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Database: UniProt
Entry: A0A0S7XF22_9BACT
LinkDB: A0A0S7XF22_9BACT
Original site: A0A0S7XF22_9BACT 
ID   A0A0S7XF22_9BACT        Unreviewed;       436 AA.
AC   A0A0S7XF22;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Pyrimidine nucleoside phosphorylase C-terminal domain-containing protein {ECO:0000259|SMART:SM00941};
GN   ORFNames=AMJ46_03880 {ECO:0000313|EMBL:KPJ61101.1};
OS   Latescibacteria bacterium DG_63.
OC   Bacteria; Candidatus Latescibacteria.
OX   NCBI_TaxID=1703781 {ECO:0000313|EMBL:KPJ61101.1, ECO:0000313|Proteomes:UP000051457};
RN   [1] {ECO:0000313|EMBL:KPJ61101.1, ECO:0000313|Proteomes:UP000051457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG_63 {ECO:0000313|EMBL:KPJ61101.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000256|ARBA:ARBA00006915}.
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:KPJ61101.1}.
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DR   EMBL; LJNC01000005; KPJ61101.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7XF22; -.
DR   PATRIC; fig|1703781.3.peg.2747; -.
DR   Proteomes; UP000051457; Unassembled WGS sequence.
DR   GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR   GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 1.
DR   InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR   InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR   InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR   InterPro; IPR035902; Nuc_phospho_transferase.
DR   InterPro; IPR036566; PYNP-like_C_sf.
DR   InterPro; IPR013102; PYNP_C.
DR   InterPro; IPR018090; Pyrmidine_PPas_bac/euk.
DR   InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR   NCBIfam; TIGR02644; Y_phosphoryl; 1.
DR   PANTHER; PTHR10515; THYMIDINE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR10515:SF0; THYMIDINE PHOSPHORYLASE; 1.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   Pfam; PF07831; PYNP_C; 1.
DR   PIRSF; PIRSF000478; TP_PyNP; 1.
DR   SMART; SM00941; PYNP_C; 1.
DR   SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1.
DR   SUPFAM; SSF54680; Pyrimidine nucleoside phosphorylase C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          345..417
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   436 AA;  46255 MW;  6B381F3A1ABF3909 CRC64;
     MNAYRIITKK RDGGSLSSEE LEFFIRGFAE GFVADYQMSA FLMAVFLNGM TTEETVALTE
     VMMGTGKVLD LSAIAGKKVD KHSTGGVGDK VSLVLAPLVA AAGVRVPMVS GRTLGHTGGT
     LDKLESIPGF RTLLSSDEFV RNVEQVGFAI AAQSSEFVPA DGGMYALRGV TGTVESTPLI
     VSSILSKKFA AGIDSIVFDV KCGAGAFMSD FSEAQGLAQE LVHVSSVMGK TGRAIITDMS
     QPLGFTVGNV LEVKESIECL RGRGPDDVRE ITLELGTEML SLAGVDSDAV KARRRLERLL
     DGGRALEAFA KFVGAQGGDR RVIDDFTLLP NASSVETVVA EGEGFVSSID ARALGELCVE
     MGGGRRRRDE EVDKSVGFSL FVKVGDEVSK GDPLCEVHLN RGASSILGRV ADAFRISETP
     CERRKLILGR LPEVPG
//
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