ID A0A072P4K2_9EURO Unreviewed; 1087 AA.
AC A0A072P4K2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=A1O9_08692 {ECO:0000313|EMBL:KEF55039.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF55039.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF55039.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF55039.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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:KEF55039.1}.
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DR EMBL; AMGV01000008; KEF55039.1; -; Genomic_DNA.
DR RefSeq; XP_013257629.1; XM_013402175.1.
DR AlphaFoldDB; A0A072P4K2; -.
DR STRING; 1182545.A0A072P4K2; -.
DR GeneID; 25283603; -.
DR VEuPathDB; FungiDB:A1O9_08692; -.
DR HOGENOM; CLU_000335_0_1_1; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000027920; 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:UP000027920}.
FT DOMAIN 23..197
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 237..425
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 886..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1015
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1087 AA; 121633 MW; 82DF8C37EFA0D8C2 CRC64;
MPDQLRAIFS YDIFNAVQSK CFSTAFQTDD NLVISAPTGS GKTVIMELAI CRLFAESHTS
DFKVVYLAPT KSLCAERYKD WRPKFSALDL HCAELTGDTD YSHLRNVQSA HLIITTPEKW
DSVTRKWKDH AKLIKLVKLF LVDEVHILKE YRGATLEAVV SRMKSVGSNI RFVALSATVP
NSDDIATWLG RNPSSLHLPA FREVFGESFR PVELCKKVCG FESKGNDFAF ESMLTKQLPD
IISRYGRGKP VMIFCSTRRA STTTAKFLAE FWLASSPSQQ LWKAHGHPLT LQSPELKAYT
AAGVAFHHGG LSPADRRAIE DGYLQGQINI ICSTSTLAVG VNLPCYLVIL KGTTCWTENG
MQEYADLEVM QMLGRAGRPQ FENSACAVIL TRKEKVKHYE LMVSGGELLE SCLHQNLIEH
LNAEVGLGTV YDRATAKQWL ASTFLYVRVR RNPSHYQFRE GCKHSGEEDL LDELCEKDIS
SLQDANLITK ATRLRSTAFG DAMAKYYVSF DTMKLFMGLP PKATLSEILS VLVQAREFKD
VRLLAGEKSF YKEINRAPEI KFPINVDIAL QAHKISLLIQ AELGNITLPD GDQYKKQLPQ
HRVDKTIVFA QSSRLVRCII DCQIHIGDSV SARHALELCR SLAAHVWDNT ASQLRQIDGL
GEVAVRKLAS ASIKTIDSLV NTEPSKIELV LGKNPPFGLG LLKKLESFPN LRVSVKETGR
ELKRGEGSTI RFKAEVGFLN DVVPQFFNKK PVYVCFLAET SDGRLVEFRR MSAKHLQNGE
EIFLSVDLVK PTPQLCCFVM CDEVAGTSRY AELNLVGLSD TIYPTQQSCH DQTGNRVLNS
HGRVHEDILD DEFDDGGIED KDLLSLEMDV EQVEVVEDID ELLAKETKQQ KRQGSKPSNY
DSGSEDTDVA TFKEPMKLRN GRWTCQHNCN NKGRKCKHKC CREGVAKPKR RPKLEGGPRS
EENGQRRLTD LTTIKTRTGQ PSQKSKSLGL HTSVFGDETF RGTADAERPP DEPPLKKAKF
SNGQKGDIQQ ARRDKYQPKE PTPFDASSAI RRGEQNKGPD SHSSFETSPP LPDLDFPMDD
MTALDCD
//
