ID A0A452I8J4_9SAUR Unreviewed; 1661 AA.
AC A0A452I8J4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000023980.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000023980.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSGAGT00000027309.1; ENSGAGP00000023980.1; ENSGAGG00000017535.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
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:UP000291020};
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..598
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 652..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 1264..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1459..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1661 AA; 189658 MW; 11C153F0637B8F61 CRC64;
MGVPKFYRWV SERYPCLSQV LKEHQIPEFD NLYLDMNGII HQCSHPNDDD VHFRISDDKI
FADIFHYLEV LFRIIKPRKV FFMAVDGVAP RAKMNQQRGR RFRSAREAED KIKKALEKGD
ILPTEARFDS NCITPGTDFM ARLHEHLKYF VNMKISTDKS WHGVTVYLSG HETPGEGEHK
IMEFIRSEKT KPDYNPNTRH CLYGLDADLI MLGLTSHESH FSLLREEVRF GGKKSQRACA
PEETTFHLLH LSLMREYIDY EFSPVKDKIS FQYDIERIID DWILMGFLVG NDFIPHLPHL
HINHDALPLL YKTYMAILPE LGGYINESGH LNLQRFEKYL TKLSDFDREH FSEVFVDLKW
FESKVGNKYL NEAAGIAAEE ARSHKQKKQK IQENSMCLAA LEKTEDGIMT SSKNALEDEQ
EDEDLFETEF RQYKRTYYMT KMGVEVVSDD FLADQAECYV QAIQWILHYY YHGVQSWSWY
YPYHYAPYLS DIRNISKLKI QFELGKPFMP FEQLLAVLPA ASKDLLPKCY EYLMTSEDSP
IIEYYPPDFK TDLNGKQQEW EAVVLIPFID EKRLLQAMES CNKCLSEDEK RRNTHSECLK
YWYDKDTEFK YLSPWPEKFP AIQRCHTRYK TVSLDAWHVE ITHNKITKVN KSALYFCGFP
TLKHIAHKFY LKKSGVQVFQ QSSHGENMLL EIICDKDSKE QSVENVASLV LGKSVFVNWP
HLEEARVISV SDGETKFYLE EPHGTQKLYL GNTVPPTKVV YVGEKEQNIW LKEVQGISEH
YQKRKGIIIN ETSVVVYAQL LTGRRYQLNP NGEVYLEKQW SKQVLPFVYQ TIVKDISAFD
SRFSNIKTLD DLFPPGSTVF MLGTPYYGCI GEVQDSCDVI TEGRIRVVFN IPCEPQLDSL
IQNQHKYSVK YNPGYVLASR LGVSGYLVSR FTGSIFIGRG SRRNPHGDHK ANVGLNLKFN
KKNEEVPGYT KKVRNEWMYS SAVEQLLAEY LERVPELFSY IAKNSQEDIF YEDDIWPGEE
ENGAERVQEI VAWLKAHPVS ALSRSSCDLQ ILDAAIVEKI EEELEKCKQR KSNKKVRVTV
KPHLLYRPLE QQNGVVPDRD AEYRLFDRVV NVRENFSVPV GLRGTIIGLK GASREMDVLF
EVLFDEEFPG GLTIRCSPAR GYRLPTSALI NLSHGSRSET GNQKLTAIVK PQPAVNHYNS
CPSESSSVCS QKVHLGGLNH SPRSLFVPTR AQSKQDDEFC SIWQSLQGSG KSQHVQQNMN
EKGAILPQET KPGTGNQLYK PGFNESTLKG QQRKQEPFKK FKEDSKVPRN EDQTHKISNK
QNFAGANKYN VKLLKRNESP SVPVIQKASV DESCVAGKKD SELDNLLASL KISKENEVQS
SYPKEERVTN EEHLSPQSFA MKGTQMLKEI LKIDVSDMET KNEMKPLINE VPASSARQDS
HGAAMQHRQT KKMAAYMNKP HGVGGLHNSQ ALETGGHPLL GPQSALSTPV SELSRICSLV
GMPQPDFSFL RTPQTMTVCQ VKLSNGLLVH GPQCHSENEA KERAAFFALQ RLSSLGVNFS
LPPPPPVFPN YQSMGAPVPP GSIPSVFTQP TANMMPPSAH MFGPMPWSAP VPIHGKSYYP
SSYPGNMPLA GTVPVGTHNQ FIPLQVSMTG IVLRSYFYKR C
//
