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Conserved domains on  [gi|1743119824|gb|KAA3494016|]
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multifunctional CCA addition/repair protein [Vibrio mimicus]

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;
1-402 0e+00

multifunctional CCA addition/repair protein;


:

Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 786.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   1 MQIYLVGGAVRDQLLQLPVYDRDWVVVGSSPQAMLAAGFQAVGKDFPVFLHPKTKEEHALARTERKTGVGYTGFACHYAP 80
Cdd:PRK10885    1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  81 DVTLEEDLLRRDLTINAMAQDESGQVIDPYGGQRDLAAKVLRHVSPAFVEDPLRVLRVARFAAKLAHLGFTVAEETMQLM 160
Cdd:PRK10885   81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 161 ADIAQSGELGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAVVLPELDRLFGVPQPEKWHPEIDTGIHTLMVTKQAA 240
Cdd:PRK10885  161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 241 LLSDSLPVRFSAQVHDLGKGVTPPSEWPSHKLHCHTGLKVIESLCDRIRVPNEFRDLALAVCAQHSNIHRADELKPATKL 320
Cdd:PRK10885  241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 321 KVLGLLDVWRKPERLEQVLLCCEADHRGRLGLEEKPYPQRDIFLRAYQAALSVEVQAVIRDGFQGKQIKEELDKRRIQAI 400
Cdd:PRK10885  321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400


                  ..
gi 1743119824 401 SE 402
Cdd:PRK10885  401 AA 402
 
Name Accession Description Interval E-value
cca PRK10885
multifunctional CCA addition/repair protein;
1-402 0e+00

multifunctional CCA addition/repair protein;


Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 786.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   1 MQIYLVGGAVRDQLLQLPVYDRDWVVVGSSPQAMLAAGFQAVGKDFPVFLHPKTKEEHALARTERKTGVGYTGFACHYAP 80
Cdd:PRK10885    1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  81 DVTLEEDLLRRDLTINAMAQDESGQVIDPYGGQRDLAAKVLRHVSPAFVEDPLRVLRVARFAAKLAHLGFTVAEETMQLM 160
Cdd:PRK10885   81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 161 ADIAQSGELGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAVVLPELDRLFGVPQPEKWHPEIDTGIHTLMVTKQAA 240
Cdd:PRK10885  161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 241 LLSDSLPVRFSAQVHDLGKGVTPPSEWPSHKLHCHTGLKVIESLCDRIRVPNEFRDLALAVCAQHSNIHRADELKPATKL 320
Cdd:PRK10885  241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 321 KVLGLLDVWRKPERLEQVLLCCEADHRGRLGLEEKPYPQRDIFLRAYQAALSVEVQAVIRDGFQGKQIKEELDKRRIQAI 400
Cdd:PRK10885  321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400


                  ..
gi 1743119824 401 SE 402
Cdd:PRK10885  401 AA 402
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
 1-400 1.80e-120

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: 354.89  E-value: 1.80e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   1 MQIYLVGGAVRDQLLQLPVYDRDWVVVGsSPQAMLAAG-----FQAVGKDFPVFLHP--KTKEEHALARTERKTGVGYTG 73
Cdd:COG0617    18 FEAYLVGGAVRDLLLGRPPKDIDIVTVA-TPEEVAALFrkalrTVPVGRDFGTVTVVfgGEKIEVATARTERYYGDGRRP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  74 FaCHYAPdvTLEEDLLRRDLTINAMAQDE-SGQVIDPYGGQRDLAAKVLRHVS---PAFVEDPLRVLRVARFAAKlahLG 149
Cdd:COG0617    97 F-VEFGD--TLEEDLARRDFTINALAYDLnDGELIDPFGGLADLEARVIRTVGdpeERFREDPLRILRAVRFAAR---LG 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 150 FTVAEETMQLMADIAqsGELGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAVvlpeldrlfgvpqpekwhpeidtg 229
Cdd:COG0617   171 FTIEPETLAAIREMA--GLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEV------------------------ 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 230 ihtlmvtkqaallsdsLPVRFSAQVHDLGKGVTPPSEWPSHKLHCHTGLKVIESLCDRIRVPNEFRDLALAVCAQHSNIH 309
Cdd:COG0617   225 ----------------LALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 310 RADELKPATKLKVLGlldvwRKPERLEQVLLCCEADhrgrlglEEKPYPQRDIfLRAYQAALS-----VEVQAVIRDGFQ 384
Cdd:COG0617   289 GLGELRDSAVRRLLE-----RGPEALEDLLLLRENG-------LEYPELQERL-AELLEAAWRrfqppVDGEDLMALGLK 355

