ID A0A2W1BT41_HELAM Unreviewed; 826 AA.
AC A0A2W1BT41;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN Name=HaOG204131 {ECO:0000313|EMBL:PZC76814.1};
GN ORFNames=B5X24_HaOG204131 {ECO:0000313|EMBL:PZC76814.1};
OS Helicoverpa armigera (Cotton bollworm) (Heliothis armigera).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Helicoverpa.
OX NCBI_TaxID=29058 {ECO:0000313|EMBL:PZC76814.1, ECO:0000313|Proteomes:UP000249218};
RN [1] {ECO:0000313|EMBL:PZC76814.1, ECO:0000313|Proteomes:UP000249218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Harm_GR_Male_#8 {ECO:0000313|EMBL:PZC76814.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PZC76814.1};
RX PubMed=28756777; DOI=10.1186/s12915-017-0402-6;
RA Pearce S.L., Clarke D.F., East P.D., Elfekih S., Gordon K.H., Jermiin L.S.,
RA McGaughran A., Oakeshott J.G., Papanikolaou A., Perera O.P., Rane R.V.,
RA Richards S., Tay W.T., Walsh T.K., Anderson A., Anderson C.J., Asgari S.,
RA Board P.G., Bretschneider A., Campbell P.M., Chertemps T.,
RA Christeller J.T., Coppin C.W., Downes S.J., Duan G., Farnsworth C.A.,
RA Good R.T., Han L.B., Han Y.C., Hatje K., Horne I., Huang Y.P., Hughes D.S.,
RA Jacquin-Joly E., James W., Jhangiani S., Kollmar M., Kuwar S.S., Li S.,
RA Liu N.Y., Maibeche M.T., Miller J.R., Montagne N., Perry T., Qu J.,
RA Song S.V., Sutton G.G., Vogel H., Walenz B.P., Xu W., Zhang H.J., Zou Z.,
RA Batterham P., Edwards O.R., Feyereisen R., Gibbs R.A., Heckel D.G.,
RA McGrath A., Robin C., Scherer S.E., Worley K.C., Wu Y.D.;
RT "Genomic innovations, transcriptional plasticity and gene loss underlying
RT the evolution and divergence of two highly polyphagous and invasive
RT Helicoverpa pest species.";
RL BMC Biol. 15:63-63(2017).
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 EMBL; KZ149945; PZC76814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1BT41; -.
DR Proteomes; UP000249218; Unassembled WGS sequence.
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:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd18673; PIN_XRN1-2-like; 1.
DR Gene3D; 1.25.40.1050; -; 1.
DR Gene3D; 3.40.50.12390; -; 1.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR004859; Xrn1_N.
DR InterPro; IPR017151; Xrn2/3/4.
DR PANTHER; PTHR12341:SF77; 5'-3' EXORIBONUCLEASE 2; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 2.
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:UP000249218};
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}.
FT DOMAIN 1..183
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 192..599
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT REGION 286..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 94264 MW; 7CE20B51F78CC40F CRC64;
MGVPAFFRWL SRKYPSVIVE CVEQKPTDVD GQLIYIDSSL PNPNGVEFDN LYLDMNGIIH
PCTHPEDKPP PKDEDEMMVA IFECIDRLFR IVRPRKLLYM AIDGVAPRAK MNQQRSRRFR
ASKETQEKID EIARIRDELL AKGAYLPPER PKEAHFDSNC ITPGTPFMDR LSKCLHYYIH
DSRQCGRQSA CNFFSDDGWI TDSGDVKLER VQVIMTELGH MEDEIFKRRH QNEINFKAKD
KARKRQQQRI NFEMLEKTQF APMPIGQNAK PLENVRQEAA NMRVAGMQNE AAQEQDSRGR
KRSAQAAGLD DEDDDDKNDE VRLWEQGFKE RYYESKFEVA RDNLEFRYRV ALQYVRGLCW
VLRYYYQGCA SWKWYFPYHY APFASDFVNI CGLSTKFEEG TQPFRPLEQL MGVFPAASST
HVPKPWAKLM SDPFSSIIDF YPIDFKIDLN GKKFAWQGVA LLPFVDEERL FKALEPYYGE
LTEAEKQRNI RGHDRLYVGT ANKSYDYLLG LYSEAGSKLR SLIEKQQKYP YISDGVTGEV
MLSKDCVVIG GQLPSPVIGL QPVLGNHVVC VRFLDPSYDK EFPARRLEGA VQPPRVLKPG
HLGHEENRNY RPQIGMVRSN TIATMEAAGR RMLGHHLPRQ TPYGSVPPPP QHAGHHNRSQ
SYGPRPSGYV PYQNNQEHGR SFSSGGQEQG RGYNNHSHGP RTYNQGNQDY SQNNRGYSQN
QGYSQSNQGP SRSGYGYGNQ NRFGNSGGSG YRSQSGGYES QGHQKYGGHQ TSQPTQGYSS
SSGKYGQSQG YSTQGSRDAR NRYNSDQPQS GSNRRYQGSS QGGSWR
//
