|
Name |
Accession |
Description |
Interval |
E-value |
| cca |
PRK10885 |
multifunctional CCA addition/repair protein; |
1-405 |
0e+00 |
|
multifunctional CCA addition/repair protein;
Pssm-ID: 182810 [Multi-domain] Cd Length: 409 Bit Score: 768.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 1 MKIYLVGGAVRDQLLNLPVKDRDWVVVGATPETLLQQGYQQVGKDFPVFLHPDTHEEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK10885 1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 81 DVTLEDDLQRRDLTINAIAYSAKGEYIDPYHGIDDIHAKLLRHVSDAFSEDPLRVLRVARFAARFAPLGFTIAPETMSLM 160
Cdd:PRK10885 81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 161 QEMTNSGELNALTAERVWKETEKALHSQAPQVYFEILHQCGALKILFPEINALFGVPAPKKWHPEIDTGIHTMMVLAMVS 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 241 RLTDDIAVRFSALCHDLGKGVTPVENWPHHHGHGPAGVPLVEALCQRYRIPNQIRDLAKLAAKYHDHLHRIEKMRPSKII 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 321 RLFDAIDAWRKPERIDQLAIISEADARGRQGAENLPYPQGIFFRQAFKIANQVDVKSIVSRGLKGSAIREALTKQREVAI 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400
|
....*
gi 490365910 401 IEWKS 405
Cdd:PRK10885 401 AAWKE 405
|
|
| PcnB |
COG0617 |
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ... |
1-402 |
1.26e-127 |
|
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: 373.38 E-value: 1.26e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 1 MKIYLVGGAVRDQLLNLPVKDRDWVVVgATPETLLQQG-----YQQVGKDFPVFLHP--DTHEEYALARTERKSGSGYTG 73
Cdd:COG0617 18 FEAYLVGGAVRDLLLGRPPKDIDIVTV-ATPEEVAALFrkalrTVPVGRDFGTVTVVfgGEKIEVATARTERYYGDGRRP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 74 FTCYAApdvTLEDDLQRRDLTINAIAYS-AKGEYIDPYHGIDDIHAKLLRHVSDA---FSEDPLRVLRVARFAARfapLG 149
Cdd:COG0617 97 FVEFGD---TLEEDLARRDFTINALAYDlNDGELIDPFGGLADLEARVIRTVGDPeerFREDPLRILRAVRFAAR---LG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 150 FTIAPETMSLMQEMtnSGELNALTAERVWKETEKALHSQAPQVYFEILHQCGALKIlfpeinalfgvpapkkwhpeidtg 229
Cdd:COG0617 171 FTIEPETLAAIREM--AGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEV------------------------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 230 ihtmmvlamvsrltddIAVRFSALCHDLGKGVTPVENWPHHHGHGPAGVPLVEALCQRYRIPNQIRDLAKLAAKYHDHLH 309
Cdd:COG0617 225 ----------------LALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 310 RIEKMRPSKIIRLFDaidawRKPERIDQLAIISEADARGRQGAENLpypQGIFFRQAFKIANQVDVKSIVSRGLK-GSAI 388
Cdd:COG0617 289 GLGELRDSAVRRLLE-----RGPEALEDLLLLRENGLEYPELQERL---AELLEAAWRRFQPPVDGEDLMALGLKpGPEI 360
|
410
....*....|....
gi 490365910 389 REALTKQREvAIIE 402
Cdd:COG0617 361 GEILRALRE-AVLD 373
|
|
| pcnB |
TIGR01942 |
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ... |
4-321 |
1.94e-29 |
|
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: 117.98 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 4 YLVGGAVRDQLLNLPVKDRDwVVVGATPETL--LQQGYQQVGKDFPVfLH---PDTHEEYALARTERKSGSGYTGFTCYA 78
Cdd:TIGR01942 33 YIVGGAVRDLLLGIEPKDFD-VVTSATPEEVrkLFRNSRIVGRRFRL-VHvsfGRQIIEVATFRSGHKSSVNAEGRILKD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 79 APDVTLEDDLQRRDLTINAIAYSAKGEYIDPYH-GIDDIHAKLLRHVSDAFS---EDPLRVLRVARFAARfapLGFTIAP 154
Cdd:TIGR01942 111 NVYGTLEEDAWRRDFTVNALYYDPSREVIIDYVgGMEDLKNRRLRLIGDPRSryqEDPVRMLRALRFSVK---LEFTIDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 155 ETMSLMQEMTNsgELNALTAERVWKETEKALHSQAPQVYFEILHQCGALKILFPEINALFgvpapkkwhPEIDTGIHTMM 234
Cdd:TIGR01942 188 STARPIRESAP--LLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLEPLFPSVAYAL---------RESPKFESAFT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 235 VLAMVSrLTDDIAVRfsalchdlGKGVTP-----VENWP---HHHGHGPA-GVPLVEAL-----------CQRYRIPNQI 294
Cdd:TIGR01942 257 VQALVN-DTDFRVKR--------DKPVTPaflyaALLWPglvFRVADAPDqGVMPYPAVfdairdfveeqCAPISIPKRF 327
|
330 340
....*....|....*....|....*..
