAATGELSHLTAERVWTETEKALKSNSPQVYFDVLRQCGALAVLFPEIDALFGVPAPEKWHPEIDTGIHTLMVMKVIS 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 241 RLSKDVDIRFAALCHDLGKALTPPDIWPSHPNHGEAGIPLIETLCVRLKVPTTARDLARLAARYHDKIHVINKLHANDLI 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 321 AIFDGLDSWRKPERVEQLSLISEADARGRLGLEQQPYPQGVYFRQAFAIAQAVEVKPIVEQGFKGPEIRQELTRQRIEAV 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400
|
....*....
gi 491046917 401 GNWQQRQKI 409
Cdd:PRK10885 401 AAWKEQRCP 409
|
|
| PcnB |
COG0617 |
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ... |
1-408 |
7.36e-119 |
|
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: 351.04 E-value: 7.36e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 1 MKVYLVGGAVRDQLLGLPISDRDYVVVgATPEAMLSQG-----FQQVGKDFPVFLHP--KTHEEYALARTERKIGAGYTG 73
Cdd:COG0617 18 FEAYLVGGAVRDLLLGRPPKDIDIVTV-ATPEEVAALFrkalrTVPVGRDFGTVTVVfgGEKIEVATARTERYYGDGRRP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 74 FSCYSApdvTIEDDLLRRDLTINAIAQDE-SGEIIDPFHGVIDLDKRILRHVSDA---FSEDPLRVLRVARFAARYfehG 149
Cdd:COG0617 97 FVEFGD---TLEEDLARRDFTINALAYDLnDGELIDPFGGLADLEARVIRTVGDPeerFREDPLRILRAVRFAARL---G 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 150 FTIAPETLALMQTMAatGELSHLTAERVWTETEKALKSNSPQVYFDVLRQCGALAVLfpeidalfgvpapekwhpeidtg 229
Cdd:COG0617 171 FTIEPETLAAIREMA--GLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVL----------------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 230 ihtlmvmkvisrlskdvDIRFAALCHDLGKALTPPDIWPSHPNHGEAGIPLIETLCVRLKVPTTARDLARLAARYHDKIH 309
Cdd:COG0617 226 -----------------ALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 310 VINKLHANDLIAIFDgldswRKPERVEQLSLISEadARGRLGLEQQPYPQgvYFRQAFAIAQ-AVEVKPIVEQGFK-GPE 387
Cdd:COG0617 289 GLGELRDSAVRRLLE-----RGPEALEDLLLLRE--NGLEYPELQERLAE--LLEAAWRRFQpPVDGEDLMALGLKpGPE 359
|
410 420
....*....|....*....|.
gi 491046917 388 IRQELTRQRIEAVGNWQQRQK 408
Cdd:COG0617 360 IGEILRALREAVLDGGIPNRR 380
|
|
| pcnB |
TIGR01942 |
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ... |
4-304 |
1.33e-27 |
|
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: 112.97 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 4 YLVGGAVRDQLLGLPISDRDyVVVGATPEAM--LSQGFQQVGKDFPVfLH---PKTHEEYALARTERKIGAGYTGFSCYS 78
Cdd:TIGR01942 33 YIVGGAVRDLLLGIEPKDFD-VVTSATPEEVrkLFRNSRIVGRRFRL-VHvsfGRQIIEVATFRSGHKSSVNAEGRILKD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 79 APDVTIEDDLLRRDLTINAIAQDESGEIIDPFH-GVIDLDKRILRHVSDAFS---EDPLRVLRVARFAARYfehGFTIAP 154
Cdd:TIGR01942 111 NVYGTLEEDAWRRDFTVNALYYDPSREVIIDYVgGMEDLKNRRLRLIGDPRSryqEDPVRMLRALRFSVKL---EFTIDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 155 ETLALMQTMAAtgELSHLTAERVWTETEKALKSNSPQVYFDVLRQCGALAVLFPEIDALFGvpapekwhpEIDTGIHTLM 234
Cdd:TIGR01942 188 STARPIRESAP--LLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLEPLFPSVAYALR---------ESPKFESAFT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 235 VMKVISRLSKDVDIRFAALCHDLGKALTPPDI---WPSHPNHGEAGIP--------LIETLCVRLKVP----TTARDLAR 299
