ID A0A2M9D0U7_9CELL Unreviewed; 1602 AA.
AC A0A2M9D0U7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=5'-nucleotidase {ECO:0000313|EMBL:PJJ77608.1};
GN ORFNames=CLV28_0833 {ECO:0000313|EMBL:PJJ77608.1};
OS Sediminihabitans luteus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Sediminihabitans.
OX NCBI_TaxID=1138585 {ECO:0000313|EMBL:PJJ77608.1, ECO:0000313|Proteomes:UP000231693};
RN [1] {ECO:0000313|EMBL:PJJ77608.1, ECO:0000313|Proteomes:UP000231693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25478 {ECO:0000313|EMBL:PJJ77608.1,
RC ECO:0000313|Proteomes:UP000231693};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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:PJJ77608.1}.
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DR EMBL; PGFE01000001; PJJ77608.1; -; Genomic_DNA.
DR Proteomes; UP000231693; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd12215; ChiC_BD; 2.
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; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
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; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
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; IPR029052; Metallo-depent_PP-like.
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; PF02839; CBM_5_12; 2.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF00932; LTD; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SMART; SM00495; ChtBD3; 2.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS51841; LTD; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000231693};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1602
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039652222"
FT DOMAIN 12..159
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT REGION 199..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1602 AA; 163884 MW; 0C406B534522591B CRC64;
MASCAALALA VPTAGAALGA TPAPGDPDGA HVVISEAYLV GGSAGQPFTN KFVELYNPTG
SAVDLSSWSV QYKSSSGASF SGITRLSGSI PAGGHYLVQQ GSNGAAGAAL PTPDAVGATS
LGGSSGVVAL VASQTLVANP AKGSHTADPA FVDLLGYGAA DVFEVAPGPA GQGTGTVGAL
ERTAFGNDNS ADFTFSAEVT PENSAGDGTD PDPEPTQTAT PTPTQTTTPG DVVPIAQIQG
SGERSPLVGQ TVTTRGVVTA AYPTGGLNGV TIQTEGTGGD LDLAEHTASD AIFVYSSAAA
AALEIGDHVE VTGKISEYDS KETSTSPANG SLTEISPAAG GWTVLAEPAE AVKPATVTWP
ASDAQRESLE EMLLAPQGDF TVTDNYSTNY YGSIGLAAGS SPLVQPTSVG RPGSAEATAA
AADNAARAIV LDDGATTNFN STKTAPLPYL TKDAPVRVGA AVTFTTPVVL DQRYGTWNLQ
PLAALTPAVA GTVQPATFED TREAQPEDVG GDLTVGTFNV LNYFTTTGDE LTGCTSYKDR
FGNPVTVSGG CDARGAWDAE NLDRQETKIV AAISALGADV VSLEEIENSA AFGKDRDTAL
GDLVDALNAA DGAGTWAFVA SPDALPSSED VIRTAFVYRT ATAEPVGDST ILVDDPAFDN
AREPLAQTFR PAGGTAAQDV VVIANHFKSK GSGSGADADQ GDGQGASNAS RVAQATALTA
FADDVAAAAG TEKVLLVGDF NSYAQEDPMV VLHEAGYTDL GATTGKETYQ FDGMVGSLDH
VLASPAATAA VAGTDVWNIN SVEPIANEYS RYDYNVVNLY DETPFRSSDH DPILVGLDLA
ADTTTTIDLV SINDFHGRIQ PYSNDGTTNP TLGFAGTVEA LKAQNPDGTA FVSAGDNIGA
SLFASSLQQD QPTIDVLNAL GLATSAVGNH EFDQGFSDLT GRVTDAADWS YLGANVYEKG
TTTPALPEFD VIDVDGVQVG FVGVVTQETP TLVTPAGIAD LDFGDPVDAL NRVTDDLLDG
DDANGEADVV VALVHEGAGA GTPDGASIDD EVAAGGAFAE LVEDTDPRVA AFFTGHTHKQ
YAWDAPITGT DRTRPVVQTG SYGEYVGHIS LTVDTASGDV VDHTAENVAA SKAPWSQLVA
SYPVVGEVKT IVDDALAEAA VIGSKPVGSV SADITTAFTG GKYVDGVYQG PGPAASTGRD
DRMSESTLGN LVANSLRETL ADPDRGGADF GVVNPGGLRN ELFYAPDGTV TFAEANAVLP
FVNNLWTVTL TGEQVVEMLE QQWQTNADGT RPSRPYLALG LSDNVSYTVD TADGTAAPGG
HVTSVTIDGE PIDPAGEYRV ATFSFLATGG DNFRVFTQGT DAKDSGLVDR DAWMAYLGDN
PDLAPSFART RAVVPELPGD VEAGGTTSVT VSSLDLTSIG SPANTGVSGY LVARDDAFDA
DAPGQPVGTA PVTSGSATLD VTVPTGTAAG EYDLWVVASP SGTTVRVPLT VTAPVVVDTY
QPGTVYVAGD EVVYQGVVYR ALWWTQGTTP GSTSWGAWVE VGPADGSVPV CGVAWTSSMV
YTGGEVVSHD GHRWSASWWT RNQEPGASPW GPWKDLGACP TA
//
