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Conserved domains on  [gi|504410477|ref|WP_014597579|]
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MULTISPECIES: polynucleotide adenylyltransferase PcnB [Stutzerimonas]

Protein Classification

polynucleotide adenylyltransferase PcnB( domain architecture ID 11493326)

polynucleotide adenylyltransferase PcnB, or poly(A) polymerase, creates the 3' poly(A) tail found in some mRNAs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
30-431 0e+00

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: 549.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477   30 QHSLHRNEISRHAVSVVERLQQAGYEAYVVGGCVRDLLLQLNPKDYDVATSATPEQVRAEFRNARVIGRRFKLVHVHFGR 109
Cdd:TIGR01942   6 EHNIPRQSFSAHALNVVERLKGAGYQAYIVGGAVRDLLLGIEPKDFDVVTSATPEEVRKLFRNSRIVGRRFRLVHVSFGR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  110 EIIEVATFRANHPEEddedasqlalRNESGRILRDNVYGTLEDDAQRRDFTINALYYDPTSERILDHTRGVHDIRNRLIR 189
Cdd:TIGR01942  86 QIIEVATFRSGHKSS----------VNAEGRILKDNVYGTLEEDAWRRDFTVNALYYDPSREVIIDYVGGMEDLKNRRLR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  190 LIGDPEQRYQEDPVRMLRAVRFAAKLDFEIERHSAEPIADLAELLDGIPSARLFDETLKLFLGGKAERTFELLLEYDLFA 269
Cdd:TIGR01942 156 LIGDPRSRYQEDPVRMLRALRFSVKLEFTIDESTARPIRESAPLLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  270 PLFPASAAALERNPEYAGTLIRNALAN-TDLRIQQGKPVTPAFLFAALLWPALPARVLELQDRGMPPIPAMQEAAHDIIW 348
Cdd:TIGR01942 236 PLFPSVAYALRESPKFESAFTVQALVNdTDFRVKRDKPVTPAFLYAALLWPGLVFRVADAPDQGVMPYPAVFDAIRDFVE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  349 EQCQRTAIPKRFTIPMREIWDMQERLPRRQGRRADQLLENPRFRAGYDFLLLRESAGEKTGGLGDWWTDYQEANDSERRN 428
Cdd:TIGR01942 316 EQCAPISIPKRFSIPTREIWQMQLRLERRSGMRARKLLGHARFRAAYDLLLLREVCGRENAVLGEWWTPYQLASEEERTE 395

                  ...
gi 504410477  429 MIR 431
Cdd:TIGR01942 396 MTR 398
 
Name Accession Description Interval E-value
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
30-431 0e+00

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: 549.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477   30 QHSLHRNEISRHAVSVVERLQQAGYEAYVVGGCVRDLLLQLNPKDYDVATSATPEQVRAEFRNARVIGRRFKLVHVHFGR 109
Cdd:TIGR01942   6 EHNIPRQSFSAHALNVVERLKGAGYQAYIVGGAVRDLLLGIEPKDFDVVTSATPEEVRKLFRNSRIVGRRFRLVHVSFGR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  110 EIIEVATFRANHPEEddedasqlalRNESGRILRDNVYGTLEDDAQRRDFTINALYYDPTSERILDHTRGVHDIRNRLIR 189
Cdd:TIGR01942  86 QIIEVATFRSGHKSS----------VNAEGRILKDNVYGTLEEDAWRRDFTVNALYYDPSREVIIDYVGGMEDLKNRRLR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  190 LIGDPEQRYQEDPVRMLRAVRFAAKLDFEIERHSAEPIADLAELLDGIPSARLFDETLKLFLGGKAERTFELLLEYDLFA 269
Cdd:TIGR01942 156 LIGDPRSRYQEDPVRMLRALRFSVKLEFTIDESTARPIRESAPLLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  270 PLFPASAAALERNPEYAGTLIRNALAN-TDLRIQQGKPVTPAFLFAALLWPALPARVLELQDRGMPPIPAMQEAAHDIIW 348
Cdd:TIGR01942 236 PLFPSVAYALRESPKFESAFTVQALVNdTDFRVKRDKPVTPAFLYAALLWPGLVFRVADAPDQGVMPYPAVFDAIRDFVE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  349 EQCQRTAIPKRFTIPMREIWDMQERLPRRQGRRADQLLENPRFRAGYDFLLLRESAGEKTGGLGDWWTDYQEANDSERRN 428
Cdd:TIGR01942 316 EQCAPISIPKRFSIPTREIWQMQLRLERRSGMRARKLLGHARFRAAYDLLLLREVCGRENAVLGEWWTPYQLASEEERTE 395

