ID A0A340WHL9_LIPVE Unreviewed; 1702 AA.
AC A0A340WHL9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN Name=XRN1 {ECO:0000313|RefSeq:XP_007447012.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007447012.1};
RN [1] {ECO:0000313|RefSeq:XP_007447012.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_007447012.1; XM_007446950.1.
DR GeneID; 103082255; -.
DR CTD; 54464; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 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 Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR006743};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
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..596
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 653..843
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 849..1074
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1101..1170
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 1267..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1661..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1702 AA; 193276 MW; 71E23F7EC1E883C0 CRC64;
MGVPKFYRWI SERYPCLSEV VKEHQIPEFD NLYLDMNGII HQCSHPNDDD VHFRISDDKI
FTDIFHYLEV LFRIIKPRKV FFMAVDGVAP RAKMNQQRGR RFRSAKEAED KIKKAIEKGE
TLPTEARFDS NCITPGTEFM ARLHEHLKYF VNMKISTDKS WQGVTIYFSG HETPGEGEHK
IMEFIRSEKA KPDHDPNTRH CLYGLDADLI MLGLTSHEAH FSLLREEVRF GGKKTQRVCA
PEETTFHLLH LSLMREYIDY EFSALKNKIT FKYDIERIID DWILMGFLVG NDFIPHLPHL
HINHDALPLL YGTYITILPE LGGYINESGH LNLPRFEKYL VKLSDFDREH FSEVFVDLKW
FESKVGNKYL NEAAGVAAEE AKNYKEKKKS KGQENSICWA ALDKNGEVVT SKDNLEDETE
DDDLFETEFR QYKRTYYMTK MGVDVVSDDF LADQAACYVQ AIQWILHYYY HGVQSWSWFY
PYHYAPFLSD IHNISTLKIH FELGKPFKPF EQLLAVLPAA SKNLLPTCYQ HLMTNEDSPI
IEYYPPDFKT DLNGKQQEWE AVVLIPFIDE KRLLEAMETC NHSLKKEERK RNQHSECLMC
WYDSETEFMY PSPWPEKFPA IGRCCARYRI ISLDAWRVDI SKNKITRVDQ KALYFCGFPT
LKHIKHKFFL KKSGVQVFQQ SSRGENMMLE ILVNAESDEL SVENIASSVL GKSLFVNWPH
LEEARVVGVS DGETKFYLEE PAGTQKLYLG RTAPPSKVVH LGDKEQSNWT KEVQGISEYY
LRRKGIIINE TSAVVYGQLL TGRRYQVNQN GEVRLEKQWS KQVLPFVYQT IVQDIRAFDS
RFSNIKTLDD LFPPRSMVFM LGTPYYGCTG EVQDSGDVIT EGRIRVVFSI PCEPNLDTLI
QNQHKYSIKY NPGYVLASRL GVSGYLVSRF TGSIFIGRGS RRNPHGDHKA NVGLNLKFNK
KNEEVPGYTK KVGSEWMYSS AAEQLLAEYL ERAPELFSYI AKNSQEDVFY EDDIWPGENE
NGAEKVQEII TWLKGHPVST LSRSSCDLQI LDAAIVEKIE EEVEKCKQRK NNKKVRVTVK
PHLLYRPLEQ QHGVIPDRDA EFRLFDRVVN VRENFSVPVG LRGTIIGIKG ANREADVLFE
VLFDEEFPGG LTIRCSPGRG YRLPTSALVN LSHGSRSETG NQKLTAIVKP QPAVNHYSSS
SSISSGHLGG LNHSPQSLFV PTQVPAKDDD EFCNIWQSLQ GSGKVQHFQP PLQEKGAVLP
QEISQVTQHH KSGFNENSVK QRKHEPHRKF KEECKSPKTE SRSQKISNRQ PNPGIENFLA
SLNISKENEV QSSHHEEPPS EEHLSPQSFA MGTRMLKEIL KIDGSDTVDH KNEMKQFGNE
VTVSSNRRDE YGSSSQPKQS KKLTSYMNKP HSASEYRNVQ SVDSVCWPAA SQIPPVSTPV
TELSRICSLV GMPQPDFSFL RTPQTMTVCQ VKLSNGLLVH GPQCHSENEA KEKAALFALQ
QLGSLGVNFP LPPPIFPSYP PAVPPGTIPP VFPQPTGWDH YGSNLALGAA NIMPSSSHLY
GSMPWAPPVP VPGKPFHHTS YAGTMPMAGG MPAGVHNQFI PLQVTKKRVA NKKNFENKDA
QSCQATLLQT SQSASSDVTK VIPQESLSAS LKSPQITQLA SPFQVEAASP GHSMSHHKST
PSSSRRKSRK LAVNFGVSKP SE
//
