ID M9M7G9_PSEA3 Unreviewed; 1165 AA.
AC M9M7G9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=PANT_24d00013 {ECO:0000313|EMBL:GAC77035.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC77035.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
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 -!- 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; DF196790; GAC77035.1; -; Genomic_DNA.
DR AlphaFoldDB; M9M7G9; -.
DR STRING; 1151754.M9M7G9; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000011976; 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:0008270; F:zinc ion 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 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: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.
DR SMART; SM00343; ZnF_C2HC; 1.
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|PROSITE-ProRule:PRU00047};
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:UP000011976};
KW Transcription {ECO:0000256|ARBA:ARBA00022472};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00022472};
KW Transcription termination {ECO:0000256|ARBA:ARBA00022472};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 273..286
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 21..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..632
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1165 AA; 126856 MW; B6070C20439CE2B3 CRC64;
MGVPALFRWL SKKYPRIVSS VQEEENKTAP GPDGTTITLP LDTSTPNPNG EEFDCLYLDM
NGIVHPCTHP EGKPAPETEE EMMVEVFAYT ERVVSMVRPR RLLMMAIDGV APRAKMNQQR
SRRFRAAKEA REKHEETQAA LAEWRAKGLA VTEDAPKESK KAWDSNAITP GTPFMDLLAA
SLRYWVAHKI NTDPGWKDIQ VIISDASVPG EGEHKIMEHI RRQRSHPEHD PNTKHVIYGL
DADLIMLSLA THEPYFKVLR EDVFASDNKP KTCNLCGQPG HFAASCTGAA RKKSGEHDEK
AQTPPEKKPF IFLDVATLRE YLEVELNMPN LPFAFDLERA IDDWVFLIFF VGNDFLPHLP
SLEIRDGAID TLLKIWKKEL PAMGGYLTNH GKVELARAQL ILNGLASQED EIFRRRKEEE
DRRENNKKRR EDMQKRREKE LDEGNFGNGS MVQVMQKKRP ANETEKPAFN GVSAKDARDQ
ANSNNKSYDP RNKAVVLGGD NNQVVRDRNA ARQANIDAAE ALKAELMGTD ASAKPEDESE
SQPPVKKVKT EAGAEVAVDA SQQPSSEEKA SDEAGASAGT KRKADDVDAA ATDADAVTAD
DAEVKAEDDA EAKGEDDEAD DDDEEDDVGN EDVDPVTTIK KRKVNADGTV DYEDTVKMWE
PGYRERYYRE KFGVDLSDTD FRRQVVKSYI EGLSWVLAYY YQGVPSWQWY YPFHFSPFAA
DFEDLESLDI KFELGAPFKP FEQLMGVLPA DSRASIPPAF HPLMTESDSD IIDFYPSEFE
IDMNGKKMAW QGVALLPFID EKRLLDALSD KYPLLTDDEV RRNGFGNNTL FVGDESRLYE
FLCEQIYAKK RDGDDKPFEP VPMNPALSGG ITGSVKPDPV CVPGSTFNSP LTSQDLKDIH
NDRSISVLYD FPEQKTPHRS VLLKGLKPPK RVLSAAEIDW VKRGSPDTRG RGRGRGGHSG
GPGRDFHRNG ANQNGNNAAY NDAPHQGANN GFRNGAGGAG GYGGAYAQQG YQQDYGHYGA
GNGYGGSGGG YGGYGAAGYG GQGGAYGGGY GGGYGGYGSG GSGDGYGGSG GYDAYAGYSG
GGGGGYGGGY GGYAPSAPAN APTGPRRDDR YAAYTAHDGY GGGRGYGAPP TQPSRGGGRG
GGRGGGRGGN QASYGGGGGA YGSFY
//
