ID F0UPP2_AJEC8 Unreviewed; 1451 AA.
AC F0UPP2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN Name=EXO2 {ECO:0000313|EMBL:QSS53166.1};
GN ORFNames=HCEG_06210 {ECO:0000313|EMBL:EGC46995.1}, I7I53_00340
GN {ECO:0000313|EMBL:QSS53166.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|EMBL:EGC46995.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|EMBL:EGC46995.1};
RG The Broad Institute Genome Sequencing Platform;
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QSS53166.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H88 {ECO:0000313|EMBL:QSS53166.1};
RA Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT "Chromosome-level genome assembly of a human fungal pathogen reveals
RT clustering of transcriptionally co-regulated genes.";
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multifunctional protein that exhibits several independent
CC functions at different levels of the cellular processes. 5'-3'
CC exonuclease component of the nonsense-mediated mRNA decay (NMD) which
CC is a highly conserved mRNA degradation pathway, an RNA surveillance
CC system whose role is to identify and rid cells of mRNA with premature
CC termination codons and thus prevents accumulation of potentially
CC harmful truncated proteins. {ECO:0000256|PIRNR:PIRNR006743}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR006743}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family.
CC {ECO:0000256|PIRNR:PIRNR006743}.
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DR EMBL; DS990640; EGC46995.1; -; Genomic_DNA.
DR EMBL; CP069104; QSS53166.1; -; Genomic_DNA.
DR STRING; 544711.F0UPP2; -.
DR VEuPathDB; FungiDB:I7I53_00340; -.
DR HOGENOM; CLU_001581_1_2_1; -.
DR OMA; VASWPWF; -.
DR Proteomes; UP000008142; Unassembled WGS sequence.
DR Proteomes; UP000663419; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR CDD; cd18673; PIN_XRN1-2-like; 1.
DR Gene3D; 1.25.40.1050; -; 1.
DR Gene3D; 2.170.260.40; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.30.30.750; -; 1.
DR Gene3D; 3.40.50.12390; -; 2.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR016494; 5_3_exoribonuclease_1.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR041385; SH3_12.
DR InterPro; IPR040992; XRN1_D1.
DR InterPro; IPR047007; XRN1_D1_sf.
DR InterPro; IPR041106; XRN1_D2_D3.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR004859; Xrn1_N.
DR InterPro; IPR047008; XRN1_SH3_sf.
DR PANTHER; PTHR12341:SF83; 5'-3' EXORIBONUCLEASE 1; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR Pfam; PF18129; SH3_12; 1.
DR Pfam; PF18332; XRN1_D1; 1.
DR Pfam; PF18334; XRN1_D2_D3; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF006743; Exonuclease_Xnr1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006743};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR006743};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006743};
KW Nonsense-mediated mRNA decay {ECO:0000256|PIRNR:PIRNR006743};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR006743};
KW Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT DOMAIN 1..227
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 275..679
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 728..915
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 919..1142
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1160..1230
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 455..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1451 AA; 162914 MW; 08D4CF6B611A3DC1 CRC64;
MGVPKFFRWM SERYPAISQL IAENRIPEFD CLYLDMNGII HNCTHKDSDS PTFRMTEDKM
FIAIFNYIEH LYGKIKPKQL FFMAIDGVAP RAKMNQQRAR RFRTALDAEL AKEKAIKQGI
EMPKEEAFDS NCITPGTEFM AKLTQQLKYF INKKVSEDVE WQGVEIVLSG HEVPGEGEHK
IMEYIRQSKA QPGYQPDIRH CLYGLDADLI MLGLLSHDPH FCLLREEVTF GRQSQKKSKE
LEHQNFYLMH LCMVREYLEL EFQELEEENA LQFPFDLERV IDDFILMAFF VGNDFLPNLP
NLHINEGALA WMFKVYKQVL PKLGGYINEQ GTINLERLGV LLDSLSDVEF RFFEAEFSDA
RWIKSKMKGE ELESSEPPAN AKDFAISPAQ KHIFSRIKKY VTHRPVNDQG QFVPLDLSPN
LPARDRKFVE QLADDLHLAW TTVSNEHGDR FLRVQLPSKE TQTSGSAGDD DGDDEEGQIA
LLRVMKRYEN AKVKETTAEE AQQAAEKKYE LKFQEWKDNY YKSKFGWGMD NHEEMRQLTE
NYVQGLQWVL YYYYRGVASW PWFYQYHYSP MISDVKLGLE ADMNFDLGQP FHPFEQLMGV
LPDRSKQIVP SAYHELMTSP ESPIIDFYPR DFELDMNGKK MEWEAVVKIP FIDEKRLLSA
MATKKHLLTP EENARNEFGV TLKFTYSPDI EYIYPSSLAG VFPDIAKCHC IENVFDLPTM
EGLEPFVGLV EGVKLGHEAL AGFPSLKTLP HNGQLGFHGV SVFQQESRNE SMVVTLSEPE
NRSSVELAKQ KLGQKVHVGY PFLQEAKVTR VSDELFDYMH VDGEQHVVSI PHTPSQTDQW
RRKAHQVESY YSKRLGMVVG EIESMVHVQM LKGLMKTAEG ASVKEFADIP GIETDYALQL
VVDRVMCEDD RFIEREALPV EEEFPEGTRA FFLGEYNYGA PVHITGHEAG KLSGLVSVTK
GREPEFGRDL TRAAEKLSPY SPSFAIARSL NLNPLALAKI TSSFTVVLDG QRINLGLNLK
FEAKKLKVLG YSRRGPTGWE FSEKAIDLLQ QYMIKFPEFI AGIQRKPQGD GFQATDFYPA
ETAAAKIKEI QAWLKSIEAK NFDRVPLEAE QLDSNLVKSI EQAADELLRT RPAAEAKKLK
GVPRNALLKP ADAEHRLGNQ SFSLGDRVVY AQESGKVPIA TRGTIVGLTR TSRTLLLDIV
FDVSFMSGTT LGDRCSPFRG STVPASCVLN VTNRQLIATT RAAAEQGRSQ QQQQNQPLTV
QGYGAPLGPG GKGQLKHASA PPPLRGSFRG ALTGQLGAPR GNGVFRGRGG HSQSEQTLPI
RNHHQNNASS PQPSDMRGRG GRANFTGHQN GYNPRGRGGR RGGGGGDMGA PPATPGGYVS
VERTDPLEGV IQHNPNFRPQ SYNNVPPPST LERGGSGRGR GGRGFARGGG RGGRGGRGGR
GVNNSQGATS T
//
