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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//