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Database: UniProt
Entry: A0A4V2K9K2_9APHY
LinkDB: A0A4V2K9K2_9APHY
Original site: A0A4V2K9K2_9APHY 
ID   A0A4V2K9K2_9APHY        Unreviewed;      1182 AA.
AC   A0A4V2K9K2;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE            EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN   ORFNames=BD310DRAFT_915552 {ECO:0000313|EMBL:TBU64238.1};
OS   Dichomitus squalens.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Dichomitus.
OX   NCBI_TaxID=114155 {ECO:0000313|EMBL:TBU64238.1, ECO:0000313|Proteomes:UP000292082};
RN   [1] {ECO:0000313|EMBL:TBU64238.1, ECO:0000313|Proteomes:UP000292082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 464.89 {ECO:0000313|EMBL:TBU64238.1,
RC   ECO:0000313|Proteomes:UP000292082};
RG   DOE Joint Genome Institute;
RA   Lopez S.C., Andreopoulos B., Pangilinan J., Lipzen A., Riley R.,
RA   Ahrendt S., Ng V., Barry K., Daum C., Grigoriev I.V., Hilden K.S.,
RA   Makela M.R., de Vries R.P.;
RT   "Draft genome sequences of three monokaryotic isolates of the white-rot
RT   basidiomycete fungus Dichomitus squalens.";
RL   Submitted (JAN-2019) 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   -!- 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; ML145087; TBU64238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4V2K9K2; -.
DR   STRING; 114155.A0A4V2K9K2; -.
DR   Proteomes; UP000292082; 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   Pfam; PF00098; zf-CCHC; 1.
DR   PIRSF; PIRSF037239; Exonuclease_Xrn2; 2.
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:UP000292082};
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          271..284
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          116..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          953..1079
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1114..1182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..427
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..639
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..659
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        959..980
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1008..1058
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1182 AA;  129815 MW;  4440032BD38C6087 CRC64;
     MGVPALFRWL SKKYPKIILP VIEAEQATIP DTEGNEVAVP VNIADPNPNG VEFDSLYLDM
     NGIVHPCTHP EGKPAPETEE EMMIEIFSYT ERVVNMVRPR KLLFMAIDGV APRAKMNQQR
     SRRFRSAQEA KEKEEARKES IAMWEAMGKT LSEEEKNKKA WDSNAITPGT PFMDLLASSL
     RYWVVYKMNT DPGWKDVQVI ISDASVPGEG EHKIMDFIRR QRSNPGHDPN THHVIYGLDA
     DLIMLSLATH EPHFRVLRED VFHQEGSRTA CRICGQEGHY AAQCTGTKAE IKKTPPEKKP
     FIFLDVAILR EYLEAELNVP NVPFPFNFEQ AIDDWVLLIF FVGNDFLPHL PSLEIREGAI
     DTLLKIWRTE LPRMGGYITN HGQLELSRAQ IILEGLARRE DEIFRRRRED EERQDQNAKR
     RKIEKEAGSN GASAGPSPSL NLTVAPVAPG SLPPRPDFAA KADSIGLGGP KNADTDTHTP
     TASLALAGSN RDVVANRAAI RLANMSAAEM LKAEMASLIP LKPSKSATKS STTANSAPPP
     PVVASAPARE PSSAPDATIT ATVTTTDDAD IPGLGGMTPV SSSTTVFETP MSVEPVPPVE
     DGTDDVDGEE IPAEAEDSFM TDATETELHG VKRSIDEVEA EDAEDPEDLG PSDDDDAPAE
     AETSYVLKVN PDGTVDQEDQ VKLWEPGYRE RYYSQKFGAE YSDKEFRKQV TKSYIEGMAW
     VLQYYYQGTP SWHWYYPFHF APFAADFEDL DKMDIDFTLG QPFKPFEQLM GVFPASSRSH
     IPATFHDLMT EDTSPIIDFY PSTFQIDMNG KRMAWQGVAL LPFIDEKRLL DAMGPRYPNL
     SDDEKRRNQW GNNFLFVYEA HALYPTLEAL YGKRKKDEPL PINPKLSKGI NGSLLPNPDC
     IPDSTYFSPL PSQDLPNIKN DRSLSAFYFF PKQLTPHRSI LLPGVRRPQP VLNAHDLEVA
     RRGGPERGRG RGRGGFHSER GGRDNYGGYN NQSRGFRPGG GEDRYQNGGS YQPYQQQSSY
     NNGGYQQQQS YQAYQSYQRG RGGYQQPSSN SSRGQYDDFT APSRGGRGGG RGSYGRGGAA
     YTNGPPGGYG NQGGGYGGGG RGGGYGGYGG GGNNYNQGGG GYGQGGYNPG GGYGGQAGYT
     AGGNYGYGGN QQSNGYGGGG GGGYGNSRGG YNNRGRGRGG RY
//
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