ID H2ASF0_KAZAF Unreviewed; 1499 AA.
AC H2ASF0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN Name=KAFR0C03080 {ECO:0000313|EMBL:CCF57300.1};
GN ORFNames=KAFR_0C03080 {ECO:0000313|EMBL:CCF57300.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF57300.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF57300.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE650823; CCF57300.1; -; Genomic_DNA.
DR RefSeq; XP_003956435.1; XM_003956386.1.
DR STRING; 1071382.H2ASF0; -.
DR GeneID; 13885219; -.
DR KEGG; kaf:KAFR_0C03080; -.
DR eggNOG; KOG2045; Eukaryota.
DR HOGENOM; CLU_001581_1_2_1; -.
DR InParanoid; H2ASF0; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000005220; 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 GO; GO:0006364; P:rRNA processing; 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; 3.30.1370.250; -; 1.
DR Gene3D; 3.40.50.12390; -; 2.
DR Gene3D; 6.10.140.950; -; 1.
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:SF80; 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:UP000005220};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT DOMAIN 1..227
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 272..685
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 726..920
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 924..1151
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1169..1239
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 1408..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1499 AA; 172079 MW; 7140162A956F202C CRC64;
MGIPKFFRYI SERWPMISQL IEGAQIPEFD NLYLDMNSIL HTCTHGNDDD VTKRMTEEEV
FAKIFTYIDH LFHTIKPKKV FYMAIDGVAP RAKMNQQRSR RFRTAMDAEA ALKKAIEKGE
EIPKGEPFDS NAITPGTEFM AKLTKNLKYF IHDKISNDSK WREVDVIFSG HEVPGEGEHK
IMDFIRNIRS QKDYNNNTRH CIYGLDADLI MLGLSTHAPH FALLREEVVF GRRSSKPAPL
EHQNFYLLHL SLLREYMELE FNEIADDLKF DYDFERILDD FILVMFVIGN DFLPNLPDLH
LNKGAFPVLL QTFKEALLHL DGYINENGQI NLERLRVWLN YLSQFELMNF EKNDIDVEWF
NQQLENISLE GERKRARSGK KLLLKQQKKI VGKVKPWIMH LANEKFPSDL PDDQIPTLLL
NDDKSEFNVA ENLAFLKEFA HDLGVFIVHS KSKDTYSLKL DIDGINPSET DEEHNERVGA
IRRVIKRYQQ AVLVEDAEEL EREQTLYNEK FQNWKQEYYK DKLGFAQNDS ETVTTLAKNY
VEGLQWVLYY YYRGCPSWGW YYRDHYAPRI SDLEKGLDQI IKFDKGRPFT PFEQLMAVLP
ERSKNLIPAA FRPLMYDTNS PILDFYPSQV KLDKNGKTAD WEAVVLLTFV DENRLVDAMK
PLLSKLSPEE KVRNQFGTDL KFIFSPQVDN LYKSPLSGIF SDLENNHCVE REYIPKSMDG
LSFHYGLLPG AKQGTELLAG FPTLQTLPFK YQLEYNESLV FQQASRQQSM CLHIEDIYSE
NNLTLEELSK RYMNKIVYTR WPYLRESKLV SVFDENVLFE GKEFVNEKGK KHFKIIERTC
DIQDKKNFES LKRSMLRNYG KQKAVILNDI KAIVKVLPVT GLMRTPEGAY VKTYAETPDH
YPLQLMVETI SNKDERYRER APVPISQEFP EGSRVIFLGD YAYGGDTTID GYSSESRLKI
TVKKTFSKNE PTIGKERLEI DNKLVHYIPS YVAAKKLDLN KLFLSRITSK FLIDDANGKH
VNVGIPVKYE NKQQKVLGYA RRNPKGWEYS NLTINLIREY RSRFPEFFRG LSRTGNGIPS
LQELFPGIST EVAMKKLQEI KDWLKFSEEN FVIVSNESDS LTKGSIRAVE DFIEVHSSGR
ENSETKQLTK VPRDAILNPR VSFGLLRTQR FNLGDRVVYI QDSGKVPLFS KGTVVGYTTL
GLSLSVQVLF DHEIVSGNTF GGRLRTKRGL GLDSSFLLNV TDRQFVYHSK ASKKLLEGKK
SGTKSVAARN VNMIQRKQKQ QEVATMRKQA AHDLLNIIKK TGEKPADGGQ KEPAATQERE
TLLKKSGGEN ADANLPLPNQ NVVNSVVNAV MHQFDSNDNQ MVSNGQQNVV PTMNNGVVNP
ASLPYSAPPG FVNGVPLGAG YPPNMQMSPQ VMNGQPLLPP QSFYAGPMQH PQQHHQQHSH
AHPHPQLPHQ NGHVVVNKKA SAELKQIFKS DAEQNKSQRP KKTILKRRAE TKASAEPKK
//
