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Database: UniProt
Entry: C5FI77_ARTOC
LinkDB: C5FI77_ARTOC
Original site: C5FI77_ARTOC 
ID   C5FI77_ARTOC            Unreviewed;      1412 AA.
AC   C5FI77;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE            EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN   ORFNames=MCYG_01876 {ECO:0000313|EMBL:EEQ29057.1};
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ29057.1, ECO:0000313|Proteomes:UP000002035};
RN   [1] {ECO:0000313|Proteomes:UP000002035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS995702; EEQ29057.1; -; Genomic_DNA.
DR   RefSeq; XP_002848942.1; XM_002848896.1.
DR   STRING; 554155.C5FI77; -.
DR   GeneID; 9228993; -.
DR   VEuPathDB; FungiDB:MCYG_01876; -.
DR   eggNOG; KOG2045; Eukaryota.
DR   HOGENOM; CLU_001581_1_2_1; -.
DR   OMA; VASWPWF; -.
DR   OrthoDB; 167745at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
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:UP000002035};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT   DOMAIN          1..202
FT                   /note="Xrn1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03159"
FT   DOMAIN          258..657
FT                   /note="Xrn1 helical"
FT                   /evidence="ECO:0000259|Pfam:PF17846"
FT   DOMAIN          706..893
FT                   /note="5'-3' exoribonuclease 1 D1"
FT                   /evidence="ECO:0000259|Pfam:PF18332"
FT   DOMAIN          897..1120
FT                   /note="Exoribonuclease Xrn1 D2/D3"
FT                   /evidence="ECO:0000259|Pfam:PF18334"
FT   DOMAIN          1138..1208
FT                   /note="5'-3' exoribonuclease 1 SH3-like"
FT                   /evidence="ECO:0000259|Pfam:PF18129"
FT   REGION          1221..1412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1255..1282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1314..1329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1412 AA;  159242 MW;  19FFE8C5E969EFF5 CRC64;
     MGVPKFFRWL SERYPAISQL IAENRIPEFD CLYLDMNGII HNCTHKDSDS PAFRMTEDKM
     FIAIFNYIEH LFGKIKPKRL FFMAIDGVAP RAKMNQQRAR RFRTALDAEL AKEKAIREGV
     EMPKEDAFDS NCITPGTEFM TKLTKQLRYF INKKVSEDAE WQGVEVVLSG HEVPGEGEHK
     IMEYIRQAKA QPEYDPNMRH CFTISLCSRE SDVWTAEPEE IKELEHQNFY LLHLCIVREY
     LELEFQELKL DGALQFPFDM ERVIDDFILM AFFVGNDFLP NLPNLHINEG ALAWMFKVYK
     EVLPKLGGYV NEHGKINMER LRTLLAALSD VEFRFFEAEY SDARWLKSKT LGGDQTPTLP
     DKPNVLTVTP AQKHIFNRIK KYVTHRPMDE SGHPVPLDLS PSLPAKDRKF VEQLADSLHL
     KWSSVLDNHD ERFLRLQLPV NSDDDDDDDD DDGESQIAIL RVLKKYENAK VQETTAEDAQ
     LTAEKKYEKK FQEWKDKYYK EKFGWGLENT EEMRKLTENY VQGLQWVLFY YYRGVASWPW
     FYRYHYAPMI SDIHLGLGAD VEFKLGQPFF PFQQLMGVLP DRSKKIVPVA YHSLMTTPES
     PIIDFYPRDF ELDMNGKKME WEAVVKIPFI DEERLLKAMA TKEHLLTPDE KARNTFGVTL
     KFTYSPDVEF IYPSSLPGIF PDVSRCHCIE NVFELPTMEG LDPYVGLVEG VKIGAEALAG
     FPSLQTLQQT GQLGFHGVCV FQQESRNESM VVTIVDPEIA GNTTDAKAKL GRRVHVGYPF
     LQEAKVVCVS DELFDYVQVD DEEHVVAIPH TPTQINQWKK KAEKIESYYS KRLGMIIGEV
     ETIVRVEMLK GLMKTADGAT VKEFTEIPGV ETEYAAQLIV DSVISEDLRF IERAAVPIEE
     EFPEGARAFF LGEYNYGAPV HVTGHEDGKL SGLLSAVKGK EPEFGREHVM NAEKLSKYTP
     SFAIARNLHL SPLTLAKITS SFSVNVDGTR VNLGLNLKFE AKKLKVLGYS RRGNSGWEFS
     ERAIGLLQDY MIKFPDFIAG IQRKPQGDLF EPTDFYPADI AKQKIKEIQS WLKSIESKSF
     ERVPLEAEQL DSSIVQAIEK SADELHQTRA APVAQKIRGV PRNALLKPAD AEHRLNNQHF
     QLGDRVIYAQ DSGKVPIASR GTVVGLTRTS RNLLLDVLFD VSFMSGTTLS DRCSPFRGST
     VPSSSVLNLT NRQLVALSRA TAQNKEHARE QQPSKGAKYG APQGSGGMGQ LKDASTPPPL
     TNSYRGAAIG QPSNSKVNGT PNLNWRGRGR GTLPIRNHPA HADTTGQPRP LFNRGRGNFN
     QTNAHTGNGP SGRGRGRGGY VNVESMNTDS GVLNHNPDFK PRPYNTVPPP ASLNQPTGQR
     GSAGRARGRG MARGGRGRAR AGHAGARGTT TA
//
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