Cdd:TIGR01942 257 VQALVNDTDFRVKRDKPVTPAFLYAALLWPGLvfrVADAPDQGVMPYPavfdairdFVEEQCAPISIPkrfsIPTREIWQ 336
|
....*
gi 491046917 300 LAARY 304
Cdd:TIGR01942 337 MQLRL 341
|
|
| NT_ClassII-CCAase |
cd05398 |
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ... |
1-118 |
1.68e-27 |
|
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: 106.14 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 1 MKVYLVGGAVRDQLLGLPISDRDYVVVGATPEAMlsQGFQQVGKdFPVFLHPKTHE-----------EYALARTERKiga 69
Cdd:cd05398 17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFA--EALFKKIG-GRVVGLGEEFGtatvvingltiDVATLRTETY--- 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 491046917 70 gYTGFSCYSAPDVTIEDDLLRRDLTINAIAQD-ESGEIIDPFHGVIDLDK 118
Cdd:cd05398 91 -TDPGRRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
|
|
| PolyA_pol |
pfam01743 |
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ... |
4-122 |
5.52e-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: 85.02 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 4 YLVGGAVRDQLLGLPISDRDyVVVGATPEaMLSQGFQQ-------VGKDFPVFLHPKTHEEYALA--RTERK-IGAGYTG 73
Cdd:pfam01743 2 YIVGGAVRDLLLGKTPKDVD-IATDATPE-QVATLFRRrrivhllSGIEFGTIHVIFGNQILEVAtfRIEFDeSDFRNPR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 491046917 74 FSCYSApdvTIEDDLLRRDLTINAIAQDE-SGEIIDPFHGVIDLDKRILR 122
Cdd:pfam01743 80 SEEYTG---TLEEDAKRRDFTINALAYNPnSGEVIDYFGGIKDLKSGVIR 126
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
228-322 |
1.21e-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: 41.51 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 228 TGIHTLMVMKVISRLSKDVD------IRFAALCHDLGKALTPPDIWP---SHPNHGEAGIPLIEtlcvRLKVPTTARDLA 298
Cdd:smart00471 5 VFEHSLRVAQLAAALAEELGlldielLLLAALLHDIGKPGTPDSFLVktsVLEDHHFIGAEILL----EEEEPRILEEIL 80
|
90 100
....*....|....*....|....
gi 491046917 299 RLAARYHDKIHVINKLHANDLIAI 322
Cdd:smart00471 81 RTAILSHHERPDGLRGEPITLEAR 104
|
|
| |
|
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: 755.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 1 MKVYLVGGAVRDQLLGLPISDRDYVVVGATPEAMLSQGFQQVGKDFPVFLHPKTHEEYALARTERKIGAGYTGFSCYSAP 80
Cdd:PRK10885 1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 81 DVTIEDDLLRRDLTINAIAQDESGEIIDPFHGVIDLDKRILRHVSDAFSEDPLRVLRVARFAARYFEHGFTIAPETLALM 160
Cdd:PRK10885 81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 161 QTMAATGELSHLTAERVWTETEKALKSNSPQVYFDVLRQCGALAVLFPEIDALFGVPAPEKWHPEIDTGIHTLMVMKVIS 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 241 RLSKDVDIRFAALCHDLGKALTPPDIWPSHPNHGEAGIPLIETLCVRLKVPTTARDLARLAARYHDKIHVINKLHANDLI 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 321 AIFDGLDSWRKPERVEQLSLISEADARGRLGLEQQPYPQGVYFRQAFAIAQAVEVKPIVEQGFKGPEIRQELTRQRIEAV 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400
|
....*....
