ID A0A2U4B9G0_TURTR Unreviewed; 1700 AA.
AC A0A2U4B9G0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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_019789860.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019789860.1};
RN [1] {ECO:0000313|RefSeq:XP_019789860.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019789860.1};
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_019789860.1; XM_019934301.2.
DR STRING; 9739.ENSTTRP00000012255; -.
DR GeneID; 101335167; -.
DR InParanoid; A0A2U4B9G0; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000245320; Chromosome 4.
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:UP000245320};
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..597
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 654..844
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 850..1075
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1102..1171
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 1268..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1660..1700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1700 AA; 192996 MW; 8C9607C505EE2ADC 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 EFSALKDKIT FKYDIERIID DWILMGFLVG NDFIPHLPHL
HINHDALPLL YGTYITILPE LGGYINESGH LNLPRFEKYL VKLSDFDREH FSEVFVDLKW
FESKVGNKYL NEAAGVAAEE AKNYKEKKKS KGQENSICWA ALDKNGEEVV TSKDNLEDET
EDDDLFETEF RQYKRTYYMT KMGVDVVSDD FLADQAACYV QAIQWILHYY YHGVQSWSWF
YPYHYAPFLS DIRNISTLKI HFELGKPFKP FEQLLAVLPA ASKNLLPTCY QHLMTDEDSP
IIEYYPPDFK TDLNGKQQEW EAVVLIPFID EKRLLEAMET CNHSLKKEER KRNQHSECLM
CWYDSETEFT YPSPWPEKFP AIGRCCARYR IISLDAWRVD ISKNKITRVD QKALYFCGFP
TLKHIKHKFF LKKSGVQVFQ QSSRGENMML EILVNAESDE LSVENIASSV LGKSLFVNWP
HLEEARVVGV SDGETKFYLE EPAGTQKLYL GRTAPPSKVV HLGDKEQSNW TKEVQGISEY
YLRRKGIIIN ETSAVVYGQL LTGRKYQVNQ NGEVRLEKQW SKQVLPFVYQ TIVQDIRAFD
SRFSNIKTLD DLFPPRSMVF MLGTPYYGCT GEVQDSGDVI TEGRIRVIFS IPCEPNLDAL
IQNQHKYSIK YNPGYVLASR LGVSGYLVSR FTGSIFIGRG SRRNPHGDHK ANVGLNLKFN
KKNEEVPGYT KKVGSEWMYS SAAEQLLAEY LERAPELFSY IAKNSQEDVF YEDDIWPGEN
ENGAEKVQEI ITWLKGHPVS TLSRSSCDLQ ILDAAIVEKI EEEVEKCKQR KNNKKVRVTV
KPHLLYRPLE QQHGVIPDRD AEFRLFDRVV NVRENFSVPV GLRGTIIGIK GANREADVLF
EVLFDEEFPG GLTIRCSPGR GYRLPTSALV NLSHGSRSET GNQKLTAIVK PQPAVNHYSS
SSSISSGHLG GLNHSPQSLF VPTQVPAKDD DEFCNIWQSL QGSGKVQHFQ PPLQEKGAVL
PQEISQVTQH HKSGFNENSV KQRKHEPHRK FKEECKSPKT ESRSQKISNR QPNPGIENFL
ASLNISKENE VQSSHHEEPP SEEHLSPQSF AMKGTRMLKE ILKIDGSDTV DHKNEMKQFG
NEVTVSSSRR DEYGSSSQPK QTSYMNKPHS ASEYHNVQSV DSVCWPAASQ IPPVSTPVTE
LSRICSLVGM PQPDFSFLRT PQTMTVCQVK LSNGLLVHGP QCHSENEAKE KAALFALQQL
GSLGVNFPLP PPIFPSYPPA VPPGTIPPVF PQPTGWDHYG SNLALGAANI MPSSSHLFGS
MPWAPPVPVP GKPFHHTSYA GTMPMAGGMP AGVHNQFIPL QVTKKRVANK KNFENKDAQS
CQATLLQTSQ SASSDVTKVI PQESLSASFK SPQITQLASP FQVEAASPGH SMSHHKSTPS
SSRRKSRKLA VNFGVSKPSE
//