gi 490365910 295 RDLAKLAAKYHDHLHRIEKMRPSKIIR 321
Cdd:TIGR01942 328 SIPTREIWQMQLRLERRSGMRARKLLG 354
|
|
| NT_ClassII-CCAase |
cd05398 |
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ... |
1-116 |
4.38e-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: 104.98 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 1 MKIYLVGGAVRDQLLNLPVKDRDWVVVGATPETLLQQGYQQVGKDFP--------VFLHPDTHEEYALARTERKSGSGyt 72
Cdd:cd05398 17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEALFKKIGGRVVGlgeefgtaTVVINGLTIDVATLRTETYTDPG-- 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 490365910 73 gfTCYAAPDVTLEDDLQRRDLTINAIAYS-AKGEYIDPYHGIDDI 116
Cdd:cd05398 95 --RRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDL 137
|
|
| PolyA_pol |
pfam01743 |
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ... |
3-122 |
9.26e-21 |
|
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: 87.34 E-value: 9.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 3 IYLVGGAVRDQLLNLPVKDRDwVVVGATPE---TLLQ---QGYQQVGKDFPVFLHPDTHEEYALARTerKSGSGYTGFtc 76
Cdd:pfam01743 1 LYIVGGAVRDLLLGKTPKDVD-IATDATPEqvaTLFRrrrIVHLLSGIEFGTIHVIFGNQILEVATF--RIEFDESDF-- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 490365910 77 yAAPDV-----TLEDDLQRRDLTINAIAYS-AKGEYIDPYHGIDDIHAKLLR 122
Cdd:pfam01743 76 -RNPRSeeytgTLEEDAKRRDFTINALAYNpNSGEVIDYFGGIKDLKSGVIR 126
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
231-328 |
2.70e-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: 43.44 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 231 HTMMVLAMVSRLTDDIAVRFSALCHDLGKGVTP---VENWPHHHGHGPAGVPLVEalcqRYRIPNQIRDLAKLAAKYHDH 307
Cdd:smart00471 14 QLAAALAEELGLLDIELLLLAALLHDIGKPGTPdsfLVKTSVLEDHHFIGAEILL----EEEEPRILEEILRTAILSHHE 89
|
90 100
....*....|....*....|....*
gi 490365910 308 LHRIEKMRP----SKIIRLFDAIDA 328
Cdd:smart00471 90 RPDGLRGEPitleARIVKVADRLDA 114
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| cca |
PRK10885 |
multifunctional CCA addition/repair protein; |
1-405 |
0e+00 |
|
multifunctional CCA addition/repair protein;
Pssm-ID: 182810 [Multi-domain] Cd Length: 409 Bit Score: 768.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 1 MKIYLVGGAVRDQLLNLPVKDRDWVVVGATPETLLQQGYQQVGKDFPVFLHPDTHEEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK10885 1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 81 DVTLEDDLQRRDLTINAIAYSAKGEYIDPYHGIDDIHAKLLRHVSDAFSEDPLRVLRVARFAARFAPLGFTIAPETMSLM 160
Cdd:PRK10885 81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 161 QEMTNSGELNALTAERVWKETEKALHSQAPQVYFEILHQCGALKILFPEINALFGVPAPKKWHPEIDTGIHTMMVLAMVS 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 241 RLTDDIAVRFSALCHDLGKGVTPVENWPHHHGHGPAGVPLVEALCQRYRIPNQIRDLAKLAAKYHDHLHRIEKMRPSKII 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 321 RLFDAIDAWRKPERIDQLAIISEADARGRQGAENLPYPQGIFFRQAFKIANQVDVKSIVSRGLKGSAIREALTKQREVAI 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400
