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
//