gi 491046917 401 GNWQQRQKI 409
Cdd:PRK10885 401 AAWKEQRCP 409
|
|
| PRK13298 |
PRK13298 |
tRNA CCA-pyrophosphorylase; Provisional |
1-411 |
0e+00 |
|
tRNA CCA-pyrophosphorylase; Provisional
Pssm-ID: 237338 [Multi-domain] Cd Length: 417 Bit Score: 521.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 1 MKVYLVGGAVRDQLLGLPISDRDYVVVGATPEAMLSQGFQQVGKDFPVFLHPKTHEEYALARTERKIGAGYTGFSCYSAP 80
Cdd:PRK13298 1 MKIYLVGGAVRDSLLNLPVKDKDWVVVGGTPKILLSINFQQVGKDFPVFLHPETHEEYALARTERKSGVGYTGFITDTSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 81 DVTIEDDLLRRDLTINAIAQDESGEIIDPFHGVIDLDKRILRHVSDAFSEDPLRVLRVARFAARYFEHGFTIAPETLALM 160
Cdd:PRK13298 81 DVTLEEDLIRRDLTINAIAQDENGNYIDPFQGKKDIQLRLLRHVSESFIEDPLRVLRVARFAALLVHLGFKIAKETMILM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 161 QTMAATGELSHLTAERVWTETEKALKSNSPQVYFDVLRQCGALAVLFPEIDALFGVPAPEKWH-PEIDTGIHTLMVMKVI 239
Cdd:PRK13298 161 CIMVKKHELLYLTPERIWNETEKALKTDNPHVYFQVLYECNALKFLFPEIDFLYEKPYFLNSFfKKFNLGNYILMGLSKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 240 SRLSKDVDIRFAALCHDLGKALTPPDIWPS--HPNHGEAGIPLIETLCVRLKVPTTARDLARLAARYHDKIHVINKLHAN 317
Cdd:PRK13298 241 SKLTKDIDIRFSYLCQFLGSMIPINQIKRNykKIFFDKYAASLIKNLCKRFKIPSYIRNIAVLNTGFYFFLYNIHYQSSK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 318 DLIAIFDGLDSWRKPERVEQLSLISEADARGRLGLEQQPYPQGVYFRQAFAIAQAVEVKPIVEQGFKGPEIRQELTRQRI 397
Cdd:PRK13298 321 NIITLFSKIDAWRKPDRIKKLIFLSNFNLLRNKKSINFLIKQGNFLKKAFSVTKKISIKDILKKGFKGYEIKQELYRLRI 400
|
410
....*....|....
gi 491046917 398 EAVGNWqqRQKIIV 411
Cdd:PRK13298 401 HKLKFW--RNKIIK 412
|
|
| PcnB |
COG0617 |
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ... |
1-408 |
7.36e-119 |
|
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: 351.04 E-value: 7.36e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 1 MKVYLVGGAVRDQLLGLPISDRDYVVVgATPEAMLSQG-----FQQVGKDFPVFLHP--KTHEEYALARTERKIGAGYTG 73
Cdd:COG0617 18 FEAYLVGGAVRDLLLGRPPKDIDIVTV-ATPEEVAALFrkalrTVPVGRDFGTVTVVfgGEKIEVATARTERYYGDGRRP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 74 FSCYSApdvTIEDDLLRRDLTINAIAQDE-SGEIIDPFHGVIDLDKRILRHVSDA---FSEDPLRVLRVARFAARYfehG 149
Cdd:COG0617 97 FVEFGD---TLEEDLARRDFTINALAYDLnDGELIDPFGGLADLEARVIRTVGDPeerFREDPLRILRAVRFAARL---G 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 150 FTIAPETLALMQTMAatGELSHLTAERVWTETEKALKSNSPQVYFDVLRQCGALAVLfpeidalfgvpapekwhpeidtg 229
Cdd:COG0617 171 FTIEPETLAAIREMA--GLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVL----------------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 230 ihtlmvmkvisrlskdvDIRFAALCHDLGKALTPPDIWPSHPNHGEAGIPLIETLCVRLKVPTTARDLARLAARYHDKIH 309
Cdd:COG0617 226 -----------------ALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 310 VINKLHANDLIAIFDgldswRKPERVEQLSLISEadARGRLGLEQQPYPQgvYFRQAFAIAQ-AVEVKPIVEQGFK-GPE 387
Cdd:COG0617 289 GLGELRDSAVRRLLE-----RGPEALEDLLLLRE--NGLEYPELQERLAE--LLEAAWRRFQpPVDGEDLMALGLKpGPE 359
|
410 420
....*....|....*....|.
