ID R5APZ3_9CLOT Unreviewed; 494 AA.
AC R5APZ3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Polynucleotide adenylyltransferase/metal dependent phosphohydrolase {ECO:0000313|EMBL:CCX41276.1};
GN ORFNames=BN454_00651 {ECO:0000313|EMBL:CCX41276.1};
OS Clostridium sp. CAG:1024.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262770 {ECO:0000313|EMBL:CCX41276.1, ECO:0000313|Proteomes:UP000017946};
RN [1] {ECO:0000313|EMBL:CCX41276.1, ECO:0000313|Proteomes:UP000017946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1024 {ECO:0000313|Proteomes:UP000017946};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCX41276.1}.
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DR EMBL; CAWJ010000044; CCX41276.1; -; Genomic_DNA.
DR AlphaFoldDB; R5APZ3; -.
DR STRING; 1262770.BN454_00651; -.
DR Proteomes; UP000017946; Unassembled WGS sequence.
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:0016779; F:nucleotidyltransferase activity; 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:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 1.10.246.80; -; 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; IPR006674; HD_domain.
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; PF01966; HD; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CCX41276.1};
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 ECO:0000313|EMBL:CCX41276.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017946};
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 273..439
FT /note="HD/PDEase"
FT /evidence="ECO:0000259|SMART:SM00471"
FT REGION 472..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 53204 MW; 6FD2E13048349AC1 CRC64;
MQITVPIPSA LAPLAAACRA AGGALYLVGG AVRNALLGLP HTDFDITGPL TQQAVQAVCD
QGGIPCVPMS TALGTLHIRL SDGEVYEYTP FRAERYAAGG AHRPESVRFG VSMTEDAKRR
DFTVNALYAD CGTGAISDPL SALPDLETRT LRLAAPDTLR SDALRILRLV RFSAELGFTP
DAAALAAARE NAALLADIAP ERRFSELRKI LLADTKYGNT AEERFSDGVP PLPAGERQNV
LDALLLLETI GAWESLIPAL TAGRGMGQRP DFHRYTILEH AFHAAANAAP DETLRFAALL
HDVGKPAALQ TDGNYYRHDV YGAALAREAL LALRAPNTLI HAVAAIVAGH MFDVQGTATD
ATLRLRFATW GREQTAYMIG IREADFRGCG IETTYIAERW RALFQRMLSE NTPFSMRELA
VTGSDVMAAT GLSEGAAVGA IKNKLFRHAV KRPKDNERAR LLRIAKGLAR DMGAAGRVSS
EKTPQETQHA TRNS
//