                  ...
gi 504410477  429 MIR 431
Cdd:TIGR01942 396 MTR 398
pcnB PRK11623
poly(A) polymerase I; Provisional
19-433 7.12e-153

poly(A) polymerase I; Provisional


Pssm-ID: 236939 [Multi-domain]  Cd Length: 472  Bit Score: 442.65  E-value: 7.12e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  19 PRRTPEILSSRQHSLHRNEISRHAVSVVERLQQAGYEAYVVGGCVRDLLLQLNPKDYDVATSATPEQVRAEFRNARVIGR 98
Cdd:PRK11623  32 ARPQMTVIPREQHAISRKDISENALKVLYRLNKAGYEAYLVGGGVRDLLLGKKPKDFDVTTNATPEQVRKLFRNCRLVGR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  99 RFKLVHVHFGREIIEVATFRANHP-EEDDEDASQlalRNESGRILRDNVYGTLEDDAQRRDFTINALYYDPTSERILDHT 177
Cdd:PRK11623 112 RFRLAHVMFGPEIIEVATFRGHHEgNESDRNTSQ---RGQNGMLLRDNIFGSIEEDAQRRDFTINSLYYSVADFTVRDYV 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 178 RGVHDIRNRLIRLIGDPEQRYQEDPVRMLRAVRFAAKLDFEIERHSAEPIADLAELLDGIPSARLFDETLKLFLGGKAER 257
Cdd:PRK11623 189 GGMKDLKEGVIRLIGNPETRYREDPVRMLRAVRFAAKLDMRISPETAEPIPRLATLLNDIPPARLFEESLKLLQAGYGYE 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 258 TFELLLEYDLFAPLFPASAAAL-ERNPEYAGTLIRNALANTDLRIQQGKPVTPAFLFAALLW-PALPARVLELQDRGMPP 335
Cdd:PRK11623 269 TYKLLCEYHLFQPLFPTITRYFtENGDSPMERIIEQVLKNTDTRIHNDMRVNPAFLFAAMFWyPLLEHAQKIAQESGLAY 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 336 IPAMQEAAHDIIWEQCQRTAIPKRFTIPMREIWDMQERLPRRQGRRADQLLENPRFRAGYDFLLLRESAGEKT--GGLGD 413
Cdd:PRK11623 349 YDAFALAMNDVLDEACRSLAIPKRLTTLTRDIWQLQLRMSRRQGKRAWKLMEHPKFRAAYDLLALRAEVENNAelQRLAQ 428
                        410       420
                 ....*....|....*....|
gi 504410477 414 WWTDYQEANDSERRNMIRGL 433
Cdd:PRK11623 429 WWGEFQVSAPPQQKGMLNEL 448
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
37-432 1.09e-115