                         410
                  ....*....|....*..
gi 1743119824 385 -GKQIKEELDKRRIQAI 400
Cdd:COG0617   356 pGPEIGEILRALREAVL 372
tRNA_CCA_actino TIGR02692
tRNA adenylyltransferase; The enzyme tRNA adenylyltransferase, also called ...
 2-262 1.30e-36

tRNA adenylyltransferase; The enzyme tRNA adenylyltransferase, also called tRNA-nucleotidyltransferase and CCA-adding enzyme, can add or repair the required CCA triplet at the 3'-end of tRNA molecules. Genes encoding tRNA include the CCA tail in some but not all bacteria, and this enzyme may be required for viability. Members of this family represent a distinct clade within the larger family pfam01743 (tRNA nucleotidyltransferase/poly(A) polymerase family protein). The example from Streptomyces coelicolor was shown to act as a CCA-adding enzyme and not as a poly(A) polymerase. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 131739 [Multi-domain]  Cd Length: 466  Bit Score: 138.71  E-value: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   2 QIYLVGGAVRDQLLQLPVYDRDWVVvGSSPQAML---------------AAGFQAVGKDFPVfLHPKTKEEHALARTERK 66
Cdd:TIGR02692  29 ELYLVGGSVRDALLGRLGHDLDFTT-DARPEETLailrpwadavwdtgiAFGTVGAEKDGQQ-IEITTFRSDSYDGTSRK 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  67 TGVGYTGfachyapdvTLEEDLLRRDLTINAMA----QDESGQVIDPYGGQRDLAAKVLRHVSP---AFVEDPLRVLRVA 139
Cdd:TIGR02692 107 PEVTFGD---------TLEGDLIRRDFTVNAMAvripADGSLEFHDPVGGLDDLLAKVLDTPATpeqSFGDDPLRMLRAA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 140 RFAAKlahLGFTVAEETMQLMADIAqsGELGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAVVLPELDRLfGVPQP 219
Cdd:TIGR02692 178 RFVSQ---LGFEVAPRVRAAMTEMA--DQIERISAERVRVELDKLLLGDHPRAGIDLMVETGLADRVLPEIPAL-RLEID 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1743119824 220 EKwHPEIDTGIHTLMVTKQAALLSDSLP---VRFSAQVHDLGKGVT 262
Cdd:TIGR02692 252 EH-HQHKDVYEHSLTVLRQAIDLEDDGPdlvLRWAALLHDIGKPAT 296
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
 1-118 6.35e-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: 109.60  E-value: 6.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   1 MQIYLVGGAVRDQLLQLPVYDRDWVVVGSSPQAMLA------AGFQAVGKDFPV--FLHPKTKEEHALARTERKTGVGyt 72
Cdd:cd05398    17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEAlfkkigGRVVGLGEEFGTatVVINGLTIDVATLRTETYTDPG-- 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1743119824  73 gfACHYAPDVTLEEDLLRRDLTINAMAQD-ESGQVIDPYGGQRDLAA 118
Cdd:cd05398    95 --RRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
 3-122 2.89e-19

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: 83.10  E-value: 2.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   3 IYLVGGAVRDQLLQLPVYDRDwVVVGSSPQaMLAAGFQavgKDFPVFLHpkTKEEHALA-------RTERKTGVGYTGFA 75
Cdd:pfam01743   1 LYIVGGAVRDLLLGKTPKDVD-IATDATPE-QVATLFR---RRRIVHLL--SGIEFGTIhvifgnqILEVATFRIEFDES 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1743119824  76 CHYAPDV-----TLEEDLLRRDLTINAMAQDE-SGQVIDPYGGQRDLAAKVLR 122
Cdd:pfam01743  74 DFRNPRSeeytgTLEEDAKRRDFTINALAYNPnSGEVIDYFGGIKDLKSGVIR 126
 
Name Accession Description Interval E-value
cca PRK10885
multifunctional CCA addition/repair protein;
1-402 0e+00

multifunctional CCA addition/repair protein;


Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 786.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   1 MQIYLVGGAVRDQLLQLPVYDRDWVVVGSSPQAMLAAGFQAVGKDFPVFLHPKTKEEHALARTERKTGVGYTGFACHYAP 80
Cdd:PRK10885    1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  81 DVTLEEDLLRRDLTINAMAQDESGQVIDPYGGQRDLAAKVLRHVSPAFVEDPLRVLRVARFAAKLAHLGFTVAEETMQLM 160
Cdd:PRK10885   81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 161 ADIAQSGELGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAVVLPELDRLFGVPQPEKWHPEIDTGIHTLMVTKQAA 240
Cdd:PRK10885  161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 241 LLSDSLPVRFSAQVHDLGKGVTPPSEWPSHKLHCHTGLKVIESLCDRIRVPNEFRDLALAVCAQHSNIHRADELKPATKL 320
Cdd:PRK10885  241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 321 KVLGLLDVWRKPERLEQVLLCCEADHRGRLGLEEKPYPQRDIFLRAYQAALSVEVQAVIRDGFQGKQIKEELDKRRIQAI 400
Cdd:PRK10885  321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400


                  ..
gi 1743119824 401 SE 402
Cdd:PRK10885  401 AA 402
PRK13298 PRK13298
tRNA CCA-pyrophosphorylase; Provisional
 1-402 6.20e-160

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237338 [Multi-domain]  Cd Length: 417  Bit Score: 456.11  E-value: 6.20e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   1 MQIYLVGGAVRDQLLQLPVYDRDWVVVGSSPQAMLAAGFQAVGKDFPVFLHPKTKEEHALARTERKTGVGYTGFACHYAP 80
Cdd:PRK13298    1 MKIYLVGGAVRDSLLNLPVKDKDWVVVGGTPKILLSINFQQVGKDFPVFLHPETHEEYALARTERKSGVGYTGFITDTSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  81 DVTLEEDLLRRDLTINAMAQDESGQVIDPYGGQRDLAAKVLRHVSPAFVEDPLRVLRVARFAAKLAHLGFTVAEETMQLM 160
Cdd:PRK13298   81 DVTLEEDLIRRDLTINAIAQDENGNYIDPFQGKKDIQLRLLRHVSESFIEDPLRVLRVARFAALLVHLGFKIAKETMILM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 161 ADIAQSGELGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAVVLPELDRLFGVPQPEKWH-PEIDTGIHTLMVTKQA 239
Cdd:PRK13298  161 CIMVKKHELLYLTPERIWNETEKALKTDNPHVYFQVLYECNALKFLFPEIDFLYEKPYFLNSFfKKFNLGNYILMGLSKI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 240 ALLSDSLPVRFSAQVHDLGKGVTPPSEWPSHKLHCHT--GLKVIESLCDRIRVPNEFRDLALAVCAQH---SNIHRadeL 314
Cdd:PRK13298  241 SKLTKDIDIRFSYLCQFLGSMIPINQIKRNYKKIFFDkyAASLIKNLCKRFKIPSYIRNIAVLNTGFYfflYNIHY---Q 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 315 KPATKLKVLGLLDVWRKPERLEQVLLCCEADHRGRLGLEEKPYPQRDIFLRAYQAALSVEVQAVIRDGFQGKQIKEELDK 394
Cdd:PRK13298  318 SSKNIITLFSKIDAWRKPDRIKKLIFLSNFNLLRNKKSINFLIKQGNFLKKAFSVTKKISIKDILKKGFKGYEIKQELYR 397


                  ....*...
gi 1743119824 395 RRIQAISE 402
Cdd:PRK13298  398 LRIHKLKF 405
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
 1-400 1.80e-120

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: 354.89  E-value: 1.80e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   1 MQIYLVGGAVRDQLLQLPVYDRDWVVVGsSPQAMLAAG-----FQAVGKDFPVFLHP--KTKEEHALARTERKTGVGYTG 73
Cdd:COG0617    18 FEAYLVGGAVRDLLLGRPPKDIDIVTVA-TPEEVAALFrkalrTVPVGRDFGTVTVVfgGEKIEVATARTERYYGDGRRP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  74 FaCHYAPdvTLEEDLLRRDLTINAMAQDE-SGQVIDPYGGQRDLAAKVLRHVS---PAFVEDPLRVLRVARFAAKlahLG 149
Cdd:COG0617    97 F-VEFGD--TLEEDLARRDFTINALAYDLnDGELIDPFGGLADLEARVIRTVGdpeERFREDPLRILRAVRFAAR---LG 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 150 FTVAEETMQLMADIAqsGELGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAVvlpeldrlfgvpqpekwhpeidtg 229
Cdd:COG0617   171 FTIEPETLAAIREMA--GLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEV------------------------ 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 230 ihtlmvtkqaallsdsLPVRFSAQVHDLGKGVTPPSEWPSHKLHCHTGLKVIESLCDRIRVPNEFRDLALAVCAQHSNIH 309
Cdd:COG0617   225 ----------------LALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 310 RADELKPATKLKVLGlldvwRKPERLEQVLLCCEADhrgrlglEEKPYPQRDIfLRAYQAALS-----VEVQAVIRDGFQ 384
Cdd:COG0617   289 GLGELRDSAVRRLLE-----RGPEALEDLLLLRENG-------LEYPELQERL-AELLEAAWRrfqppVDGEDLMALGLK 355

