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Conserved domains on  [gi|527036889|ref|WP_020883630|]
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MULTISPECIES: multifunctional CCA addition/repair protein [Enterobacter]

Protein Classification

multifunctional CCA addition/repair protein( domain architecture ID 11485063)

multifunctional CCA addition/repair protein catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template

CATH:  1.10.3090.10|1.10.1300.10
EC:  2.7.7.72|3.1.3.-|3.1.4.-
Gene Ontology:  GO:0004810|GO:0005524|GO:0000049|GO:0000287|GO:0004112|GO:0016791|GO:0001680
PubMed:  3009457|15210699
SCOP:  4003222|3000943

Graphical summary

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List of domain hits

 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: 821.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   1 MKSYLVGGAVRDALLGLPVKDKDWVVVGATPEEMLNAGYQQVGRDFPVFLHPQSREEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK10885   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889  81 DVTLEQDLLRRDLTINALAQDEDGQIIDAYGGQDDLRNRLLRHVSPAFSEDPLRVLRVARFAARYAHLSFRIADETLALM 160
Cdd:PRK10885  81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 161 TAMTEAGELAHLTPERVWKETENALTTRNPQVFFQVLRDCGALKVLFPEIDALFGVPAPAKWHPEIDTGVHTLMTLSMAA 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 241 MLSPEVDVRFSTLCHDLGKGLTPKAMWPRHHGHGPAGVKLVEGLCQRLRVPNEIRDLARLVAEFHDLIHTFPILKPATIV 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 321 KLFDNIDAWRKPQRVEQIALTSEADVRGRTGFEACDYPQGRLLRAAWEVAKAVPTKAVVEAGFKGPEIREELTKRRIQAV 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400


                 ....*....
gi 527036889 401 TDWKEKHCP 409
Cdd:PRK10885 401 AAWKEQRCP 409
 
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: 821.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   1 MKSYLVGGAVRDALLGLPVKDKDWVVVGATPEEMLNAGYQQVGRDFPVFLHPQSREEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK10885   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889  81 DVTLEQDLLRRDLTINALAQDEDGQIIDAYGGQDDLRNRLLRHVSPAFSEDPLRVLRVARFAARYAHLSFRIADETLALM 160
Cdd:PRK10885  81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 161 TAMTEAGELAHLTPERVWKETENALTTRNPQVFFQVLRDCGALKVLFPEIDALFGVPAPAKWHPEIDTGVHTLMTLSMAA 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 241 MLSPEVDVRFSTLCHDLGKGLTPKAMWPRHHGHGPAGVKLVEGLCQRLRVPNEIRDLARLVAEFHDLIHTFPILKPATIV 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 321 KLFDNIDAWRKPQRVEQIALTSEADVRGRTGFEACDYPQGRLLRAAWEVAKAVPTKAVVEAGFKGPEIREELTKRRIQAV 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400


                 ....*....
gi 527036889 401 TDWKEKHCP 409
Cdd:PRK10885 401 AAWKEQRCP 409
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
 1-403 8.35e-124

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: 363.75  E-value: 8.35e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   1 MKSYLVGGAVRDALLGLPVKDKDWVVVgATPEEMLNAG-----YQQVGRDFPVFLHP--QSREEYALARTERKSGSGYTG 73
Cdd:COG0617   18 FEAYLVGGAVRDLLLGRPPKDIDIVTV-ATPEEVAALFrkalrTVPVGRDFGTVTVVfgGEKIEVATARTERYYGDGRRP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889  74 FTCYAApdvTLEQDLLRRDLTINALAQDE-DGQIIDAYGGQDDLRNRLLRHVS---PAFSEDPLRVLRVARFAARyahLS 149
Cdd:COG0617   97 FVEFGD---TLEEDLARRDFTINALAYDLnDGELIDPFGGLADLEARVIRTVGdpeERFREDPLRILRAVRFAAR---LG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 150 FRIADETLALMTAMteAGELAHLTPERVWKETENALTTRNPQVFFQVLRDCGALKVLfpeidalfgvpapakwhpeidtg 229
Cdd:COG0617  171 FTIEPETLAAIREM--AGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVL----------------------- 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 230 vhtlmtlsmaamlspevDVRFSTLCHDLGKGLTPKAMWPRHHGHGPAGVKLVEGLCQRLRVPNEIRDLARLVAEFHDLIH 309
Cdd:COG0617  226 -----------------ALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 310 TFPILKPATIVKLFDnidawRKPQRVEQIALTSEADVRGRTGFEACDypqgRLLRAAWEVAK-AVPTKAVVEAGFK-GPE 387
Cdd:COG0617  289 GLGELRDSAVRRLLE-----RGPEALEDLLLLRENGLEYPELQERLA----ELLEAAWRRFQpPVDGEDLMALGLKpGPE 359