gi 491046917 388 IRQELTRQRIEAVGNWQQRQK 408
Cdd:COG0617 360 IGEILRALREAVLDGGIPNRR 380
|
|
| PRK13297 |
PRK13297 |
tRNA CCA-pyrophosphorylase; Provisional |
1-401 |
2.25e-94 |
|
tRNA CCA-pyrophosphorylase; Provisional
Pssm-ID: 139469 [Multi-domain] Cd Length: 364 Bit Score: 287.66 E-value: 2.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 1 MKVYLVGGAVRDQLLGLPISDRDYVVVGATPEAMLSQGFQQVGKDFPVFLHPKTHEEYALARTERKIGAGYTGFSCYSAP 80
Cdd:PRK13297 12 LQVYIVGGAVRDALLGLPAGDRDWVVVGATPEDMARRGFIPVGGDFPVFLHPRTKEEYALARTERKSGRGYKGFTFYTGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 81 DVTIEDDLLRRDLTINAIAQDESGEIIDPFHGVIDLDKRILRHVSDAFSEDPLRVLRVARFAARYFEhgFTIAPETLALM 160
Cdd:PRK13297 92 DVTLEQDLQRRDLTVNAIARTPQGELVDPLDGVADVRARVLRHVGEAFAEDPVRILRLGRFAARFGD--FSIAPETMQLC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 161 QTMAATGELSHLTAERVWTETEKALKSNSPQVYFDVLRQCGALAVLFPEIDALFGVpapekwHPEIDTGihtlmvmkviS 240
Cdd:PRK13297 170 RRMVEAGEADALVPERVWKEVSRGLMAQAPSRMLDVLARAGALARVMPELHDDAAV------RAEIDRA----------A 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 241 RLSKDVDIRFAALCHdlgkaLTP-PDiwpshpnhgeagiplieTLCVRLKVPTTARDLARLAARYHDKIHVINKLHAN-D 318
Cdd:PRK13297 234 AAGLPLAGRYALLCR-----HTPeRD-----------------ALGRRLRAPVECMDQARLLPLAVDALAASATPAAQlD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 319 LIAIFDGLdswRKPER----VEQLSLISEADARGrlgleqqpypqgvyFRQAFAIAQAVEVKPIVEQGFKGP-EIRQELT 393
Cdd:PRK13297 292 LIERCDAL---RKPERfdalLQAAAIVAPVDLSA--------------WRARVQAVRAIDAGAIARQCAGDPaRIKPALR 354
|
....*...
gi 491046917 394 RQRIEAVG 401
Cdd:PRK13297 355 QARLQALG 362
|
|
| PRK13296 |
PRK13296 |
CCA tRNA nucleotidyltransferase; |
1-217 |
5.62e-82 |
|
CCA tRNA nucleotidyltransferase;
Pssm-ID: 106256 [Multi-domain] Cd Length: 360 Bit Score: 255.68 E-value: 5.62e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 1 MKVYLVGGAVRDQLLGLPISDRDYVVVGATPEAMLSQGFQQVGKDFPVFLHPKTHEEYALARTERKIGAGYTGFSCYSAP 80
Cdd:PRK13296 1 MKFYLVGGAVRDMLLGITPKDKDWVVVGATEDEMLANGFIKIAANFPVFIHPQTKQEYALARSEKKTASGYHGFEVNFSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 81 DVTIEDDLLRRDLTINAIAQDESGEIIDPFHGVIDLDKRILRHVSDAFSEDPLRVLRVARFAARYFEHGFTIAPETLALM 160
Cdd:PRK13296 81 YITLEDDLKRRDLTINSIAIDQNNKVIDPFNGQADLQNRILRHTSIAFIEDPLRVVRLARFKAQLSNFNFSIAQEMLALI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491046917 161 QTMAATGELSHLTAERVWTETEKALksNSPQVYFDVLRQCGALAVLFPEID-ALFGVP 217
Cdd:PRK13296 161 KELVKTGELNHLTRERLHIEFVKAL--NNPKIFFTTLKELEALKIIFPNIScILPLIP 216
|
|
| PRK13299 |
PRK13299 |
tRNA CCA-pyrophosphorylase; Provisional |
4-236 |
1.42e-39 |
|
tRNA CCA-pyrophosphorylase; Provisional
Pssm-ID: 237339 [Multi-domain] Cd Length: 394 Bit Score: 145.75 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 4 YLVGGAVRDQLLGLPISDRDyVVVGATPEAmLSQGFQ---QVGKDFP--VFLHPKTHEEYALARTErkigAGYTGFSCYS 78
Cdd:PRK13299 24 YFVGGSVRDYLLGRPIHDVD-IATSAYPEE-VKAIFPrtvDVGIEHGtvLVLENGEEYEVTTFRTE----SEYVDYRRPS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 79 apDVT----IEDDLLRRDLTINAIAQDESGEIIDPFHGVIDLDKRILRHVSDA---FSEDPLRVLRVARFAAryfEHGFT 151
Cdd:PRK13299 98 --EVTfvrsLEEDLKRRDFTINAIAMDENGEIIDLFDGLEDLKNRLIRAVGNAeerFQEDALRMMRAVRFAS---QLGFD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 152 IAPETLALMQTMAATgeLSHLTAERVWTETEKALKSNSPQVYFDVLRQCGalavLFPEI-------DALFGVPAPEKWHP 224
Cdd:PRK13299 173 LETETFEAMKTQAPL--LEKISVERIFVEFEKLLLGPFWRKGLKLLIETG----LYNYLpglkgkeENLLKLTQLLWFSF 246
|
250
....*....|..
