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Database: UniProt
Entry: A0A1V6R9M4_9EURO
LinkDB: A0A1V6R9M4_9EURO
Original site: A0A1V6R9M4_9EURO 
ID   A0A1V6R9M4_9EURO        Unreviewed;      1370 AA.
AC   A0A1V6R9M4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=CAP-Gly domain-containing protein {ECO:0000259|PROSITE:PS50245};
GN   ORFNames=PENVUL_c077G09233 {ECO:0000313|EMBL:OQD97892.1};
OS   Penicillium vulpinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=29845 {ECO:0000313|EMBL:OQD97892.1, ECO:0000313|Proteomes:UP000191518};
RN   [1] {ECO:0000313|Proteomes:UP000191518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00011010}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQD97892.1}.
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DR   EMBL; MDYP01000077; OQD97892.1; -; Genomic_DNA.
DR   STRING; 29845.A0A1V6R9M4; -.
DR   OrthoDB; 9423at2759; -.
DR   Proteomes; UP000191518; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR022157; Dynactin.
DR   PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR   PANTHER; PTHR18916:SF6; DYNACTIN SUBUNIT 1; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12455; Dynactin; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Dynein {ECO:0000256|ARBA:ARBA00023017};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191518}.
FT   DOMAIN          26..68
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          78..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1034..1181
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        78..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1370 AA;  153310 MW;  993284F5F643755B CRC64;
     MSGQALSIGT VIELPDGRQA TVRFIGITHF ADGQWIGLEL DEPTGKNDGA VQGERYFDCG
     PGHGMFVRPT VVGKIVQPQP ESKQTTKPAT SAAGSKAQPK PGISTGMRKQ TGVPPTAARR
     QSTNAASTPT PAPKGLAARS ALRSPTKSPT KQLATAAGPA IRPSIGSTSR TSTVASNRPR
     LAPSNRSSLG PSPTQHTVSR GSRPSVSGPA GRASRPGSQS TVTSPTAGLT KRPSLRQVSN
     TKASDGGDMG MSGRSGDPTD TESPDPEGEG VQDGGTTAPK ATRQPMATTR LAASRPGAPL
     SASQRQGQSA AVNRELEELN AKLKVMEKKR ADDKEKLKTL EQLQAERDKF ETIIQKLQAK
     YQPQQMEVTE LRKKLKELET RSDDVERMQA EHESLMEMAT LDREMAEETA EAFKHECAAL
     RSKMDELSLE VEVLREENEE YSQETTPEDR TTHGWLQMEK TNERLREALI RLRDMTQQQE
     ADLKAQIKEL EDDLEEYATI KSDYEAAKER ILVAEANVDD LKQQLETALG AEEMIEELAD
     KNMRYQDEIN ELKAAIEDLE SLKEISDEME YTHIETEKQL QEEIEYREGV FSDQCRKITQ
     QDEVIEDLEY TLTRFRDLVT NLQCDLDDMR TTKQVSEAET TENAMRHRQM QDLNMKLQAN
     QSKALTKSID VELARMEAEE NAQHLSMVKL YLPEYFEGER NSIQALLRFK RVAFKANVMS
     STLQEKGSEH SVLSNEEIFQ AHVVLEYLMW ISNVCDRFVN YITACSPEQF GGIKIAMFEM
     EPVERMLNFW IEPLKKDEVN LAKLAVELQR SIALLAHLAE TLLPSSLEMF ADELCMRAHL
     SQLYIEHSAG AISRVKLIIS SKMLAAAEGD EENLIALNKL DAFTPQARGY KVAMGKISRC
     LDDLRSRSLA LPREAEEPFK KIENETKQLS ELARKIGESL VILTSDEGRT EQFSPEEILD
     CMLQAAVAFT SSSDTPDESN DPVSLLFTRL REVGDQFEEL DSISSDLSRT TEFERAAYPW
     IARAAELKSN KMTSPDADEE IRQLRNEIHE ASAALGVKDN TLEEQGLKIE HLESRMREAS
     KKAAMVKDLE AKIEEIQAAA SELEKIVEQQ KKELQTAEAE RDDFMARLER MKRMSGTAGL
     TTTGNGVAIA TEASLAAMDE NESLRAEVES LQAAVRFLRE ENRRSNILDP YSVQRSTEMH
     AWLDAPLVRA NPTPEQEKIQ RTALESRDVM NHLLKLTKES RVTDLKSTMA AQASDDNDSN
     NAGRTVWRPS RTRLRYQVLQ QRENFEHWAE WRDEIVNHER EQDRLVAAKQ ERAMRDRVSR
     HSHKASVEFP QGLGHGMMGR AWQILGMQKH RKTGSISTPA PDGVEIVATD
//
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