ID A0A168RL98_ABSGL Unreviewed; 1129 AA.
AC A0A168RL98;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 26.
DE RecName: Full=Ribonuclease II/R domain-containing protein {ECO:0000259|SMART:SM00955};
GN Name=ABSGL_12729.1 scaffold 13359 {ECO:0000313|EMBL:SAM07095.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM07095.1};
RN [1] {ECO:0000313|EMBL:SAM07095.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM07095.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT554703; SAM07095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168RL98; -.
DR STRING; 4829.A0A168RL98; -.
DR InParanoid; A0A168RL98; -.
DR OMA; YTHFCHP; -.
DR OrthoDB; 945235at2759; -.
DR Proteomes; UP000078561; 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:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 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:UP000078561}.
FT DOMAIN 596..904
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 126896 MW; C04707AC7290E74A CRC64;
MDDQHQTAPE STRGLFDPPE KVFIAPSDKR RSFNGLGDRN SLSLQQQQQQ RRPRSRSSVT
ADNVGHIQAG GLGTRRSYNN NNSNFGLHTL PEEGANDRKR EQLGGSMTVD SLQDMINTLK
TMPSRDDANR RKSVNQQRMS SSSIKQQHTL DIDDNDDDEV YRENARAEAE AKLMGTYQRI
STLDSSNSNL RFLGSTSTRP YSGNGNDTPT AAPSTSTSKR MSLQQLPTLN ENVEDGAKRN
SNRNSRRIQF NKPLNLDEAK KQHRRSASYS SSMYLNEGPI GGNGGDNDWR ASAPPPSIRH
STGNASTPLI SGSSSSSSSL SAPSFNLVPF TPTRVNFSRD DANPHQRRQL FIAHLPFSAL
TPLFRSRQLV RGTLRVNKRN RSDAYVACEE LDDDIYVCGS RDRNRALEGD VVAVRLVDVE
RVLREKKEKE EAKLVRNGGH VRTRQPDEED ENEIIFGGDE DIDVMKPKYC GVVVAILERA
QNQVFSGTLN LRRPNNKRAQ EENQQQENGG QNNSRSAETP RIVWFKAVDK RVPLIAIPIE
QAPTDFVDDN ESYADRLFVS SIKRWPITSL HPFGTLEREL GQIIKLDVQT MAILADNNVT
HTEFSDQANS PLDKEARARG VRVDLIHKSV PMLPTALTQK VTNLVPNQTR FAFSVIWKLD
SDGKVLDTRF GKSIIKSCAS LTYDDVQDVV DGQTLALDGV DQSLASDIET DVHLLYKIAS
QLRTRRFAPG GAMSQQREEL GFTFDHPVDN DHSIPSGVGI SRKPDASVTV KEFLLLANQS
VAQKISRHLP ELALLRRQAK PMERKIMELE QYANRHLGVQ LDASSAYSLE RSIRAIENDK
VRKMVSILVL KTMQAPKYFC TGVLDILKFT HYSLNTPLFT HFTAPSRRFA DIIVHRQLES
ALADDRHFYL DRDTVQKLGQ HCNVKKEAAA IAREQSGLLF LSLYLNERAI VPPNGNTNIK
IIYREAQVIS VFDDYFDVMI PDLNLERRIH LVNLPVWRSE LDVSRRALTM FWKKGVDTST
GKQQQWGMSD DEYEDLDEEC LLADMHDTAE TSIVDNLAIA TTSMVSTRQT SRLSKRQSII
QARLSSSTAY SPEQSSQTIQ ALDRIRVILT IEMVRTPPLI RVLAANPYA
//