ID A2R8R8_ASPNC Unreviewed; 1961 AA.
AC A2R8R8;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Contig An16c0240, genomic contig {ECO:0000313|EMBL:CAK47061.1};
DE Flags: Fragment;
GN ORFNames=An16g08120 {ECO:0000313|EMBL:CAK47061.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK47061.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK47061.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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DR EMBL; AM270376; CAK47061.1; -; Genomic_DNA.
DR RefSeq; XP_001398110.1; XM_001398073.1.
DR EnsemblFungi; CAK47061; CAK47061; An16g08120.
DR GeneID; 4989203; -.
DR KEGG; ang:An16g08120; -.
DR VEuPathDB; FungiDB:An16g08120; -.
DR HOGENOM; CLU_000335_1_0_1; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000006706; Chromosome 5R.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR CDD; cd18019; DEXHc_Brr2_1; 1.
DR CDD; cd18021; DEXHc_Brr2_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; 1.
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; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR048863; BRR2_plug.
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; 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:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF21188; BRR2_plug; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
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; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
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; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 545..729
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 768..976
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1396..1572
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 51..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..215
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..261
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1961
FT /evidence="ECO:0000313|EMBL:CAK47061.1"
SQ SEQUENCE 1961 AA; 221117 MW; C1B41CFCF12BD587 CRC64;
MADQNISQYK YSAMSNLVLQ ADRRFISRVN DEPTGDPESL AGRISIREMG GRMARDDAPK
TKKKTVGPTD IERGAIREGE DVLAREQRKT QRGQPAQLRG QGILSAADAL VEGLKYRPRT
PATRATYDLI LTMTATHLGD VPHEVVRSAA DAVLELLKDE EMKDFDKKKE IDDLLGSSMN
PKEFNELVNL GKKITDYDAQ DEDEEMGEGL EGEGEGELDE RQGVAVVFDE EDEDDERMGT
VDEIRDDDEL SEDEEADQQE ATGIDETTTE KADLEGLEEA EEMVIDGGVG RDADRRDKGS
TIPAREIDAY WLQRQIGAAY SDAHIQHEKA TQALDILGGQ GEDGAERPLR DVENDLMELF
DYENPDLVAK LVTNRDKIVW VTRWRRVAED ADARHLVESE MVEAGHRQIL DEIRGKSTRS
EGAGRPEKKI KLDLMDVDVP SAPQQAEEKP TEGGLVRGLQ PKRLINLENL VFHQGNHLMT
NPNVKLPQGS TKRTFKGYEE IHVPPPQAKR EPGEKNIPAT ELPEWARVGF GSAKELNRVQ
SKCFPSAFHD DGNMLVCAPT GSGKTNVAML TILREIGKNR NPETGEIMLD DFKIIYISPL
KALVQEQVGN LGKRLEPYGI KVAELSGDRQ LTKQQIAETQ IIVTTPEKFD VITRKASETS
YTRLVRLVVI DEIHLLHDDR GPVIESIVSR TIRKVEQTGD PVRIVGLSAT LPNYRDVASF
LRVDPLKGLF HFDGSYRPCP LKQEFIGVTD KKAIKQLKTM NDICYNKVLE QVGQRRNQML
IFVHSRKETA KTAKYIRDKA LEMETIGQIL RSDAASRAIL AEEAETVDDP SLKDLLPYGL
GIHHAGLSLA DRDSVQALFS DGSIQVLVCT ATLAWGVNLP AHTVIIKGTQ IYSPEKGSWV
ELSPQDVLQM LGRAGRPQYD TFGEGIIITS QTEIQYYLSL MNQQLPIESQ LMSKLADNMN
AEIVLGNIRT RDEGVDWLGY TYLFVRMLRS PGLYSVGADY EEDEALEQKR VDLVHSAAVI
LERAGLVKYD KKTGRLQSTE LGRIASHYYI GHNSMLTYSQ HIQPSITPIE LFRIFALSDE
FKYIPVRQDE KLELAKLLGR VPVPVKEGID EPHSKINVLL QAYISRLKLE GLALMADMVY
VTQSAGRILR ALFEISLKKG WSSVAKTALN LCKMAERRMW PTMTPLRQFP TCPRDILQKA
ERIDVPWASY FDLDPPRMGE LLGMPKAGRV VCDLVSKFPR LEVQAQVQPV TRSMLRVELT
ITPNFVWDEA LHGNAQDFWI LVEDCDGEEI LFHDQFLLRG DIAQSEMNEH LVEFTVPITE
PMPPNYFISL VSDRWMHSET KIAVSFQKLI LPERFPPHTP LLDMQRAPVK ALKRDEYQQL
YPEWQYFNKI QTQTFKSLFD TDDNVFIGAP TGSGKTVCAE LALLRHWTQE DSGRAVYIAP
FQELVDQRLA DWEKRLSNIA GGKTIVKLTG ETTADLRLLE RADLVLATPT QWDVLSRQWR
KRKNVRAVQL FIADEIQMLG GYGGYVYEVV VSRMHSMALE TESGMRIVGL SVPLANARDL
GEWIGANKHT IYNFSPHARP VPLELHIQSF TIPHFPSLML AMARPAYLSI LQLSPDKPAI
VFVPSRKQTR ATAMDLLAAC ATDDDEDRFL NADVNELAPL LSRINERTLA ESLTHGIGYY
HEALSPTDKR IVSHLFSIGA IQVLLASRDV CWELNLTAHL VIVMGTQFFE GREHRYIDYP
ISEILQMFGK ASRPGEDKIG RGVLMVPAVK REYYKKFLNE ALPVESHLQA YLHDAFVTEI
STRTIGSTQD AIDWMTHTYF YRRLLANPSF YGLTDVSHEG LSTFLSELLE NTLKELSDAK
IVDLDEEDDS VSPLNAAMIG SYYNISFITM QTFLLSLSAR TKLKGILEIV TSATEFESIQ
MRRHEDHILR RVYDRVPVKM SQVAYDSPHF KAFVLLQAHF S
//
