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Database: UniProt
Entry: D3I9D4_9BACT
LinkDB: D3I9D4_9BACT
Original site: D3I9D4_9BACT 
ID   D3I9D4_9BACT            Unreviewed;       475 AA.
AC   D3I9D4;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=HD/PDEase domain-containing protein {ECO:0000259|SMART:SM00471};
GN   ORFNames=HMPREF0669_00038 {ECO:0000313|EMBL:EFC71366.1};
OS   Prevotella sp. oral taxon 299 str. F0039.
OG   Plasmid unnamed {ECO:0000313|EMBL:EFC71366.1}.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=575614 {ECO:0000313|EMBL:EFC71366.1, ECO:0000313|Proteomes:UP000015929};
RN   [1] {ECO:0000313|EMBL:EFC71366.1, ECO:0000313|Proteomes:UP000015929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0039 {ECO:0000313|EMBL:EFC71366.1,
RC   ECO:0000313|Proteomes:UP000015929};
RC   PLASMID=unnamed {ECO:0000313|EMBL:EFC71366.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFC71366.1, ECO:0000313|Proteomes:UP000015929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0039 {ECO:0000313|EMBL:EFC71366.1,
RC   ECO:0000313|Proteomes:UP000015929};
RC   PLASMID=Plasmid {ECO:0000313|Proteomes:UP000015929};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA   Blanton J.M., Tanner A.C., Dewhirst F.E., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. Oral Taxon 299 strain F0039.";
RL   Submitted (JUN-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}.
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DR   EMBL; CP003667; EFC71366.1; -; Genomic_DNA.
DR   RefSeq; WP_009227214.1; NC_022111.1.
DR   AlphaFoldDB; D3I9D4; -.
DR   KEGG; pro:HMPREF0669_00038; -.
DR   HOGENOM; CLU_015961_6_1_10; -.
DR   OrthoDB; 9805698at2; -.
DR   Proteomes; UP000015929; Plasmid.
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; 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; 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   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   Plasmid {ECO:0000313|EMBL:EFC71366.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015929};
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          259..366
FT                   /note="HD/PDEase"
FT                   /evidence="ECO:0000259|SMART:SM00471"
SQ   SEQUENCE   475 AA;  54151 MW;  DB7CDDABAF2B2E3C CRC64;
     MRNLSNSDLA KILNQDIFHL ISKAADALSL ECYVVGGYVR DLFLERPSKD IDVVVVGSGI
     AVAEKLKATL GRGAHLSVFR NFGTAQVKYK GIEVEFVGAR RESYQRNSRK PIVEDGTLED
     DQNRRDFTIN ALAVCLNSAR FGELVDPFYG IEDLEDGIIR TPLEPNITFS DDPLRMLRCI
     RFATQLNFFI EDETFDALIE NAERIKIISG ERISDELNKI MLCKTPSKGF IDLYRCGLLQ
     IILPELCALD IVETRNGRAH KNNFYHTLEV LDNIAKHTDN LWLRWGALLH DIGKPKSKRW
     ENIAGWTFHN HNFIGAKMVP QMFRRLKLPL DAKMKYVQSM VDLHMRPIVI ADDVVTDSAV
     RRLINDAGDN IDDLMTLCEA DITTKNSMRK QRFLDNFRIV REKIEDLKER DYKRALQPVI
     DGNEIMEMFN LPQGPAVGTL KQTLKNAVLD NVVPNEREAL MELLTNKAKQ MGLIS
//
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