ID U5RXY1_9CLOT Unreviewed; 388 AA.
AC U5RXY1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=CCA tRNA nucleotidyltransferase {ECO:0000313|EMBL:AGY77422.1};
GN ORFNames=CAETHG_3219 {ECO:0000313|EMBL:AGY77422.1};
OS Clostridium autoethanogenum DSM 10061.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY77422.1, ECO:0000313|Proteomes:UP000017590};
RN [1] {ECO:0000313|EMBL:AGY77422.1, ECO:0000313|Proteomes:UP000017590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY77422.1};
RX PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT "Comparison of single-molecule sequencing and hybrid approaches for
RT finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT systems in industrial relevant Clostridia.";
RL Biotechnol. Biofuels 7:40-40(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000256|ARBA:ARBA00007265,
CC ECO:0000256|RuleBase:RU003953}.
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DR EMBL; CP006763; AGY77422.1; -; Genomic_DNA.
DR RefSeq; WP_013237793.1; NZ_CP012395.1.
DR AlphaFoldDB; U5RXY1; -.
DR KEGG; cah:CAETHG_3219; -.
DR PATRIC; fig|1341692.11.peg.3231; -.
DR HOGENOM; CLU_015961_5_1_9; -.
DR Proteomes; UP000017590; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR PANTHER; PTHR47788:SF1; A-ADDING TRNA NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR47788; POLYA POLYMERASE; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 29..150
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
SQ SEQUENCE 388 AA; 45034 MW; 767335A21EC0D888 CRC64;
MNILKAFTIE QIQIINLIKA ICKSNGIKAY IVGGAVRDAF LGNKVKDIDI CIDKNPNFII
GKLNGIKCFQ YYDKFQTASL LFQNEVNIDL IRCRKEYYAR DGELPIIDPS NIYNDLRRRD
FTANALAYDI VTGSLIDIYG GLEDIKNKSL QKIHLNSYRE DPTRIFRAVK YAVRYGFDLK
DKDEIINCVN EGVFNLISND RIVKEIYHLC EEKMWIKNIL MCGNLKIFNV NREKLEIGNE
NYNNTDKRIL RLFYALEDKK CAHILGENSV LDSKLKVSIK NFTENYQKIA SLILNAMDNY
ELYKILKGIN DYGLILLKWN DKLKYKIYNY VHNMYHYKSS LNGKFISSIG IQNGKAIGEV
LNYMTKIELN SMIKYGKKYL VKNLGEII
//
