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Database: UniProt
Entry: A0A0N8HXR7_9MICC
LinkDB: A0A0N8HXR7_9MICC
Original site: A0A0N8HXR7_9MICC 
ID   A0A0N8HXR7_9MICC        Unreviewed;      1494 AA.
AC   A0A0N8HXR7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Multifunctional nuclease/2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'-nucleotidase/3'-nucleotidase {ECO:0000313|EMBL:KPN18233.1};
GN   ORFNames=AO716_10185 {ECO:0000313|EMBL:KPN18233.1};
OS   Arthrobacter sp. Edens01.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1732020 {ECO:0000313|EMBL:KPN18233.1, ECO:0000313|Proteomes:UP000054460};
RN   [1] {ECO:0000313|EMBL:KPN18233.1, ECO:0000313|Proteomes:UP000054460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Edens01 {ECO:0000313|EMBL:KPN18233.1,
RC   ECO:0000313|Proteomes:UP000054460};
RA   Couger M.B.;
RT   "Draft Genome of Arthrobacter sp. strain Edens01.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPN18233.1}.
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DR   EMBL; LKIU01000005; KPN18233.1; -; Genomic_DNA.
DR   RefSeq; WP_055240707.1; NZ_LKIU01000005.1.
DR   STRING; 1732020.AO716_10185; -.
DR   OrthoDB; 1016457at2; -.
DR   Proteomes; UP000054460; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   CDD; cd10283; MnuA_DNase1-like; 1.
DR   CDD; cd04486; YhcR_OBF_like; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR008334; 5'-Nucleotdase_C.
DR   InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR   InterPro; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR047971; ExeM-like.
DR   InterPro; IPR001322; Lamin_tail_dom.
DR   InterPro; IPR036415; Lamin_tail_dom_sf.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   NCBIfam; NF033681; ExeM_NucH_DNase; 1.
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; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF00932; LTD; 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; SSF56219; DNase I-like; 1.
DR   SUPFAM; SSF74853; Lamin A/C globular tail domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS51841; LTD; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054460};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..1494
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006026715"
FT   DOMAIN          25..166
FT                   /note="LTD"
FT                   /evidence="ECO:0000259|PROSITE:PS51841"
FT   REGION          172..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1494 AA;  154188 MW;  485CEDA5D604711B CRC64;
     MRFTRWRAAL GTALSAGLLA GPLAALPAHA EEAAPSGVVI NEAYLSGGSA NAPFTNKFVE
     LYNPTSSAVS LDGWSLQYRA AGSTGAPTGI GRLSGSIPAG GYYLIQGASN GSSGVALPAA
     DATIGASFSG ASGTLVLANQ AAAVNPLPTG SVTTQPGVVD LLGYGSSNTF ETAPATAPAG
     NSDPKSLNRT DFADSNNNAA DFALSTSVTP TNTAGTGTVP DPEPTDPEPT DPEPTDPPAG
     TVAIAEIQGT GDASPLVGAN VTTRGNVTAA YPTGGFSGYY IQTPGTGGEL DPATHTASDG
     IFVFSAATVG QVAVGDYVEV TGTVGEYFGL TQLTVPAGSM TKLSEAAEEV KPATVPWPAT
     DTERETLEGM LLAPQGEFTV TDNYTLNQYA EIGLAAGSET LVQPTAVAPV GTPEHAAVVA
     NNAAKAVKLD DGATTNFLSA ANQSKPLPYL TSTDPVRIGA PVSFTTNVIL DFRNSAWRFQ
     PLTELTPANA ETVQPASFEN TRTAAPQSVG GNLKLAAFNV LNYFSTTGDD LTGCTYYNDR
     SGAPVTVRGG CDARGAANEA NLDRQQAKIV AAINSLGADV VGLMEIENSA ELGQDRDTAL
     AHLTEALNAA APGTWDYVRS PAALPDDEDV IRTAFIYRTA TAEPVGDSVI LNDESVFSNA
     REPLAQAFKP AGGEDSESFV AIANHFKSKG SAPSSGENAD NGQGGWNADR VRQAQAVAEF
     ADTVAQEAGT ERVFLLGDFN SYAAEDPMQV FAEAGYVNLG KATGKHSYAF SGLVGSLDHV
     LASPAAAEDV TGTDIWNINS VESIAFEYSR YNYNATDYYA ADPYRSSDHD PILVGMDLTP
     AEAEVTDLNL LNINDFHGRI DANTVNFAGT VEQLKAAAPE GSSLFLSAGD NIGASLFASS
     VQEDQPTIDV LNALDLRASA VGNHEFDGGF ADLTDRVVPA SQFEYLGANV YLKGTTTPAL
     PEYTILDVDG VQVAVIGAVT EETGTLVSPG GIADLEFGDP VEAVNRVAEQ LVADGLADVI
     IAEYHEGAGS GTPDGASLEE EIAGGGAFAE IVTETSALVD AIYTGHTHKQ YAWDAPVPGV
     DGKTRPVVQT GSYGEFIGQI ELAYNAETDE VLSYTAGNVA RTTTPAADLV AAYPAVAEVS
     RIVDAALAYA AEVGNQPIGS VTADITTAFA GTSRDDRGNE STLGNLVADS LLSSLGSPER
     GGAEIGVVNP GGLRAELYYG EDGVITYAEA NAVLPFVNNL WTTTLTGAQL KSVLEEQWQP
     DGSSRTFLAL GLSDNVTYTY DPDQPRGSRI QSVTVNGEAL DTTRAYRVGT FSFLAQGGDN
     FSTFAQGTDT RDSGLIDRDA WISYLQASSP VSPDFARQGV IVKAAPANVQ AGSSVSFAVD
     KLDLTSLGSP ANTTLAVSWV PAGGTAVALG SVPVTAGAAS VTAAIPASAS GNGTLVLTAD
     PSGTTVSIPV TVDEAPQQPT CIRPVPPKNW WDVRGWLKYA VDYARYLICT ISRG
//
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