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Database: UniProt
Entry: A1UPB3_MYCSK
LinkDB: A1UPB3_MYCSK
Original site: A1UPB3_MYCSK 
ID   A1UPB3_MYCSK            Unreviewed;       489 AA.
AC   A1UPB3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Metal dependent phosphohydrolase {ECO:0000313|EMBL:ABL94671.1};
GN   OrderedLocusNames=Mkms_5486 {ECO:0000313|EMBL:ABL94671.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL94671.1};
RN   [1] {ECO:0000313|EMBL:ABL94671.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL94671.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP000518; ABL94671.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UPB3; -.
DR   STRING; 189918.Mkms_5486; -.
DR   KEGG; mkm:Mkms_5486; -.
DR   HOGENOM; CLU_015961_6_1_11; -.
DR   OrthoDB; 9805698at2; -.
DR   GO; GO:0016787; F:hydrolase activity; 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:InterPro.
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; 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   InterPro; IPR014065; tRNA_adenylyltransferase.
DR   NCBIfam; TIGR00277; HDIG; 1.
DR   NCBIfam; TIGR02692; tRNA_CCA_actino; 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   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
DR   PROSITE; PS51831; HD; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:ABL94671.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          272..391
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   COILED          397..431
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   489 AA;  54322 MW;  1CE1E0DBFDB52D15 CRC64;
     MPHDPDDAED DTALLARAAV ALNRDGEVLR DIGAVFAEAG HTLYLVGGSV RDALLGRLGT
     DLDFTTDARP EQMQAFLRPW ADALWDTGIE FGTVGVGKAG HRMEITTFRA DSYDQVSRNP
     AVRYGDRLED DLVRRDFTVN AMAVAITAAG PGEFHDPLGG LAALRAKVLD TPSAPEVSFG
     DDPLRMLRAA RFASQLGFGV APRVRTAMTE MAPQLSRITV ERVAAELDKL LLGADPVTGI
     DLMVQTGLGD VVLPEVGGMR LAIDEHHQHK DVYWHSLTVL RQAIDLEDGP DLVLRWAALL
     HDIGKPATRR HEPDGGVSFH HHEVVGAKMA RKRMRALKYS KQMVDDVSQL VFLHLRFHGY
     GDAKGPGKWT DSAVRRYVTD AGPLLDRLHK LVRADCTTRN KRRAARLQAN YDDLERRIAE
     LAAKEDLQRV RPDLDGNEIM RLLDIPAGPQ VGEAWRHLKE LRLERGPLSH DEAVDELLKW
     WNAEPRRDV
//
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