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Database: UniProt
Entry: A0A150V4P9_9PEZI
LinkDB: A0A150V4P9_9PEZI
Original site: A0A150V4P9_9PEZI 
ID   A0A150V4P9_9PEZI        Unreviewed;      1348 AA.
AC   A0A150V4P9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-JUN-2023, entry version 23.
DE   RecName: Full=Ribonuclease II/R domain-containing protein {ECO:0000259|SMART:SM00955};
GN   ORFNames=M433DRAFT_250752 {ECO:0000313|EMBL:KYG45526.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG45526.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG45526.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG45526.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
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:KYG45526.1}.
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DR   EMBL; JPDO01000159; KYG45526.1; -; Genomic_DNA.
DR   STRING; 766039.A0A150V4P9; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR   Gene3D; 2.40.50.690; -; 1.
DR   Gene3D; 2.40.50.700; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR041505; Dis3_CSD2.
DR   InterPro; IPR041093; Dis3l2_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001900; RNase_II/R.
DR   PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR   PANTHER; PTHR23355:SF62; WALL BIOGENESIS PROTEIN PHOSPHATASE SSD1, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G11420)-RELATED; 1.
DR   Pfam; PF17877; Dis3l2_C_term; 1.
DR   Pfam; PF17849; OB_Dis3; 1.
DR   Pfam; PF00773; RNB; 1.
DR   SMART; SM00955; RNB; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT   DOMAIN          753..1086
FT                   /note="Ribonuclease II/R"
FT                   /evidence="ECO:0000259|SMART:SM00955"
FT   REGION          113..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1197..1305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..520
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..541
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..642
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1258..1303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1348 AA;  149192 MW;  D64EC52876E28B5C CRC64;
     MDQPGQGPPG PAGRRLHIAH RRSPSEMTPL MMEQLALAQQ IEMLQQQQQQ IAATHQQYVN
     MGMIPQQQQL PNQFQQLQGQ MQNLNISPNP NAFQFAQQQM GQQHLGIPMA GGMAAPGPAH
     RRNQSAMPNM GLGSMGPPPA PSSGASGFSD FGNFGAGQQR ENNAPRGRGG GAVGGGHNRR
     HSLALPEAKK AAELAEAKRK TSGFQFPPPG GTSPSASNRS VSPGQTGETL QTPQSATRGG
     LSPRGHGRSQ SMAVGGRGMA AVTRGGPAGF QFPSPQTNND MGAGQSDLNR RGSQGHGRTG
     SRNFEGNWRQ QQAPAPGEPQ HQNMGNFQVN QHNAGFQPGH RHRGSVQAQS VNSLQGFQYQ
     SQPQLMQLPQ GQVLQQPNLF NQQLNALQLA QLQAYQQAGL PVPNFAQLAG QHNAPSFGNQ
     QQQQQRKTLF TPYLPQATLP ALLADGQLVA GILRVNKKNR SDAYVTTTDL DADIFICGSK
     DRNRALEGDL VAVELLDVDE VWAQKREKEE KKKRKDITDQ RSGNITAVND ATTQPESSSA
     AQDGGIRRRG SLKQRPTQKK NDDVEVEGQS LLLMEEDEIN DEQKPLYAGH IVAVIERVAG
     QMFSGSLGLL RPSSQATKEK QEAERREREG GNPRQHDRQQ ERPKIVWFKP TDKRVPLIAI
     PTEQAPKDFV EKHQDYANKI FVACIKRWPI TSLHPFGTLV EQLGEAGDLK VETDALLRDN
     NFGPDDFSDA VIKNVGYDDW KVANDGEEAL RHRRDFREEK TFTIDPNGSK ELDDAIHFKN
     LGDGLVEIGM HVTDVAHFVK VNSLVDREAK KRGTAVYLMN RTVNMLPPKL SQDVCCLSPG
     EERYAISVVF KVNVATGRII EEDTWMGKSI IKSSGKLSYE EVDAVINGNA SEIDEERKAQ
     ILMLHNITQK FRQARFGGDE AIVPPLRLLY QLDDENVPVE QNIFDSSPAH EMIEELSHKT
     NAAVAEKIYA AMPDRALLRR QANPNPRRLQ TFAERMMNIG IDVDISSSAA LQNSLFRIED
     DDIRKGMETL VIKSMQRAKY FVPSKIPDDW LSHYALNLPL YTHFTNPSRR YADIVVHRQL
     ESVLSGGTIE FNEDVDTLAK TAETCNTKKD SAHAAQEQSV HIESCRMMNR RSEEQGGDLI
     SVGIVICVYE SAFDVLIPEY GFEKRVHCDQ LPLKKAEFDK NKRLLELYWE KGVPSSAFVP
     EDERPQAKGH RPTNSTIARE TAAKHEAARK VMNTGSIDTN DVEALFDDDD DNTSEMTDHH
     NSGVSLNGDR ATQSGPPSPT RNGLAPQRSK SDSKLINSHS GPEAKLTNKE KYLGYFTLRE
     ENGNHIQDVR EMTRVPILLK TDMTKSPP
//
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