|
....*
gi 490365910 401 IEWKS 405
Cdd:PRK10885 401 AAWKE 405
|
|
| PRK13298 |
PRK13298 |
tRNA CCA-pyrophosphorylase; Provisional |
1-404 |
0e+00 |
|
tRNA CCA-pyrophosphorylase; Provisional
Pssm-ID: 237338 [Multi-domain] Cd Length: 417 Bit Score: 540.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 1 MKIYLVGGAVRDQLLNLPVKDRDWVVVGATPETLLQQGYQQVGKDFPVFLHPDTHEEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK13298 1 MKIYLVGGAVRDSLLNLPVKDKDWVVVGGTPKILLSINFQQVGKDFPVFLHPETHEEYALARTERKSGVGYTGFITDTSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 81 DVTLEDDLQRRDLTINAIAYSAKGEYIDPYHGIDDIHAKLLRHVSDAFSEDPLRVLRVARFAARFAPLGFTIAPETMSLM 160
Cdd:PRK13298 81 DVTLEEDLIRRDLTINAIAQDENGNYIDPFQGKKDIQLRLLRHVSESFIEDPLRVLRVARFAALLVHLGFKIAKETMILM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 161 QEMTNSGELNALTAERVWKETEKALHSQAPQVYFEILHQCGALKILFPEINALFGVPAPKKWH-PEIDTGIHTMMVLAMV 239
Cdd:PRK13298 161 CIMVKKHELLYLTPERIWNETEKALKTDNPHVYFQVLYECNALKFLFPEIDFLYEKPYFLNSFfKKFNLGNYILMGLSKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 240 SRLTDDIAVRFSALCHDLGKG--VTPVENWPHHHGHGPAGVPLVEALCQRYRIPNQIRDLAKLAAKYHDHLHRIEKMRPS 317
Cdd:PRK13298 241 SKLTKDIDIRFSYLCQFLGSMipINQIKRNYKKIFFDKYAASLIKNLCKRFKIPSYIRNIAVLNTGFYFFLYNIHYQSSK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 318 KIIRLFDAIDAWRKPERIDQLAIISEADARGRQGAENLPYPQGIFFRQAFKIANQVDVKSIVSRGLKGSAIREALTKQRE 397
Cdd:PRK13298 321 NIITLFSKIDAWRKPDRIKKLIFLSNFNLLRNKKSINFLIKQGNFLKKAFSVTKKISIKDILKKGFKGYEIKQELYRLRI 400
|
....*..
gi 490365910 398 VAIIEWK 404
Cdd:PRK13298 401 HKLKFWR 407
|
|
| PcnB |
COG0617 |
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ... |
1-402 |
1.26e-127 |
|
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: 373.38 E-value: 1.26e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 1 MKIYLVGGAVRDQLLNLPVKDRDWVVVgATPETLLQQG-----YQQVGKDFPVFLHP--DTHEEYALARTERKSGSGYTG 73
Cdd:COG0617 18 FEAYLVGGAVRDLLLGRPPKDIDIVTV-ATPEEVAALFrkalrTVPVGRDFGTVTVVfgGEKIEVATARTERYYGDGRRP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 74 FTCYAApdvTLEDDLQRRDLTINAIAYS-AKGEYIDPYHGIDDIHAKLLRHVSDA---FSEDPLRVLRVARFAARfapLG 149
Cdd:COG0617 97 FVEFGD---TLEEDLARRDFTINALAYDlNDGELIDPFGGLADLEARVIRTVGDPeerFREDPLRILRAVRFAAR---LG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 150 FTIAPETMSLMQEMtnSGELNALTAERVWKETEKALHSQAPQVYFEILHQCGALKIlfpeinalfgvpapkkwhpeidtg 229
Cdd:COG0617 171 FTIEPETLAAIREM--AGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEV------------------------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 230 ihtmmvlamvsrltddIAVRFSALCHDLGKGVTPVENWPHHHGHGPAGVPLVEALCQRYRIPNQIRDLAKLAAKYHDHLH 309
Cdd:COG0617 225 ----------------LALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 310 RIEKMRPSKIIRLFDaidawRKPERIDQLAIISEADARGRQGAENLpypQGIFFRQAFKIANQVDVKSIVSRGLK-GSAI 388
Cdd:COG0617 289 GLGELRDSAVRRLLE-----RGPEALEDLLLLRENGLEYPELQERL---AELLEAAWRRFQPPVDGEDLMALGLKpGPEI 360
|
410
....*....|....