                        410
                 ....*....|....*.
gi 527036889 388 IREELTKRRIQAVTDW 403
Cdd:COG0617  360 IGEILRALREAVLDGG 375
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
 1-118 4.60e-29

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: 110.38  E-value: 4.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   1 MKSYLVGGAVRDALLGLPVKDKDWVVVGATPEEMLNAGYQQVGRDFP--------VFLHPQSREEYALARTERKSGSGyt 72
Cdd:cd05398   17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEALFKKIGGRVVGlgeefgtaTVVINGLTIDVATLRTETYTDPG-- 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 527036889  73 gfTCYAAPDVTLEQDLLRRDLTINALAQD-EDGQIIDAYGGQDDLRN 118
Cdd:cd05398   95 --RRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
 2-214 7.88e-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: 116.44  E-value: 7.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889    2 KSYLVGGAVRDALLGLPVKDKDwVVVGATPEEM--LNAGYQQVGRDFPVFLHPQSRE--EYALARTERKSGSGYTGFTCY 77
Cdd:TIGR01942  31 QAYIVGGAVRDLLLGIEPKDFD-VVTSATPEEVrkLFRNSRIVGRRFRLVHVSFGRQiiEVATFRSGHKSSVNAEGRILK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   78 AAPDVTLEQDLLRRDLTINALAQD-EDGQIIDAYGGQDDLRNRLLRHVSPAFS---EDPLRVLRVARFAARYAhlsFRIA 153
Cdd:TIGR01942 110 DNVYGTLEEDAWRRDFTVNALYYDpSREVIIDYVGGMEDLKNRRLRLIGDPRSryqEDPVRMLRALRFSVKLE---FTID 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036889  154 DETLALMTAMteAGELAHLTPERVWKETENALTTRNPQVFFQVLRDCGALKVLFPEIDALF 214
Cdd:TIGR01942 187 ESTARPIRES--APLLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLEPLFPSVAYAL 245
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
 4-122 1.07e-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: 89.65  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889    4 YLVGGAVRDALLGLPVKDKDwVVVGATPEEMLNA------GYQQVGRDFPVFLHPQSREEYALARTerKSGSGYTGFtcy 77
Cdd:pfam01743   2 YIVGGAVRDLLLGKTPKDVD-IATDATPEQVATLfrrrriVHLLSGIEFGTIHVIFGNQILEVATF--RIEFDESDF--- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 527036889   78 AAPDV-----TLEQDLLRRDLTINALAQDE-DGQIIDAYGGQDDLRNRLLR 122
Cdd:pfam01743  76 RNPRSeeytgTLEEDAKRRDFTINALAYNPnSGEVIDYFGGIKDLKSGVIR 126
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 228-328 1.62e-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: 44.21  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   228 TGVHTLMTLSMAAMLSPEVD------VRFSTLCHDLGKGLTPKAMWPR---HHGHGPAGVKLVEglcqRLRVPNEIRDLA 298
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELGlldielLLLAALLHDIGKPGTPDSFLVKtsvLEDHHFIGAEILL----EEEEPRILEEIL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 527036889   299 RLVAEFHDLIHTF----PILKPATIVKLFDNIDA 328
Cdd:smart00471  81 RTAILSHHERPDGlrgePITLEARIVKVADRLDA 114
 
