ID A0A1E8EXW7_9CLOT Unreviewed; 459 AA.
AC A0A1E8EXW7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Multifunctional CCA protein {ECO:0000313|EMBL:OFI05519.1};
GN Name=cca_2 {ECO:0000313|EMBL:OFI05519.1};
GN ORFNames=CLOACE_16770 {ECO:0000313|EMBL:OFI05519.1};
OS Clostridium acetireducens DSM 10703.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121290 {ECO:0000313|EMBL:OFI05519.1, ECO:0000313|Proteomes:UP000175744};
RN [1] {ECO:0000313|EMBL:OFI05519.1, ECO:0000313|Proteomes:UP000175744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10703 {ECO:0000313|EMBL:OFI05519.1,
RC ECO:0000313|Proteomes:UP000175744};
RA Poehlein A., Fluechter S., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium acetireducens DSM 10703.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU003953}.
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:OFI05519.1}.
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DR EMBL; LZFO01000025; OFI05519.1; -; Genomic_DNA.
DR RefSeq; WP_070110645.1; NZ_LZFO01000025.1.
DR AlphaFoldDB; A0A1E8EXW7; -.
DR STRING; 1121290.CLAOCE_16770; -.
DR PATRIC; fig|1121290.3.peg.1667; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000175744; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
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; IPR003607; HD/PDEase_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR PANTHER; PTHR47545; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR PANTHER; PTHR47545:SF1; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000175744};
KW RNA repair {ECO:0000256|ARBA:ARBA00022800};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 19..130
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 155..216
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
SQ SEQUENCE 459 AA; 54211 MW; 017F78747ACC9A49 CRC64;
MKQIVEDLIS LLIICRGEAY IVGGYIRDKL LNFKELPKDI DIVYKGDLNV YIDKLKSKGY
NFFQLNKELG IYRIIVKDKI VDITKMKGNC IEEDLAKRDF TINSIAFKLM DNKIIDPFEG
RKDIKTKTLR QVNENVIGED PVRILRGIRF YIKYGLHFTK STEETIFFQV QNISKCAKER
VFSEFMNIIQ CDNSGIAFDL LDKYNVLKNL LPYIDDLKCI GKCKYHIVDA FTHMNISYKY
FKKIFKDRQK FMGFNIEFLN KNLGGFCLKD YTAFATFAHD IGKFKCYKNN NGKVSFYGHN
ISGAKIANNF CNYFKFPKKA VKLITTVIEA HMYPLGIFKN FNSNYKKHFY NFFYKYDRYV
PYILIVSFCD VYATRSLLDP ENELEKYKKF IKNLFKEYYI YRSILDKRIL KGDEIKNVIE
IESNKIGKVI DYINKIAYIN GIKDKDNIIS YIRSNKKYF
//