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: 344.88  E-value: 1.09e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  37 EISRHAVSVVERLQQAGYEAYVVGGCVRDLLLQLNPKDYDVATSATPEQVRAEFR---NARVIGRRFKLVHVHFGREIIE 113
Cdd:COG0617    1 RLSPNALKVLEALEEAGFEAYLVGGAVRDLLLGRPPKDIDIVTVATPEEVAALFRkalRTVPVGRDFGTVTVVFGGEKIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 114 VATFRANHPEEDdedasqlalrnesGRiLRDNVYG-TLEDDAQRRDFTINALYYDPTSERILDHTRGVHDIRNRLIRLIG 192
Cdd:COG0617   81 VATARTERYYGD-------------GR-RPFVEFGdTLEEDLARRDFTINALAYDLNDGELIDPFGGLADLEARVIRTVG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 193 DPEQRYQEDPVRMLRAVRFAAKLDFEIERHSAEPIADLAELLDGIPSARLFDETLKLFLGGKAERTFELLLEYDLFAPLf 272
Cdd:COG0617  147 DPEERFREDPLRILRAVRFAARLGFTIEPETLAAIREMAGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVL- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 273 pasaaalernpeyagtlirnalantdlriqqgkpvtpAFLFAALLWPALPARVLElqdRGMPPIPAMQEAAHDIIWEQCQ 352
Cdd:COG0617  226 -------------------------------------ALRLAALLHDLGKPATRE---DGLPTFHGHEEAGAELAEALLK 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 353 RTAIPKRFTIPMREIWDMQERLPRRQGRRADQLLE--NPRFRAGYDFLLLRESAGEKTGGLGDWWtDYQEANDSERRNMI 430
Cdd:COG0617  266 RLRLPNRERKLVRELVELHLRFHGLGELRDSAVRRllERGPEALEDLLLLRENGLEYPELQERLA-ELLEAAWRRFQPPV 344

                 ..
gi 504410477 431 RG 432
Cdd:COG0617  345 DG 346
PolyA_pol_arg_C pfam12626
Polymerase A arginine-rich C-terminus; The C-terminus of polymerase A in E coli is ...
331-435 5.50e-50

Polymerase A arginine-rich C-terminus; The C-terminus of polymerase A in E coli is arginine-rich and is necessary for full functioning of the enzyme.


Pssm-ID: 463647 [Multi-domain]  Cd Length: 116  Bit Score: 165.84  E-value: 5.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  331 RGMPPIPAMQEAAHDIIWEQCQRTAIPKRFTIPMREIWDMQERLPRRQGRRADQLLENPRFRAGYDFLLLRESAGEKTGG 410
Cdd:pfam12626   1 QGLPPYDALQLAADEVLDEQCQRVAIPRRFTAPMREIWLLQPRLEKRQGKRPFRLLEHPRFRAAYDFLLLRAESGEVLQE 80
                          90       100
                  ....*....|....*....|....*
gi 504410477  411 LGDWWTDYQEANDSERRNMIRGLSG 435
Cdd:pfam12626  81 LAEWWTRFQEADEAEREAMIAELGA 105
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
42-185 5.15e-37

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: 132.33  E-value: 5.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  42 AVSVVERLQQA-GYEAYVVGGCVRDLLLQLNPKDYDVATSA-TPEQVR--AEFRNARVIGR--RFKLVHVHFGREIIEVA 115
Cdd:cd05398    4 LLKLLRELKKAlGYEAYLVGGAVRDLLLGRPPKDIDIATDAdGPEFAEalFKKIGGRVVGLgeEFGTATVVINGLTIDVA 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 116 TFRANHPEEDdedasqlalrnesGRILRDNVYgTLEDDAQRRDFTINALYYDPTSERILDHTRGVHDIRN 185
Cdd:cd05398   84 TLRTETYTDP-------------GRRPPVVGF-TIEEDLLRRDFTINAMAYDLDDGELIDPFGGLKDLEN 139
 
Name Accession Description Interval E-value
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
30-431 0e+00

