ID A0A498C1Q3_9MICO Unreviewed; 1593 AA.
AC A0A498C1Q3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=5'-nucleotidase {ECO:0000313|EMBL:RLK49515.1};
GN ORFNames=C7474_1673 {ECO:0000313|EMBL:RLK49515.1};
OS Microbacterium telephonicum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1714841 {ECO:0000313|EMBL:RLK49515.1, ECO:0000313|Proteomes:UP000273158};
RN [1] {ECO:0000313|EMBL:RLK49515.1, ECO:0000313|Proteomes:UP000273158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2T63 {ECO:0000313|EMBL:RLK49515.1,
RC ECO:0000313|Proteomes:UP000273158};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
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:RLK49515.1}.
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DR EMBL; RCDB01000002; RLK49515.1; -; Genomic_DNA.
DR Proteomes; UP000273158; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR032109; Big_3_5.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR047971; ExeM-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; NF033681; ExeM_NucH_DNase; 1.
DR PANTHER; PTHR42834; ENDONUCLEASE/EXONUCLEASE/PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G09210); 1.
DR PANTHER; PTHR42834:SF1; ENDONUCLEASE_EXONUCLEASE_PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G09210); 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF16640; Big_3_5; 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; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS51841; LTD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000273158};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..45
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 46..1593
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019748015"
FT DOMAIN 41..178
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT REGION 209..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1593 AA; 161514 MW; 1F367B8CF38312D7 CRC64;
MTHSPAALPE SPLLPQRSRR RAIAAVTVAV TALAGVALAP LPASAAVSAD ADLVISEVYG
GGGNNGAAFN QDFIELANVG DAPAVLTDYS VQYASAGGTS WQVTALGDIE LPAGGRLLIG
QAFGSNTTLP AIAADVTGTV AMSGTGGKVA LVQGTAALSG ATGIAELPAV VDLVGWGAAN
AYAGTAPAPA TTNATSVSRD AAAANTADNA ADFTVGAPTP QGLGGGTPTP TPTATATPTP
TPTPTPTTPA VVPIAEIQGT GDTSPLAGQT VTTTGVVTAH YPTGGFNGYV IQTPGTGGAL
DPATHTASDA IFVYAPGLVG DVAPGDTVEV TGVVSEYYGL TQLTVRSGGA TVVADAAAPV
PATVAWPTTD AARESLESML VAPTGPFTVS NTYSTNQYGE VGLAAGSTPL RQPTDVGAPG
SAEAAATAAD NAARAVVLDD GASTNFLSGA NSALTPAYVS QTEPIIVGAG VAFTAPLIVD
YRNNAWKLNP TAALVGDGTG ADAAVFADTR TDAPAAVGGD LSVASFNVLN YFTTLGTDTA
SCVAYTDRFG DGVTVREGCD QRGAWDAADL QRQQDKIVAA ISALDADVVG LMEIENSAAL
GEQPDEATAT LVAALNDAAG TDEWAFVPSS SDLPPASGQD VITNAIIYRA DAATPVGASR
ALGDQSGDDQ AFGNAREPIA QVFEPADGGA PLLFVVNHFK SKGSAGPWPG DADTGDGQGA
SNESRVRQAT ALRDWVDEVR GDVDAVALVG DFNSYTQEDP LRVLYDAGYT NVESALGVDT
QSYSFQGLSG SLDHVLLNDA ALARATGADI WNINSGESLA LEYSRFRYHG TEFYAPDAYR
SSDHDPVVVG LSAEAAPVEL TLLGINDFHG RIDANTVKFA GTVEQQREAA SGPLLFLSAG
DNIGASLFPS SVAQDQPTID VLNALGLQAT AVGNHEFDRG FADLAGRVSD ASDYPQLGAN
VYEKGTTTPA LDEYALLDAG DLTVGVIGAV TEETPTLVSP AGIADLDFGD PVEAVNRVAA
QLSDGDPSNG EADVLVALYH EGAGAGTPDG ATLDEELAAG GAFAAIVNDT TPDVDAIFTG
HTHKEYAWSA PVPGTDRTRP VVQTGSYGAN LGKITLSVDP ASGEVTAHTE ENIARTTTPD
ADLVAAYPRV AEVRQIVADA LAAAAEIGNT AVAEVSGDIT TAFSGGSYQN GVYTGGTRDD
RASESALGNA VGTMLRDSLS ALPNGAQIGV TNPGGLRSDL WDTQAEFGAN AVPGMPDGTI
SYSQANAVLP FNNTLALVTL TGAQFTTMLE QQWQRDAAGN VPSRPYLQLG LSDNVSYTYD
PALPEGSRIT SVTIDGAPLD PDASYRVGTF SFLATGGDNF RIFTEGTDYV DTGLLDYEQW
IDHLADGSPV APDYAKHAVQ VSGVPETVAP GGNVSFSVAG LNLTSRGAPE NTALTVSLGE
QTLGEVAVTG GAASVSVTLP AGTPAGAAVL TLTAAPSGTT VQVPITVEQQ TPKAETSTRL
IALLPVHLNR LLPTTLLASV TQDGGRPNGV VEFRENGEGG TLVGTAEVRR GIATLRLGNL
SRGTHTYTAV FVPDDPTTVA GSVSGAVSVY ALR
//
