ID B8N676_ASPFN Unreviewed; 1072 AA.
AC B8N676;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Regulator of nonsense transcripts, putative {ECO:0000313|EMBL:EED54588.1};
GN ORFNames=AFLA_018400 {ECO:0000313|EMBL:EED54588.1}, G4B84_006392
GN {ECO:0000313|EMBL:QMW31011.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED54588.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED54588.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC {ECO:0000313|EMBL:EED54588.1};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2] {ECO:0000313|EMBL:QMW31011.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW31011.1,
RC ECO:0000313|Proteomes:UP000515286};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
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DR EMBL; EQ963474; EED54588.1; -; Genomic_DNA.
DR EMBL; CP059869; QMW31011.1; -; Genomic_DNA.
DR RefSeq; XP_002375860.1; XM_002375819.1.
DR AlphaFoldDB; B8N676; -.
DR STRING; 332952.B8N676; -.
DR EnsemblFungi; EED54588; EED54588; AFLA_018400.
DR VEuPathDB; FungiDB:AFLA_002303; -.
DR eggNOG; KOG1802; Eukaryota.
DR HOGENOM; CLU_001666_4_0_1; -.
DR OMA; VRSNDNQ; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd21407; 1B_UPF1-like; 1.
DR CDD; cd18039; DEXXQc_UPF1; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR CDD; cd21400; ZBD_UPF1-like; 1.
DR Gene3D; 2.40.30.230; -; 1.
DR Gene3D; 6.10.140.1240; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR040812; UPF1_1B_dom.
DR InterPro; IPR018999; UPF1_CH/ZBD.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF364; REGULATOR OF NONSENSE TRANSCRIPTS 1; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF18141; UPF1_1B_dom; 1.
DR Pfam; PF09416; UPF1_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51997; UPF1_CH_RICH; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01341}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01341};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01341}.
FT DOMAIN 58..215
FT /note="Upf1"
FT /evidence="ECO:0000259|PROSITE:PS51997"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..98
FT /note="C3H"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 80..108
FT /note="CC/SHH/C"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 126..156
FT /note="C4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 118040 MW; EE136375AC2D3E6F CRC64;
MAALGDDSRE LDDITGGLRP RRHDDDDDGS DNGDDDLEST TSAPAAENAE NQRHTEEEKE
LPPHACAYCG IHNPSSVVKC LSCSKWFCSA RGNTSSSHIV NHLVRARHKE VQLHPASSLG
DTILECYNCG TKNVFLLGFI PAKSDTVVVL LCRQPCAAMP SSKDMNWDTS RWQPLIEDRS
FLPWLVAAPS DQEQLRARHL SPQLIAKLEE MWKENSQATF SDLEKATAVD DEPAPVLLRY
DDAFQYQNIF GPLVKIEADY DRKLKESQSQ DGLIVRWDLG LNNKHLASFI LPKLELGDVK
LAVGDEMRLK YTGELRPKWE GVGYVIKIPN NQSDEVTIEL RAKGDHKSVP TECTHNFTAD
YVWKSTSFDR MQLAMKTFAV DEMSVSGYIF HRLLGHEVAA APMKTQMPKK FSVPGLPELN
GSQINAVKSV LQRPLSLIQG PPGTGKTVTS ATIIYHLAKL NGGQVLVCAP SNVAVDQLCE
RIHRTGLKTV RVTAKSREDV ESPVGFLSLH EQVRLNDSNI ELLKLNQLKA ELGELSSQDE
KRLKQLTRSA EREILNNADV ICCTCVGAGD PRLAKLKFRT VLIDESTQSA EPECMIPLVL
GCKQVVLVGD HQQLGPVIMN KKAAKAGLNQ SLFERLVILG CSPIRLNVQY RMHPCLSEFP
SNMFYEGSLQ NGISSIERLR RDVDFPWPIS DNPMMFWSNL GNEEISASGT SYLNRTEATN
VEKIVTRFFK AGVQPGDIGI ITPYEGQRSY IVSSMQATGT FKKEHYKEIE VASVDAFQGR
EKDFIILSCV RSNDHQGIGF LSDPRRLNVA LTRAKYGLAI LGNPKVLSKH PLWNCLLQHF
KERHCLVEGP LSNLQESLIQ FSRPKQAYRG PQRFQMAYNH ASSVTSGMMN GKNGHRNDFH
DTGSVVGYIP DDVSSVHSSA LGGVGIPSGY PPMFQNFADS WPALPGNRRA NGNRGKGAPS
IAGESIAATE SDVTASIIDG KSVDQGGVSL AGLSIHDMSK QPSLSQSDRL KRYVESGGRE
PYKPGVADNN SIFGGSSASI RVTRGVPGHI IDDDDTRSVS TAFASQVGGN YD
//
