ID A0A444UMJ1_ACIRT Unreviewed; 1655 AA.
AC A0A444UMJ1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN ORFNames=EOD39_3514 {ECO:0000313|EMBL:RXM36420.1};
OS Acipenser ruthenus (Sterlet sturgeon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=7906 {ECO:0000313|EMBL:RXM36420.1, ECO:0000313|Proteomes:UP000289886};
RN [1] {ECO:0000313|EMBL:RXM36420.1, ECO:0000313|Proteomes:UP000289886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WHYD16114868_AA {ECO:0000313|EMBL:RXM36420.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RXM36420.1};
RA Wei Q.;
RT "Draft Genome and Complete Hox-Cluster Characterization of the Sterlet
RT Sturgeon (Acipenser ruthenus).";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR006743}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family.
CC {ECO:0000256|PIRNR:PIRNR006743}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXM36420.1}.
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DR EMBL; SCEB01214245; RXM36420.1; -; Genomic_DNA.
DR Proteomes; UP000289886; 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; 3.
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:UP000289886};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT DOMAIN 1..209
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 216..543
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 595..782
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 788..1014
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1041..1110
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 1181..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1553..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1607..1622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1655 AA; 187393 MW; E0892D963275AAE0 CRC64;
MGVPKFYRWI SERYPCLSEV VKEHQIPEFD NLYLDMNGII HQCSHPNDED VHFRISEEKI
FADIFHYLEV LFRIIKPMKV FFMAVDGVAP RAKMNQQRGR RFRSAKEAED KIKKALEKGE
TLPTEARFDS NCITPGTGFM ARLQEQLKYF VNSKISTDKS WQGVHVYLSG HETPGEGEHK
IMEFIRSEKA NPDHDPNTRH CLYGLDADLG KISFEYDLER IIDDWILMGF LVGNDFIPHL
PHFHINHDAL PLLYRTYISI LPKLEGYIND NGNLNLVNFE KYLEKLSEYD REHFNEVFVD
LKWFESKVGN KYLNEAAGTT AEEERNRNRK KQKEDSLCLA ALDGNKEVDG APTKDCPDND
NEEEDLFETE FRQYKRSYYM TKMGVEVVSD EFLAGQAECY VLAIQWILHY YYHGVQSWSW
YYPYHYAPYL SDIRNFSKMK LLFDMGKPFL PFEQLLGVLP AASKDLLPKG YQDLMISEGS
PILEYYPLDF KTDLNGKQQE WEAVVLIPFI DEKRLLAAME PNSKFLTMDE KQRNRHSECA
VYCYDKDVEF LYPSPLPDKF PSLVKCHARY KTIPMDAWHV DLTYVGIKVH NSDVYFCGFP
TLKHIKHKFY KKKNSVQVFQ QSSRGESMML EIMPSDEETP RCEDVASLVL GKSVFVNWPH
LEEARVVAVS DGETKFFLEE PLGEQKLYTG KTVPPTKMAY LSDKEQNTWL KEVQGISEFY
NRRKGIVINE TAVLLFAQLL TGRKYVLNQN GEVHLEKQWS KQIIPFVYQA VVKDIVSFDS
SFSHFKTIDE LFSPETTVFM LGNPYYGCMG ETQVSSDVIG EGRIRVIFTI PCEPQLDALI
QNQHKYSIRY NPGYVLASRL GISGYLVSRF SGSIFIGRGS KRNQHGEQKA NVGLNLKFNK
KNEEVPGYTK KSGNEWLYSV AVEELLAEYV ERFPEVFSYV SKNSHNDVFY EDDIWPGEEE
NGAERVHEIT AWLKAHPVSS SSRASCDQQI LDTLIVEKIE EELEKCKQTR SNKKVRVTVK
PHLLFRPLEQ HHGVIPDKDA EYHLFDRVVN VRESFSVPLG LRGTVIGIKG AEREAEVLYE
VLFDKEFAGG LTIRCSPGRG YRLPPSALVN LTHGSRLENG FQKLTAIVKP QPASASPHST
YSATAQKVQI GGLNHSPRSP FVPTQLNGGK QHYDLRAENH ANRHSPQKAL NQSTAQKSHV
KDDEFSNVWQ SLQGSGNPQN PPHHWQENSS GGNERQNIRV LKRNEDYNAV STAHPLGSVH
TPSRKAHTEF EELIANLKIS KGNEAQPAQT KEELSNEEPL SPQSFAMKGT LMLKEMLKID
SSSSVPADKD KQSSTVAAYP SNPANTTGHH SRRRSTKKLA AHINTPHVAG APQHGQGSET
SVQHHGPPQP PVPTVVTELS RVCASLGMSQ PEFGYLRTPQ GMAVCQVKLS SGLLVHGPQC
QSENEAKEKA ALFALQRLSS VGSGFPLPQH MFSNLQQIRT AFPTGPIPSV FGQPPGNLMM
HPTPHGYGQM HWGAPVQVHG QPFYPGPYQG NRHPASAMPI GTHNQFVPLQ VTKKRATGKK
NYETREYNSS QYVRSQKNEQ AVKPQAADVA PQMTTAAPGH VASPQASLAA QEYQDQQGPS
TPRQNPNPNP TTPGSSAKRR PRKLAVNFDA AKVSE
//