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: 549.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477   30 QHSLHRNEISRHAVSVVERLQQAGYEAYVVGGCVRDLLLQLNPKDYDVATSATPEQVRAEFRNARVIGRRFKLVHVHFGR 109
Cdd:TIGR01942   6 EHNIPRQSFSAHALNVVERLKGAGYQAYIVGGAVRDLLLGIEPKDFDVVTSATPEEVRKLFRNSRIVGRRFRLVHVSFGR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  110 EIIEVATFRANHPEEddedasqlalRNESGRILRDNVYGTLEDDAQRRDFTINALYYDPTSERILDHTRGVHDIRNRLIR 189
Cdd:TIGR01942  86 QIIEVATFRSGHKSS----------VNAEGRILKDNVYGTLEEDAWRRDFTVNALYYDPSREVIIDYVGGMEDLKNRRLR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  190 LIGDPEQRYQEDPVRMLRAVRFAAKLDFEIERHSAEPIADLAELLDGIPSARLFDETLKLFLGGKAERTFELLLEYDLFA 269
Cdd:TIGR01942 156 LIGDPRSRYQEDPVRMLRALRFSVKLEFTIDESTARPIRESAPLLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  270 PLFPASAAALERNPEYAGTLIRNALAN-TDLRIQQGKPVTPAFLFAALLWPALPARVLELQDRGMPPIPAMQEAAHDIIW 348
Cdd:TIGR01942 236 PLFPSVAYALRESPKFESAFTVQALVNdTDFRVKRDKPVTPAFLYAALLWPGLVFRVADAPDQGVMPYPAVFDAIRDFVE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  349 EQCQRTAIPKRFTIPMREIWDMQERLPRRQGRRADQLLENPRFRAGYDFLLLRESAGEKTGGLGDWWTDYQEANDSERRN 428
Cdd:TIGR01942 316 EQCAPISIPKRFSIPTREIWQMQLRLERRSGMRARKLLGHARFRAAYDLLLLREVCGRENAVLGEWWTPYQLASEEERTE 395

                  ...
gi 504410477  429 MIR 431
Cdd:TIGR01942 396 MTR 398
pcnB PRK11623
poly(A) polymerase I; Provisional
19-433 7.12e-153

poly(A) polymerase I; Provisional


Pssm-ID: 236939 [Multi-domain]  Cd Length: 472  Bit Score: 442.65  E-value: 7.12e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  19 PRRTPEILSSRQHSLHRNEISRHAVSVVERLQQAGYEAYVVGGCVRDLLLQLNPKDYDVATSATPEQVRAEFRNARVIGR 98
Cdd:PRK11623  32 ARPQMTVIPREQHAISRKDISENALKVLYRLNKAGYEAYLVGGGVRDLLLGKKPKDFDVTTNATPEQVRKLFRNCRLVGR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  99 RFKLVHVHFGREIIEVATFRANHP-EEDDEDASQlalRNESGRILRDNVYGTLEDDAQRRDFTINALYYDPTSERILDHT 177
Cdd:PRK11623 112 RFRLAHVMFGPEIIEVATFRGHHEgNESDRNTSQ---RGQNGMLLRDNIFGSIEEDAQRRDFTINSLYYSVADFTVRDYV 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 178 RGVHDIRNRLIRLIGDPEQRYQEDPVRMLRAVRFAAKLDFEIERHSAEPIADLAELLDGIPSARLFDETLKLFLGGKAER 257
Cdd:PRK11623 189 GGMKDLKEGVIRLIGNPETRYREDPVRMLRAVRFAAKLDMRISPETAEPIPRLATLLNDIPPARLFEESLKLLQAGYGYE 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 258 TFELLLEYDLFAPLFPASAAAL-ERNPEYAGTLIRNALANTDLRIQQGKPVTPAFLFAALLW-PALPARVLELQDRGMPP 335
Cdd:PRK11623 269 TYKLLCEYHLFQPLFPTITRYFtENGDSPMERIIEQVLKNTDTRIHNDMRVNPAFLFAAMFWyPLLEHAQKIAQESGLAY 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 336 IPAMQEAAHDIIWEQCQRTAIPKRFTIPMREIWDMQERLPRRQGRRADQLLENPRFRAGYDFLLLRESAGEKT--GGLGD 413
Cdd:PRK11623 349 YDAFALAMNDVLDEACRSLAIPKRLTTLTRDIWQLQLRMSRRQGKRAWKLMEHPKFRAAYDLLALRAEVENNAelQRLAQ 428
                        410       420
                 ....*....|....*....|
gi 504410477 414 WWTDYQEANDSERRNMIRGL 433
Cdd:PRK11623 429 WWGEFQVSAPPQQKGMLNEL 448
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
37-432 1.09e-115

