ID W2RHY6_PHYPN Unreviewed; 435 AA.
AC W2RHY6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
GN ORFNames=PPTG_01179 {ECO:0000313|EMBL:ETN25043.1};
OS Phytophthora parasitica (strain INRA-310).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN25043.1, ECO:0000313|Proteomes:UP000018817};
RN [1] {ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN25043.1, ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|EMBL:ETN25043.1,
RC ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 1 complex that are thought to be involved in
CC linking dynein to cargos and to adapter proteins that regulate dynein
CC function. Cytoplasmic dynein 1 acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules. May
CC play a role in binding dynein to membranous organelles or chromosomes.
CC {ECO:0000256|RuleBase:RU366047}.
CC -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two
CC catalytic heavy chains (HCs) and a number of non-catalytic subunits
CC presented by intermediate chains (ICs).
CC {ECO:0000256|RuleBase:RU366047}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|RuleBase:RU366047}.
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000256|ARBA:ARBA00006831, ECO:0000256|RuleBase:RU366047}.
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DR EMBL; KI669561; ETN25043.1; -; Genomic_DNA.
DR RefSeq; XP_008891035.1; XM_008892787.1.
DR AlphaFoldDB; W2RHY6; -.
DR STRING; 761204.W2RHY6; -.
DR EnsemblProtists; ETN25043; ETN25043; PPTG_01179.
DR GeneID; 20171495; -.
DR VEuPathDB; FungiDB:PPTG_01179; -.
DR OMA; VMLEKDF; -.
DR OrthoDB; 48125at2759; -.
DR Proteomes; UP000018817; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IEA:UniProtKB-UniRule.
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 CDD; cd00882; Ras_like_GTPase; 1.
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; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU366047};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU366047};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|RuleBase:RU366047}; Dynein {ECO:0000256|RuleBase:RU366047};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU366047};
KW Motor protein {ECO:0000256|RuleBase:RU366047};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366047};
KW Reference proteome {ECO:0000313|Proteomes:UP000018817};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT REGION 375..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 48320 MW; 8FF7182EE7BC1155 CRC64;
MATGEDLWQQ MLRDCSVRSK LPVANFLLVG DAESGKSALL ARLDEAKSTP SETADETHAV
DTLLAFKTLD VLDPRAKESG GDASEDVMAH IGTWSLNDLN LKDLIKIAVK PQTLQKTVVA
IVLDLSRPWT IKSSLEQWLS ALEGQLLEQI NQLAPETRNE LYGAIKQHIL AYEDPSVDHS
APTPMDTSTN EFMEEGVLSK NLGVPLVIVV AKADLRPENS VKMDYIEYTL RQFAIRYGAS
VVFTSAKTGS NVDTLRKYIL HRAYPSQFKF TEPPQLVDHN SIFIPSGYDS FELVNQSLVG
SQARWPTDKP FEKIVPAPTE ETDDAAATLA TDIRVDTHEQ WLEKLEKAAG AGLEELQKQS
IEASKKAEQA AVARRAAADR RKREEKDVSS KHLQNFFNNL LSRPEKTRSS RSMSDKKKEK
SDKALGDQEA KRSAV
//
