ID A0A1X2IT08_9FUNG Unreviewed; 808 AA.
AC A0A1X2IT08;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 03-MAY-2023, entry version 23.
DE RecName: Full=DIS3-like exonuclease 2 {ECO:0000256|HAMAP-Rule:MF_03045};
DE EC=3.1.13.- {ECO:0000256|HAMAP-Rule:MF_03045};
GN ORFNames=BCR42DRAFT_321271 {ECO:0000313|EMBL:ORZ21103.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ21103.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ21103.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ21103.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5'-exoribonuclease that specifically recognizes RNAs
CC polyuridylated at their 3' end and mediates their degradation.
CC Component of an exosome-independent RNA degradation pathway that
CC mediates degradation of cytoplasmic mRNAs that have been deadenylated
CC and subsequently uridylated at their 3'. {ECO:0000256|HAMAP-
CC Rule:MF_03045}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03045};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03045};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03045}.
CC Cytoplasm, P-body {ECO:0000256|HAMAP-Rule:MF_03045}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. DIS3L2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03045}.
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:ORZ21103.1}.
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DR EMBL; MCGE01000005; ORZ21103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2IT08; -.
DR STRING; 90262.A0A1X2IT08; -.
DR OrthoDB; 945235at2759; -.
DR Proteomes; UP000193560; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IEA:InterPro.
DR GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; IEA:UniProtKB-UniRule.
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 HAMAP; MF_03045; DIS3L2; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR028591; DIS3L2.
DR InterPro; IPR041093; Dis3l2_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
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; 2.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03045};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_03045};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03045};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03045};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_03045};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03045}; Nuclease {ECO:0000256|HAMAP-Rule:MF_03045};
KW Reference proteome {ECO:0000313|Proteomes:UP000193560};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03045}.
FT DOMAIN 269..608
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
FT REGION 68..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
FT SITE 289
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03045"
SQ SEQUENCE 808 AA; 92310 MW; 6778211227A7BEB1 CRC64;
MIEAIENGTL YQGILRINRR TRTDSYVTSD DLEYDIYIQG LRDRNRALEG DMVAVRLLNV
DTIWDRKKYK DSQKNQNQSS EDKNGCNVGI EIETDDEDNV DKNKPKLCGQ VVGILHRMEG
QQYTGTLNID RHVGPSSDSK EKDDDDDTND EPGPITPNNN HIRLLWLRPT DKRAPFIAIP
VSHAPDDFLK DPSKYKNEIF AAKATRWPID SQFPFGKLMS DIGPLGEMAV EAESILANNN
IQDTDFSSKA LNALPKTPWT IPEKEYKTRR DLRSERIFTI DPETAKDLDD ALHITRLENQ
QYEVGVHIAD VSYFLKRNTQ LDVEAKDRGT STYLVDRVIP MLPSLLCEQL CSLNPGVERL
AFSVIWKMDS AGNILDTWFG RTIIKSCAKL AYDDAQSVID KNDLPTTAKV VDHSVASVEQ
DILDLHKLSL CMRKRRYENG ALSMNSIKLS FKLDDDGEPE KVWVYQLKEA NRLIEEFMLR
ANMSVAEKIC EHYPGEAMLR RHEPPIERRL DEFISVAQSL GYYIDGSTSG TLQASFDAIE
SEDVKYVLRI LAIKPMRRAK YFCVGSFDDT SKYLHFALNV PMYTHFTSPI RRYADVIVHR
QLESILQGKD ECGYQKKTVQ SIALQCNRKK DGAKNAQEQS GHLYLSRYLA RISQTDGPII
RDAIVLQVNS DVFDLLVPDY GLESRVYMDA MPLERFHYDT DDNSLVVFWK EDGVMNMDTV
GKIREINKAT NDKIDNAAEK EQNIPESDSA LSNKSPKGHQ GFDHCHLETS NRMQKFKTFT
KFKVLIQVNT ERTPPINNIY PVNPFLKK
//
