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Database: UniProt
Entry: A0A316UCG1_9BASI
LinkDB: A0A316UCG1_9BASI
Original site: A0A316UCG1_9BASI 
ID   A0A316UCG1_9BASI        Unreviewed;      1469 AA.
AC   A0A316UCG1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Putative cytoplasmic dynein heavy chain 2 {ECO:0000313|EMBL:PWN22869.1};
GN   ORFNames=BCV69DRAFT_280481 {ECO:0000313|EMBL:PWN22869.1};
OS   Pseudomicrostroma glucosiphilum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC   Pseudomicrostroma.
OX   NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN22869.1, ECO:0000313|Proteomes:UP000245942};
RN   [1] {ECO:0000313|EMBL:PWN22869.1, ECO:0000313|Proteomes:UP000245942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN22869.1,
RC   ECO:0000313|Proteomes:UP000245942};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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DR   EMBL; KZ819322; PWN22869.1; -; Genomic_DNA.
DR   STRING; 1684307.A0A316UCG1; -.
DR   OrthoDB; 312195at2759; -.
DR   Proteomes; UP000245942; Unassembled WGS sequence.
DR   GO; GO:0030286; C:dynein complex; IEA:InterPro.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro.
DR   GO; GO:0051959; F:dynein light intermediate chain binding; IEA:InterPro.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   Gene3D; 1.10.8.1220; -; 1.
DR   Gene3D; 1.20.1270.280; -; 1.
DR   Gene3D; 1.20.920.20; -; 1.
DR   Gene3D; 3.10.490.20; -; 1.
DR   Gene3D; 6.10.140.1060; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
DR   InterPro; IPR035706; AAA_9.
DR   InterPro; IPR041658; AAA_lid_11.
DR   InterPro; IPR042219; AAA_lid_11_sf.
DR   InterPro; IPR026983; DHC_fam.
DR   InterPro; IPR041228; Dynein_C.
DR   InterPro; IPR043160; Dynein_C_barrel.
DR   InterPro; IPR024743; Dynein_HC_stalk.
DR   InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR   PANTHER; PTHR45703:SF34; DYNEIN HEAVY CHAIN, CYTOPLASMIC; 1.
DR   Pfam; PF12781; AAA_9; 1.
DR   Pfam; PF18198; AAA_lid_11; 1.
DR   Pfam; PF18199; Dynein_C; 1.
DR   Pfam; PF03028; Dynein_heavy; 1.
DR   Pfam; PF12777; MT; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245942}.
FT   DOMAIN          23..351
FT                   /note="Dynein heavy chain coiled coil stalk"
FT                   /evidence="ECO:0000259|Pfam:PF12777"
FT   DOMAIN          384..604
FT                   /note="Dynein heavy chain ATP-binding dynein motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12781"
FT   DOMAIN          864..971
FT                   /note="Dynein heavy chain region D6 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF03028"
FT   DOMAIN          1005..1152
FT                   /note="Dynein heavy chain AAA lid"
FT                   /evidence="ECO:0000259|Pfam:PF18198"
FT   DOMAIN          1160..1466
FT                   /note="Dynein heavy chain C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18199"
FT   REGION          56..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1175..1197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          253..287
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        56..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1469 AA;  164229 MW;  DC70EE60DC3B9F61 CRC64;
     MIHHYVQLSN EKRGGLEEEQ RHLNVGLDKL KETVSAVSDL QKSLAVKRTQ LTAKNSEANE
     KLQSMVAGQK QTEEQKQASL ALQSDLERQE TEISERREVV MADLADAEPA VQEAQASVSN
     IKKQHLTEVR SMGNPPAPVK NAMESVCIAL GHKVDSWRDV QGIIRRDDFI ASIVNYDTEH
     MMTRPVREKM KRDYLSKPGY DFETINRASK ACGPLAKWVI AQVRFSEILD RVGPLRDEVE
     SLEQQTEETK QHALHLTAMI RELELDIEQY KNEYATLISE TQAIKMEMET VQKRVDRSIQ
     LLDSLGSEKE RWDMASQSFE TQMSTIVGDA LLCAAFLTYA GFFDQAYRGF LWAGWKEHAK
     QIDLKHKAEI SPVDYLSNAD DRLTWQQMGL PNDSLAMENV IILLRCRRTA LVIDPSGQAT
     SFLLALYKER KIVQTSFLDP TAFVKSLESA LRFGSPMLVS DAEHFDPILN PVLNSEFRKT
     GGRVLIRLGP AEIDYNPNFH LVLATRASDQ DWSPDICSRV TFCNFTTTRA SLQNQCLDAV
     LKAERPDTDK KRTDLMKLQG EFRLRLRHLE KALLNALNES QGNILDDDKV IDTLETLKKE
     AAEVTAKVEE TDSIIAEVEE VTNKYVPLAK ACSSLFFIID QLHLISHFYQ FSLRFFLDIF
     EFVLLKNPRL AGVTDAAQRM AILRDDLFLH VYKRTSRALA HQDHVMLATL LAQVWAKEGD
     EAEAFEGEEF AFLLEGGDSV GSAPVDLGAA ANDLFDVEDR RKLAAFLKLP ALRGVPTHIK
     DHVDDWQVFR SSNNPESDMP HFYNADDEVS PLRDCILRLL IVKCFRPDRI DQAMIKLNNV
     AFGSDFLSES VYDLQSLVKD EVTATTPVAL CSVPGFDASY RVDTLVKSMD VRCTSIAMGS
     QEGFTLADQA IATGARNGKW VLLKNVHLAP TWLSQLEKKL SGLNPHRDFR LFLTCETNPV
     IPINFLRASR ILMNEPPPGL KASMLDLLRA LPPSRLQRSP AEATRLFFLL AFFHSTVIER
     LRYTPLGWSK SFEFNDSDAE AALDTIEAWL GRVAKGRSNI NPASIPWDAL RSLIKEAIYG
     GKIDNEADQR LLDSFVDAIF TPQAYESTFH LVNDEAQPLQ APDGTRIDQF LAWTNALPEQ
     QPPQWLALPP TAERVIATAQ GVSLLSKLVR MRQLADDDGE RGGEASTEES AIGSGGGTVV
     KAAQPAWMKA LQQNATQWTA ALPEHLSNLS NDGAGSISDP LYRFWAREHR TAAGLLRTVR
     ADLREVIEVC EGSARQTNHN RKLLDGLPKG VIPSHWMQYA VPKSMSLSQW VSDFAQRLSQ
     IEVVAKESRY ERVGITLGLL FTPAAYLTAT RQYVAHRTKV SLDNLQLELR LNDANAEGGF
     LLEGLKLEGA RWSDSQLSLN DGSTATLQPS SLVWLPTGGS QNQQQRNLVP LSVYLNGDRS
     TSLFSTRVAA EAGLTAAKVA QRAVALRAA
//
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