ID C6HR92_AJECH Unreviewed; 1628 AA.
AC C6HR92;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Kinesin family protein {ECO:0000313|EMBL:EER37026.1};
GN ORFNames=HCDG_08477 {ECO:0000313|EMBL:EER37026.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER37026.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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; GG692436; EER37026.1; -; Genomic_DNA.
DR STRING; 544712.C6HR92; -.
DR VEuPathDB; FungiDB:HCDG_08477; -.
DR eggNOG; KOG0245; Eukaryota.
DR HOGENOM; CLU_001485_10_0_1; -.
DR OMA; RIDKPKR; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 2.
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; 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; IPR049780; PH_KIFIA_KIFIB.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
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:UP000002624};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 8..319
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1501..1614
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 569..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 392..430
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 716..790
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 655..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1480
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 1628 AA; 181257 MW; 5B07183580368B76 CRC64;
MAPGGGGNIK VVVRVRPFNG RELDRKAKCI VQMKGSQTVL TPPPGAEEKS RKGAKQGGAA
VEGPKVFAFD KSYWSFNRSD PHFAGQDDLF EDLGKPLLDN AFQGYNNCIF AYGQTGSGKS
YSMMGDLLNP TTKGNLKVRE HPSTGPYVED LAKLVVRSFQ EIENLMDEGN KARTVAATNM
NETSSRSHAV FTLTVTQKRH DTETTMDTEK VSRISLVDLA GSERATSTGA TGARLKEGAE
INRSLSTLGR VIAALADLSA GKKKSASMVP YRDSVLTWLL KDSLGGNSMT AMIAAISPAD
INYDETLSTL RYADSAKRIK NHAVVNEDPN ARMIRELKEE LAQLRGKLGG GAVAGSAVGG
GLAEEVYPPG TPLDQQMVSI AQADGSIKKV SKAEIVEQLN QSEKLYKDLN QTWEEKLQKT
EEIHKEREAA LEELGISIEK GFVGLSTPKK IPHLVNLSDD PLLTECLVYN IKPGTTTVGN
VDTAATSEIR LNGSKILHHH CSFENVDNVV TIVPNEGAAV MVNGLRIDKP KRLRSGFRII
LGDFHIFRFN HPQEARAERV EQSLLRHSIT TSQLGSPAPG RMGHDRSMSK AGSEVDGESS
RAESPLPSHR GRDSDWFYAR REAASAILGP DQKISHLTDD ELNALFDDVQ KARAVRRGRP
ESKLLDGEDD SDSLSSYPVR EKYMSNGTID NFSLDTALTM PGTPRQADDE DGEVDNTALQ
MVRDDMQQQL DRQKEEYKTK IATAAGAASP DLEELRVEKA RMEDALKVAK EEFQQELQKQ
KKEFESQIKH MGYLGPQRIF ETGFTPLEPG EMSIARSVVL HWRQRNYVRM AESVLQHASL
LKEAQVMSNI MDKHVVFQFV VVDVGHHMAS SYDLVLNGIS GDDDVALEDA KKPCIGVRVI
DFKHNVIYIW SIDKLQRRVQ SMRQMHQYID RPDYIQHFKL ENPFSETCTP QYSLVGDADI
PLAAVFESRV QDFSVEAISP YTQSVVGIIK LSLEPSSAQA PSSTLKFNVV MRDMVGFAER
EGTDVHAQLF VPGVSDEGGA TTTQMINGFD ENSIRFESVH SMSLPLNSPR NSTLKVCIFA
SVTSMHLDKL LSWDEMRDSP ESPPQKRKTP RIPESEFYQE ERHDIFVRIQ ILELAENGEY
IPVDVVQSNS LDAGTYQLHQ GLQRRIVVNL THNSTESLPW EDVTNLRVGT IRLLDPWGKI
PDADLKSLDV PLKLIQEPMV TDNADGTSNV TLVGQWDSSL HGSLLLDRIT ADKYRVQISL
RWNLISPRLQ EPIVFELDQT LQILGRAYVR PQSMFKQFWS SIRVVHSTVG MFSVAVRPIS
AKRAADLWRM NTQNDYVKGE ELLTNWAPRK VSLIRDFISA RKKRQRLAEI DAARGALSTR
TLTPLSTNGR STPLQGQDGG SERRDMLLRK YLDLWSTKKD LTEIILIKDH TEPPTRGAAF
ARNFSAATSL ASTSGDCSSI PAEQSLQSSP PPLPSHQQHH LQEPSRPRFV ATIQHIPKNP
TVLKSGYLYT PDDTYSNWVR RFVELRVPYL HIHSVPDGDE INAINLRNSR VDHEPDFARL
LDGGVRTSRD GDGLSMRGRP NLFAIYGTQN TFPFAARTEA QKVEWILKID QGYFSTQANG
DRGGRSNR
//