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: 821.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   1 MKSYLVGGAVRDALLGLPVKDKDWVVVGATPEEMLNAGYQQVGRDFPVFLHPQSREEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK10885   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889  81 DVTLEQDLLRRDLTINALAQDEDGQIIDAYGGQDDLRNRLLRHVSPAFSEDPLRVLRVARFAARYAHLSFRIADETLALM 160
Cdd:PRK10885  81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 161 TAMTEAGELAHLTPERVWKETENALTTRNPQVFFQVLRDCGALKVLFPEIDALFGVPAPAKWHPEIDTGVHTLMTLSMAA 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 241 MLSPEVDVRFSTLCHDLGKGLTPKAMWPRHHGHGPAGVKLVEGLCQRLRVPNEIRDLARLVAEFHDLIHTFPILKPATIV 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 321 KLFDNIDAWRKPQRVEQIALTSEADVRGRTGFEACDYPQGRLLRAAWEVAKAVPTKAVVEAGFKGPEIREELTKRRIQAV 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400


                 ....*....
gi 527036889 401 TDWKEKHCP 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: 538.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   1 MKSYLVGGAVRDALLGLPVKDKDWVVVGATPEEMLNAGYQQVGRDFPVFLHPQSREEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK13298   1 MKIYLVGGAVRDSLLNLPVKDKDWVVVGGTPKILLSINFQQVGKDFPVFLHPETHEEYALARTERKSGVGYTGFITDTSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889  81 DVTLEQDLLRRDLTINALAQDEDGQIIDAYGGQDDLRNRLLRHVSPAFSEDPLRVLRVARFAARYAHLSFRIADETLALM 160
Cdd:PRK13298  81 DVTLEEDLIRRDLTINAIAQDENGNYIDPFQGKKDIQLRLLRHVSESFIEDPLRVLRVARFAALLVHLGFKIAKETMILM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 161 TAMTEAGELAHLTPERVWKETENALTTRNPQVFFQVLRDCGALKVLFPEIDALFGVPAPAKWH-PEIDTGVHTLMTLSMA 239
Cdd:PRK13298 161 CIMVKKHELLYLTPERIWNETEKALKTDNPHVYFQVLYECNALKFLFPEIDFLYEKPYFLNSFfKKFNLGNYILMGLSKI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 240 AMLSPEVDVRFSTLCHDLGKG--LTPKAMWPRHHGHGPAGVKLVEGLCQRLRVPNEIRDLARLVAEFHDLIHTFPILKPA 317
Cdd:PRK13298 241 SKLTKDIDIRFSYLCQFLGSMipINQIKRNYKKIFFDKYAASLIKNLCKRFKIPSYIRNIAVLNTGFYFFLYNIHYQSSK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 318 TIVKLFDNIDAWRKPQRVEQIALTSEADVRGRTGFEACDYPQGRLLRAAWEVAKAVPTKAVVEAGFKGPEIREELTKRRI 397
Cdd:PRK13298 321 NIITLFSKIDAWRKPDRIKKLIFLSNFNLLRNKKSINFLIKQGNFLKKAFSVTKKISIKDILKKGFKGYEIKQELYRLRI 400


                 ....*....
gi 527036889 398 QAVTDWKEK 406
Cdd:PRK13298 401 HKLKFWRNK 409
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
 1-403 8.35e-124

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: 363.75  E-value: 8.35e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   1 MKSYLVGGAVRDALLGLPVKDKDWVVVgATPEEMLNAG-----YQQVGRDFPVFLHP--QSREEYALARTERKSGSGYTG 73
Cdd:COG0617   18 FEAYLVGGAVRDLLLGRPPKDIDIVTV-ATPEEVAALFrkalrTVPVGRDFGTVTVVfgGEKIEVATARTERYYGDGRRP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889  74 FTCYAApdvTLEQDLLRRDLTINALAQDE-DGQIIDAYGGQDDLRNRLLRHVS---PAFSEDPLRVLRVARFAARyahLS 149
Cdd:COG0617   97 FVEFGD---TLEEDLARRDFTINALAYDLnDGELIDPFGGLADLEARVIRTVGdpeERFREDPLRILRAVRFAAR---LG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 150 FRIADETLALMTAMteAGELAHLTPERVWKETENALTTRNPQVFFQVLRDCGALKVLfpeidalfgvpapakwhpeidtg 229
Cdd:COG0617  171 FTIEPETLAAIREM--AGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVL----------------------- 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 230 vhtlmtlsmaamlspevDVRFSTLCHDLGKGLTPKAMWPRHHGHGPAGVKLVEGLCQRLRVPNEIRDLARLVAEFHDLIH 309
Cdd:COG0617  226 -----------------ALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 310 TFPILKPATIVKLFDnidawRKPQRVEQIALTSEADVRGRTGFEACDypqgRLLRAAWEVAK-AVPTKAVVEAGFK-GPE 387
Cdd:COG0617  289 GLGELRDSAVRRLLE-----RGPEALEDLLLLRENGLEYPELQERLA----ELLEAAWRRFQpPVDGEDLMALGLKpGPE 359

