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Database: UniProt
Entry: B0CXF3_LACBS
LinkDB: B0CXF3_LACBS
Original site: B0CXF3_LACBS 
ID   B0CXF3_LACBS            Unreviewed;       563 AA.
AC   B0CXF3;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Dynein 1 light intermediate chain {ECO:0000313|EMBL:EDR12252.1};
GN   ORFNames=LACBIDRAFT_311460 {ECO:0000313|EMBL:EDR12252.1};
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:EDR12252.1, 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 dynein light intermediate chain family.
CC       {ECO:0000256|ARBA:ARBA00006831}.
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DR   EMBL; DS547094; EDR12252.1; -; Genomic_DNA.
DR   RefSeq; XP_001876516.1; XM_001876481.1.
DR   AlphaFoldDB; B0CXF3; -.
DR   STRING; 486041.B0CXF3; -.
DR   GeneID; 6072422; -.
DR   KEGG; lbc:LACBIDRAFT_311460; -.
DR   HOGENOM; CLU_021937_1_0_1; -.
DR   InParanoid; B0CXF3; -.
DR   OrthoDB; 48125at2759; -.
DR   Proteomes; UP000001194; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR008467; Dynein1_light_intermed_chain.
DR   InterPro; IPR022780; Dynein_light_int_chain.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12688; DYNEIN LIGHT INTERMEDIATE CHAIN; 1.
DR   PANTHER; PTHR12688:SF0; DYNEIN LIGHT INTERMEDIATE CHAIN; 1.
DR   Pfam; PF05783; DLIC; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001194};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   REGION          376..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..417
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  60316 MW;  1D51D956500C7CCA CRC64;
     MDFSRSSTPE APPQDLWSSI LDSVSSSRSI PSKQILLLGQ PSTGKSTLAA ALLQKPVTDD
     GKDDQRTDFA VGYDFASVRD EADEDTLARL SVYTVPSAAP YYTALLPHFL PPRFSLPHTL
     VVIVLDWTRP WTFVDELQTW LEWVESWAKG DGSRELEIVR EECRERLQSY LQHYTEPSTD
     PLPTSNSTLS TTLLPLGPGS FTHNSAGVPI IVTCTKADLI DDGNDMAAGT SGMGSMVKGK
     GGEWEERTDG IMQVLRTICL KYGASLFYTT PLPANLQVLR QHALNMLFMP PAPSPGMGTS
     GEAQAPVRNL FPFNHKPNTL DRDRIVVPAG WDSWGKITVM RDGFDAKMWG EAWEKDLEVD
     AGGEGGAKRL YTTFVPDQGQ KPPPLPPFNN PTPEQAFLAK NYDENSKKSD RDPRGAFRNP
     ADIAGTSAGI VGPLGSSSFD LPNVVRALSE METGIGGPPP TSAEAAPRRA PAGRTAASGR
     PTGLSTLGTS GMSPTHGAGR TPTSPAPAAG TPSPTSGGQT QHELLHNFFQ SLLSSKDRPG
     ASAAAASRPN VNGNAHTTDE PNN
//
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