ID A1DP28_NEOFI Unreviewed; 1449 AA.
AC A1DP28;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=NFIA_059000 {ECO:0000313|EMBL:EAW16549.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW16549.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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};
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DR EMBL; DS027698; EAW16549.1; -; Genomic_DNA.
DR RefSeq; XP_001258446.1; XM_001258445.1.
DR STRING; 331117.A1DP28; -.
DR EnsemblFungi; EAW16549; EAW16549; NFIA_059000.
DR GeneID; 4584962; -.
DR KEGG; nfi:NFIA_059000; -.
DR VEuPathDB; FungiDB:NFIA_059000; -.
DR eggNOG; KOG0952; Eukaryota.
DR HOGENOM; CLU_000335_0_4_1; -.
DR OMA; VYGYQSH; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000006702; 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, ECO:0000313|EMBL:EAW16549.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702}.
FT DOMAIN 253..427
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 467..655
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1449 AA; 162194 MW; ED5FD784DDE12E45 CRC64;
MGRKSHQPFS IARHSASNQR PMGARRPQLG LPASKAIIDQ RLIEGSQISQ PWNRPRGYES
QNVEPHSQLV GPDLQSFRSD DHQLDAFDLE LLAQADESNR NPLRQPANLN YPSVQPRNDG
AKQVSRFFQT SSHITPLRSL DSSSSDVGLG SPSSPLSRLQ LGKTIVTRRE QEYQATGPSR
QYNEDQLSHE EDSPSHGTST LSIGTAQCQK SHFENIPMSV RGIVLVSVHE LPDSYRSIFH
FPVFNAVQSK CFQRVYKTDD NIVLAAPTGS GKTVIMELAI CRLLSTLKDE RFKVVYQAPT
KSLCSERFRD WNRKFMSLGL QCAELTGDTD HTQLRSVQNS QIIVTTPEKW DSMTRKWKDH
ARLMQLVKLF LIDEIHILKE ARGATLEAVV SRMKTFGSNV RFVALSATVP NSEDIASWLG
KDATNQHVPA HREHFGEDFR PVKLQKFVYG YQSHSNDFAF DKLCSSKLPD ILGTHSCRKP
IMIFCCTRNS CVATAKELAR LWSMTNPPAR LWKVSGKHLE AHNADLRTTL MAGVAFHHAG
LDPADRHTVE SGYLQGHVAV ICCTSTLAVG VNLPCHLVII KGTVGWQDGG CKEYSDLEMM
QMLGRAGRPQ FDDSAIAVIM TRKDRVQHYE KLVSGCETLE SCLHLNLIDH LNAEIGLGTV
TDVDSAVRWL AGTFLFVRLR RNPKHYQLKE GATKDDEDEM LRQICEKDIR LLQETGLVAS
DRLKSTPFGD AMARYYVRFD TMKTLLALKS HATVSQVLSA IAEAEEFREI RLKAGEKSLY
KELNRANGIR FPAKVDIALP AHKILLLIQS ELGGVEYPDG EQYQKHKFAF QQDKNFVFSH
INRLIRCVID CQISLEDSIT ARNALELARS FGAKVWDNCP LQMKQIDQVG IVAVRKLAAA
GITSIDALEA TEPHRIDMIM SRNPPFGMKL LARVADFPKL RVNVKLVGKE IKPGKPVRIR
FEAEIAFMNE KTPTFFQRRP VYVCFLAETS DGHLIDFRRI SASKLQQSQE ISLDAELKRP
GLHITCYAMC DEIAGTLRSA ELKPELPNVS FPSRPSQALE SMQRPRVNVP SRDTDDTPIN
ANDRGADDIE NDDWLFDDLM ETDEASNWAG VNQSTGTSRS RTEEKGSKEC NSENSLPGND
KEPPRLDNGR YACNHRCKDK TTCKHLCCRE GLEKPHKVTR KQSTNGNQAK SGLNQLTLSA
SIPRTKAGRT STIEARDKGN ITDIGDIFHL SFTSHVSKPQ CSSSDYGDDS FDDLPSPSKL
LVGFSTGTTT QVNEKTETNA SECDDITEAD DTWTDVDDLF TYTVQPSSTD SPDQVKIHTA
TSATRKQDQT LVPPDNPMFG RSVVSNENDI PRASETDVDK GLDPSRVSDE HRGRKRGLSW
LCERAHSDER MEKRTKHDEP GQIPRGQVET ALEINASVQG SANPPEVPKD WDDIDPALLH
QFKDIVNFF
//