                        410
                 ....*....|....*.
gi 527036889 388 IREELTKRRIQAVTDW 403
Cdd:COG0617  360 IGEILRALREAVLDGG 375
PRK13297 PRK13297
tRNA CCA-pyrophosphorylase; Provisional
 1-345 6.27e-96

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 139469 [Multi-domain]  Cd Length: 364  Bit Score: 291.90  E-value: 6.27e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   1 MKSYLVGGAVRDALLGLPVKDKDWVVVGATPEEMLNAGYQQVGRDFPVFLHPQSREEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK13297  12 LQVYIVGGAVRDALLGLPAGDRDWVVVGATPEDMARRGFIPVGGDFPVFLHPRTKEEYALARTERKSGRGYKGFTFYTGA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889  81 DVTLEQDLLRRDLTINALAQDEDGQIIDAYGGQDDLRNRLLRHVSPAFSEDPLRVLRVARFAARYAhlSFRIADETLALM 160
Cdd:PRK13297  92 DVTLEQDLQRRDLTVNAIARTPQGELVDPLDGVADVRARVLRHVGEAFAEDPVRILRLGRFAARFG--DFSIAPETMQLC 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 161 TAMTEAGELAHLTPERVWKETENALTTRNPQVFFQVLRDCGALKVLFPEIDALFGVpapakwHPEIDTgvhtlmtlsmAA 240
Cdd:PRK13297 170 RRMVEAGEADALVPERVWKEVSRGLMAQAPSRMLDVLARAGALARVMPELHDDAAV------RAEIDR----------AA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 241 MLSPEVDVRFSTLCHdlgkgLTPKAmwprhhghgpagvklvEGLCQRLRVPNEIRDLARLVAEFHDLIHTFPIlkPATIV 320
Cdd:PRK13297 234 AAGLPLAGRYALLCR-----HTPER----------------DALGRRLRAPVECMDQARLLPLAVDALAASAT--PAAQL 290

                        330       340
                 ....*....|....*....|....*....
gi 527036889 321 KLFDNIDAWRKPQR----VEQIALTSEAD 345
Cdd:PRK13297 291 DLIERCDALRKPERfdalLQAAAIVAPVD 319
PRK13296 PRK13296
CCA tRNA nucleotidyltransferase;
1-217 2.73e-86

CCA tRNA nucleotidyltransferase;


Pssm-ID: 106256 [Multi-domain]  Cd Length: 360  Bit Score: 266.85  E-value: 2.73e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   1 MKSYLVGGAVRDALLGLPVKDKDWVVVGATPEEMLNAGYQQVGRDFPVFLHPQSREEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK13296   1 MKFYLVGGAVRDMLLGITPKDKDWVVVGATEDEMLANGFIKIAANFPVFIHPQTKQEYALARSEKKTASGYHGFEVNFSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889  81 DVTLEQDLLRRDLTINALAQDEDGQIIDAYGGQDDLRNRLLRHVSPAFSEDPLRVLRVARFAARYAHLSFRIADETLALM 160
Cdd:PRK13296  81 YITLEDDLKRRDLTINSIAIDQNNKVIDPFNGQADLQNRILRHTSIAFIEDPLRVVRLARFKAQLSNFNFSIAQEMLALI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 527036889 161 TAMTEAGELAHLTPERVWKETENALttRNPQVFFQVLRDCGALKVLFPEID-ALFGVP 217
Cdd:PRK13296 161 KELVKTGELNHLTRERLHIEFVKAL--NNPKIFFTTLKELEALKIIFPNIScILPLIP 216
PRK13299 PRK13299
tRNA CCA-pyrophosphorylase; Provisional
 4-238 1.00e-38

