ID A0A1S9DN25_ASPOZ Unreviewed; 1454 AA.
AC A0A1S9DN25;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=OAory_01062900 {ECO:0000313|EMBL:OOO10482.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO10482.1, ECO:0000313|Proteomes:UP000190312};
RN [1] {ECO:0000313|EMBL:OOO10482.1, ECO:0000313|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000313|EMBL:OOO10482.1,
RC ECO:0000313|Proteomes:UP000190312};
RA Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA Jeennor S., Laoteng K.;
RT "Genome sequencing of Aspergillus oryzae BCC7051.";
RL Submitted (OCT-2016) 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:ARBA00001665};
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:OOO10482.1}.
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DR EMBL; MKZY01000004; OOO10482.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:AO090003000433; -.
DR eggNOG; KOG0952; Eukaryota.
DR Proteomes; UP000190312; 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; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
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; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02889; Sec63; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
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:UP000190312}.
FT DOMAIN 243..417
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 457..645
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1454 AA; 164340 MW; 853B40147224EC9C CRC64;
MRRKPYSSFP ASRQGASYRR TAGTQLRTPI RSDVRTALDQ RFSEGARNSS SLGGSRREEL
PISTPRAEAL CRDDDLLFDA FVDEDLELLA QSDESARTRQ SIFSTTESQL HTREEPQNGA
PALVSRYFCE TPHLTPYQSV ASSSSDIEIR SPSSPLLRLQ AERTRPYLAQ DNDSKGRYQD
HQLRPEQFEK SHIAAILEQR TPFQDMPVSI RGIVLVSVHE LPDKYGSLFH FPAFNAIQSK
CFQSVYKGDD NIVLAAPTGS GKTVVMELAI CRLLNNLKDE RFKVIYQAPT KSLCSERFRD
WNRKFHSLGL QCAELTGDTD YTQMRSVQNS QIIITTPEKW DSVTRKWKDH ARLMQLVKLF
LIDEVHILKE SRGATLEAVV SRMKTIGSNV RFVALSATIP NSEDIATWLG KDATNQHVPA
HREHFGEEFR PVRLQRFVYG YQSQGNDFAF DKMCSSKLPD ILAMHSCRKP IMIFCCTRNS
SVATAKELAR LWSMSNPPAR LWKGPSKSFE FNNIDLKTTS AAGVAFHHAG LNPGDRQTIE
NGFLQGQINI ICCTSTLAVG VNLPCHLVII KNTVGWLDGG CKEYSDLEIM QMLGRAGRPQ
FDKDAVAVIL TRKERVDYYE RLVSGSESLE SCLHLNLIDH LNAEIGLGNV TSVESAIRWL
AGTFLFVRLR RNPTHYQLRE GAKREDEDEM LRQICEKDIR LLQESNLVTT ESLRSTQFGD
AMARYYVRFE TMKTFLTLKR HATMSQILSV ISQAEEFRDV RLKAGEKSLY KEINRETGIM
IPVKVDIALP AHKTSLLIQS ELGAVEFPND EQFQKHKFAF QQDKGFVFSH VNRLIRCIID
CQISLQDSVA TRNALELARS FGAKVWDRSP FQMKQIEQIG VVAVRKLAAA GITSLEALEC
AEPHQIDMIL SKNPPFGLKL LGRLSEFPKL RVSVKMIRKE AKHGNPVRIH FKAEVAFMNE
KCPTTFQRRP VHVCFLAETS NGLMIDFRRM SASKVQSSQE IPLHIEMNSP DQYITCYAMC
DDIAGTLRSA ELRPALPSSL FSFCSNKESD ETNQKHMMNM SRRRSNTSLR AIPNKEYNPD
SFDSDDSLFN DFLQDDKATN WATMEYIACP TSKNKPQEKT SKKSKKSKEA KDVNKAEEPT
QLRNGRWSCN HKCKDKTMCK HLCCREGLEK PPKMNRKHSN GGADRSNRLN QLTLSATITK
HNTQIGNPGK RRTRKDSMTD SESQEMLQKP SQEPNLGLSD TASKDLICPD VNTKDSSSDY
GDDSFSDLPS PSDLLIGRTT RLTDRRAQTT SKETYLNKNV RTKDDWIYTD EPWLTLPSSL
PNSLVQGKDA TSTTAAETSR GSVLEPKACS SNGSQGAKND NQATTETNEI EYIGRKRRRS
LASGDKAHDK RITKRHIDDQ AAEACASLRQ YHSTDTLSGY HQNPQPYEPA DLPAIWDDID
STLLDEFKDI VNFF
//
