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
//