ID A0A177WX05_BATDL Unreviewed; 1094 AA.
AC A0A177WX05;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=BDEG_27224 {ECO:0000313|EMBL:OAJ43910.1};
OS Batrachochytrium dendrobatidis (strain JEL423).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=403673 {ECO:0000313|EMBL:OAJ43910.1, ECO:0000313|Proteomes:UP000077115};
RN [1] {ECO:0000313|EMBL:OAJ43910.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ43910.1,
RC ECO:0000313|Proteomes:UP000077115};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Cuomo C., Devon K., Jaffe D., Butler J.,
RA Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA O'Leary S., Kodira C., Zeng Q., Yandava C., Alvarado L., Longcore J.,
RA James T.;
RT "The Genome Sequence of Batrachochytrium dendrobatidis JEL423.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAJ43910.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ43910.1,
RC ECO:0000313|Proteomes:UP000077115};
RA Cuomo C.A., Farrer R.A., James T., Longcore J., Birren B.;
RT "Lineage-specific infection strategies underlie the spectrum of fungal
RT disease in amphibians.";
RL Submitted (MAY-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 -!- 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}.
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DR EMBL; DS022311; OAJ43910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177WX05; -.
DR STRING; 403673.A0A177WX05; -.
DR VEuPathDB; FungiDB:BDEG_27224; -.
DR Proteomes; UP000077115; 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; -; 1.
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 InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR12341:SF41; 5'-3' EXORIBONUCLEASE 1; 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 SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000077115};
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};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 173..186
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 314..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 122388 MW; 9CCB4EA36B80F7EB CRC64;
MHSLYCNQSL DGVAPRAKMN QQRSRRFRAA QEEQQKKDAE DRIRKQLMED GHTQAETVKK
AHFDSNCITP GTPFMDQLAI CLRYYVAKKL SEDAGWNGLK VIISDASIPG EGEHKIMDYI
RRQRNQPGYD AQTHHVLYGL DADLIMLALA THEPHFNILR EDVFFKDGKQ NGCFICGKVG
HMAWQCTGKK ADNANQIAEK TIATGEKPYI FLHVNVLREY LEVELSVPNL SFEWDFERAI
DDWVFLCFFV GNDFLPHLPS LEIREGAIDQ LIKLWKQYLD QWGGFLTDSG DLELKRVQEL
MIELGKVEDA TFQKRREEEE RRRQNRIRRK QDTKNRLEGH GRNNRAESHK RFPTDEPIEI
LEQMTDLEVL PVRGTDPKKR GDLNRKAVKI ASGTKKENLA AAEVLRNRLA ASKSATLSAD
NSSKPDQDAA VVSSKKSASG KKRTVDEAQA LSESDKGDTS TKTQSISDHS SKRVAMDATL
DGSDNPIETD EMEEIVVEST SVAAIPPKPV LVPVPVEAAT PTAQVDSDDE APADDVRLWE
SGWKQRYYRT KFQVELDDTS FREQVVTSYV EGLCWVLKYY YQGVQSWKWY YPYHYAPFSS
DCDFIGRLDI KFELGTPFLP VEQLMGVLPA ASMQHIPPPL RPLMTEPSSN IIDFYPVDFP
IDLNGKKYSW QGVALLPFID ENRLLKAIVP IYNQFSEDEK RRNTLGHEIV VVGATHPLFD
DFCGLYGHGG HTKMVPLDPV RSDKFFGFVE PEDTFTAPGS SFESPLEDLG MTAIESNNSL
SAKYFMPVTP AGYKYLARLL PQVQFPKKVL DESDRHAVRV GYNSQRNGRR GGSVRINRGG
AQRVTGMGPG NNGHNGGGYA HSRGGYNDRN SHRGGYQNGQ PHRALHASNG SEQPYMGGGG
YGSYSDHGRN LSGNHGAAYT PSNYSYGNNQ YESQSNYSNN PSRGGPPSYG NNGRSGSSRG
GYSHHQQQEH GHGQHRNQYQ QSNYGGGYAQ QYPASEGQFG NNQPQQGAAI VTNLLNQLSG
DSHGQHRPPQ HEGYQNSWSS YEAPHNPASR GGHHPHSAQT SQHPAGNIGW NRNVSNGQRG
RGSRGGRGSH RGQR
//
