ID A0A0V1HVQ7_9BILA Unreviewed; 556 AA.
AC A0A0V1HVQ7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=purine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00011886};
DE EC=2.4.2.1 {ECO:0000256|ARBA:ARBA00011886};
DE AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|ARBA:ARBA00031036};
GN Name=RPS5 {ECO:0000313|EMBL:KRZ14582.1};
GN ORFNames=T11_14095 {ECO:0000313|EMBL:KRZ14582.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ14582.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ14582.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ14582.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC phosphate + guanine; Xref=Rhea:RHEA:27738, ChEBI:CHEBI:16235,
CC ChEBI:CHEBI:17172, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyinosine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC phosphate + hypoxanthine; Xref=Rhea:RHEA:27750, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:28997, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023950};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine;
CC Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235, ChEBI:CHEBI:16750,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023970};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate +
CC hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023918};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000256|ARBA:ARBA00005058}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006751}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC {ECO:0000256|ARBA:ARBA00007151, ECO:0000256|RuleBase:RU003619}.
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:KRZ14582.1}.
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DR EMBL; JYDP01000023; KRZ14582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HVQ7; -.
DR STRING; 268475.A0A0V1HVQ7; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd09009; PNP-EcPNPII_like; 1.
DR CDD; cd14867; uS7_Eukaryote; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR Gene3D; 1.10.455.10; Ribosomal protein S7 domain; 1.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR011268; Purine_phosphorylase.
DR InterPro; IPR000235; Ribosomal_uS7.
DR InterPro; IPR020606; Ribosomal_uS7_CS.
DR InterPro; IPR023798; Ribosomal_uS7_dom.
DR InterPro; IPR036823; Ribosomal_uS7_dom_sf.
DR InterPro; IPR005716; Ribosomal_uS7_euk/arc.
DR NCBIfam; TIGR01697; PNPH-PUNA-XAPA; 1.
DR NCBIfam; TIGR01028; uS7_euk_arch; 1.
DR PANTHER; PTHR11205:SF18; 40S RIBOSOMAL PROTEIN S5; 1.
DR PANTHER; PTHR11205; RIBOSOMAL PROTEIN S7; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR SUPFAM; SSF47973; Ribosomal protein S7; 1.
DR PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU003619};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU003619}.
FT DOMAIN 97..347
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT DOMAIN 409..556
FT /note="Small ribosomal subunit protein uS7"
FT /evidence="ECO:0000259|Pfam:PF00177"
SQ SEQUENCE 556 AA; 62233 MW; 1D68615D487F3321 CRC64;
MLREKFLNSR ILYNRVYVIG RQVSDYSMFL FVQIRWACLF QLFLSYIVYL SFEPQQHFIS
LRSRKEMARS FPVAVDYDSL LETSNFIKRK LTVVPELGLI CGTGLGELAD SLSNVITLNY
TDIPGFPVPS VEGHEGQFVC GKLGGKWIFC MRGRCHTYEG YQPIECAMPV RVMFLLGIKK
VILTAAAGAL NSNYKVGDVM LINDHFCLAS LAGISPLMGP NDARFGPRFP DMKGAYSTKL
RSLFRVAGKE SGFSVRLHDG VYGMIGGPAF ATPIENKFIR MAGSDVVGMS IVWESTVAHH
CGMEVLAVAV ITSISEDNAC KTTLHDDVLA IGKQVCRHLV PIFEKFIESF KKMSVFEYQY
NPVSDLPNIK LFGKWPLDSV DINDMSLVDY IAVKEKHAKF LPHSAGRYQV KRFRKAQCPI
VERLVCSLMM HGRNNGKKLM ALRIVRDAFE IINLHTGENP VQVLVNAIIN SGPREDSTRI
GRAGTVRRQA VDVSPLRRVN QAIWLLCTGA REASFRNIKT IAECLSDELI NAAKGSSNSY
AIKKKDELER VAKSNR
//
