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Conserved domains on  [gi|490365910|ref|WP_004245574|]
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MULTISPECIES: multifunctional CCA addition/repair protein [Proteus]

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

Graphical summary

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List of domain hits

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
 
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
 
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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