1OU5,1MIW,1MIY


Conserved Protein Domain Family
NT_ClassII-CCAase

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cd05398: NT_ClassII-CCAase 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 143388
Aligned: 93 rows
Threshold Bit Score: 102.286
Created: 18-May-2007
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 14 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Comment:The active site annotation includes NTP- and metal-binding residues, as well as residues involved in primer tRNA binding in Aquifex aeolicus Aase.
  • Structure:1MIY_A, Bacillus stearothermophilus CCA-adding enzyme monomer bound with CTP and Mg2+, contacts determined at 4.5A
    View structure with Cn3D
  • Structure:1MIW_A, Bacillus stearothermophilus CCA-adding enzyme homodimer, bound with ATP and Mg2+, contacts determined at 4.5A.
    View structure with Cn3D
  • Comment:Some members of this group form dimers in solution.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                          ##  ##          # #                           
1OU5_A        56 TEGLKSLTELFVKe-------------NHELRIAGGAVRDLLNGV--KPQDIDFATTA-TPTQMKEMFqs--agIRMInn 117 human
1MIY_A         5 FQEALGIIQQLKQh-------------GYDAYFVGGAVRDLLLGR--PIGDVDIATSA-LPEDVMAIF------PKTIdv 62  Geobacillus ste...
YP_001397139   1 MNYIKKFIYDAKDtin---------evEGELYLVGGYIRNKLMNIasQPKDADFVFNGdIHEFISKLQnk---gYKFFpi 68  Clostridium klu...
NP_925870     15 MPQLTSLLDAIPFapa---------dwPGPLALVGGSVRDALLNRtrVPLDLDFVCPGpVAERARVLArrlgagFAVLda 85  Gloeobacter vio...
YP_001317995   1 MNKIIACILETGKv------------sNIDIYLVGGSIRDFLLNR--NIKDLDLIIKEdPGRFAEKIAkel-qgSYFVld 65  Alkaliphilus me...
NP_603150     10 SDVEIGILNKLNE--------------YGKGYIVGGAIRDILLGL--KPKDVDFTTNL-PYETLKKLFse--ynLKEIgk 70  Fusobacterium n...
ZP_01289830   11 HSYPAELATALAGac----------gaQRELYIAGGAVRDWLRGC--RSRDLDFTVPAgGIAFARRLAaq--lqASLVil 76  delta proteobac...
YP_066646     29 SPDIVTALFAVSRq------------lDAEVWVAGGPVRDYFLGR--SAKDLDLVTGAgAIDFCRRLLrql-geGSLVpl 93  Desulfotalea ps...
NP_621809      1 MATIPRLIRKLGRe-------------AYNVYIVGGYIRDRILNK--EAKDYDFVVKG-NAEEIAKLAaek-mgGSFVpf 63  Thermoanaerobac...
YP_001090384   6 LTDHTLIIDELEKsikfhnlnfilgflPKGSYLVGGYIRDIILGRktEKLDVDIVVPLkAIEIGKKIAen--ieSKFIvl 83  Prochlorococcus...
Feature 1            #             #    #                              ####  #                   
1OU5_A       118 rgekHGTITARLH-EENFEITTLRidvttdg------rhaeveFTTDWq-KDAERRDLTINSMFLGFD---------GTL 180 human
1MIY_A        63 g-skHGTVVVVHK-GKAYEVTTFKtdgdyed-----yrrpesvTFVRSleEDLKRRDFTMNAIAMDEY---------GTI 126 Geobacillus ste...
YP_001397139  69 k-esVSIYRCIKD-KNKIDVSLMK-------------------GNSIE--EDLENRDFTINALALRFSd--------NKI 117 Clostridium klu...
NP_925870     86 ---eHEIVRLVLDsGITLDFARRQ-------------------GADLV--SDLARRDYTVNAIAWDVHa--------GEL 133 Gloeobacter vio...
YP_001317995  66 --qdRGIHRVKVKdGITIDLAKFQ-------------------GEDIL--ADLAKRDYTINAMAYPLEsgwp--ideSQL 120 Alkaliphilus me...
NP_603150     71 ---sFGVLRIKIN-DIDYEIAKFRednyeekdglkiipegkkvSFVDDikNDLTRRDFTINAMAYNEV---------EGI 137 Fusobacterium n...
ZP_01289830   77 d-peHDLARVVWR-DLDLDCSGLRe-----------------kATGMA--EDLRRRDFTINAMAVALEvrdkrcrqqPGL 135 delta proteobac...
YP_066646     94 segdEEACRIVYR-HEIVDISSFRa-----------------sASSLE--EDLALRDFTLNAMALPLStlr---gekVDL 150 Desulfotalea ps...
NP_621809     64 m-aeKGTYRIVVG-DEILDFTNLR-------------------GKDIY--EDLAHRDFTINAMAIRLTdhf----efEYI 116 Thermoanaerobac...
YP_001090384  84 d-ekREVVRIFLN-NIDIDIANQV-------------------SSTIE--GDLFSRDFSINSIAFLLDk--------KCL 132 Prochlorococcus...
Feature 1                    
1OU5_A       181 FDYFNGYEDLKN 192 human
1MIY_A       127 IDPFGGREAIRR 138 Geobacillus stearothermophilus
YP_001397139 118 IDPFYGRKAIQS 129 Clostridium kluyveri DSM 555
NP_925870    134 FDPFDGRGDLTR 145 Gloeobacter violaceus PCC 7421
YP_001317995 121 IDPYGGQQDIKE 132 Alkaliphilus metalliredigens QYMF
NP_603150    138 VDLYNGQKDIEN 149 Fusobacterium nucleatum subsp. nucleatum ATCC 25586
ZP_01289830  136 LDPTGGRQDLAA 147 delta proteobacterium MLMS-1
YP_066646    151 IDPFSGRDDLAD 162 Desulfotalea psychrophila LSv54
NP_621809    117 IDPFGGLKDIKN 128 Thermoanaerobacter tengcongensis MB4
YP_001090384 133 LDPLNGLKDLEI 144 Prochlorococcus marinus str. MIT 9301

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