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: 344.88  E-value: 1.09e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  37 EISRHAVSVVERLQQAGYEAYVVGGCVRDLLLQLNPKDYDVATSATPEQVRAEFR---NARVIGRRFKLVHVHFGREIIE 113
Cdd:COG0617    1 RLSPNALKVLEALEEAGFEAYLVGGAVRDLLLGRPPKDIDIVTVATPEEVAALFRkalRTVPVGRDFGTVTVVFGGEKIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 114 VATFRANHPEEDdedasqlalrnesGRiLRDNVYG-TLEDDAQRRDFTINALYYDPTSERILDHTRGVHDIRNRLIRLIG 192
Cdd:COG0617   81 VATARTERYYGD-------------GR-RPFVEFGdTLEEDLARRDFTINALAYDLNDGELIDPFGGLADLEARVIRTVG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 193 DPEQRYQEDPVRMLRAVRFAAKLDFEIERHSAEPIADLAELLDGIPSARLFDETLKLFLGGKAERTFELLLEYDLFAPLf 272
Cdd:COG0617  147 DPEERFREDPLRILRAVRFAARLGFTIEPETLAAIREMAGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVL- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 273 pasaaalernpeyagtlirnalantdlriqqgkpvtpAFLFAALLWPALPARVLElqdRGMPPIPAMQEAAHDIIWEQCQ 352
Cdd:COG0617  226 -------------------------------------ALRLAALLHDLGKPATRE---DGLPTFHGHEEAGAELAEALLK 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 353 RTAIPKRFTIPMREIWDMQERLPRRQGRRADQLLE--NPRFRAGYDFLLLRESAGEKTGGLGDWWtDYQEANDSERRNMI 430
Cdd:COG0617  266 RLRLPNRERKLVRELVELHLRFHGLGELRDSAVRRllERGPEALEDLLLLRENGLEYPELQERLA-ELLEAAWRRFQPPV 344

                 ..
gi 504410477 431 RG 432
Cdd:COG0617  345 DG 346
PRK13299 PRK13299
tRNA CCA-pyrophosphorylase; Provisional
36-285 3.82e-63

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237339 [Multi-domain]  Cd Length: 394  Bit Score: 209.70  E-value: 3.82e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  36 NEISRHAVSVVERLQQAGYEAYVVGGCVRDLLLQLNPKDYDVATSATPEQVRAEFRNARVIGRRFKLVHVHFGREIIEVA 115
Cdd:PRK13299   3 PSEFQKALPILEKIKEAGFEAYFVGGSVRDYLLGRPIHDVDIATSAYPEEVKAIFPRTVDVGIEHGTVLVLENGEEYEVT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 116 TFRAnhpEEDDEDASqlalRNESGRILRDnvygtLEDDAQRRDFTINALYYDPTSErILDHTRGVHDIRNRLIRLIGDPE 195
Cdd:PRK13299  83 TFRT---ESEYVDYR----RPSEVTFVRS-----LEEDLKRRDFTINAIAMDENGE-IIDLFDGLEDLKNRLIRAVGNAE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 196 QRYQEDPVRMLRAVRFAAKLDFEIERHSAEPIADLAELLDGIPSARLFDETLKLFLGGKAERTFELLLEYDLFA--PLFP 273
Cdd:PRK13299 150 ERFQEDALRMMRAVRFASQLGFDLETETFEAMKTQAPLLEKISVERIFVEFEKLLLGPFWRKGLKLLIETGLYNylPGLK 229
                        250
                 ....*....|..
gi 504410477 274 ASAAALERNPEY 285
Cdd:PRK13299 230 GKEENLLKLTQL 241
PolyA_pol_arg_C pfam12626
Polymerase A arginine-rich C-terminus; The C-terminus of polymerase A in E coli is ...
331-435 5.50e-50

Polymerase A arginine-rich C-terminus; The C-terminus of polymerase A in E coli is arginine-rich and is necessary for full functioning of the enzyme.