gi 490365910 389 REALTKQREvAIIE 402
Cdd:COG0617 361 GEILRALRE-AVLD 373
|
|
| PRK13297 |
PRK13297 |
tRNA CCA-pyrophosphorylase; Provisional |
1-346 |
2.60e-100 |
|
tRNA CCA-pyrophosphorylase; Provisional
Pssm-ID: 139469 [Multi-domain] Cd Length: 364 Bit Score: 302.68 E-value: 2.60e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 1 MKIYLVGGAVRDQLLNLPVKDRDWVVVGATPETLLQQGYQQVGKDFPVFLHPDTHEEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK13297 12 LQVYIVGGAVRDALLGLPAGDRDWVVVGATPEDMARRGFIPVGGDFPVFLHPRTKEEYALARTERKSGRGYKGFTFYTGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 81 DVTLEDDLQRRDLTINAIAYSAKGEYIDPYHGIDDIHAKLLRHVSDAFSEDPLRVLRVARFAARFAplGFTIAPETMSLM 160
Cdd:PRK13297 92 DVTLEQDLQRRDLTVNAIARTPQGELVDPLDGVADVRARVLRHVGEAFAEDPVRILRLGRFAARFG--DFSIAPETMQLC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 161 QEMTNSGELNALTAERVWKETEKALHSQAPQVYFEILHQCGALKILFPEINALFGVpapkkwHPEIDTGIHTMMVLAMvs 240
Cdd:PRK13297 170 RRMVEAGEADALVPERVWKEVSRGLMAQAPSRMLDVLARAGALARVMPELHDDAAV------RAEIDRAAAAGLPLAG-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 241 rltddiavRFSALCHDlgkgvtpvenwphhhghgpagVPLVEALCQRYRIPNQIRDLAKLAAKYHDHLHriEKMRPSKII 320
Cdd:PRK13297 242 --------RYALLCRH---------------------TPERDALGRRLRAPVECMDQARLLPLAVDALA--ASATPAAQL 290
|
330 340 350
....*....|....*....|....*....|
gi 490365910 321 RLFDAIDAWRKPERIDQL----AIISEADA 346
Cdd:PRK13297 291 DLIERCDALRKPERFDALlqaaAIVAPVDL 320
|
|
| PRK13296 |
PRK13296 |
CCA tRNA nucleotidyltransferase; |
1-217 |
6.83e-81 |
|
CCA tRNA nucleotidyltransferase;
Pssm-ID: 106256 [Multi-domain] Cd Length: 360 Bit Score: 252.60 E-value: 6.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 1 MKIYLVGGAVRDQLLNLPVKDRDWVVVGATPETLLQQGYQQVGKDFPVFLHPDTHEEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK13296 1 MKFYLVGGAVRDMLLGITPKDKDWVVVGATEDEMLANGFIKIAANFPVFIHPQTKQEYALARSEKKTASGYHGFEVNFSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 81 DVTLEDDLQRRDLTINAIAYSAKGEYIDPYHGIDDIHAKLLRHVSDAFSEDPLRVLRVARFAARFAPLGFTIAPETMSLM 160
Cdd:PRK13296 81 YITLEDDLKRRDLTINSIAIDQNNKVIDPFNGQADLQNRILRHTSIAFIEDPLRVVRLARFKAQLSNFNFSIAQEMLALI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490365910 161 QEMTNSGELNALTAERVWKETEKALHSqaPQVYFEILHQCGALKILFPEIN-ALFGVP 217
Cdd:PRK13296 161 KELVKTGELNHLTRERLHIEFVKALNN--PKIFFTTLKELEALKIIFPNIScILPLIP 216
|
|
| PRK13299 |
PRK13299 |
tRNA CCA-pyrophosphorylase; Provisional |
4-238 |
2.19e-37 |
|
tRNA CCA-pyrophosphorylase; Provisional
Pssm-ID: 237339 [Multi-domain] Cd Length: 394 Bit Score: 139.59 E-value: 2.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 4 YLVGGAVRDQLLNLPVKDRDwVVVGATPE---TLLQQGYQqVGKDFPVFLHPDTHEEYALA--RTErksgSGYTGftcYA 78
Cdd:PRK13299 24 YFVGGSVRDYLLGRPIHDVD-IATSAYPEevkAIFPRTVD-VGIEHGTVLVLENGEEYEVTtfRTE----SEYVD---YR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 79 APD-VT----LEDDLQRRDLTINAIAYSAKGEYIDPYHGIDDIHAKLLRHVSDA---FSEDPLRVLRVARFAARfapLGF 150
Cdd:PRK13299 95 RPSeVTfvrsLEEDLKRRDFTINAIAMDENGEIIDLFDGLEDLKNRLIRAVGNAeerFQEDALRMMRAVRFASQ---LGF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 151 TIAPETmslMQEMTNSGELNALTA-ERVWKETEKALHSQAPQVYFEILHQCGALKILfPEI----NALFGVPAPKKWHPE 225
Cdd:PRK13299 172 DLETET---FEAMKTQAPLLEKISvERIFVEFEKLLLGPFWRKGLKLLIETGLYNYL-PGLkgkeENLLKLTQLLWFSFE 247
|
250
....*....|...
