ID D4ALN0_ARTBC Unreviewed; 1038 AA.
AC D4ALN0;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=ARB_05228 {ECO:0000313|EMBL:EFE36289.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE36289.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. May promote
CC termination of transcription by RNA polymerase II.
CC {ECO:0000256|PIRNR:PIRNR037239}.
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. Required for the
CC processing of nuclear mRNA and rRNA precursors. May promote termination
CC of transcription by RNA polymerase II. {ECO:0000256|ARBA:ARBA00025537}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EFE36289.1}.
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DR EMBL; ABSU01000002; EFE36289.1; -; Genomic_DNA.
DR RefSeq; XP_003016934.1; XM_003016888.1.
DR AlphaFoldDB; D4ALN0; -.
DR STRING; 663331.D4ALN0; -.
DR GeneID; 9526574; -.
DR KEGG; abe:ARB_05228; -.
DR eggNOG; KOG2044; Eukaryota.
DR HOGENOM; CLU_006038_1_1_1; -.
DR OMA; CLHYYVH; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000008866; 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:SF41; 5'-3' EXORIBONUCLEASE 1; 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; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008866};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW Transcription {ECO:0000256|ARBA:ARBA00022472};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00022472};
KW Transcription termination {ECO:0000256|ARBA:ARBA00022472}.
FT DOMAIN 1..259
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 331..853
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT REGION 412..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..559
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 115781 MW; 0FDFD626079755E4 CRC64;
MGVPALFRWL SSKYPKIVSA VVEEQPQEID GQEIPVDITK PNPNGEEMDN LYLDMNGIVH
PCTHPEGKPP PANEGEMMLE IFKYTDRVVN MVRPRKVLMI AVDGVAPRAK MNQQRSRRFR
SAQDAKAEDE KKVEFAKLLK KQKRGKKDVT ITEEVITKTW DTNVITPGTP FMDILALALR
YWVAYKLSTD PGWEKLKVII SDATVPGEGE HKIMEFIRSQ RACPEYDPNT RHVIYGLDAD
LIMLGLGTHE PHFRVLREDV FFQESKARTC KLCGQAGHVE EACTGKAKEK RGEFDEKQKG
NPLKPFIWLH VSVLREYLAV EMQVPQQPFP FDLERALDDW VFMCFFVGND FLPHLPSLEI
RENGIDTLIA IWRDNIPQMG GYLTKDGRVD LAKAQLILQG LAKQEDAIFR RRRQTEERRN
ANAKRRQEED RQRRNNNNDH ARKKRRGSRG AEPVPDIPPL VVPGKGELSR AERELTHAMV
VNRGAVYKAN MANKSAAAAL KAQLLSGGTA EDGVDTTNAQ DSAPSGIPGS KLGKRKSDVF
ENSNTEAEAE EEDEEEEDTV EVPAKPKEDE MPPDTVRLWE DGYADRYYEQ KFGVSPKDIA
FRHKVARAYV EGLSWVLLYY FQGCPSWTWY YPYHYAPFAA DFVDIGEMDV QFTKGTPFKP
FEQLMGVLPA ASNHAIPEVF RDLMSDENSE IIDFYPEDFP VDLNGKKFAW QGVALLPFID
EKRLLAAMGK RYHLLSEEEQ ARNAMGKDVL LLSEKHPLYE SLTANFYSKK QVSSKLKLNM
RISEGLGGKV EKNESYLPHS SLSLEVDGAD IPALDEDRSI SVYYEMPRSM HTHKSMLLRG
VKFKEPALDK ADLEITRNKA RHSGRSFGGA PLHSSRGGRG RGGGRGGGQI SYASNDRPNP
FAAHVAPGYI PPPHMGGGPP GYNPAPPNMY NGPDRYRSQG GYPRGGGGGG GGGYGGGYGG
HYQQPPPHSW AQHDGPAYNH PPRNAYQDRA HYQRGGSSGY GRGGGGGGGS YDGRGGGGYY
GSRGSGRGRG RGDGYGRY
//