Pssm-ID: 463647 [Multi-domain]  Cd Length: 116  Bit Score: 165.84  E-value: 5.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  331 RGMPPIPAMQEAAHDIIWEQCQRTAIPKRFTIPMREIWDMQERLPRRQGRRADQLLENPRFRAGYDFLLLRESAGEKTGG 410
Cdd:pfam12626   1 QGLPPYDALQLAADEVLDEQCQRVAIPRRFTAPMREIWLLQPRLEKRQGKRPFRLLEHPRFRAAYDFLLLRAESGEVLQE 80
                          90       100
                  ....*....|....*....|....*
gi 504410477  411 LGDWWTDYQEANDSERRNMIRGLSG 435
Cdd:pfam12626  81 LAEWWTRFQEADEAEREAMIAELGA 105
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
56-189 1.34e-44

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: 152.05  E-value: 1.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477   56 AYVVGGCVRDLLLQLNPKDYDVATSATPEQVRAEFRNARVI----GRRFKLVHVHFGREIIEVATFRANHPEEDdedasq 131
Cdd:pfam01743   1 LYIVGGAVRDLLLGKTPKDVDIATDATPEQVATLFRRRRIVhllsGIEFGTIHVIFGNQILEVATFRIEFDESD------ 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504410477  132 lalrnesGRILRDNVY-GTLEDDAQRRDFTINALYYDPTSERILDHTRGVHDIRNRLIR 189
Cdd:pfam01743  75 -------FRNPRSEEYtGTLEEDAKRRDFTINALAYNPNSGEVIDYFGGIKDLKSGVIR 126
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
42-185 5.15e-37

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: 132.33  E-value: 5.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  42 AVSVVERLQQA-GYEAYVVGGCVRDLLLQLNPKDYDVATSA-TPEQVR--AEFRNARVIGR--RFKLVHVHFGREIIEVA 115
Cdd:cd05398    4 LLKLLRELKKAlGYEAYLVGGAVRDLLLGRPPKDIDIATDAdGPEFAEalFKKIGGRVVGLgeEFGTATVVINGLTIDVA 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 116 TFRANHPEEDdedasqlalrnesGRILRDNVYgTLEDDAQRRDFTINALYYDPTSERILDHTRGVHDIRN 185
Cdd:cd05398   84 TLRTETYTDP-------------GRRPPVVGF-TIEEDLLRRDFTINAMAYDLDDGELIDPFGGLKDLEN 139
PolyA_pol_RNAbd pfam12627
Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA ...
216-279 2.25e-18

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: 78.68  E-value: 2.25e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504410477  216 DFEIERHSAEPIADLAELLDGIPSARLFDETLKLFLGGKAERTFELLLEYDLFAPLFPASAAAL 279
Cdd:pfam12627   1 GFTIEPETREAIRKLAPLLKKISPERIFEELLKLLLSGHPERGLELLRETGLLEYLFPELAAAL 64
cca PRK10885
multifunctional CCA addition/repair protein;
57-273 1.07e-17

multifunctional CCA addition/repair protein;


Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 84.91  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  57 YVVGGCVRDLLLQLNPKDYD-VATSATPEQVRAefRNARVIGRRFKLvhvhfgreiievatFRanHPEEDDEDAsqLAlR 135
Cdd:PRK10885   4 YLVGGAVRDALLGLPVKDRDwVVVGATPEEMLA--QGYQQVGKDFPV--------------FL--HPKTHEEYA--LA-R 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 136 NE--SGRilrdnVYG----------TLEDDAQRRDFTINALYYDPTSErILDHTRGVHDIRNRLIRLIGDPeqrYQEDPV 203
Cdd:PRK10885  63 TErkSGR-----GYTgftcyaapdvTLEEDLIRRDLTINAMAQDDDGE-LIDPYGGQRDLEARLLRHVSPA---FAEDPL 133
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504410477 204 RMLRAVRFAAK---LDFEIERHSAEPIADLAEL--LDGIPSARLFDETLKLFLGGKAERTFELLLEYDLFAPLFP 273
Cdd:PRK10885 134 RVLRVARFAARfahLGFRIAPETLALMREMVASgeLDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLP 208
PRK13298 PRK13298
tRNA CCA-pyrophosphorylase; Provisional
55-273 1.88e-17

