ID A7F162_SCLS1 Unreviewed; 624 AA.
AC A7F162;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDN95454.1};
GN ORFNames=SS1G_11332 {ECO:0000313|EMBL:EDN95454.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN95454.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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DR EMBL; CH476638; EDN95454.1; -; Genomic_DNA.
DR RefSeq; XP_001587340.1; XM_001587290.1.
DR AlphaFoldDB; A7F162; -.
DR SMR; A7F162; -.
DR STRING; 665079.A7F162; -.
DR GeneID; 5483640; -.
DR KEGG; ssl:SS1G_11332; -.
DR InParanoid; A7F162; -.
DR OMA; PISFYRV; -.
DR OrthoDB; 5490776at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd07407; MPP_YHR202W_N; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 2.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR014485; Pesterase_C1039.
DR InterPro; IPR041823; YHR202W_N.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR PANTHER; PTHR11575:SF43; SER_THR PROTEIN PHOSPHATASE FAMILY (AFU_ORTHOLOGUE AFUA_3G04160); 1.
DR PIRSF; PIRSF017316; Pesterase_C1039; 1.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..624
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002708062"
SQ SEQUENCE 624 AA; 70045 MW; BCA9844EFF87D078 CRC64;
MTKRLLTLTG LLTSLAAGTQ PSAPPAIPAP MRPLQWGQLN FLQTTDTHGW HAGHLQEAQY
SADWGDYISF AEQMKKQADD KGVDLLLVDT GDRIEGNGLY DASDPKGLYT YDIFREQDID
IICTGNHELY KVDAAAREYD QTVPNFKGNY LASNLDYIHP KTGNQIPMAR RYRKFTTKNQ
GIKVVAFGFL FNFNRNANNT VVQEVEKTIK EEWFQQAIRE DADLFVVIGH VTLDGPEYKA
IYKALREQNW DTPIQFFGGH SHIRSFAKYD SKAYGIQSGR YMETIGWMSI EGIKKNAKEN
SPANEVISDA QGFNAKKHAR MSFQRRYIDN NLFGYHFHTG LNDTTFPTEH GKNVSSSIAK
ARKALNLDHN FGCAPKDLWM SRAKYPSKDS LFSWLGDEVM PDIVTHPDRQ DVPTIAITNT
GAMRFDIFKG AFTRDTTFII SPFVSKFLFI KDVPLTAAEN VLTLLNSGGN IFSSSNLDLN
NLAPPEHLSY KTDILAPLIP ISELPPLSHA QSPLLSSSSI YKPNLIPGYT TKDGGGSDGD
DTIHAPITFH RVPNCIESRI NFHSTDPNPV TVDLVFIDFI KPWVLVALRY SGADYTNEDV
SGYRNETLTD LMAGWIKEHW GQDC
//