                         410
                  ....*....|....*..
gi 1743119824 385 -GKQIKEELDKRRIQAI 400
Cdd:COG0617   356 pGPEIGEILRALREAVL 372
PRK13297 PRK13297
tRNA CCA-pyrophosphorylase; Provisional
 1-301 2.66e-87

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 139469 [Multi-domain]  Cd Length: 364  Bit Score: 269.17  E-value: 2.66e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   1 MQIYLVGGAVRDQLLQLPVYDRDWVVVGSSPQAMLAAGFQAVGKDFPVFLHPKTKEEHALARTERKTGVGYTGFACHYAP 80
Cdd:PRK13297   12 LQVYIVGGAVRDALLGLPAGDRDWVVVGATPEDMARRGFIPVGGDFPVFLHPRTKEEYALARTERKSGRGYKGFTFYTGA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  81 DVTLEEDLLRRDLTINAMAQDESGQVIDPYGGQRDLAAKVLRHVSPAFVEDPLRVLRVARFAAKLAHlgFTVAEETMQLM 160
Cdd:PRK13297   92 DVTLEQDLQRRDLTVNAIARTPQGELVDPLDGVADVRARVLRHVGEAFAEDPVRILRLGRFAARFGD--FSIAPETMQLC 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 161 ADIAQSGELGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAVVLPEL----------DRLF--GVPQPEKW------ 222
Cdd:PRK13297  170 RRMVEAGEADALVPERVWKEVSRGLMAQAPSRMLDVLARAGALARVMPELhddaavraeiDRAAaaGLPLAGRYallcrh 249

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743119824 223 HPEIDTGIHTLMVTKQAALLSDSLPVRFSAqvhdLGKGVTPPSEwpshklhchtgLKVIESlCDRIRVPNEFRDLALAV 301
Cdd:PRK13297  250 TPERDALGRRLRAPVECMDQARLLPLAVDA----LAASATPAAQ-----------LDLIER-CDALRKPERFDALLQAA 312
PRK13296 PRK13296
CCA tRNA nucleotidyltransferase;
1-217 1.22e-82

CCA tRNA nucleotidyltransferase;


Pssm-ID: 106256 [Multi-domain]  Cd Length: 360  Bit Score: 257.22  E-value: 1.22e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   1 MQIYLVGGAVRDQLLQLPVYDRDWVVVGSSPQAMLAAGFQAVGKDFPVFLHPKTKEEHALARTERKTGVGYTGFACHYAP 80
Cdd:PRK13296    1 MKFYLVGGAVRDMLLGITPKDKDWVVVGATEDEMLANGFIKIAANFPVFIHPQTKQEYALARSEKKTASGYHGFEVNFSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  81 DVTLEEDLLRRDLTINAMAQDESGQVIDPYGGQRDLAAKVLRHVSPAFVEDPLRVLRVARFAAKLAHLGFTVAEETMQLM 160
Cdd:PRK13296   81 YITLEDDLKRRDLTINSIAIDQNNKVIDPFNGQADLQNRILRHTSIAFIEDPLRVVRLARFKAQLSNFNFSIAQEMLALI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1743119824 161 ADIAQSGELGHLTAERVWQEWHKSLstNHPEVFLQVLRDCGALAVVLPELDR-LFGVP 217
Cdd:PRK13296  161 KELVKTGELNHLTRERLHIEFVKAL--NNPKIFFTTLKELEALKIIFPNISCiLPLIP 216
tRNA_CCA_actino TIGR02692
tRNA adenylyltransferase; The enzyme tRNA adenylyltransferase, also called ...
 2-262 1.30e-36

