ID W5MMT7_LEPOC Unreviewed; 1729 AA.
AC W5MMT7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=5'-3' exoribonuclease 1 {ECO:0000313|Ensembl:ENSLOCP00000009696.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009696.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000009696.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01015287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000009707.1; ENSLOCP00000009696.1; ENSLOCG00000007944.1.
DR GeneTree; ENSGT00670000098080; -.
DR HOGENOM; CLU_001581_3_0_1; -.
DR Proteomes; UP000018468; Linkage group LG14.
DR Bgee; ENSLOCG00000007944; Expressed in liver and 13 other cell types or tissues.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:InterPro.
DR CDD; cd18673; PIN_XRN1-2-like; 1.
DR Gene3D; 1.25.40.1050; -; 1.
DR Gene3D; 2.170.260.40; -; 1.
DR Gene3D; 2.30.30.750; -; 1.
DR Gene3D; 3.40.50.12390; -; 1.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR016494; 5_3_exoribonuclease_1.
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; 2.
PE 4: Predicted;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 1..227
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 274..606
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 652..839
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 848..1080
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1107..1176
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 1249..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1421..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1666..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1299
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"
FT COMPBIAS 1380..1402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1729 AA; 196319 MW; B1AF24821565D35A CRC64;
MGVPKFYRWI SERYPCLSEV VKEHQIPEFD NLYLDMNGII HQCSHPNDED VHFRISEEKI
FADIFHYLEV LFRIIKPRKV FFMAVDGVAP RAKMNQQRGR RFRSAKEAED KIKKALEKGE
VLPTEARFDS NCITPGTEFM ARLQEQLEYF VHNKISTEKS WQRVRVYLSG HETPGEGEHK
IMEFIRSENA RPDHDPNTRH CLYGLDADLI MLGLTSHEPH FSLLREEVRF GGKKSQKRIS
TPEETTFHLL HLSLMREYID YEFSELRDKI SFEYNLERII DDWILMGFLV GNDFIPHLPH
LHINHDALPL LYRTYISVLP KLGGYINENG NLNLANFEKY LEKLSEFDRE HFSEVFVDLK
WFETKVGNKY LNEAAGIAAE EAKSREGKRN KMLEDSLCLA ALDENKDTEG LPTKDCVEED
GEDDDMFETE FRQYKRTYYM TKMEVEVVSD EFLAGQAECY VRAIQWILHY YYHGVQSWSW
YYPYHYAPFL SDIRNISKLE MRFEMAKPFM PFEQLLAVLP AASKDLLPEC YRHLMTSEGS
AIIEYYPLDF KTDLNGKQQE WEAVVLIPFI DEKRLLSAME PYNAFLTKSE QERNRHSECA
VYWYDKDTDF QYPSPLPGKF PDIVKCHVRH ELISMDAWRV DPSYTRRKVD PGALYFCGFP
TLKHIRHKFY KKKNGVQVFQ QSSRGENMIL EIIPEDNVEP ECADVASSVL DKSVFVNWPH
LEEARIVAVS DGETKFYLEE PPGVQKLYSG KTVPPTKVVY LSDKEQSIWL KEVQSIVEFY
NRRKGIIINE TAVLLYGQLM TGRKYVLDQK GGVHLEKQWA KQIIPFAYQT IVQDLKTFDS
SVSCFKTLEE LFTPGTTVFM LGNPYYGSVG EVLDSSDVIS EGRFRVLFTV PCEPQLDALI
HNQHKYSVKY SPGYVLASRL GITTYLVSRF SGSIFIGRGS KQNPHGEQKV NVGLNLKFNK
KNEEVPGYTK KSGNEWLYSV AVEELLAEYL ERFSEIFSYV SRNSHEDVFY EDDVWPGEDE
NGYDFKTRAE KVQEITSWLK THPVSSSSRA SCDLQILDTA IVEKIEEEVD KCKQKRSTKK
VRVTVKPHLL YRPLEQQHGI IPDKDADYHL FDRVVNVREN FSVPLGLRGT VIGIKGADRE
DEILYEVVFD EEFVGGLTIR CSSGKGYRLP PSALINLTHG IRLEYGAQKL TAIVKPQPAS
ASHQNSYFPA SSLNPHKVQI GGLNHSPCSP FVPTQQLNGR QVYNLRADNQ GNWHSQKTFN
QKNTQKSHAK EDEFSSVWQS LQGSGAPQNP PALWQNSGQA RRTKEEDRNQ RNDTQQASRA
QNKPVSSGAG RTKASIRVLK RNEDLNAVDS AQPHSSSQDT SNKVSTEFEE LIANLKISKG
GGTLPSQTKD QIHTTEEPLS PQSFAMKGTL MLKEMLKIDG SSSADSEKVK PSPVEPVASA
TTTSYQPRRR PSKKLAAHIN KPNVPGVAQH GPGADKPGQC LPPHQPLIPT VASELSRICL
GLGMSVPEFA FLRTPQGMTI CQVKLSNGLL VHGPQCQSES EAKEKAALFA LQRLNSVGSG
FPLAQPMFSG MQQMRATLPS GPVHSVFGQP PGNLLMHPPA HGYGPLHWGA PVQMQGQAFY
QGTYPGARPP APAVPIGTHN QFVPLQVTKK RAAGKKNLEA REYYNSQYRI TAPPATVTPS
QTPPTSQEPQ ERSTSSTLKQ NPNPQTTGSS AKRKPRKLAV NFDAAKVSD
//
