ID A8P3K5_COPC7 Unreviewed; 1468 AA.
AC A8P3K5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN ORFNames=CC1G_11892 {ECO:0000313|EMBL:EAU83256.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU83256.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU83256.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
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:EAU83256.2}.
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DR EMBL; AACS02000004; EAU83256.2; -; Genomic_DNA.
DR RefSeq; XP_001838563.2; XM_001838511.2.
DR STRING; 240176.A8P3K5; -.
DR GeneID; 6015155; -.
DR KEGG; cci:CC1G_11892; -.
DR VEuPathDB; FungiDB:CC1G_11892; -.
DR eggNOG; KOG2045; Eukaryota.
DR HOGENOM; CLU_001581_1_2_1; -.
DR InParanoid; A8P3K5; -.
DR OMA; VASWPWF; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000001861; 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:SF41; 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:UP000001861};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT DOMAIN 44..254
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 300..714
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 762..953
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 957..1181
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1201..1267
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 1275..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1304
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1468 AA; 165658 MW; A33F5B506F2D52FC CRC64;
MRSDLVRDAH IEHILHWRRD RGPDDALDAL VIVRTVEEMV ERRERYPLTS QLIQENKIPE
FDFNGIIHNC SHPNDEDAHF RLSEEQIFTS IFAYVDHLFE KIKPKKLFFM AVDGVAPRAK
MNQQRSRRFR TAKEAKEVRE KAERRGEKLP EEKAFDSNCI TPGTPFMARL SAQLRYFINK
KITEDSNWRS VEVVLSGHEV PGEGEHKIME YIRLSRAQPD YNPNVRHCLY GLDADLIMLG
LLSHDPHFCL LREEVKFGPQ RKKGNQSLES TNFYLLHLSL MREYLDLEFR DIEHVLPFPY
NLERVIDDFI LLAVFVGNDF LPNLPDLHIH ENGLEKLFDV YKKALPGLNG YINESGTINV
QRLQVVLDEM AVWEREIFEK EYADMNWFKG KQARHVKEME MGRKRSKLVL TKRQREIFDK
VKAFVLENRK APSLEHFKAA RLEMVNDFPA RERAFITQLS QDLHLSLRWD EYDEEDNNVV
TWRFPRALEV SEDAEDEEGE WEDMQEDEEN VIAVDRVLNK YEKAPVEDPD AEGDFDARYE
RSIKEKMDEW KRSYYREKLE ISYDDPKEMG DLVYRYVEGL QWVMHYYYSG VASWGWFYNY
HYAPRISDLR NVDQMTFNFE LGKPFKPYEQ LMGVLPVASK DHIPLAYQDL MYDPNSPILD
FYPLEFESDL NGKKQDWEAV VKIPFIDEER LLKAMASREH RLTPEERQRN TWGTSTKFSH
GTGEPTVYPS SLPGFFPPIY RCTCVMEPFD LPTLDGLHLV PGLCDGVFLG AEALAGFPSL
KTLPHSATLG YHGVNIHGSE SRNKSMIVHI ENPYENTKPE EIAQKFIDER IFMGWPFLQE
GKVVAVSDSL FKYERMAVVP GRPAKIVSTP HSPQGLGHWA SKAERIEQVY SKRCGVLTGS
VGVLLHIRPL KGLKRLETGA LVKDYEGPDK EIEQAVQMCL QEVVSEDPRY MERAPPPLHE
EFPDGSKVFF LGEHAYGVAA QVSATTQNTL SVIVAFFPAE RQEIDKFKAI VDTRKSSRYF
PSYRVADMLG MSGRALGKIT SSFLVLTSDE QKTNLGLSLK FEAKSMKVID YSRKDGRNWE
YSEKAVELIR EYKAAFPEVF ASLDNGGDAI ARATDIFPEA EADARVKEIK AWLKTKGVRD
FEPVSLFCDQ LSKETIEEIE QLADSITKSK SSSQIKKAIV KGIPRQAVLK PSHAVYRLQN
QHFALGDRVT MVQDSGGVPL AVKGVVVGLN ARSMDVLWDV AFISGTTLNN RCSQYRGSTV
AFNSCLNLTN PQFVTSTNPQ APPPVRPQIP FNPKFGPHPP IQPAPGQTAA SGFRPGPHAH
QNGTHSTGPG PQIKIMSNPN RGRGGFVNGV GRGGHPGGKP GVPGPAHVVP AVNPGRGGHV
NGAAPRGAQA SAAAGPSAPA AQVQPIPAAN EPAPHASGDF GPRGRGRGRG GPPPFRGHIR
GGFDRGRGGG RGGFRGRGGR GFAPPLAS
//