gi 491046917 225 EIDTGIHTLMVM 236
Cdd:PRK13299 247 ETSEQAWAALLI 258
|
|
| pcnB |
TIGR01942 |
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ... |
4-304 |
1.33e-27 |
|
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: 112.97 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 4 YLVGGAVRDQLLGLPISDRDyVVVGATPEAM--LSQGFQQVGKDFPVfLH---PKTHEEYALARTERKIGAGYTGFSCYS 78
Cdd:TIGR01942 33 YIVGGAVRDLLLGIEPKDFD-VVTSATPEEVrkLFRNSRIVGRRFRL-VHvsfGRQIIEVATFRSGHKSSVNAEGRILKD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 79 APDVTIEDDLLRRDLTINAIAQDESGEIIDPFH-GVIDLDKRILRHVSDAFS---EDPLRVLRVARFAARYfehGFTIAP 154
Cdd:TIGR01942 111 NVYGTLEEDAWRRDFTVNALYYDPSREVIIDYVgGMEDLKNRRLRLIGDPRSryqEDPVRMLRALRFSVKL---EFTIDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 155 ETLALMQTMAAtgELSHLTAERVWTETEKALKSNSPQVYFDVLRQCGALAVLFPEIDALFGvpapekwhpEIDTGIHTLM 234
Cdd:TIGR01942 188 STARPIRESAP--LLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLEPLFPSVAYALR---------ESPKFESAFT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 235 VMKVISRLSKDVDIRFAALCHDLGKALTPPDI---WPSHPNHGEAGIP--------LIETLCVRLKVP----TTARDLAR 299
Cdd:TIGR01942 257 VQALVNDTDFRVKRDKPVTPAFLYAALLWPGLvfrVADAPDQGVMPYPavfdairdFVEEQCAPISIPkrfsIPTREIWQ 336
|
....*
gi 491046917 300 LAARY 304
Cdd:TIGR01942 337 MQLRL 341
|
|
| NT_ClassII-CCAase |
cd05398 |
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ... |
1-118 |
1.68e-27 |
|
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: 106.14 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 1 MKVYLVGGAVRDQLLGLPISDRDYVVVGATPEAMlsQGFQQVGKdFPVFLHPKTHE-----------EYALARTERKiga 69
Cdd:cd05398 17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFA--EALFKKIG-GRVVGLGEEFGtatvvingltiDVATLRTETY--- 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 491046917 70 gYTGFSCYSAPDVTIEDDLLRRDLTINAIAQD-ESGEIIDPFHGVIDLDK 118
Cdd:cd05398 91 -TDPGRRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
|
|
| PolyA_pol |
pfam01743 |
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ... |
4-122 |
5.52e-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: 85.02 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 4 YLVGGAVRDQLLGLPISDRDyVVVGATPEaMLSQGFQQ-------VGKDFPVFLHPKTHEEYALA--RTERK-IGAGYTG 73
Cdd:pfam01743 2 YIVGGAVRDLLLGKTPKDVD-IATDATPE-QVATLFRRrrivhllSGIEFGTIHVIFGNQILEVAtfRIEFDeSDFRNPR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 491046917 74 FSCYSApdvTIEDDLLRRDLTINAIAQDE-SGEIIDPFHGVIDLDKRILR 122
Cdd:pfam01743 80 SEEYTG---TLEEDAKRRDFTINALAYNPnSGEVIDYFGGIKDLKSGVIR 126
|
|
| PolyA_pol_RNAbd |
pfam12627 |
Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA ... |
149-214 |
1.26e-15 |