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237339 [Multi-domain]  Cd Length: 394  Bit Score: 143.44  E-value: 1.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   4 YLVGGAVRDALLGLPVKDKDwVVVGATPEEmLNAGYQ---QVGRDFPVFLHPQSREEYALA--RTErksgSGYTGftcYA 78
Cdd:PRK13299  24 YFVGGSVRDYLLGRPIHDVD-IATSAYPEE-VKAIFPrtvDVGIEHGTVLVLENGEEYEVTtfRTE----SEYVD---YR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889  79 APD-VT----LEQDLLRRDLTINALAQDEDGQIIDAYGGQDDLRNRLLRHV-SPA--FSEDPLRVLRVARFAARyahLSF 150
Cdd:PRK13299  95 RPSeVTfvrsLEEDLKRRDFTINAIAMDENGEIIDLFDGLEDLKNRLIRAVgNAEerFQEDALRMMRAVRFASQ---LGF 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 151 RIADETLAlmtAMTEAGE-LAHLTPERVWKETENALTTRNPQVFFQVLRDCGALKVLfPEI----DALFGVPAPAKWHPE 225
Cdd:PRK13299 172 DLETETFE---AMKTQAPlLEKISVERIFVEFEKLLLGPFWRKGLKLLIETGLYNYL-PGLkgkeENLLKLTQLLWFSFE 247

                        250
                 ....*....|...
gi 527036889 226 IDTGVHTLMTLSM 238
Cdd:PRK13299 248 TSEQAWAALLISL 260
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
 1-118 4.60e-29

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: 110.38  E-value: 4.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   1 MKSYLVGGAVRDALLGLPVKDKDWVVVGATPEEMLNAGYQQVGRDFP--------VFLHPQSREEYALARTERKSGSGyt 72
Cdd:cd05398   17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEALFKKIGGRVVGlgeefgtaTVVINGLTIDVATLRTETYTDPG-- 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 527036889  73 gfTCYAAPDVTLEQDLLRRDLTINALAQD-EDGQIIDAYGGQDDLRN 118
Cdd:cd05398   95 --RRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
 2-214 7.88e-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: 116.44  E-value: 7.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889    2 KSYLVGGAVRDALLGLPVKDKDwVVVGATPEEM--LNAGYQQVGRDFPVFLHPQSRE--EYALARTERKSGSGYTGFTCY 77
Cdd:TIGR01942  31 QAYIVGGAVRDLLLGIEPKDFD-VVTSATPEEVrkLFRNSRIVGRRFRLVHVSFGRQiiEVATFRSGHKSSVNAEGRILK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   78 AAPDVTLEQDLLRRDLTINALAQD-EDGQIIDAYGGQDDLRNRLLRHVSPAFS---EDPLRVLRVARFAARYAhlsFRIA 153
Cdd:TIGR01942 110 DNVYGTLEEDAWRRDFTVNALYYDpSREVIIDYVGGMEDLKNRRLRLIGDPRSryqEDPVRMLRALRFSVKLE---FTID 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036889  154 DETLALMTAMteAGELAHLTPERVWKETENALTTRNPQVFFQVLRDCGALKVLFPEIDALF 214
Cdd:TIGR01942 187 ESTARPIRES--APLLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLEPLFPSVAYAL 245
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
 4-122 1.07e-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: 89.65  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889    4 YLVGGAVRDALLGLPVKDKDwVVVGATPEEMLNA------GYQQVGRDFPVFLHPQSREEYALARTerKSGSGYTGFtcy 77
Cdd:pfam01743   2 YIVGGAVRDLLLGKTPKDVD-IATDATPEQVATLfrrrriVHLLSGIEFGTIHVIFGNQILEVATF--RIEFDESDF--- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 527036889   78 AAPDV-----TLEQDLLRRDLTINALAQDE-DGQIIDAYGGQDDLRNRLLR 122
Cdd:pfam01743  76 RNPRSeeytgTLEEDAKRRDFTINALAYNPnSGEVIDYFGGIKDLKSGVIR 126
pcnB PRK11623
poly(A) polymerase I; Provisional
 3-214 6.65e-16

