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Database: UniProt
Entry: B0DL92_LACBS
LinkDB: B0DL92_LACBS
Original site: B0DL92_LACBS 
ID   B0DL92_LACBS            Unreviewed;       735 AA.
AC   B0DL92;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EDR04610.1};
GN   ORFNames=LACBIDRAFT_304268 {ECO:0000313|EMBL:EDR04610.1};
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN   [1] {ECO:0000313|EMBL:EDR04610.1, ECO:0000313|Proteomes:UP000001194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446}.
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DR   EMBL; DS547117; EDR04610.1; -; Genomic_DNA.
DR   RefSeq; XP_001884782.1; XM_001884747.1.
DR   AlphaFoldDB; B0DL92; -.
DR   STRING; 486041.B0DL92; -.
DR   GeneID; 6080435; -.
DR   KEGG; lbc:LACBIDRAFT_304268; -.
DR   HOGENOM; CLU_001103_19_4_1; -.
DR   InParanoid; B0DL92; -.
DR   OrthoDB; 1615163at2759; -.
DR   Proteomes; UP000001194; 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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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   PANTHER; PTHR13710:SF154; DNA HELICASE; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
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:UP000001194}.
FT   DOMAIN          54..231
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          268..419
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          643..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        714..735
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   735 AA;  80691 MW;  E53874CDF9C0A689 CRC64;
     MPPRNSKSKN IHPNQLATNV WTALKPNDLK DIAQKVKEKF KWDHEPRPFQ VDAIVAQLKR
     EDVLIHAGTG SGKTAVAAGP HAHEKMQGKV MFMISPLIAL QDEQVKTFHE EFKLEAVAVN
     SAQGGCTKEI MADIIAGRWA IVILSPEMIL SKKFINGVIR KPEMSRRVLS VVVDEAHVVS
     HWGSGFRKKY GTLGVLRALL PKGTPVVAMS ATLAGRVRKD VLAKLQFDPK KFTYLNLGND
     RPNVSLVVRA IQNPMNTYSD LKFLIPKGIR SASGVLKGFI YADNVSGGLD MVDYLDGLLP
     TELRGKGLIR PYNAGLSKEC RDLVMELFKA GIVRILVCTD AAGMGCNIPD IDIVVQWKLT
     ATVSAFVQRA GRAARASGRT GLAVMLVEKS IYDADLHKGC QDEQKTKAKK TICQSPNYPK
     AKTKEYAIRR GVRRGAYGGL FDEVATGVDV PVDVSSIDEG AHGFVQSTSC RRGVLTDIYG
     NEKAAPTVPC CDICNPELLD RTRPAPPRPN AQKKAATYEG VNSTTKSSLQ EWRTKIWNRD
     FEDAIFSPAG ILSDGALEKL ASVTSPIENL IGLERAIGGW AWFGTYGDEL LAEIKTLPFK
     SIPKQKQKRA AKRSMVDVAD GESLAKRTCV SAAPTPVTRV AVAPTPVQPT SHSSLPIAGP
     STPMRTYSYS QYPQSSTPGH PGTRYYHPSY YLTPPRNHNS PQQPYLYYPY YPSPNYHQLP
     PQYRPPNPNT GPPHT
//
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