ID A0A1F8KCB8_9CHLR Unreviewed; 822 AA.
AC A0A1F8KCB8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=HD/PDEase domain-containing protein {ECO:0000259|SMART:SM00471};
GN ORFNames=A2X25_12400 {ECO:0000313|EMBL:OGN71947.1};
OS Chloroflexi bacterium GWB2_49_20.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797612 {ECO:0000313|EMBL:OGN71947.1, ECO:0000313|Proteomes:UP000178842};
RN [1] {ECO:0000313|EMBL:OGN71947.1, ECO:0000313|Proteomes:UP000178842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGN71947.1}.
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DR EMBL; MGMF01000026; OGN71947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8KCB8; -.
DR STRING; 1797612.A2X25_12400; -.
DR Proteomes; UP000178842; 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: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; cd00077; HDc; 1.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR043734; DUF5678.
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; PF00561; Abhydrolase_1; 1.
DR Pfam; PF18929; DUF5678; 1.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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 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 320..476
FT /note="HD/PDEase"
FT /evidence="ECO:0000259|SMART:SM00471"
SQ SEQUENCE 822 AA; 91623 MW; 40C66F2F4AD21661 CRC64;
MMEPDNPSEE ELNPYYGRWV ALLRGKVVAQ GGTPEQALRA AQKSRYKEKP EIVYMSGLND
LNFPPLFDTI RNLLADEEGV FLVGGVVRDV FLKRSSHDLD FAVKKNAIQL ARKVADKLKA
EFYPLDIERD TGRVLITGQN GSRQAIDFAA FRGDDLETDL RGRDFTINAM AIDPKNLSLH
DPLGGLSDLR EKCLRACSGS SFKDDPVRIL RAIRLAAAFG FRILPESRQA MKDSADQLAK
VSPERQRDEL FRILEGPRPA ISIKALDMLG ALEPVLPELL SLKGVQQAHP HVQDVWSHTM
SIISHLETIL AALSADYEPE TASDYYHGVL VLKIGRYRKH LSEHLSNISN NNRTWREILF
FSALYHDIAK PGKSVTGVEG HIRFWGHEDD GADIVSMRAH KLALSNDEIN RLSVIVRNHM
RIHFHTKRLT DEKKLPTRRA IYRFFRDVGE AGVDICLLTL ADLWATYENS LPEETWVTCL
DVVRIFLESW WEKKTELIAP PQLISGVDLM QALSLEPGPE VGRLLEAVRE AQVVNEVNDS
LSALNYARDY RDKLHKGEVM EYALVNNIRL AFFQRPGSGM PIVLIHGYPL DHTIWQPIIP
ILEKDAHLIL PDLRGHGSSP TPEGTYSVEN MADDISGLLD FLRVRKAILV GHSLGGYVAL
AFANKYPQKL KGLGLVASKT NADNASQKEA RLKAIADIQV NGIAPVADTM SAKLVVNPNL
MPELHKLIMK MDPAGAIGAL YAMAERDDSS KVVANLKIPI MVVAGVADVL IPIETSRQMT
NLSSTSTYME LEGVGHMPML EAPIKTAEAI NKLINEGNRF KL
//
