ID Q0CVF4_ASPTN Unreviewed; 1344 AA.
AC Q0CVF4;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=DEAD/DEAH box helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ATEG_02330 {ECO:0000313|EMBL:EAU37292.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU37292.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CH476596; EAU37292.1; -; Genomic_DNA.
DR RefSeq; XP_001211508.1; XM_001211508.1.
DR STRING; 341663.Q0CVF4; -.
DR EnsemblFungi; EAU37292; EAU37292; ATEG_02330.
DR GeneID; 4317179; -.
DR VEuPathDB; FungiDB:ATEG_02330; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_001832_4_0_1; -.
DR OMA; LFRVCNM; -.
DR OrthoDB; 53793at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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; IPR015940; UBA.
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 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.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963}.
FT DOMAIN 329..369
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 390..489
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 572..748
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 808..978
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1344 AA; 149107 MW; 5D086E27BC5DA3EC CRC64;
MGPKKKGDAR GGPKPRDLSK PKLRLNGRQK TAKKPQAPTE EPKKAICEAD DRRRLLGLAK
FAGEYAVGAL SEAEMGEARV YNGYVSSVIL KRVDPKTRET ITLPPMRLPP SHRHLAAQAT
ALEARHFAAT YALYRVCNMR NLHMMLPPTY KELWKNEFAQ LKAADTKEGK GWMYEADPFL
AKQERESAAA DLEKKRKERE KTQAKSKETR IDLGLGSSGG DNKGRRLWSN APKVDLGSKA
RREIEGLLRQ HAIWNPYNVR IPEAECKTII NEFTGLGFRR SHVEEATAAC KDREEVLEWL
LIYVPEDDLP SWCLPEGYSA GVSLASDDLA RESKTKRLAS MGYPADICSR ILDSNKGDEL
AAAEFLQTTL VHGEVSPVGS TSSDEDSWDE EQETLEAIFG ERYSRRSPKV CEIKGEDSDL
FEALSFRFQR PSGHYPSSVP VISIQAKSIP SYIRLSAIRQ AVKHAEENFL GEPMIYNILD
WMESNLPLIM DNPGKLRDIS TVTASQTTTG TTMELPTRQS RKKAKQLSWQ PESPQSVSLR
EAWEARQTTK AQQEMTRKRQ SLPAWNIQDA IISAVNTNQV TIISGETGSG KSTQSVQFVL
DDMIRRGLGA IANIVCTQPR RISALGLADR VSDERCSSVG DEVGYVIRGD SKVKSGVTKI
TFVTTGVLLR RIQSASGADG NVAGSLSDVT HVVVDEVHER SLDTDFLLAL LRDVVRHRKD
IKIILMSATL DADIFIKYFG GRQNVGLVNI PGRTFPVEDY YLDDVVRDTG FSPELTERDF
EDDMPSSQGE ESLGKLLRSV GMGINYELIA STVRYIDAQL GDKPGGILIF LPGTLEIDRC
LNAVKRIPNA HPLPLHASLL PAEQRRVFLA PPKGKRKVIA ATNVAETSIT IEDVVAVIDT
GRVKETSYDP KDNMVRLKEV WASQAACKQR RGRAGRVRAG TCYKLYTRKA EANMAPRPDP
EIRRVPLEQL CLSVKSMQGI DDVATFLANT ITPPESIAVE GALSFLHRVG ALDHDRLTAL
GRYLSMIPAD LRCAKLMVYG SIFGCIDACV SIAAILTVKS PFVSPRERRD EADAARASFS
RGDGDLLTDL AAYQQWSERV QAHGYWQTQS WCSANFLSHQ TLRDISSNKA QFLTSLKDAS
ILPVDYAESD PRWNRNSSNR SLLRALVAGA FQPQLAQISF PDKKFASSVT GTVEIDPDAR
TIKYFNQENG RVFIHPSSLL FSAQSYSGAA AYLSYFSKMA TSKVFIRDLT PFNAYALLLF
CGSIDLDTMG RGLIVDGWLR LRGWARIGVL VSRLRMMLDE IIAARIDRPP TLTAVEDKCG
GTDSTADQVI EVVKRLIEFN GLDQ
//
