ID A0A1Y2HX03_9FUNG Unreviewed; 1214 AA.
AC A0A1Y2HX03;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=BCR44DRAFT_115720 {ECO:0000313|EMBL:ORZ39039.1};
OS Catenaria anguillulae PL171.
OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC Blastocladiomycetes; Blastocladiales; Catenariaceae; Catenaria.
OX NCBI_TaxID=765915 {ECO:0000313|EMBL:ORZ39039.1, ECO:0000313|Proteomes:UP000193411};
RN [1] {ECO:0000313|EMBL:ORZ39039.1, ECO:0000313|Proteomes:UP000193411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL171 {ECO:0000313|EMBL:ORZ39039.1,
RC ECO:0000313|Proteomes:UP000193411};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:ORZ39039.1}.
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DR EMBL; MCFL01000006; ORZ39039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2HX03; -.
DR STRING; 765915.A0A1Y2HX03; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000193411; 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:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-KW.
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; -; 2.
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:SF81; 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; 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 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:UP000193411};
KW Transcription {ECO:0000256|ARBA:ARBA00022472};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00022472};
KW Transcription termination {ECO:0000256|ARBA:ARBA00022472}.
FT DOMAIN 1..255
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 343..506
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 575..951
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT REGION 566..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1032
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1214 AA; 136544 MW; D65C0FF96BDC09D7 CRC64;
MGVPSLFRWL QSRYPRVTSK VIEIQPTEIN GVTIPVDFSL PNPNGYEFDN LYLDMNGIIH
PCCRPSDGRP APETVDDMFI AIFEYIDRLM AMVRPRKLVY MAVDGVAPRA KMNQQRSRRF
RAAQDAAMAR AVEEEVFART LEENPFADIS APGEKFDSNC ITPGTPFMAN LVVALRYYVQ
HRLNTHPGWR NLKVLMSDAS VPGEGEHKVM DYIRRQRCDP HYDPNTHHVL YGLDADLIFL
GLATHEPHFF ILREDVYEID RRQRESRGCD RCGQLGHFTF RCNQRPLPAN LLKEQQAKNT
AMALATKDKS DWIDPYLFFK VSVMREYLQA ELYFDGKRVG FDFDFERVLD DWVFICFFVG
NDFLPHHPAL EIREGAIDLL TDVYRTNLKR MGGYLTEHGI LNLERVQYIF EDLARHESDI
FHAREHKERE YHDSNRKKQY HRYKDFGYSK DDMDKMLKLY DKVNDLRAAG DLHEAEKIEK
KLRKMEVDLA NEAEQGIARS ESTSKYADDK YMEQQAEEQD EASAADAPVS IAGSGMHVTD
IKDKSDNSTL VQFRNATFDV QALAQPLGRK SQSKTEAATA AKRTASEAHI DEEPNELEPP
AKKLEGEPTA DDDQVDDPMA YVDEPEVEPE DEVEDSDVPD SDVSVVALTK AELLAQNRKF
KSGNADLGAP GYIERYYADK FGDSSIDMRR KVGHEYVIGL CWVLHYYIKG CPSWKWYYPY
HYAPFASDIM DIDQLGDTVT FELGTPFKPI EQLMGVFPAA SKAHIPSVFH DLMTQEDSEI
IDFYPTEFVI DLNGKTMLWQ GVALLPFIDE KRLLAAMAPL YPLLTEEDRF LNTLGQEVMM
VSHANPLFPT MCMAYSKSAK SGTTTVTGAD VDGTWIDLPM QQAHIAGQVI ADPRACFPGA
TLLPPFPNHT STMLPIKNNK AISVVYRHPN YKHSEFVPGL LKGVKTPRSN LSWGEIEGSF
RKTRGRNPHV MAEKFTHVRL VPPPGVNGGR GGGYGHGGER DGGYQQHGGG SRNSYEDRGR
NSNEDRGRQY DSRGRGGYGG YNDRGHRDQY GGGQQQQTHD RGRYGGGGYQ GGYHGDHRQQ
QQRNSWNGGY SHGNSRGNQP RSNAPSAPAP APAAAPQFAA PSIPAGGGQQ HAQMLALQLQ
LQQQLLAQRQ AQQAQPRGTP IGVPMRPPGP PPTSSASAPQ QQQQQQQQQQ QRPPPGNLAW
SRNLQRGGGP PSGR
//
