ID B8N5X3_ASPFN Unreviewed; 1259 AA.
AC B8N5X3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=DEAD/DEAH box helicase, putative {ECO:0000313|EMBL:EED54214.1};
GN ORFNames=AFLA_014660 {ECO:0000313|EMBL:EED54214.1};
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:EED54214.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED54214.1, 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};
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).
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DR EMBL; EQ963474; EED54214.1; -; Genomic_DNA.
DR RefSeq; XP_002375486.1; XM_002375445.1.
DR AlphaFoldDB; B8N5X3; -.
DR SMR; B8N5X3; -.
DR STRING; 332952.B8N5X3; -.
DR EnsemblFungi; EED54214; EED54214; AFLA_014660.
DR VEuPathDB; FungiDB:AFLA_001904; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_001832_4_0_1; -.
DR OMA; LFRVCNM; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50908; RWD; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:EED54214.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 307..406
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 489..665
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 724..894
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 10..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 139816 MW; 9E7C94B93E65C588 CRC64;
MSAVILKRVD PKTREATTLP PMKPPPSHKH LAAQPTALEA RHFAAVYALY RVCNMRNIHM
MLPPTYKKLW KEDFADIKTA DTKEGKGWMY EADPFLAKQE RESAAADLEK KRKEREKNQA
KAKDQPAVEL GLGSSGDNRG KRIWSNAPKV DLGSKVRREI ETLLQQHAIW NPYNVKIPES
ERNSIIEEFT RLGFRRSHVD EATSACKDRE EVLEWLLIYV PEDDLPSWCL PESYSAGVSL
ASDDLAREAK IKRLATIGYS ADLCSRALDS KQGDELATAE MLQHTLVYGT SSTAGAVSSE
GDDSWAEEQE TLEAIFGERY IKVSPKVCEI KSESSDLPES TTFRFQRPSN HYPSSVPIIS
IQAKGIPSYI RLSAIRQAVK HAEENFLGEP MVYNVLDWLE MHLPEIMQNP GKLRDIATVA
ATPSTTGSIL ELPVRQSRKK SREISWQPGS PQSISVREAW QARQSTPAQQ DMTRKRESLP
AWNIQDAIVR AVNSHQVTII SGETGSGKST QSVQFILDDM IRRDLGGIAN IICTQPRRIS
ALGLADRVSD ERCTSVGDEV GYVIRGDSKV KSGATKITFV TTGVLLRRIQ SGSGADGNVA
GSLADVTHIV VDEVHERSLD TDFLLALLRD VLRYRKDIKV ILMSATLDAE IFINYFGGRQ
NVGLVNIPGR TFPVSDFYLD DIIRDTGFSP ELAERDFEED SSPQGEESLG KILRNMGMGI
NYELITSTVR YVDAQLGDQP GGILIFLPGT LEIERCLNAV KRIPNVHPLP LHASLLPAEQ
RRVFLSPPKG KRKVIAATNV AETSITIEDV VAVIDTGRVK ETSYDPKDNM VRLQEVWASQ
AACKQRRGRA GRVRAGACYK LYTRQAENKM APRPDPEIRR VPLEQLCLSV KSMQGINDVA
TFLANTITPP ESVAVEGALG FLHRVGALDH DKLTALGRYL SMIPADLRCA KLMVYGSIFN
CIDHCITISA ILTVKSPFVS PRDKREDANA AKASFSRGDG DLLTDLTAYQ QWSERVKAQG
YWQTQSWCSA NFLSHQTLRD ISSNKAQLLT SLKDAGLLPV DYSSDSADPR WNRNAGNRSL
LRALIAGAFQ PQIAQISFPD KKFMSSVTGT VEVDPDARTI KYFNQENGRV FIHPSSLLFS
AQSYPGSAAY LSYFTKMATS KVFIRDLTPF NAYSLLLFCG SIDLDTTGRG LIVDGWLRLR
GWARIGVLVS RLRMMVDEII AARIDNPASL SIDRAGKDDI TGRVIEVVKR LIELNGLDQ
//
