ID A0A0F0KRS8_9MICO Unreviewed; 1546 AA.
AC A0A0F0KRS8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Endonuclease YhcR {ECO:0000313|EMBL:KJL23622.1};
DE EC=3.1.31.- {ECO:0000313|EMBL:KJL23622.1};
GN Name=yhcR {ECO:0000313|EMBL:KJL23622.1};
GN ORFNames=RN50_00960 {ECO:0000313|EMBL:KJL23622.1};
OS Microbacterium foliorum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=104336 {ECO:0000313|EMBL:KJL23622.1, ECO:0000313|Proteomes:UP000033572};
RN [1] {ECO:0000313|EMBL:KJL23622.1, ECO:0000313|Proteomes:UP000033572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12966 {ECO:0000313|EMBL:KJL23622.1,
RC ECO:0000313|Proteomes:UP000033572};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL23622.1}.
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DR EMBL; JYIU01000035; KJL23622.1; -; Genomic_DNA.
DR RefSeq; WP_045253378.1; NZ_JYIU01000035.1.
DR KEGG; mfol:DXT68_04465; -.
DR PATRIC; fig|104336.4.peg.984; -.
DR Proteomes; UP000033572; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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; 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; 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 Endonuclease {ECO:0000313|EMBL:KJL23622.1};
KW Hydrolase {ECO:0000313|EMBL:KJL23622.1};
KW Nuclease {ECO:0000313|EMBL:KJL23622.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033572}.
FT DOMAIN 42..180
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT REGION 184..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1546 AA; 159140 MW; E70A1B166A9694DE CRC64;
MMSAPDAVNH EVPGSDRRSR GRLGVLAATC VAALGASALI AAPASADVAG TGVVINEAYL
SGGSAGAAFT NKFVELYNPT AAPVTLDGLS LQYRSATGTG ASNGVAPLTG VIPAGGHYLV
QAGSNGANGA ALPAADAVST LNPSGTNGTL ALVEGTAAVT LTPGSITGVD GVIDVLGYGT
SNTFEKTAAT PPTGNTDVKS LNRTEGKDTD DNRADFALSA TITPQNSGGT DPGTDPGTDP
GTDPAAVSIA EVQGTTDVSP LNGQTVTVQG IVTADHRTGG YKGIVIQTQG SGGATDATPG
ASDGVFVFLN ALAPTLEIGD LVSVTGGVSE YFGQTQINPT ALSGISVVQA AVGVPEVTPL
PDTVVGADRE QFENMLVAPE GTYRVASSHQ LYNFGALWLN AGADLNVKST ELARPGDEAA
AIAAANRANR ILLDDGWSIQ VTNNGHPNDQ PYFTKDLVVR NGDTVDFSDR GYVLQYGFDD
WRLQPVVPID STSPADLKAG FTATNPRSDS APSVGGDVQV ASFNVFNYFT TLKSTNSNAR
GAANAAQFEI QKSKIVAAIN GLDAEIVSLM EIENSIKLGG SLDEALADLV DGLNDALGDD
VWDYVRTPAE LNDAATTDFI TSAIIYKKGA VDTVGDSLTV RDESVWGNAR EPIAQAFDID
GRIVTVVANH FKSKSAPEGG GAEPADGQGF FNADRVKQAN SLKAFTDEIE QTTGSADILL
IGDFNAYAKE DPIDVFTSAG WSDVAREKAP DQHTYSFDGE LGSLDHVLAS PSLSASITGA
GVWSINSPEW SDRGYAFGAT EAGTPFRSSD HDPIIVGVSS AVPPVSIDVV TINDFHGRIE
ADGAAAGAAV VAGAVKQFRE ANPNTIFAGA GDLIGASTFT SFINDDNPTI DALNAAGLDV
SAAGNHEFDQ GWEDLRDRVQ DRADWEYISS NVFLTETGEP ALAPAWVKEL DGVRVGFVGA
VTEDLDSLVS PEGIAGLEVR SIADSVNAVA DDLRDGDDSN GEADVVILLV HEGAESTELS
AITPTSPLGE IVYGVDDDVD AIVSAHTHLA YNHVIDGRPV VSAGQYGENL GLMNLQVDPK
TKELLSITNE IKPLTSAGQP LYPAVPEVAD IVAKAKAEAD VLGAVKVGDI TADFNRARQS
NGSENRGGES TIGNFVADVQ KWSTGADIAL MNPGGIRANL TYASSNANDP AGNVTYREAA
TVQPFANTLV TLALTGAQLK GVLEEQWQPA GSARPFLKLG VSEGLVYTYD PAAAQGSRIT
SITLDGTAID PTANYTVAAN SFLAAGGDNF GTFKSGAGKR DTGKIDLQSM VDWFDANKTA
TPDLAQRAVG VSVSAPDADG YRAGDQVTVA LSSLAFSAGE QAPGEVTLSL GEAQLASGAV
DPTIVDTTDE AGRASLTFAV PSGIYGAQQL TVSVAGTGTT VQVPFTIAGE EEPEQFAGTI
ELGSSKVAAG KKLQINGEGY VAGETVTIEL QPKKGKPVEV GTVQVGVDGT FSTSVTVPKS
APSGKYTVSV AQADGDAATA TVTVNRPGGI IGAILDWLWD LLTRWF
//
