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Database: UniProt
Entry: F0U736_AJEC8
LinkDB: F0U736_AJEC8
Original site: F0U736_AJEC8 
ID   F0U736_AJEC8            Unreviewed;      1674 AA.
AC   F0U736;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=Kinesin family protein {ECO:0000313|EMBL:EGC40718.1};
GN   ORFNames=HCEG_00080 {ECO:0000313|EMBL:EGC40718.1}, I7I53_08600
GN   {ECO:0000313|EMBL:QSS52848.1};
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN   [1] {ECO:0000313|Proteomes:UP000008142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EGC40718.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|EMBL:EGC40718.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QSS52848.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H88 {ECO:0000313|EMBL:QSS52848.1};
RA   Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA   Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT   "Chromosome-level genome assembly of a human fungal pathogen reveals
RT   clustering of transcriptionally co-regulated genes.";
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   EMBL; DS990636; EGC40718.1; -; Genomic_DNA.
DR   EMBL; CP069103; QSS52848.1; -; Genomic_DNA.
DR   STRING; 544711.F0U736; -.
DR   VEuPathDB; FungiDB:I7I53_08600; -.
DR   HOGENOM; CLU_001485_20_0_1; -.
DR   OMA; RIDKPKR; -.
DR   Proteomes; UP000008142; Unassembled WGS sequence.
DR   Proteomes; UP000663419; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd22705; FHA_KIF1; 1.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR   InterPro; IPR032405; Kinesin_assoc.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR24115:SF802; KINESIN-LIKE PROTEIN UNC-104; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000008142}.
FT   DOMAIN          8..365
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1547..1660
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          37..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          740..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1427..1448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1499..1530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          438..476
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          762..836
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        701..722
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1427..1444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1499..1526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         113..120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1674 AA;  186522 MW;  049AF61A178210C3 CRC64;
     MAPGGGGNIK VVVRVRPFNG RELDRKAKCI VQMKGSQTVL TPPPGAEEKS RKGAKQGGAA
     VEGPKVFAFD KSYWSFNRSD PHFAGQDDLF EDLGKPLLDN AFQGYNNCIF AYGQTGSGKS
     YSMMGYGEEA GVIPKICKDM FLRISALQSA DKNLTCTVEV SYLEIYNERV RDLLNPTTKG
     NLKVREHPST GPYVEDLAKL VVRSFQEIEN LMDEGNKART VAATNMNETS SRSHAVFTLT
     VTQKRHDTET TMDTEKVSRI SLVDLAGSER ATSTGATGAR LKEGAEINRS LSTLGRVIAA
     LADLSAGKKK SASMVPYRDS VLTWLLKDSL GGNSMTAMIA AISPADINYD ETLSTLRYAD
     SAKRIKNHAV VNEDPNARMI RELKEELAQL RGKLGGGAVA GSAVGGGLAE EVYPPGTPLD
     QQMVSIAQAD GSIKKVSKAE IVEQLNQSEK LYKDLNQTWE EKLQKTEEIH KEREAALEEL
     GISIEKGFVG LSTPKKIPHL VNLSDDPLLT ECLVYNIKPG TTTVGNVDTA ATSEIRLNGS
     KILHHHCSFE NVDNVVTIVP NEGAAVMVNG LRIDKPKRLR SGFRIILGDF HIFRFNHPQE
     ARAERVEQSL LRHSITTSQL GSPAPGRMGH DRSMSKAGSE VDGESSRAES PLPSHRGRDS
     DWFYARREAA SAILGPDQKI SHLTDDELNA LFDDVQKARA VRRGRPESKL LDGEDDSDSL
     SSYPVREKYM SNGTIDNFSL DTALTMPGTP RQADDEDGEV DNTALQMVRD DMQQQLDRQK
     EEYKTKIATA AGAASPDLEE LRVEKARMED ALKVAKEEFQ QELQKQKKEF ESQIKHMGYL
     GPQRIFETGF TPLEPGEMSI ARSVVLHWRQ RNYVRMAESV LQHASLLKEA QVMSNIMDKH
     VVFQFVVVDV GHHMASSYDL VLNGISGDDD VALEDAKKPC IGVRVIDFKH NVIYIWSIDK
     LQRRVQSMRQ MHQYIDRPDY IQHFKLENPF SETCTPQYSL VGDADIPLAA VFESRVQDFS
     VEAISPYTQS VVGIIKLSLE PSSAQAPSST LKFNVVMRDM VGFAEREGTD VHAQLFVPGV
     SDEGGATTTQ MINGFDENSI RFESVHSMSL PLNSPRNSTL KVCIFASVTS MHLDKLLSWD
     EMRDSLESPP QKRKTPRIPE SEFYQEERHD IFVRIQILEL AENGEYIPVD VVQSNSLDAG
     TYQLHQGLQR RIVVNLTHNS TESLPWEDVT NLRVGTIRLL DPWGKIPDAD LKSLDVPLKL
     IQEPMVTDNA DGTSNVTLVG QWDSSLHGSL LLDRITADKY RVQISLRWNL ISPRLQEPIV
     FELDQTLQIL GRAYVRPQSM FKQFWSSIRV VHSTVGMFSV AVRPISAKRA ADLWRMNTQN
     DYVKGEELLT NWAPRKVSLI RDFISARKKR QRLAEIDAAR GALSTRTLTP LSTNGRSTPL
     QGQDGGSERR DMLLRKYLDL WSTKKDLTEI ILIKDHTEPP TRGAAFARNF SAATSLASTS
     GDCSSIPAEQ SLQSSPPPLP SHQQHHLQEP SRPRFVATIQ HIPKNPTVLK SGYLYTPDDT
     YSNWVRRFVE LRVPYLHIHS VPDGDEINAI NLRNSRVDHE PDFARLLDGG VRTSRDGDGL
     SMRGRPNLFA IYGTQNTFPF AARTEAQKVE WILKIDQGYF STQANGDRGG RSNR
//
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