ID A0A0S7DYZ0_9EURO Unreviewed; 1079 AA.
AC A0A0S7DYZ0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAF4182412.1};
GN ORFNames=CNMCM8060_006816 {ECO:0000313|EMBL:KAF4182412.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:KAF4182412.1, ECO:0000313|Proteomes:UP000713487};
RN [1] {ECO:0000313|EMBL:KAF4182412.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4182412.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [2] {ECO:0000313|EMBL:KAF4182412.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4182412.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-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}.
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:KAF4182412.1}.
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; JAAAPS010000004; KAF4182412.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DYZ0; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_8162; -.
DR Proteomes; UP000713487; Unassembled WGS sequence.
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 REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..105
FT /note="C3H"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 87..115
FT /note="CC/SHH/C"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 133..163
FT /note="C4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 1053..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 118658 MW; B5A1155B412C8B36 CRC64;
MAAIGDGRAP ADLDETTLNM TGGPRPRRHD DEDDGSDNYG DDDVDSVTSA AVTGRRQNEG
NLEEEKELPP HACAYCGIHN PSSVVKCLAC SKWFCSARGN TSSSHIVNHL VRARHKEVQL
HPASSLGDTI LECYNCGTKN VFLLGFIPAK SDTVVVLLCR QPCAAMPSSK DMNWDTSRWQ
PLIEDRSFLP WLVAAPSDQE QLRARHLSPQ LIAKLEEMWK ENSQATFADL EKATAVDDEP
APVLLRYDDA FQYQNIFGPL VKIEADYDRK LKESQSQDGL IVRWDLGLNN KHLASFILPK
LELGDVKLAV GDEMRLKYTG ELRPKWEGVG YVIKIPNNQS DEVTIELRAK GDHKSVPTEC
THNFTADYVW KSTSFDRMQL AMKTFAVDEM SVSGYIFHRL LGHEVAAAPM KTQLPKKFSV
PGLPELNGSQ INAVKSVLQR PMSLIQGPPG TGKTVTSATI IYHLAKINGG QVLVCAPSNV
AVDQLCERIH RTGLKTVRVT AKSREDVESP VGFLSLHEQV RLNDSNIELI KLNQLKAELG
ELSSQDEKRL KQLTRSAERE ILNNADVICC TCVGAGDPRL AKLKFRTVLI DESTQSAEPE
CMIPLVLGCK QVVLVGDHQQ LGPVIMNKKA AKAGLNQSLF ERLVILGCSP IRLNVQYRMH
PCLSEFPSNM FYEGSLQNGV SAFDRLRRDV DFPWPVVDSP MMFWSNLGNE EISASGTSYL
NRTEATNVEK IVTRFFKAGV QPADIGIITP YEGQRSYIVS SMQANGTFKK EHYKEIEVAS
VDAFQGREKD FIILSCVRSN DHQGIGFLSD PRRLNVALTR AKYGLVILGN PKVLSKHPLW
NCLLQHFKER HCLVEGPLSN LQESLIQFSR PKQSYRGPQR FQMAYNHASN VTSGMMNGRN
GHRNEFHDTG SVIGYIPDDV SSVHSSALGG VSIPSGYPPM FQNFADAWPA LPGARRANGA
RGKGAPSVAG ESVAATESDI TGSIIDGRSV DQGGVSLAGL SINDMSKQPS LSQSDRLKRY
VESGGREPYR AGVPDNGSIF GGSSASIRVT RGVPGHVHDD DDTRSVSTAF ASQVGGNYD
//
