ID A0A1J9QSU2_9EURO Unreviewed; 1653 AA.
AC A0A1J9QSU2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Kinesin family protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACJ73_05345 {ECO:0000313|EMBL:OJD23299.1};
OS Blastomyces percursus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD23299.1, ECO:0000313|Proteomes:UP000242791};
RN [1] {ECO:0000313|EMBL:OJD23299.1, ECO:0000313|Proteomes:UP000242791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI222 {ECO:0000313|EMBL:OJD23299.1,
RC ECO:0000313|Proteomes:UP000242791};
RA Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (AUG-2015) 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}.
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:OJD23299.1}.
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DR EMBL; LGTZ01000827; OJD23299.1; -; Genomic_DNA.
DR STRING; 1658174.A0A1J9QSU2; -.
DR VEuPathDB; FungiDB:ACJ73_05345; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000242791; 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; 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; 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; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR PANTHER; PTHR47117:SF1; 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 Pfam; PF00169; PH; 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:UP000242791};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 1..333
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1521..1636
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 408..446
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 732..807
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 585..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1653 AA; 183694 MW; DDAFE6CED27AD461 CRC64;
MKGSQTVLTP PPGAEEKSRR GGKQGGGSVE GPKVFAFDKS YWSFNRNDPH YAGQNNLFED
LGAPLLDNAF QGYNNCIFAY GQTGSGKSYS MMGYGEEAGV IPKICKDMFR RIAALQSADK
NLTCTVEVSY LEIYNERVRD LLNPTTKGNL KVREHPSTGP YVEDLAKLVV QSFQEIENLM
DEGNKARTVA ATNMNETSSR SHAVFTLTVT QKRHDTETTM DTEKVSRISL VDLAGSERAT
STGATGARLK EGAEINRSLS TLGRVIAALA DLSAGKKKNA SMVPYRDSVL TWLLKDSLGG
NSMTAMIAAI SPADINYDET LSTLRYADSA KRIKNHAVVN EDPNARMIRE LKEELAQLRS
KLGDGGAVAG GGAPGGGLAE EVYPPGTPLE QQMVSIAQAD GTIKKVSKAE IVEQLNQSEK
LYTDLNQTWE EKLQKTEEIH KEREAALEEL GISIEKGFVG LSTPKKIPHL VNLSDDPLLA
ECLVYNIKPG TTTVGNVDTA ATSEIRLNGS KILHQHCSFE NVDNVVTIVP NEGAAVMVNG
LRIDKPKRLR SGFRIILGDF HIFRFNHPQE ARAERVEQSL LRHSITTSQF GSPAPGKTSH
DRSMSKAGSE VDGDSSRAES PLLSQRGRDS DWFFARREAA SAILGPDQKI SHLTDDELDA
LFDDVQKARA VRRGRPESKL IDGEDDSDSL SSYPVREKYM SNGTIDNFSL DTALTMPGTP
RQGEDEDGDV DNTALQMVRD DMQRQLDRQK EEYKGKIAAA AAGTASPDLE ELRLEKARME
DALKAAKEEF QQQLQKQKEE FESQIKDMGY TGPQRIFETG FTQLDPGEIP IARSVVLHWQ
QRNYVRMAES ALQHASLLKE AQVMSQIMDK HVVFQFVIVD VGHNMASSYD LVLNGISGDD
DVALEDAKKP CIGVRVIDFK HNVIYIWSID KLQRRVQSMR QMHQYIDRPD YIQHFKLENP
FSETCTPQYS LVGDADIPLT AVFESRVQDF SIEAISPYTQ SVVGIIKLSL EPSSAQAPSS
TLKFNVVMRD MVGFAEREGT DVHAQLFVPG VSDEGGATTT QMISGFDENS IRFESVHSMS
LPLNSPRNST LKVCIFASVT AMHLDKLLSW DEMRDSPEAP PQKRKTPRIP ESEFYQEERH
DVFVRVQILE LSENGEYMPV EVVQSNSLDA GTYQLHQGLQ RRIVVNLTHS STESLPWEDI
TALRVGTVRL LDPWGKIPDV DLKSSDVPLK LIQEPMVTDN SDGTSNVTIV GQWDSSLHGS
LLLDRTTADK YRVQISLRWN LISRRLQEPI VFELDQTLQI LGRAYIRPQS MFKQFWSSIR
VVHSTVGMFS VAVRPISAKR AADLWRMNTQ NDYVKGEELL TAWAPRKVSL IRDFIGARKR
RQRLAEIDAA RGALSTRTLT PLPTNGRSTP LQGQDGSERR DILLRKYLDL WSTKQDPTEI
ILVKDHTEPP SRGAAFARNP SSTTSPATTT TSVDCSPISS EQAQMAQPPP EQQQRQQRQQ
NQQPSKPRFV ATIQHIPKNP TVLKSGYLYT PDDANNLWMR RFVELRLPYL HIHSVPDGDE
INAINLRNSR VDHEPDFARL LDGGGGSGSS RNGDGLSMRG RPNLFAVYGT QNTFLFAART
EAQKVEWILK IDQGYFSTQA NGNGGGSGRS SRG
//
