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Database: UniProt
Entry: A0A066XZI9_COLSU
LinkDB: A0A066XZI9_COLSU
Original site: A0A066XZI9_COLSU 
ID   A0A066XZI9_COLSU        Unreviewed;      1346 AA.
AC   A0A066XZI9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Nucleoside phosphorylase domain-containing protein {ECO:0000259|Pfam:PF01048};
GN   ORFNames=CSUB01_11138 {ECO:0000313|EMBL:KDN71400.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN71400.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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:KDN71400.1}.
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DR   EMBL; JMSE01000187; KDN71400.1; -; Genomic_DNA.
DR   STRING; 1173701.A0A066XZI9; -.
DR   eggNOG; KOG4177; Eukaryota.
DR   HOGENOM; CLU_000288_34_2_1; -.
DR   OMA; DQEGHAD; -.
DR   OrthoDB; 1837258at2759; -.
DR   Proteomes; UP000027238; 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; 4.
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; PTHR46082:SF11; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR46082; ATP/GTP-BINDING PROTEIN-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 3.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 10.
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; 3.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027238}.
FT   DOMAIN          71..357
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   REPEAT          1140..1172
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1174..1203
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1204..1236
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1237..1281
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1282..1314
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          28..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1070..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1346 AA;  150211 MW;  CC9AF924C00B4F9C CRC64;
     MSGYGHHDDQ AGLNPHFGGA RRHFEKKRTM SALSDKDEST HALPKRPRLA DEPLDQPGYT
     VIKLSHEDYT VGWVCALPLE MAAASAMLDE THEPLAMNPN DSNVYTFGRI GSHNVVIACL
     PSGQYGTNSA AVVANNMRWS FPSICIGLMV GIGGGVPGKV DIRLGDVVVS NPTGGSPGVV
     QYDFGKAVHE GRFEHTGTLN KPPQSVLTAV SKLRASHEAQ PNRIPAILAD IERNPNMSTY
     LYKSMDEDRL FQASYEHTGG ETCDDCGMSQ IVKRDPRQAA ATPKIHYGII ASGNQVMKHA
     QTRDRLAKDL GIICFEMEAA GLMDNFPCLV VRGICDYSDS HKAKRWQRYA AATAAAYAKE
     LLDLITPYRD VILTAKTAMP DSVELLPIPD HRKMLLDSLK FSQIDKRQAN IKAAHAKTCE
     WLTKHPYYIA WMDRQKYSQH HGFLWIRGKP GAGKSTLMKF AFFRAKRAKR KHGTLISFFF
     NARGETLEKT TLGMYRSLLY QLLENMPDLQ QTLLDDLDLE PMGQPVSEGS GLALDQLKDL
     FRNAVRRLGQ RQLTCFIDAL DECDDNEVSD MVKCFEDLGQ YAVQNDIHFY VCFSSRHYPY
     IDIFYGQKLI LEDRGGHEKD LQDYVRSELR AGSGPKSEQV IAEILRKASG VFMWVVLVVD
     ILNKEYGRGR LFAVEKRLKD IPSELSKLFQ NILTRDQEGM EDLLLCIQLL LYSQRPLKRE
     EYYFAIASGL EPDTLGEWDP EDITHKFMDR LIVSSSKGLA ETTRSDDRTV QFIHESVRDF
     LLKDNGLRTL WPDLGDNFEG RSHDRLKDCC HTYSTQANIL AYLPEDKFLL KTSKEEAQGP
     RENIAKRFPF LEYATNQVLH HAEAAAVHAI SQAKFLEDLP VGSWIQMNNL FEKVMVRRHK
     PSSTSLLYIA AAKGLTRLVK MMLGCNVDVD TVGGRYNYPL LAAMSEGHED TVDLLLDCIA
     KKLRKNEAGA NSDVEYSRGG YTISLSLDCK HKGAPTALYI AAESKGIDIA KRLFELGASP
     GFMGSASNSP LVRAVEKNNE AFVRLFLHER SKSRSSPSPV ENRLTFASAN EEHDGEKRLP
     GLDEHTVPSP GDDSKASTPV QETWDLHASL ALIAAIKTGN EEVAKLLLDS QPDVRWADRY
     GRTALHVACE HSKEAVVRLL LNAGADPNQK DITYGRTPLH RASNAAIAKM LLENGADFNA
     ANKAGWTPLH DACRWGRLEI AELLVEARAN LDTHDNEGAT PLHHARSRDK LGPLFYAVEW
     NNERCWDVLL SHGADPDASD NEGWTPLSLN IAANRLNALK LLLENGADPT KSGPHGEALL
     DMAIRLGRNE MLQPLEEAIK KRRITQ
//
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