XRN2_CHICK
ID XRN2_CHICK Reviewed; 949 AA.
AC Q5ZIP4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=5'-3' exoribonuclease 2;
DE EC=3.1.13.-;
GN Name=XRN2; ORFNames=RCJMB04_24h23;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. May promote the
CC termination of transcription by RNA polymerase II (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ720740; CAG32399.1; -; mRNA.
DR RefSeq; NP_001026204.1; NM_001031033.1.
DR AlphaFoldDB; Q5ZIP4; -.
DR SMR; Q5ZIP4; -.
DR STRING; 9031.ENSGALP00000013622; -.
DR PaxDb; Q5ZIP4; -.
DR PRIDE; Q5ZIP4; -.
DR Ensembl; ENSGALT00000013637; ENSGALP00000013622; ENSGALG00000008372.
DR GeneID; 421236; -.
DR KEGG; gga:421236; -.
DR CTD; 22803; -.
DR VEuPathDB; HostDB:geneid_421236; -.
DR eggNOG; KOG2044; Eukaryota.
DR GeneTree; ENSGT00670000098098; -.
DR HOGENOM; CLU_006038_1_2_1; -.
DR InParanoid; Q5ZIP4; -.
DR OMA; CLHYYVH; -.
DR OrthoDB; 685597at2759; -.
DR PhylomeDB; Q5ZIP4; -.
DR TreeFam; TF105977; -.
DR Reactome; R-GGA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q5ZIP4; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000008372; Expressed in colon and 12 other tissues.
DR GO; GO:0016235; C:aggresome; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0001147; F:transcription termination site sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR004859; Put_53exo.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR017151; Xrn2/3/4.
DR PANTHER; PTHR12341; PTHR12341; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
PE 2: Evidence at transcript level;
KW Exonuclease; Hydrolase; Metal-binding; mRNA processing; Nuclease; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Transcription termination; Zinc; Zinc-finger.
FT CHAIN 1..949
FT /note="5'-3' exoribonuclease 2"
FT /id="PRO_0000249913"
FT ZN_FING 261..278
FT /note="CCHC-type"
FT REGION 410..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 108542 MW; 22368CED6C1EE1A3 CRC64;
MGVPAFFRWL SRKYPSIIVN CVEEKAKECN GVKASVDTSK PNPNEVEFDN LYLDMNGIIH
PCTHPEDKPA PKNEDEMMVA IFEYIDRIFN IVRPRRLLYM AIDGVAPRAK MNQQRSRRFR
ASKEGMEAAE EKQKIRQEIL AKGGILPPEE VKERFDSNCI TPGTEFMDNL AKCLRYYIAD
RLNSDPGWKN LTVILSDASA PGEGEHKIMD YIRRQRAQPN HDPNTHHCLC GADADLIMLG
LATHEPHFTI IREEFKPNKP KPCALCNQMG HEVKDCQGLP REKQGKHDQF ADSLPASEQE
FIFIRLCVLR EYLERELTMA SLPFTFDFER SVDDWVFMCF FVGNDFLPHL PSLEIREGAI
DRLVNIYKNV VHKTGGYLTE SGFVNLQRVQ MIMLAVGEVE DSIFKKRKDD DDNFKRRQKE
KKKRMKRDHP SFIPGGQFSP QALGNRSSPQ AISNPRQTAF EMRMHDRQNS TMSSPNTSLN
SDGSPSPARG IKRKSEDSDS EPEPEDNIRL WESGWKQRYY KNKFDVDASD EKFRRKVVQS
YVEGLCWVLR YYYQGCASWN WYYPFHYAPF ASDFEGIADM PSDFEKGSKP FKPLEQLMGV
FPAASGNFLP PTWRKLMTDP ESSIIDFYPE DFAIDLNGKK YAWQGVALLP FVDERRLRAA
LEEVYPDLTP EENRRNSLGG DVLFVGKHHP LCDFIVEQYK SKNTEPVDMP PELCYGIQGK
LTPNENAVLP DKTVESPVPM LRDLTQNSAV SISFKDPQFD EDFIFKATVL PGAKKPPPVL
KPGDWEKTNN DGRPWRPQLG FNRDRKPVHL DQSAFRTLGH AMPRERGMPG MYANAVPLGA
YGSPYTRPLM SGQQQIPKLL SNLRPQESWR GPTPLFQQAP QRTAGAAPLL AWNRMLPAQS
QYPPGQYQGL GGPMSYPQRP EDRMDRGRQA YGPGRPYLLP PPSGRYSWN
