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Database: UniProt
Entry: A0A1F6BLC9_9BACT
LinkDB: A0A1F6BLC9_9BACT
Original site: A0A1F6BLC9_9BACT 
ID   A0A1F6BLC9_9BACT        Unreviewed;       490 AA.
AC   A0A1F6BLC9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=HD domain-containing protein {ECO:0000259|PROSITE:PS51831};
GN   ORFNames=A2110_01555 {ECO:0000313|EMBL:OGG37729.1};
OS   Candidatus Jorgensenbacteria bacterium GWA1_54_12.
OC   Bacteria; Candidatus Jorgensenbacteria.
OX   NCBI_TaxID=1798468 {ECO:0000313|EMBL:OGG37729.1, ECO:0000313|Proteomes:UP000176273};
RN   [1] {ECO:0000313|EMBL:OGG37729.1, ECO:0000313|Proteomes:UP000176273}
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:OGG37729.1}.
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DR   EMBL; MFKH01000004; OGG37729.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6BLC9; -.
DR   STRING; 1798468.A2110_01555; -.
DR   Proteomes; UP000176273; Unassembled WGS sequence.
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   CDD; cd00077; HDc; 1.
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; IPR006675; HDIG_dom.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002646; PolA_pol_head_dom.
DR   InterPro; IPR032828; PolyA_RNA-bd.
DR   NCBIfam; TIGR00277; HDIG; 1.
DR   PANTHER; PTHR46173; CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR46173:SF1; CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 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.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   RNA-binding {ECO:0000256|RuleBase:RU003953};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT   DOMAIN          255..369
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
SQ   SEQUENCE   490 AA;  55506 MW;  8BEE6478E0A714CA CRC64;
     MAYSLPQEVR EIVEGLHREG YGAYPVGGCV RDLVIGRAPK DWDVTTDATP EEVQKIFPES
     VYENEFGTVG VKTGSDDATL TIVEVTTFRK EGRYSDKRHP DEVTFAKTID DDLSRRDFTV
     NALALNVAEE QEVIDPYGGR RDLKNKVIRA VGNPAERFKE DALRLVRAPR LVTELGIAEG
     WHIEDKTYAA IREHASLLRE IAVERVRDEL VRLMLGQDAA QGLRLLEELG LLQYIMPEVR
     EGIGIDQAKH HTFTVWEHGI RSLQYAAERG FSLTVRMSAL LHDVGKPRTK AGEGEAATFY
     NHEIVGARMT RELLTRLAFP KQFVQDVAHL VRYHLFYYNV GEVTEAGVRR FVRRAGVEYI
     DDLLRLREAD RIGSGVPKAF PYKLRHLLYM IEKVRRDPLS VKALAVDGEA VMKTVGLVPG
     PRVGWILNAL MEEVLDAPEK NTEELLTKRM KALAKLSDEE LQEKGEKGKR QMEEFERGVE
     AEIKGKYRVG
//
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