ID D9T0R7_MICAI Unreviewed; 580 AA.
AC D9T0R7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=5'-Nucleotidase domain-containing protein {ECO:0000313|EMBL:ADL49437.1};
GN OrderedLocusNames=Micau_5934 {ECO:0000313|EMBL:ADL49437.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL49437.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL49437.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
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DR EMBL; CP002162; ADL49437.1; -; Genomic_DNA.
DR RefSeq; WP_013289034.1; NC_014391.1.
DR AlphaFoldDB; D9T0R7; -.
DR STRING; 644283.Micau_5934; -.
DR KEGG; mau:Micau_5934; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_5_2_11; -.
DR OrthoDB; 1016457at2; -.
DR Proteomes; UP000001908; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000001908};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 27..580
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5039754621"
FT DOMAIN 43..289
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 387..538
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 580 AA; 60148 MW; 8153FA74AE0FD372 CRC64;
MSVTGMRRRA AVGLAALAAT AFTAVAVTPD QAEARPKPVD VQLLAINDFH GNLEPPTGSS
GTIEGQPAGG AEYLASHLKS MRAAAKQQGK GTVTVAAGDL IGASPLLSAA FHDEPTIEEM
NLAGLEFASV GNHEFDEGAA ELLRMQRGGC HPVDGCADGT PFGGAKFKYL SANAFKTSTG
LPLMQPFGIK IVKGVPIGFI GMTLEGTPNI VSQQGVAGLR FTDEADTANK YAKILRLLGV
KSIVVLLHEG GVQNGGGIND CTGFSGPIVD IANRMDPSID VIVSGHTHAA YNCNINGKLV
TSASSFGRLV TQIDLKIDPR TRDVVTASAN NVVVTRDVEK DPASTELINR YKTALGPVAD
RVVGETTAAI TKTQENLYQT GVDVNGKPTY QTGESPLGNL IADAQLAATD TEQNAVAAFM
NPGGVRADLD AGPVTYAEAF TVQPFANNLV TLDLTGAQLY CMLEQQFTVA RVLYASSTVN
YVVDVNGTTA PAGTPCAGTR VVRGSLTING TPVTDTATYR VTVNNFLAGG GDGFSVLTGG
TNAVTGQIDL DAFTAYLTEK SPVSPPALDR IRTTTEVAAG
//