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237338 [Multi-domain]  Cd Length: 417  Bit Score: 84.01  E-value: 1.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  55 EAYVVGGCVRDLLLQLNPKDYD-VATSATPEQVRAefRNARVIGRRFKLVHvhfgreiievatfranHPEEDDEDAsqLA 133
Cdd:PRK13298   2 KIYLVGGAVRDSLLNLPVKDKDwVVVGGTPKILLS--INFQQVGKDFPVFL----------------HPETHEEYA--LA 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 134 lRNE-------SGRILRDNVYGTLEDDAQRRDFTINALYYDpTSERILDHTRGVHDIRNRLIRLIgdpEQRYQEDPVRML 206
Cdd:PRK13298  62 -RTErksgvgyTGFITDTSSDVTLEEDLIRRDLTINAIAQD-ENGNYIDPFQGKKDIQLRLLRHV---SESFIEDPLRVL 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504410477 207 RAVRFAAK---LDFEIERHSAE---PIADLAELLDGIPSaRLFDETLKLFLGGKAERTFELLLEYDLFAPLFP 273
Cdd:PRK13298 137 RVARFAALlvhLGFKIAKETMIlmcIMVKKHELLYLTPE-RIWNETEKALKTDNPHVYFQVLYECNALKFLFP 208
PRK13296 PRK13296
CCA tRNA nucleotidyltransferase;
55-285 3.24e-17

CCA tRNA nucleotidyltransferase;


Pssm-ID: 106256 [Multi-domain]  Cd Length: 360  Bit Score: 82.73  E-value: 3.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  55 EAYVVGGCVRDLLLQLNPKDYD-VATSATPEQVraefrnarvIGRRFKLVHVHFGREIievatfranHPEEDDEDAsqLA 133
Cdd:PRK13296   2 KFYLVGGAVRDMLLGITPKDKDwVVVGATEDEM---------LANGFIKIAANFPVFI---------HPQTKQEYA--LA 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 134 lRNES-------GRILRDNVYGTLEDDAQRRDFTINALYYDpTSERILDHTRGVHDIRNRLIRligDPEQRYQEDPVRML 206
Cdd:PRK13296  62 -RSEKktasgyhGFEVNFSKYITLEDDLKRRDLTINSIAID-QNNKVIDPFNGQADLQNRILR---HTSIAFIEDPLRVV 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 207 RAVRFAAKL---DFEIERHSAEPIADLAEL--LDGIPSARLFDETLKLFLGGKAerTFELLLEYDLFAPLFPASAAALE- 280
Cdd:PRK13296 137 RLARFKAQLsnfNFSIAQEMLALIKELVKTgeLNHLTRERLHIEFVKALNNPKI--FFTTLKELEALKIIFPNISCILPl 214
                        250
                 ....*....|..
gi 504410477 281 -------RNPEY 285
Cdd:PRK13296 215 ipnksffENPIY 226
PRK13297 PRK13297
tRNA CCA-pyrophosphorylase; Provisional
52-219 1.29e-15

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 139469 [Multi-domain]  Cd Length: 364  Bit Score: 78.11  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477  52 AGYEAYVVGGCVRDLLLQLNPKDYD-VATSATPEQVraefrnARvigRRFKLVHVHFGREIievatfranHPEEDDEDAS 130
Cdd:PRK13297  10 AGLQVYIVGGAVRDALLGLPAGDRDwVVVGATPEDM------AR---RGFIPVGGDFPVFL---------HPRTKEEYAL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410477 131 QLALRnESGRILRDNVYGT-----LEDDAQRRDFTINALYYDPTSErILDHTRGVHDIRNRLIRLIGDPeqrYQEDPVRM 205
Cdd:PRK13297  72 ARTER-KSGRGYKGFTFYTgadvtLEQDLQRRDLTVNAIARTPQGE-LVDPLDGVADVRARVLRHVGEA---FAEDPVRI 146
                        170
                 ....*....|....*
gi 504410477 206 LRAVRFAAKL-DFEI 219
Cdd:PRK13297 147 LRLGRFAARFgDFSI 161
PHA01806 PHA01806
hypothetical protein
56-89 3.96e-03

hypothetical protein


Pssm-ID: 222838  Cd Length: 200  Bit Score: 38.32  E-value: 3.96e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 504410477  56 AYVVGGCVRDLLLQLNPKDYDVATsATPEQVRAE 89
Cdd:PHA01806  38 VALAGGAARDLMHGAEPKDIDIAL-YGMDDRQAE 70
 
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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