ID A5DFA2_PICGU Unreviewed; 753 AA.
AC A5DFA2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=Nudix hydrolase domain-containing protein {ECO:0000259|PROSITE:PS51462};
GN ORFNames=PGUG_01953 {ECO:0000313|EMBL:EDK37855.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK37855.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK37855.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005279}.
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DR EMBL; CH408156; EDK37855.2; -; Genomic_DNA.
DR RefSeq; XP_001486282.1; XM_001486232.1.
DR AlphaFoldDB; A5DFA2; -.
DR STRING; 294746.A5DFA2; -.
DR GeneID; 5127729; -.
DR KEGG; pgu:PGUG_01953; -.
DR VEuPathDB; FungiDB:PGUG_01953; -.
DR eggNOG; KOG2937; Eukaryota.
DR HOGENOM; CLU_014214_0_0_1; -.
DR InParanoid; A5DFA2; -.
DR OMA; PLIWKWG; -.
DR OrthoDB; 1472at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0140933; F:5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd03672; Dcp2p; 1.
DR Gene3D; 1.10.10.1050; Dcp2, box A domain; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR007722; DCP2_BoxA.
DR InterPro; IPR036189; DCP2_BoxA_sf.
DR InterPro; IPR044099; Dcp2_NUDIX.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR23114; M7GPPPN-MRNA HYDROLASE; 1.
DR PANTHER; PTHR23114:SF17; M7GPPPN-MRNA HYDROLASE; 1.
DR Pfam; PF05026; DCP2; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SMART; SM01125; DCP2; 1.
DR SUPFAM; SSF140586; Dcp2 domain-like; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997}.
FT DOMAIN 99..225
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 337..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 83444 MW; 88409252CCC1E0E2 CRC64;
MSLQLSDGLA NQPLDLVLED LLVRFLANVP DEDLSSIERV LFQVEEAQWF YTDFLRQKSP
YLPQLKMKGF AAQLLEKCPL IWKWGNPSDA LGKFGRYKST IPVRGVALFN KDLTKMVLVK
GTESNSWSFP RGKISKDEAD TVCAARECYE ETSYDVKDAI SEDNCIERTI RGKNYKIYLV
KNVPEDFDFQ PIVRGEIAKI QWHDIKTTGK KVKSNPNQYF IVSAIWKPLT RWVNKNRGVS
NEEELLVKAE FRLKEYLGIS PKAQENVDAG RELLNILQGS SKETSNNLQA ASQNQVSSYQ
QFIHSSLPQH LHNSLPFFPY APAPPMPMYY PSFIPPQSLS QPPAPQPQSV PSVDAQPNPS
TLQKPAMSSV APNSKEFLSI LSQPKKSTAP TPEELPKKST LESNRSKAQQ LMSLFKKAEP
AKEPTSEPVK EPTSTEPKES APASIEAAKP EPSPRVSQFD IENSSPNLGV LGVQQASNEL
EESLRSSHPG SGNNSRPSTP AGKLKILKRP TASGDKQNAS SELLSLLKPK QTPKSTEENP
QSPKVQEKIN GNSKASSDLL SLLKKPRSPE QPTVNTPEVV YDSTKSKQEE SNSEEFQDFE
DFEDFDALDQ SFGAPPTNFH QHFDIDSDDE HEEEEQVEPV PVMPPKIQVL KRNQENSDEG
AGKSLLHLLN GKTKDVSPKT DFSSIYGTDS AQGSEEPQFV PPVTSPSQAA SSSFLSILTR
PTESNPQVSS PPAQKNANSP AKNILDILHG RAK
//
