ID B2UM12_AKKM8 Unreviewed; 464 AA.
AC B2UM12;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Polynucleotide adenylyltransferase/metal dependent phosphohydrolase {ECO:0000313|EMBL:ACD05456.1};
DE EC=2.7.7.72 {ECO:0000313|EMBL:ACD05456.1};
GN OrderedLocusNames=Amuc_1636 {ECO:0000313|EMBL:ACD05456.1};
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD05456.1, ECO:0000313|Proteomes:UP000001031};
RN [1] {ECO:0000313|Proteomes:UP000001031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013
RC / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031};
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(2011).
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}.
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DR EMBL; CP001071; ACD05456.1; -; Genomic_DNA.
DR AlphaFoldDB; B2UM12; -.
DR STRING; 349741.Amuc_1636; -.
DR PaxDb; 349741-Amuc_1636; -.
DR KEGG; amu:Amuc_1636; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_6_2_0; -.
DR BioCyc; AMUC349741:G1GBX-1744-MONOMER; -.
DR Proteomes; UP000001031; Chromosome.
DR GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
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; IPR032810; CCA-adding_enz_C.
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; PTHR46173; CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR46173:SF1; CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR Pfam; PF13735; tRNA_NucTran2_2; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ACD05456.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ACD05456.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001031};
KW RNA-binding {ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT DOMAIN 28..151
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 180..237
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 313..443
FT /note="CCA-adding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13735"
SQ SEQUENCE 464 AA; 52747 MW; 4A310841287B13D5 CRC64;
MIRFMEGILL RKAAEDVARV LSGAGHTVYF VGGCVRDRLL GYSVKDIDIA TSARPDEVLR
LFPDAWEVGA AFGVVLVRRE GFSFEVATFR RDGSYRDGRR PEDVCFTDAE EDARRRDFTM
NGLFEDPFSS PPGRVVDYVG GVEDIRARVL RCIGEPDRRF EEDSLRLMRA VRFAVTREVQ
VEKETCSSIF RNAPLLARIS PERIREELDR ILLSPGRKRG VEMLVETGLM KHVIPEIYDM
IGCTQPPQWH PEGDVYTHTL MMLDALGRDG SPVSLKLALG VLLHDIGKPP CRQVDETGRI
RFSGHDKEGS SMARVILRRL KYSNAVVDAV CSMVERHMRF INVRQMRKST LRMFMNAPHF
RDELELHRLD CLSSNGLMDN WQFVRDFMDS YRNAPLVPPP LVTGRDLVNL GLSPGPDFGK
WLSRLQELQL EGTLRTREEA LLQLGQIAPV EQNALAEYLK KLAL
//