tRNA adenylyltransferase; The enzyme tRNA adenylyltransferase, also called tRNA-nucleotidyltransferase and CCA-adding enzyme, can add or repair the required CCA triplet at the 3'-end of tRNA molecules. Genes encoding tRNA include the CCA tail in some but not all bacteria, and this enzyme may be required for viability. Members of this family represent a distinct clade within the larger family pfam01743 (tRNA nucleotidyltransferase/poly(A) polymerase family protein). The example from Streptomyces coelicolor was shown to act as a CCA-adding enzyme and not as a poly(A) polymerase. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 131739 [Multi-domain]  Cd Length: 466  Bit Score: 138.71  E-value: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   2 QIYLVGGAVRDQLLQLPVYDRDWVVvGSSPQAML---------------AAGFQAVGKDFPVfLHPKTKEEHALARTERK 66
Cdd:TIGR02692  29 ELYLVGGSVRDALLGRLGHDLDFTT-DARPEETLailrpwadavwdtgiAFGTVGAEKDGQQ-IEITTFRSDSYDGTSRK 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  67 TGVGYTGfachyapdvTLEEDLLRRDLTINAMA----QDESGQVIDPYGGQRDLAAKVLRHVSP---AFVEDPLRVLRVA 139
Cdd:TIGR02692 107 PEVTFGD---------TLEGDLIRRDFTVNAMAvripADGSLEFHDPVGGLDDLLAKVLDTPATpeqSFGDDPLRMLRAA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 140 RFAAKlahLGFTVAEETMQLMADIAqsGELGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAVVLPELDRLfGVPQP 219
Cdd:TIGR02692 178 RFVSQ---LGFEVAPRVRAAMTEMA--DQIERISAERVRVELDKLLLGDHPRAGIDLMVETGLADRVLPEIPAL-RLEID 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1743119824 220 EKwHPEIDTGIHTLMVTKQAALLSDSLP---VRFSAQVHDLGKGVT 262
Cdd:TIGR02692 252 EH-HQHKDVYEHSLTVLRQAIDLEDDGPdlvLRWAALLHDIGKPAT 296
PRK13299 PRK13299
tRNA CCA-pyrophosphorylase; Provisional
 4-230 2.13e-34

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237339 [Multi-domain]  Cd Length: 394  Bit Score: 131.50  E-value: 2.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   4 YLVGGAVRDQLLQLPVYDRDwVVVGSSPQAmLAAGFQavgKDFPV--------FLHPKTKEEHALARTERktgvGYTGFA 75
Cdd:PRK13299   24 YFVGGSVRDYLLGRPIHDVD-IATSAYPEE-VKAIFP---RTVDVgiehgtvlVLENGEEYEVTTFRTES----EYVDYR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  76 chyAPD-VT----LEEDLLRRDLTINAMAQDESGQVIDPYGGQRDLAAKVLRHV-SPA--FVEDPLRVLRVARFAAKlah 147
Cdd:PRK13299   95 ---RPSeVTfvrsLEEDLKRRDFTINAIAMDENGEIIDLFDGLEDLKNRLIRAVgNAEerFQEDALRMMRAVRFASQ--- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 148 LGFTVAEETMQLMADiaQSGELGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAvVLPEL----DRLFGVPQPEKWH 223
Cdd:PRK13299  169 LGFDLETETFEAMKT--QAPLLEKISVERIFVEFEKLLLGPFWRKGLKLLIETGLYN-YLPGLkgkeENLLKLTQLLWFS 245


                  ....*..
gi 1743119824 224 PEIDTGI 230
Cdd:PRK13299  246 FETSEQA 252
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
 1-118 6.35e-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: 109.60  E-value: 6.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   1 MQIYLVGGAVRDQLLQLPVYDRDWVVVGSSPQAMLA------AGFQAVGKDFPV--FLHPKTKEEHALARTERKTGVGyt 72
Cdd:cd05398    17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEAlfkkigGRVVGLGEEFGTatVVINGLTIDVATLRTETYTDPG-- 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1743119824  73 gfACHYAPDVTLEEDLLRRDLTINAMAQD-ESGQVIDPYGGQRDLAA 118
Cdd:cd05398    95 --RRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
 2-249 5.63e-24