|
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: 70.98 E-value: 1.26e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046917 149 GFTIAPETLALMQTMAAtgELSHLTAERVWTETEKALKSNSPQVYFDVLRQCGALAVLFPEIDALF 214
Cdd:pfam12627 1 GFTIEPETREAIRKLAP--LLKKISPERIFEELLKLLLSGHPERGLELLRETGLLEYLFPELAAAL 64
|
|
| pcnB |
PRK11623 |
poly(A) polymerase I; Provisional |
4-214 |
2.22e-14 |
|
poly(A) polymerase I; Provisional
Pssm-ID: 236939 [Multi-domain] Cd Length: 472 Bit Score: 74.40 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 4 YLVGGAVRDQLLGLPISDRDyVVVGATPEAM--LSQGFQQVGKDFP---VFLHPKT---------HEEYALARTERKigA 69
Cdd:PRK11623 70 YLVGGGVRDLLLGKKPKDFD-VTTNATPEQVrkLFRNCRLVGRRFRlahVMFGPEIievatfrghHEGNESDRNTSQ--R 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 70 GYTGFSCYSAPDVTIEDDLLRRDLTINAI---AQDESgeIIDPFHGVIDLDKRILRHVSDA---FSEDPLRVLRVARFAA 143
Cdd:PRK11623 147 GQNGMLLRDNIFGSIEEDAQRRDFTINSLyysVADFT--VRDYVGGMKDLKEGVIRLIGNPetrYREDPVRMLRAVRFAA 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046917 144 RYfehGFTIAPETLALMQTMAATgeLSHLTAERVWTETEKALKSNSPQVYFDVLRQCGALAVLFPEIDALF 214
Cdd:PRK11623 225 KL---DMRISPETAEPIPRLATL--LNDIPPARLFEESLKLLQAGYGYETYKLLCEYHLFQPLFPTITRYF 290
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
227-305 |
1.17e-05 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 45.02 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 227 DTGIHTLMVMKVISRLSKDVD--------IRFAALCHDLGKALTPPDI----WPSHPNHGEAGIPLIETLcVRLKVPTTA 294
Cdd:cd00077 2 HRFEHSLRVAQLARRLAEELGlseedielLRLAALLHDIGKPGTPDAIteeeSELEKDHAIVGAEILREL-LLEEVIKLI 80
|
90
....*....|.
gi 491046917 295 RDLARLAARYH 305
Cdd:cd00077 81 DELILAVDASH 91
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
228-308 |
1.47e-05 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 43.76 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 228 TGIHTLMVMKVISRLSKDVD------IRFAALCHDLGKALTPPDI--WPSHPNHGEAGIPLIETLCVRLKVpttaRDLAR 299
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGeldrelLLLAALLHDIGKGPFGDEKpeFEIFLGHAVVGAEILRELEKRLGL----EDVLK 76
|
....*....
gi 491046917 300 LAARYHDKI 308
Cdd:pfam01966 77 LILEHHESW 85
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
228-322 |
1.21e-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: 41.51 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046917 228 TGIHTLMVMKVISRLSKDVD------IRFAALCHDLGKALTPPDIWP---SHPNHGEAGIPLIEtlcvRLKVPTTARDLA 298
Cdd:smart00471 5 VFEHSLRVAQLAAALAEELGlldielLLLAALLHDIGKPGTPDSFLVktsVLEDHHFIGAEILL----EEEEPRILEEIL 80
|
90 100
....*....|....*....|....
gi 491046917 299 RLAARYHDKIHVINKLHANDLIAI 322
Cdd:smart00471 81 RTAILSHHERPDGLRGEPITLEAR 104
|
|
| |
