ID A0A0L6WSC8_9AGAR Unreviewed; 1269 AA.
AC A0A0L6WSC8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=J132_00808 {ECO:0000313|EMBL:KNZ78445.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ78445.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) 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};
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DR EMBL; KQ412478; KNZ78445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6WSC8; -.
DR STRING; 1306850.A0A0L6WSC8; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000053712; 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 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; 2.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 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:KNZ78445.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053712}.
FT DOMAIN 18..214
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 252..454
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 865..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1269 AA; 142665 MW; 42CBD6E90578A9A9 CRC64;
MYRSIFKFGV FNAVQSSCFS DVCDKSILWL SPTGSGKTVL FELAIIRMLS LPDNTDRHMK
CVYIAPTKAL CSERYRDWTT KFDPLGITCS ELTGDTIHFG KGVWGDAKKA SIIITTVRTT
RLSEVRKFIT WMKGEKWDSL TRNWNDHHQI LSSIRLLLVD EVHILNESRG STLEVVVSRM
RTRGSSVRFL FVSATVPNIQ DIAAWIGSNG QSNIPAKVFQ FGEEFRPCKL TRFVIGVSRP
KGQNDFAFSK SLDYKLFMAL QQYSMGKPIM VFCSTRKGYF SNCSLGVFTT AEQLMKDYLE
AENGRKSLPW SHPKRNEHSF HDKRLADLAS VGIGVHHAGL TLDDRKATET LYLNGTLRVI
VATSTLAVGV NLPAHMVVIK GVQTFNNNTS VEYSDLDIMQ MLGRAGRPQF DKDGIALIIC
ETELEQKYRT LVQGKTILES TLHTNLAEHL NSEIGLGTIT SISTAKTWLR GSFLFQRLQK
NPNHYSLGKD DNQTWEERVD ELVLQSVEKL RQTQLVINGP RSDQLISTDF GDIMSKLYIR
QSTMGLILTL PERLTLREIL GLISMSAVLG GISLNTPEYK SADSQPQLEA FGIFRHVSRI
ARAVVEVGVF KQLGGQVKYG LELLRCLTAK AWEDRPIVLR QLEQIGEKSI KVLAEHGIIS
ISHLLNQDAL RIEALLNRRS PFGLELLASA QEFPRYSLNI TQLGVSSNGG KDPVEIELSI
QCGLEQVQNY RPPKFKKSKG YNGDMTVVLT ISSDLELFDY RRISTKSLKE KKTFNVTAEL
SRPSQSINVL ITSETIAGLV VQQSYKPALS PQEFPTRNTR PPTTTDIDLV GLEDDPDFWN
MDIGEEVLPV VRDLTKPKGD ATKLESLGAD LCPDKDQNEK DFSSSQNTKS GVLLRSLDRQ
TQKRMQNGNF ECNHSCRDKK KCRHLCCRDG LPEKPKKRPS AEKSIETSRK QQNRIATEAT
RSKISTSTRR MKDPRLEQLE SLHKQSNVSS NLQLSLGHRL KLEPSVELKR KQKPIPDFKL
DYSDLKDLDK VNRTGYDPVE LEDDEDDLPE AVGISNVDRP RTPPSETSYS NSDIDSLIRA
VPLNDELLTV ASGCIESEAS DRKPLASFNK RKRTTEPNAS NKRIRREELE NQSQCHEMIR
TTHQERAKDA IGVVNKRESL FLSDDTHEVE EDFGCDKPTK VCDWLLGTSL LESDGPSLPS
DYLDHDPTPD LTLSTAISNS FKDLGPQEAQ HTSLIGKTLP RTDTYEKEKS SDDFAELDAW
LNSGAVEIL
//
