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Database: UniProt
Entry: A0A674C0F7_SALTR
LinkDB: A0A674C0F7_SALTR
Original site: A0A674C0F7_SALTR 
ID   A0A674C0F7_SALTR        Unreviewed;       801 AA.
AC   A0A674C0F7;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE            EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN   Name=LOC115174957 {ECO:0000313|Ensembl:ENSSTUP00000077042.1};
OS   Salmo trutta (Brown trout).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000077042.1, ECO:0000313|Proteomes:UP000472277};
RN   [1] {ECO:0000313|Ensembl:ENSSTUP00000077042.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. May promote
CC       termination of transcription by RNA polymerase II.
CC       {ECO:0000256|PIRNR:PIRNR037239}.
CC   -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006994,
CC       ECO:0000256|PIRNR:PIRNR037239}.
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DR   AlphaFoldDB; A0A674C0F7; -.
DR   Ensembl; ENSSTUT00000082058.1; ENSSTUP00000077042.1; ENSSTUG00000033801.1.
DR   GeneTree; ENSGT00670000098098; -.
DR   Proteomes; UP000472277; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd18673; PIN_XRN1-2-like; 1.
DR   Gene3D; 1.25.40.1050; -; 1.
DR   Gene3D; 3.40.50.12390; -; 2.
DR   InterPro; IPR027073; 5_3_exoribonuclease.
DR   InterPro; IPR041412; Xrn1_helical.
DR   InterPro; IPR004859; Xrn1_N.
DR   InterPro; IPR017151; Xrn2/3/4.
DR   InterPro; IPR001878; Znf_CCHC.
DR   PANTHER; PTHR12341:SF77; 5'-3' EXORIBONUCLEASE 2; 1.
DR   PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR   Pfam; PF17846; XRN_M; 2.
DR   Pfam; PF03159; XRN_N; 1.
DR   PIRSF; PIRSF037239; Exonuclease_Xrn2; 2.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR037239};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW   ECO:0000256|PIRNR:PIRNR037239};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR037239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472277};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00047}.
FT   DOMAIN          263..276
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          447..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          743..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   801 AA;  91873 MW;  38C7AA76589ADC98 CRC64;
     MGVPAFFRWL SRKYSTIVVH CTEERSKECN GVRIPVDTSK PNPNEVEFDN LYLDMNGIIH
     PCTHPEDKAA PKNEDEMMVA IFEYMDRLFN IVRPRRVLYM AIDGVAPRAK MNQQRSRRFR
     ASKEGVELVE EKSRIREEIL GKGGYLPPVE IKERFDSNCI TPGTEFMDNL AKCLRYYVAD
     RLSNDPGWRN ITVILSDASV PGEGEHKIMD YIRRQRAQPH HDPNTHHCLC GADADLIMLG
     LATHEPNFTI IREEFKPNQP RPCAMCGQKG HEIKDCQGVA REKQGEHDEF ADTMPASEQE
     FIFIRLCVLR EYLERELTMA SLPFPFDFER TVDDWVFMCF FVGNDFLPHL PSLEIREGAI
     DRLVGIYKDV VHKTGGYITE NGFVKLESVE LIMQAIGVAE DNIFKKRKED DNICMKICRQ
     LVETDLLPDG LGIIICKDVC FVQAGSSDGQ DGRGVKRKAD SDSEPEPEDN VRLWEDGWKQ
     RYYKTKFDVD ATDDDFRKKV VKSYVEGLCW VLRYYYQGCA SWKWYFPFHY APFASDFKDI
     KGMFTDFELG TKPFKPLEQL MGVFPAASGN FLPPTWRSLM SNPESSIIDF YPDDFAIDLN
     GKKYAWQGVA LLPFVDERRL RAALAEVYPN LSPEENKRNS LGSDMLFVGK SHPCCDFIQE
     LYRGESHEGT EMPAELCHGI QGTLNLDEDP ILPDRPVQSP IPMLRDIAQN TAIGVKYKDP
     QYRETFVFKA VILPGAKMPE KVLKPGDWER GNRGRGNWRP QLGFNSNRQQ VHLDQSAFRA
     LGYKYSVDIV NAYRANPSLS F
//
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