ID M1WGC5_CLAP2 Unreviewed; 669 AA.
AC M1WGC5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase {ECO:0000256|ARBA:ARBA00012633};
DE EC=3.1.3.7 {ECO:0000256|ARBA:ARBA00012633};
GN ORFNames=CPUR_08360 {ECO:0000313|EMBL:CCE34428.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE34428.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE34428.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE34428.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001625};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 family.
CC {ECO:0000256|RuleBase:RU003869}.
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:CCE34428.1}.
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DR EMBL; CAGA01000088; CCE34428.1; -; Genomic_DNA.
DR AlphaFoldDB; M1WGC5; -.
DR STRING; 1111077.M1WGC5; -.
DR VEuPathDB; FungiDB:CPUR_08360; -.
DR eggNOG; KOG1528; Eukaryota.
DR eggNOG; KOG3254; Eukaryota.
DR HOGENOM; CLU_410487_0_0_1; -.
DR OrthoDB; 5486961at2759; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd01517; PAP_phosphatase; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR Gene3D; 3.90.930.12; Ribosomal protein L6, alpha-beta domain; 2.
DR InterPro; IPR006239; Bisphos_HAL2.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR InterPro; IPR036789; Ribosomal_uL6-like_a/b-dom_sf.
DR InterPro; IPR020040; Ribosomal_uL6_a/b-dom.
DR InterPro; IPR019906; Ribosomal_uL6_bac-type.
DR NCBIfam; TIGR01330; bisphos_HAL2; 1.
DR PANTHER; PTHR43200:SF6; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE; 1.
DR PANTHER; PTHR43200; PHOSPHATASE; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR Pfam; PF00347; Ribosomal_L6; 1.
DR PRINTS; PR00059; RIBOSOMALL6.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR SUPFAM; SSF56053; Ribosomal protein L6; 2.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016801};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU003869};
KW Ribosomal protein {ECO:0000256|RuleBase:RU003869}.
FT DOMAIN 85..149
FT /note="Large ribosomal subunit protein uL6 alpha-beta"
FT /evidence="ECO:0000259|Pfam:PF00347"
SQ SEQUENCE 669 AA; 71653 MW; DAB8651F0941CAAC CRC64;
MASKLVPSRS GPVGHALRPS LGSPLPGFLL PAWQRQMLPP RQFSTTTQRS SKLGRTPIAI
PPGVELSISE LKTIRVKTSY KPVLKKTITL KGPLGQLLLD VPEYMSLEKN TENNTLLLHV
ESPEDRAQKM MWGTSWSYLN NCVTGVSEGH NAIVRLVGVG YRATVEARPL KEKYPGQMFL
CLKLGFSHPI EEGIPKGVTV SAPSPTRILM EGMDRVELMS FADIHSETAS DVVASSTTSH
PVLDSSSLAL ALLTPYPLIA RLCRLGQLYR QLLIPHSPSP SLHTSARAAP ASKMVTSPSY
TRELRVAQLA VQRATILTQR VFHEKAKGAL DKDDKSPVTV GDFGAQALII AALRHNFPQD
AIIAEEEAAP LRADAHLRET VFDLVKNTKL DTTAVASAEG DDTDGEAFLG GSIPDVDSML
DLIDRGSSLG GAKGRVWTID PIDGTKGFLR GGQYAVCLGL LVDGEVRVGV LGCPNLPVDD
AARLTAETGS KQTSEEDGKA NSEPRGVLFS AVQHKGADSR PLTTGALSSQ AKPMSMRVID
SLASATFCES VEAGHSAHGD QAAIAQKLGI TQPSVRMDSQ AKYGSIARGA GDIYLRLPVK
ATYQEKIWDH AAGDLIVRES GGQVTDIHGK RLDFSVGRTL AKNKGVVAAP LGVHERVLKA
VQEVLKIGE
//