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: 102.57  E-value: 5.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   2 QIYLVGGAVRDQLLQLPVYDRDwVVVGSSPQAM--LAAGFQAVGKDFPVfLH---PKTKEEHALARTERKTGVGYTGFAC 76
Cdd:TIGR01942  31 QAYIVGGAVRDLLLGIEPKDFD-VVTSATPEEVrkLFRNSRIVGRRFRL-VHvsfGRQIIEVATFRSGHKSSVNAEGRIL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  77 HYAPDVTLEEDLLRRDLTINAMAQD-ESGQVIDPYGGQRDLAAKVLRHVSPA---FVEDPLRVLRVARFAAKlahLGFTV 152
Cdd:TIGR01942 109 KDNVYGTLEEDAWRRDFTVNALYYDpSREVIIDYVGGMEDLKNRRLRLIGDPrsrYQEDPVRMLRALRFSVK---LEFTI 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 153 AEETmqlMADIAQSG-ELGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAVVLPELDRLFgvpqpekwhPEIDTGIH 231
Cdd:TIGR01942 186 DEST---ARPIRESApLLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLEPLFPSVAYAL---------RESPKFES 253

                         250
                  ....*....|....*...
gi 1743119824 232 TLMVtkQAALLSDSLPVR 249
Cdd:TIGR01942 254 AFTV--QALVNDTDFRVK 269
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
 3-122 2.89e-19

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: 83.10  E-value: 2.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   3 IYLVGGAVRDQLLQLPVYDRDwVVVGSSPQaMLAAGFQavgKDFPVFLHpkTKEEHALA-------RTERKTGVGYTGFA 75
Cdd:pfam01743   1 LYIVGGAVRDLLLGKTPKDVD-IATDATPE-QVATLFR---RRRIVHLL--SGIEFGTIhvifgnqILEVATFRIEFDES 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1743119824  76 CHYAPDV-----TLEEDLLRRDLTINAMAQDE-SGQVIDPYGGQRDLAAKVLR 122
Cdd:pfam01743  74 DFRNPRSeeytgTLEEDAKRRDFTINALAYNPnSGEVIDYFGGIKDLKSGVIR 126
PolyA_pol_RNAbd pfam12627
Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA ...
 149-214 2.30e-12

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: 61.73  E-value: 2.30e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743119824 149 GFTVAEETMQLMADIAQsgELGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAVVLPELDRLF 214
Cdd:pfam12627   1 GFTIEPETREAIRKLAP--LLKKISPERIFEELLKLLLSGHPERGLELLRETGLLEYLFPELAAAL 64
pcnB PRK11623
poly(A) polymerase I; Provisional
 2-214 2.31e-10

poly(A) polymerase I; Provisional


Pssm-ID: 236939 [Multi-domain]  Cd Length: 472  Bit Score: 62.08  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824   2 QIYLVGGAVRDQLLQLPVYDRDwVVVGSSPQAM--LAAGFQAVGKDFP---VFLHPKTKE------EHALARTERKTGV- 69
Cdd:PRK11623   68 EAYLVGGGVRDLLLGKKPKDFD-VTTNATPEQVrkLFRNCRLVGRRFRlahVMFGPEIIEvatfrgHHEGNESDRNTSQr 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824  70 GYTGFACHYAPDVTLEEDLLRRDLTINAM---AQDESgqVIDPYGGQRDLAAKVLRHV-SPA--FVEDPLRVLRVARFAA 143
Cdd:PRK11623  147 GQNGMLLRDNIFGSIEEDAQRRDFTINSLyysVADFT--VRDYVGGMKDLKEGVIRLIgNPEtrYREDPVRMLRAVRFAA 224

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743119824 144 KlahLGFTVAEETMQLMADIAQSgeLGHLTAERVWQEWHKSLSTNHPEVFLQVLRDCGALAVVLPELDRLF 214
Cdd:PRK11623  225 K---LDMRISPETAEPIPRLATL--LNDIPPARLFEESLKLLQAGYGYETYKLLCEYHLFQPLFPTITRYF 290
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 227-360 1.72e-06

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 47.33  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743119824 227 DTGIHTLMVTKQAALLSDSLP--------VRFSAQVHDLGKGVTPPS----EWPSHKLHCHTGLKVIESLcDRIRVPNEF 294
Cdd:cd00077     2 HRFEHSLRVAQLARRLAEELGlseedielLRLAALLHDIGKPGTPDAiteeESELEKDHAIVGAEILREL-LLEEVIKLI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743119824 295 RDLALAVCAQHsnihradelkpATKLKVLGLLDVWRKPERLEQVLLCCEADHRGRLGLEEKPYPQR 360
Cdd:cd00077    81 DELILAVDASH-----------HERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRDSREKRRR 135
 
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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