ID A0A328S4Q1_9EURY Unreviewed; 455 AA.
AC A0A328S4Q1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=CCA-adding enzyme {ECO:0000256|HAMAP-Rule:MF_01264};
DE EC=2.7.7.72 {ECO:0000256|HAMAP-Rule:MF_01264};
DE AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01264};
DE AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01264};
DE AltName: Full=tRNA adenylyl-/cytidylyl- transferase {ECO:0000256|HAMAP-Rule:MF_01264};
DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01264};
DE AltName: Full=tRNA-NT {ECO:0000256|HAMAP-Rule:MF_01264};
GN Name=cca {ECO:0000256|HAMAP-Rule:MF_01264};
GN ORFNames=BZ135_04435 {ECO:0000313|EMBL:RAP45997.1};
OS Methanosphaera sp. rholeuAM6.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=1945580 {ECO:0000313|EMBL:RAP45997.1, ECO:0000313|Proteomes:UP000248984};
RN [1] {ECO:0000313|EMBL:RAP45997.1, ECO:0000313|Proteomes:UP000248984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RholeuAM6 {ECO:0000313|EMBL:RAP45997.1};
RA Hoedt E.C., Parks D.H., Rosewarne C.P., Denman S.E., Mcsweeney C.S.,
RA O Cuiv P., Hugenholtz P., Tyson G.W., Morrison M.;
RT "Culture- and metagenomics-based expansion of the genus Methanosphaera
RT reveals their evolutionary depth and metabolic versatility.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
CC terminal CCA sequence in tRNAs without using a nucleic acid template.
CC Adds these three nucleotides in the order of C, C, and A to the tRNA
CC nucleotide-73, using CTP and ATP as substrates and producing inorganic
CC pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA
CC processing and repair. Also involved in tRNA surveillance by mediating
CC tandem CCA addition to generate a CCACCA at the 3' terminus of unstable
CC tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs
CC are marked with CCACCA and rapidly degraded. {ECO:0000256|HAMAP-
CC Rule:MF_01264}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108;
CC Evidence={ECO:0000256|ARBA:ARBA00034429};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + O-(5'-adenylyl)-L-tyrosyl-[protein] = diphosphate + O-
CC [5'-(adenylyl-(5'->3')-adenylyl)]-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:66528, Rhea:RHEA-COMP:13846, Rhea:RHEA-COMP:17046,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83624,
CC ChEBI:CHEBI:167160; Evidence={ECO:0000256|ARBA:ARBA00035071};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3
CC diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA-
CC COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01264};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tRNA with a 3' CCA end + ATP + 2 CTP = a tRNA with a 3'
CC CCACCA end + 3 diphosphate; Xref=Rhea:RHEA:76235, Rhea:RHEA-
CC COMP:10468, Rhea:RHEA-COMP:18655, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:83071,
CC ChEBI:CHEBI:195187; Evidence={ECO:0000256|HAMAP-Rule:MF_01264};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01264};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01264}.
CC -!- MISCELLANEOUS: A single active site specifically recognizes both ATP
CC and CTP and is responsible for their addition. {ECO:0000256|HAMAP-
CC Rule:MF_01264}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. Archaeal CCA-adding enzyme subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01264}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAP45997.1}.
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DR EMBL; MVAA01000072; RAP45997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328S4Q1; -.
DR Proteomes; UP000248984; Unassembled WGS sequence.
DR GO; GO:0070733; F:AMPylase activity; IEA:RHEA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProtKB-UniRule.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR Gene3D; 3.30.70.1550; Archaeal tRNA CCA-adding enzyme catalytic domain; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.1410.30; CCA tRNA nucleotidyltransferase, domain 2; 1.
DR Gene3D; 3.30.70.590; Poly(A) polymerase predicted RNA binding domain; 1.
DR HAMAP; MF_01264; CCA_arch; 1.
DR InterPro; IPR048833; CAA_C.
DR InterPro; IPR008229; CCA-adding_arc.
DR InterPro; IPR042090; CCA_tRNA_nucleotrans_2.
DR InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR015329; tRNA_NucTransf2.
DR NCBIfam; TIGR03671; cca_archaeal; 1.
DR PANTHER; PTHR39643; CCA-ADDING ENZYME; 1.
DR PANTHER; PTHR39643:SF1; CCA-ADDING ENZYME; 1.
DR Pfam; PF21133; CAA_C_arc; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF09249; tRNA_NucTransf2; 1.
DR PIRSF; PIRSF005335; CCA_arch; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF55003; PAP/Archaeal CCA-adding enzyme, C-terminal domain; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01264};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01264};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01264};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01264}; Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01264};
KW Reference proteome {ECO:0000313|Proteomes:UP000248984};
KW RNA repair {ECO:0000256|ARBA:ARBA00022800, ECO:0000256|HAMAP-
KW Rule:MF_01264};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01264};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01264};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01264}.
FT DOMAIN 31..139
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 153..265
FT /note="tRNA nucleotidyltransferase substrate binding"
FT /evidence="ECO:0000259|Pfam:PF09249"
FT DOMAIN 283..422
FT /note="CCA-adding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21133"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 49
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 52
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 63
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 139
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 159
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 168
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
SQ SEQUENCE 455 AA; 53180 MW; 724E5B4A2A77A245 CRC64;
MIYEQILKDI EPSVEDRQKI IDFSDKLMNI INEYANTKNV DIKCRLVGSM AKKTSLIDKA
DIDIFMTFPL SYSEDELKEY GLEFGKKCIE EVNGKQEIRY ASHPYVTGLI DGYEVDFVPC
YDIRDSSQLK SAVDRTILHT DYVQKHLTDE EANQVLLLKK FMTSVNTYGA NFKVSGFSGY
LCELLILKYH TFDNVAEEAA SKWKNGFMID LEDYGTAPKF NAPFIVVDPV DKNRNVAAAL
SMQKLSEFIV ACRNYLENPS EEYFKDKRIN ATKEELLSEF NKRGTECYVL SFKVPDLPDD
VIYPQIKKTM NSFVKVSQMY DFDIIENNYY IDSENYAHII FEYEVDRLSN VKIHHGPMVR
YREDGFKFKN KYPNAYVKNN QWISISERKY KTVTEMIENI IKKENRSILK LGKNVTDEIT
SNSTFESVYN VIDNEREEDY VNLFMHLNPD YRLIR
//