poly(A) polymerase I; Provisional


Pssm-ID: 236939 [Multi-domain]  Cd Length: 472  Bit Score: 79.41  E-value: 6.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   3 SYLVGGAVRDALLGLPVKDKDwVVVGATPEEM--LNAGYQQVGRDFP---VFLHPQ---------SREEYALARTErkSG 68
Cdd:PRK11623  69 AYLVGGGVRDLLLGKKPKDFD-VTTNATPEQVrkLFRNCRLVGRRFRlahVMFGPEiievatfrgHHEGNESDRNT--SQ 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889  69 SGYTGFTCYAAPDVTLEQDLLRRDLTINALAQD-EDGQIIDAYGGQDDLRN---RLLRHVSPAFSEDPLRVLRVARFAAR 144
Cdd:PRK11623 146 RGQNGMLLRDNIFGSIEEDAQRRDFTINSLYYSvADFTVRDYVGGMKDLKEgviRLIGNPETRYREDPVRMLRAVRFAAK 225

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 145 yahLSFRIADETLALMTAMteAGELAHLTPERVWKETENALTTRNPQVFFQVLRDCGALKVLFPEIDALF 214
Cdd:PRK11623 226 ---LDMRISPETAEPIPRL--ATLLNDIPPARLFEESLKLLQAGYGYETYKLLCEYHLFQPLFPTITRYF 290
PolyA_pol_RNAbd pfam12627
Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA ...
 150-214 9.16e-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: 62.89  E-value: 9.16e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036889  150 FRIADETLALMTAMteAGELAHLTPERVWKETENALTTRNPQVFFQVLRDCGALKVLFPEIDALF 214
Cdd:pfam12627   2 FTIEPETREAIRKL--APLLKKISPERIFEELLKLLLSGHPERGLELLRETGLLEYLFPELAAAL 64
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 231-329 1.83e-09

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 54.93  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889  231 HTLMTLSMAAMLSPEVD------VRFSTLCHDLGKGLTP--KAMWPRHHGHGPAGVKLVEGLCQRLRVpneiRDLARLVA 302
Cdd:pfam01966   4 HSLRVALLARELAEELGeldrelLLLAALLHDIGKGPFGdeKPEFEIFLGHAVVGAEILRELEKRLGL----EDVLKLIL 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 527036889  303 EFHDLI----HTFPILKPATIVKLFDNIDAW 329
Cdd:pfam01966  80 EHHESWegagYPEEISLEARIVKLADRLDAL 110
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 227-343 5.19e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 51.57  E-value: 5.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889 227 DTGVHTLMTLSMAAMLSPEVD--------VRFSTLCHDLGKGLTP----KAMWPRHHGHGPAGVKLVEGLcQRLRVPNEI 294
Cdd:cd00077    2 HRFEHSLRVAQLARRLAEELGlseedielLRLAALLHDIGKPGTPdaitEEESELEKDHAIVGAEILREL-LLEEVIKLI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 527036889 295 RDLARLVAEFH----------DLIHTFPILKPATIVKLFDNIDAWRKPQRVEQIALTSE 343
Cdd:cd00077   81 DELILAVDASHherldglgypDGLKGEEITLEARIVKLADRLDALRRDSREKRRRIAEE 139
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 228-328 1.62e-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: 44.21  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036889   228 TGVHTLMTLSMAAMLSPEVD------VRFSTLCHDLGKGLTPKAMWPR---HHGHGPAGVKLVEglcqRLRVPNEIRDLA 298
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELGlldielLLLAALLHDIGKPGTPDSFLVKtsvLEDHHFIGAEILL----EEEEPRILEEIL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 527036889   299 RLVAEFHDLIHTF----PILKPATIVKLFDNIDA 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 3.94e-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: 36.16  E-value: 3.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036889  231 HTLMT----LSMAAMLSPEVD-VRFSTLCHDLGKGLTPKAMwpRHHGHGPAGVKLVEGLCQRLRVPNEIRD 296
Cdd:TIGR00277   8 HSLEVaklaEALARELGLDVElARRGALLHDIGKPITREGV--IFESHVVVGAEIARKYGEPLEVIDIIAE 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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