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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//