ID A0A0A2VX51_BEABA Unreviewed; 1083 AA.
AC A0A0A2VX51;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Regulator of nonsense transcripts 1 {ECO:0000313|EMBL:KGQ05334.1};
GN ORFNames=BBAD15_g9403 {ECO:0000313|EMBL:KGQ05334.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ05334.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ05334.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ05334.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGQ05334.1}.
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DR EMBL; ANFO01000955; KGQ05334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VX51; -.
DR STRING; 1245745.A0A0A2VX51; -.
DR EnsemblFungi; BB8028_0004g03980.1; BB8028_0004g03980.1; BB8028_0004g03980.
DR eggNOG; KOG1802; Eukaryota.
DR HOGENOM; CLU_001666_4_0_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR006935; Helicase/UvrB_N.
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; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF18141; UPF1_1B_dom; 1.
DR Pfam; PF09416; UPF1_Zn_bind; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51997; UPF1_CH_RICH; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
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 Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01341};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01341}.
FT DOMAIN 86..243
FT /note="Upf1"
FT /evidence="ECO:0000259|PROSITE:PS51997"
FT REGION 38..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..126
FT /note="C3H"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 108..136
FT /note="CC/SHH/C"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 154..184
FT /note="C4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 969..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 120061 MW; 9749C1FF9E27B21D CRC64;
MEGAFTHVGN HLVSDSAAAI NAGNDDLSTL DPDERLLYGK YSDHGGRRRA DDDDNQTETF
EDDNDSLASI PVDEMVGLNL KNTDEEKELP AYACAYCGIH APASVVKCLV CNKWFCSARG
NSTSSHIINH LVRARHKEVQ LHPESALGDT ILECYSCGTK NSFLLGFIPA KSDSVVVLLC
RQPCAASASN KDMNWDPSRW EPLIKERAFL DWLVSAPSEA EQLRARHMSP NTIARLEEMW
KLEPNATISD LDKGQTVDDD PDPVLLKYDD AFHYQNIFGP LVKMESDYDK KLKEAQSEDN
LTVEWSQGLN NKHLATFNLR KIESGEVKLA VGDEMLLRYN GELREPWQGV GYVMKIPNSQ
SDEVCLELRK NGNDRSVPTD LSHNFSADYV WKATSYDRMQ LAMKTFAVDD MSVSGFIFHT
LLGHDVQLQP MKSNLPKKWS APGLPDLNQS QVDAIRSVLQ KPLSLIQGPP GTGKTVTSAT
IIYHLSKISG NQVLVCAPSN VAVDQLCERI HRTGLKVVRL TAKSREDVES SVSFLALHEQ
VRMSEHNSEF AKLSQLKNEA GELSSQDEKK FRQLTKAAER EILNNADVVC CTCVGAGDPR
LSKLKFRSVL IDESTQSAEP ECIIPLMLGC KQVVLVGDHK QLGPVIMNKK AAKAGLSQSL
FERLMQLRLQ PILLNTQYRM HPCLSEFPSN MFYDGSLQNG VTQEQRIRKD VDFPWPVAEM
PMMFWSNIGN EEISTSGTSY LNRTEASNVE KIVTRFFKAG VKPSEIGVIT PYEGQRSYIV
TTMQNAGTSK KEYYKSVEVA SVDAFQGREK DFIVLSCVRS NENQGIGFLS DPRRLNVALT
RAKYGVVILG NPRVLSKHEL WYNLLTHFRD RRCFVEGPLT NFQQCLLQFS KPRSHRQKLG
NQIPTGGYQN QNGRFHGSST IRDFDSSSMM SYVPDDVSSI HGSTFGGAAL NSAYPSMFSN
FAPEQWPGLP GVGAHGHRSG KSRARTAESV AGESVANSET TDTSSSIIGS RGVGQGGVSL
GAGLQDAVTG MRAISYTQSD RLRQYVESGA RNPPNNRYGS RRHDDDDRSV STAFHSQVGG
GYD
//
