ID S8C1I4_DACHA Unreviewed; 611 AA.
AC S8C1I4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=PhoD-like phosphatase metallophosphatase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=H072_4661 {ECO:0000313|EMBL:EPS41442.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS41442.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS41442.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS41442.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EPS41442.1}.
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DR EMBL; AQGS01000240; EPS41442.1; -; Genomic_DNA.
DR RefSeq; XP_011110558.1; XM_011112256.1.
DR AlphaFoldDB; S8C1I4; -.
DR STRING; 1284197.S8C1I4; -.
DR eggNOG; ENOG502QU5W; Eukaryota.
DR HOGENOM; CLU_015982_0_0_1; -.
DR OMA; HWTDGWD; -.
DR OrthoDB; 5487555at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR CDD; cd07389; MPP_PhoD; 1.
DR Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR018946; PhoD-like_MPP.
DR InterPro; IPR038607; PhoD-like_sf.
DR InterPro; IPR032093; PhoD_N.
DR PANTHER; PTHR43606; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR PANTHER; PTHR43606:SF2; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR Pfam; PF09423; PhoD; 1.
DR Pfam; PF16655; PhoD_N; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..611
FT /note="PhoD-like phosphatase metallophosphatase domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004548840"
FT DOMAIN 61..175
FT /note="Phospholipase D N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16655"
FT DOMAIN 188..564
FT /note="PhoD-like phosphatase metallophosphatase"
FT /evidence="ECO:0000259|Pfam:PF09423"
SQ SEQUENCE 611 AA; 69304 MW; 864F50FCB3A145A9 CRC64;
MKLLPIITYL TIPLASAYWS SNLNYLSPSS HHPSLGISIN RVAKRSNSGT SYDPAVLKFT
HGVASGDPTA TSVILWTRLS PITDAADNNG GSIGLEPLYW HGPKLTSTAP ICAEWKVAKD
SGMRNVVSRG KAYTSSDIDF TVKVEAKGLQ PFTRYYYQFN ICNSDVKSPL GRTKTAPEEN
DRVSRVRFAV YSCAFFTFGY FNAYGQSVRK DSVDYVLHLG DYIYEYGNSA RGPQIGRKFK
PDHEIFTLYE YRERYATYRT DEDLLLSHQN YPWISTWDDH EVADNTWRDG YSKLNNTENS
FIIDDPVSFD QRKTNAVRAY FEWMPLRQVD MDDNLRIWRS TSFGKLVDLT VLDTRQYDRS
ITDVNYIHDY ISSIANEVSR SQMGPRQEAW FFNQLSDSHK RGATWRLVGS QTMFSYTNLS
SPFSDIEGGF FSDLALDTWQ GYIASRNRTL HHLYSNNIGN NIFLAGDIHS NWVSDLVWLN
STNPNPDPAT HPDYDPKTGK GSIGVEFVGT AVTSQGSVGW NGTLERGQKL ADWSIKTNPS
VQWVERYYRG YFELDFSHEV LKATYFGMKD ISTRNSEEVE LARFEVFNGE NKVHRPVAGG
KVAAGAIKPQ L
//