gi 490365910 226 IDTGIHTMMVLAM 238
Cdd:PRK13299 248 TSEQAWAALLISL 260
|
|
| pcnB |
TIGR01942 |
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ... |
4-321 |
1.94e-29 |
|
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: 117.98 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 4 YLVGGAVRDQLLNLPVKDRDwVVVGATPETL--LQQGYQQVGKDFPVfLH---PDTHEEYALARTERKSGSGYTGFTCYA 78
Cdd:TIGR01942 33 YIVGGAVRDLLLGIEPKDFD-VVTSATPEEVrkLFRNSRIVGRRFRL-VHvsfGRQIIEVATFRSGHKSSVNAEGRILKD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 79 APDVTLEDDLQRRDLTINAIAYSAKGEYIDPYH-GIDDIHAKLLRHVSDAFS---EDPLRVLRVARFAARfapLGFTIAP 154
Cdd:TIGR01942 111 NVYGTLEEDAWRRDFTVNALYYDPSREVIIDYVgGMEDLKNRRLRLIGDPRSryqEDPVRMLRALRFSVK---LEFTIDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 155 ETMSLMQEMTNsgELNALTAERVWKETEKALHSQAPQVYFEILHQCGALKILFPEINALFgvpapkkwhPEIDTGIHTMM 234
Cdd:TIGR01942 188 STARPIRESAP--LLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLEPLFPSVAYAL---------RESPKFESAFT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 235 VLAMVSrLTDDIAVRfsalchdlGKGVTP-----VENWP---HHHGHGPA-GVPLVEAL-----------CQRYRIPNQI 294
Cdd:TIGR01942 257 VQALVN-DTDFRVKR--------DKPVTPaflyaALLWPglvFRVADAPDqGVMPYPAVfdairdfveeqCAPISIPKRF 327
|
330 340
....*....|....*....|....*..
gi 490365910 295 RDLAKLAAKYHDHLHRIEKMRPSKIIR 321
Cdd:TIGR01942 328 SIPTREIWQMQLRLERRSGMRARKLLG 354
|
|
| NT_ClassII-CCAase |
cd05398 |
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ... |
1-116 |
4.38e-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: 104.98 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 1 MKIYLVGGAVRDQLLNLPVKDRDWVVVGATPETLLQQGYQQVGKDFP--------VFLHPDTHEEYALARTERKSGSGyt 72
Cdd:cd05398 17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEALFKKIGGRVVGlgeefgtaTVVINGLTIDVATLRTETYTDPG-- 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 490365910 73 gfTCYAAPDVTLEDDLQRRDLTINAIAYS-AKGEYIDPYHGIDDI 116
Cdd:cd05398 95 --RRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDL 137
|
|
| PolyA_pol |
pfam01743 |
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ... |
3-122 |
9.26e-21 |
|
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: 87.34 E-value: 9.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 3 IYLVGGAVRDQLLNLPVKDRDwVVVGATPE---TLLQ---QGYQQVGKDFPVFLHPDTHEEYALARTerKSGSGYTGFtc 76
Cdd:pfam01743 1 LYIVGGAVRDLLLGKTPKDVD-IATDATPEqvaTLFRrrrIVHLLSGIEFGTIHVIFGNQILEVATF--RIEFDESDF-- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 490365910 77 yAAPDV-----TLEDDLQRRDLTINAIAYS-AKGEYIDPYHGIDDIHAKLLR 122
Cdd:pfam01743 76 -RNPRSeeytgTLEEDAKRRDFTINALAYNpNSGEVIDYFGGIKDLKSGVIR 126
|
|
| pcnB |
PRK11623 |
poly(A) polymerase I; Provisional |
4-214 |
3.09e-16 |
|
poly(A) polymerase I; Provisional
