ID S8B9A8_DACHA Unreviewed; 1521 AA.
AC S8B9A8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Nucleoside phosphorylase domain-containing protein {ECO:0000259|Pfam:PF01048};
GN ORFNames=H072_10925 {ECO:0000313|EMBL:EPS35673.1};
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:EPS35673.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS35673.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS35673.1,
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:EPS35673.1}.
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DR EMBL; AQGS01001087; EPS35673.1; -; Genomic_DNA.
DR RefSeq; XP_011116319.1; XM_011118017.1.
DR STRING; 1284197.S8B9A8; -.
DR eggNOG; KOG4177; Eukaryota.
DR HOGENOM; CLU_000288_34_2_1; -.
DR OrthoDB; 2723492at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24189; MYOTROPHIN; 1.
DR PANTHER; PTHR24189:SF50; MYOTROPHIN-RELATED; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SMART; SM00248; ANK; 17.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 7.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 14..281
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT REPEAT 948..980
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 981..1013
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1129..1161
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1198..1230
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1272..1304
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1339..1373
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1374..1406
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1450..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1479
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1521 AA; 168198 MW; 1F35F0797318F2BA CRC64;
MALEPDSHNA YTVGWICAQP KELTAATAIL DHTYKALPSP ANDNNTYTLG AIGEHNVVIT
CLPKGKAGTN QAAAVAAQMA AAFPSIKVGL LVGVGSGIPP NVRLGDVVVG TPVGEYPGVV
QWDMGKAEKE GKFKRTGSLN SPPNVLLTAL TKLESRQEMC GTKIPEYLDE LKAKWPRLGK
KYSWTGALKD PIAEEDEEED GDREPGEPHI HYGLIASGNQ VIQDADMRDK LNGSLGGDVL
CLETEAAGLM DFPSIAIRGI CDYADARKCK DWQEYSAAVA AGFAKELLEE VQPGHLDKEK
PLKDLLNKIH DDVAVVRAKL DRKEDLEILD WITTLEYDAI NNDFFKRRQP GTGQWLLESQ
KYQTFSGSTP GQVLFCPGMP GSGKTILSST VIHDLKTRFS DGSVGIAYMY CNFKRKEDQD
LDSVLRSLLR QLLQGRSSLP QPLMELFKEC KRKKRRASFD EIVTTFHLVT AIYTKVFIVI
DALDEWTESV ETRGRFLTEI FKLHNKCDMN IFATSRFIPE VTDRFKCYPK LEIQAHEDDI
RSYLDGKIVK SEESLLLKYN EEIKKSIVEI ARGMFLLAQL HFEAIKTKTT LKKLRAGLKA
LPSGEAAYDC AYQDAMARIE VLDADHRCLA KQVLSWIVYS RRPLTTLELQ HAIAVEIGET
DLDNENFTEV SRMVSVCTGL VTVDEESNII RLVHYTTQEY FERTRKKWFP TTEADITRIC
ITYLSYSKFA NGPLFDEEAF ETRLQENSLY KYAALNWGSH ARYSMLGATP LVLSILEGDD
LKFKAWIQVV TSVRPSKSHR KAWKEPEDWH YPEMAQGLHF AAAFGLVECI EVMLPKCTTI
EIDDGFGRTP MSWATLCRQE DAMKLLFKHG AKLTSIIGEM PLLCWAANSG HLSIVKLLLE
LGARPDECDL CGQLARAASN GHEEVVGLLL TNGANVDGIK INGGFPRTQG TPLWEAAKNH
HIGVVRILLD LGADPNQVGI RRTAPLYEAV GNGATDISRL LIDKGAITED RDHHGKVKTV
MGVEEWHPRT LLKTSFKGRY EALVNIFLEE LGPSKIQGEK GYYALLDAAK SGMYHKVTEL
VKQCAGTKFR DDCNDVALAE AARTGLNNEI QIIEFLLGEG ASIEGRDKDG RTALIKAACY
GDLELIKFLL EHGADLENKD RWGQTALATI ASVGDEEFLE IAVFLVRSGS NIETRNAEGQ
TPLAIAAKQS LGLMHLLLLK LGADPGTKDD LMRTPLMHSV KAFSNYVSVY DYCTLIDLIA
KDCPDIDARD VEGNTALSLA AALPYHPVVE IMKEYGADVE CRNNHGRTPL ILAITPRGAP
VVEFLLEWSK STLEVKDDRG YTPLLAAASL GSSLWKVTKV LLSYGADVDA TDKTGRTPLS
FAASVGCRKT AKMLIEAGAK LDAKDDIGRT PFQVALDGGQ AVVAQLLFDA SAGIRTATAE
ELRKLEDIKA AQNETTDAES EVDGDGDGDG DDDDDDWPMG IWEQSQWVLS RPVRWRTAWE
DQYGHKEHEP GTTDRGACNC Q
//
