ID   A0A0S7DS79_9EURO        Unreviewed;      2003 AA.
AC   A0A0S7DS79;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GIM39362.1};
GN   ORFNames=ALT_007842 {ECO:0000313|EMBL:GIM39362.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM39362.1};
RN   [1] {ECO:0000313|EMBL:GIM39362.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM39362.1};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT   lentulus IFM 54703T.";
RL   Genome Announc. 4:e01568-15(2016).
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:GIM39362.1}.
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DR   EMBL; BCLY01000009; GIM39362.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7DS79; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_5024; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0010467; P:gene expression; IEA:UniProt.
DR   GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR   CDD; cd18020; DEXHc_ASCC3_1; 1.
DR   CDD; cd18022; DEXHc_ASCC3_2; 1.
DR   CDD; cd18795; SF2_C_Ski2; 2.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   PANTHER; PTHR47961:SF13; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 2.
DR   Pfam; PF02889; Sec63; 2.
DR   PIRSF; PIRSF039073; BRR2; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00490; HELICc; 2.
DR   SMART; SM00973; Sec63; 2.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 2.
PE   4: Predicted;
SQ   SEQUENCE   2003 AA;  224553 MW;  D51BABD36EF799CC CRC64;
     MDGTGPTEQW LSQLTAMREA IAALKLPKDP ATEQLSYGSD LDLDLDDDYS SPGTVDDIWD
     IISSDDETTD DLDDINGVPL PPAPSTALYD QAWLEQKCQA ITLQKPGMSA QELAGQITAS
     LATDSGDDEL QMSLAEVVGF DDLDFVIELI GHRAEILASM TSKTEAQTDG LMAGKLQTRA
     EREQALRQQD FEHKHAPLLP AQARSEPRYP HVFKTHDSRN TLALGGKRYG LPVGSKQIDE
     QRYTEFEIPA SRVGTLASSQ KLVEIKSLDG LCRGTFKGYK TLNRMQSLLY DVAYKTSENM
     LICAPTGAGK TDAAMLTILN TIGKNTVPNP IEQPDATEFA VQVDDFKIVY VAPMKALAAE
     VTEKLGKRLA WLGIRVRELT GDMQLTKREI VETQIIVTTP EKWDVVTRKS TGDTELVQKV
     RLLIIDEVHM LHDERGAVIE SLVARTQRQV ESTQSLIRIV GLSATLPNYV DVAEFLKVNK
     MAGLFFFDAS FRPVPLEQHF IGVKGKPGSK QSRENLDIVA FEKVREMLER GHQIMVFVHS
     RKDTVLTARM LRQMAVENGC EDLFSCHEHE NYSNALRDMK HARARELRDL FASGFGTHHA
     GMTRSDRNLM ERMFSEGLIK VLCCTATLAW GVNLPAAAVV IKGTQLYNPQ EGKFVDLGIL
     DVLQIFGRAG RPQFQDTGIG FICTTHDKLH HYLSAVTSQQ PIESRFSSRL VDNLNAEISL
     GTVTSVSEGV QWLGYSYLFV RMLREPRNYG IDFAEIRDDP MLVQRRRQLI IQAARVLQKS
     QMIIFNEKTE ELRAKDVGRI ASQYYVLQTS IEIFNEMMRP RSGEADVLRM ISMSGEFDNI
     QARENESKEL DRLRDEAIQT EVDGGNDSPH AKTNILLQSY ISRAKLEDFA LVSDMGYVAQ
     NAARICRALF MIALNRRWGY QCQVLLSLCK SIEKQIWPFD HPFHQFDLPQ PILKNLDEKL
     PTSSLESMRE MDVAEIGQLV HNQRMGKTLS KLLDNFPTLS VEAEIAPLNR DVLRIRLSLY
     PEFTWNDRHH GASEAYWIWV ENSETSEIYH HEYFILSRKK LHDEHELNFT IPLSDPLPSQ
     IYVRAISDRW LGAETVTPVS FQHLIRPDTE SVYTDLLNLQ PLPISALKNP ILEELYGQRF
     QFFNPMQTQI FHLLYHTSAN VLLGSPTGSG KTVACELAMW WAFREKPGSK VVYIAPMKAL
     VRERVMDWGK RLTAPMGLKL VELTGDNTPD TRTIRDADII ITTPEKWDGI SRSWQTRDYV
     RKVSLVIIDE IHLLGGDRGP ILEIIVSRMN YIASQSKGSV RLMGMSTACA NATDLANWLG
     VKEGLFNFRH SVRPVPLEIY IDGFPEQRGF CPLMQSMNRP TFLAIKSHSP EKPVIVFVAS
     RRQTRLTAKD LINYCGMEDN PRRFVRMSEE DLQLNLARVK DEALREALSF GIGLHHAGLV
     ESDRQLAEEL FANNKIQILV ATSTLAWGVN LPAHLVVVKG TQYFDAKIEG YRDMDLTDVL
     QMLGRAGRPQ FDSSGIARIF TQESKKAFYK HFLHTGFPVE STLHKVLDNH LGAEISAGTI
     ATKQDALDYL TWTFFFRRLH KNPSYYGLEI SAEEHNTMAA QAIAQDFMID LVDESLGELA
     ESSCVVFDSA TGEVDSTPFG KIMSYYYLSH KTVRYLMSHA KPNPTFHDVL SWMCSATEFD
     ELPVRHNEDL INAELARNLP LSVESMGDLP LWDPHVKAFL LLQAYMSRID LPISDYVGDQ
     TSVLDQGIRI IQASIDIMAE LGYIRACETL VSLLQSIKSA RWPEDNALSI LPGIEPATKL
     QGLPGSLVAL SSLPTTSVSG LARKLQLPAQ FTKAASYLPQ ISVSVANVSS TGITVSLSRR
     NPPTNPEHRV YAPRFPKPQT EGYFLIVCSA SADGKDGELL ALKRVSWSSN NKNQSSHSGS
     GCGSSQNSSG RNNHRNGPLT VRSSVKFPQD LLAQYTSATG KGVNIKVISD TYPGMQWVVS
     NVEVQLRPET QSVPESSNYP EKA
//