Pssm-ID: 236939 [Multi-domain] Cd Length: 472 Bit Score: 80.18 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 4 YLVGGAVRDQLLNLPVKDRDwVVVGATPETL--LQQGYQQVGKDFP---VFLHPDT---------HEEYALARTErkSGS 69
Cdd:PRK11623 70 YLVGGGVRDLLLGKKPKDFD-VTTNATPEQVrkLFRNCRLVGRRFRlahVMFGPEIievatfrghHEGNESDRNT--SQR 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 70 GYTGFTCYAAPDVTLEDDLQRRDLTINAIAYSAKGEYIDPY-HGIDDIHAKLLRHVSDA---FSEDPLRVLRVARFAARf 145
Cdd:PRK11623 147 GQNGMLLRDNIFGSIEEDAQRRDFTINSLYYSVADFTVRDYvGGMKDLKEGVIRLIGNPetrYREDPVRMLRAVRFAAK- 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490365910 146 apLGFTIAPETMSLMQEMtnSGELNALTAERVWKETEKALhsQAPQVY--FEILHQCGALKILFPEINALF 214
Cdd:PRK11623 226 --LDMRISPETAEPIPRL--ATLLNDIPPARLFEESLKLL--QAGYGYetYKLLCEYHLFQPLFPTITRYF 290
|
|
| PolyA_pol_RNAbd |
pfam12627 |
Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA ... |
149-214 |
1.73e-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: 64.81 E-value: 1.73e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490365910 149 GFTIAPETMSLMQEMtnSGELNALTAERVWKETEKALHSQAPQVYFEILHQCGALKILFPEINALF 214
Cdd:pfam12627 1 GFTIEPETREAIRKL--APLLKKISPERIFEELLKLLLSGHPERGLELLRETGLLEYLFPELAAAL 64
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
228-329 |
6.46e-07 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 47.62 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 228 TGIHTMMVLAMVSRLTDDIA------VRFSALCHDLGKGVTPVEN--WPHHHGHGPAGVPLVEALCqryrIPNQIRDLAK 299
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGeldrelLLLAALLHDIGKGPFGDEKpeFEIFLGHAVVGAEILRELE----KRLGLEDVLK 76
|
90 100 110
....*....|....*....|....*....|....
gi 490365910 300 LAAKYHDHLHRIEKMRP----SKIIRLFDAIDAW 329
Cdd:pfam01966 77 LILEHHESWEGAGYPEEisleARIVKLADRLDAL 110
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
227-343 |
1.73e-06 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 47.33 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 227 DTGIHTMMVLAMVSRL--------TDDIAVRFSALCHDLGKGVTP----VENWPHHHGHGPAGVPLVEALcQRYRIPNQI 294
Cdd:cd00077 2 HRFEHSLRVAQLARRLaeelglseEDIELLRLAALLHDIGKPGTPdaitEEESELEKDHAIVGAEILREL-LLEEVIKLI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 490365910 295 RDLAKLAAKYH----------DHLHRIEKMRPSKIIRLFDAIDAWRKPERIDQLAIISE 343
Cdd:cd00077 81 DELILAVDASHherldglgypDGLKGEEITLEARIVKLADRLDALRRDSREKRRRIAEE 139
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
231-328 |
2.70e-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: 43.44 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365910 231 HTMMVLAMVSRLTDDIAVRFSALCHDLGKGVTP---VENWPHHHGHGPAGVPLVEalcqRYRIPNQIRDLAKLAAKYHDH 307
Cdd:smart00471 14 QLAAALAEELGLLDIELLLLAALLHDIGKPGTPdsfLVKTSVLEDHHFIGAEILL----EEEEPRILEEILRTAILSHHE 89
|
90 100
....*....|....*....|....*
gi 490365910 308 LHRIEKMRP----SKIIRLFDAIDA 328
Cdd:smart00471 90 RPDGLRGEPitleARIVKVADRLDA 114
|
|
|