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Database: UniProt
Entry: A0A316UNR6_9BASI
LinkDB: A0A316UNR6_9BASI
Original site: A0A316UNR6_9BASI 
ID   A0A316UNR6_9BASI        Unreviewed;      1642 AA.
AC   A0A316UNR6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Kinesin-like protein unc-104 {ECO:0000256|ARBA:ARBA00020751};
GN   ORFNames=BDZ90DRAFT_253771 {ECO:0000313|EMBL:PWN26418.1};
OS   Jaminaea rosea.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC   Jaminaea.
OX   NCBI_TaxID=1569628 {ECO:0000313|EMBL:PWN26418.1, ECO:0000313|Proteomes:UP000245884};
RN   [1] {ECO:0000313|EMBL:PWN26418.1, ECO:0000313|Proteomes:UP000245884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 5214 {ECO:0000313|EMBL:PWN26418.1,
RC   ECO:0000313|Proteomes:UP000245884};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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; KZ819671; PWN26418.1; -; Genomic_DNA.
DR   STRING; 1569628.A0A316UNR6; -.
DR   OrthoDB; 126886at2759; -.
DR   Proteomes; UP000245884; 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; cd01365; KISc_KIF1A_KIF1B; 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; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF5; -; 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; SM00240; FHA; 1.
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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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:UP000245884}.
FT   DOMAIN          6..361
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1528..1638
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          37..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1080..1106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1468..1513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..716
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1468..1509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         101..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1642 AA;  178020 MW;  1AE58CC4B39B1BCC CRC64;
     MADSGNIKVV VRCRPLNSRE RNRGASKLID VNDQHQLVLN PPNDTDQRES NARATKKKAM
     PFSFDRAYDE DTEQRTLFEY VGVDLLEHSF NGFNTCVFAY GQTGSGKSHS MVGYAEAKGL
     IPLTCSKLFN DAQEKMEQDP NLRIRVEVSY IEIYNEKVRD LLNPKNKGNL KVREHPSLGP
     YVEDLSKLVV SSFSDVENLM DEGNKARTVA ATNMNETSSR SHAVFTLVVT QRRKDEQTGL
     EAEKVSRISL VDLAGSERAN STGATGSRLK EGANINRSLT TLGKVIAALA TASSVEASAT
     STPRSKKSAA DHVPYRDSVL TWLLKDSLGG NSKTAMIAAI SPADYEETLS TLRYADQAKK
     IKNKAVVNED PNAKLIRELK EELEMLRARA GGGAGGGMGG AGESGWDPSL PPSQQVVRYQ
     TKSGEMKTVT KAELQEQMEQ NEKLMSSLNE SWEEKLQRTQ EIQLEREKAL EELGITIDKG
     NVGVHAPKNL PHLVNLNEDA LMNECLIYQL KPGTTVVGNL DAPSSSVQIR LSGSNILAEH
     CRFTNDDEGV VTLHAMPDSM TMVNGKRILP ANPKRLRSGY RVILGDFHVF RVNNPSEVRK
     ARAAQRPDSP ASEDGQDVDW TYARREAIMN HLNGQGQDVG LDHLSNEDLD RLFDDISRVR
     NRKAATSRPE SRLSSALDGS ESSPRPYSMS TWTDDTSVED PWSDSIASTR PASTTVVSED
     PALEAPPSIE KEAAMLRATI QEYEQKFQKL GVNVAAAQEE PPLTPRQRQV ALDALAKWRT
     RTTVSMAEDV LSHASALKEA NVIARQLNKG TTYQFICIDP PPLSNPTSTI ESIAGCDDVA
     DPELASCVKP CVAVRVVDAV NRSVYVWSLP NLLGRLGKMR NLTAYVDRPE YSQHFNWGDP
     FYESPAPAYT YLGAALVPLM PLSQRESARY SKVPILATMD DEVVGECSVE VKFVSLAAPP
     ATKANGHAAS PSSRSFLVAG HKLGLQITVD SVTGISRALY HAIHAQLRLS SIAGAHIERD
     DSFASPPVEG DTAAEVKLRK TVGLVLTEAT IAHLKAGYAA VEFHVRPSDQ HLARVLARDA
     GGSEGQRHLH PSPPPTLSHS TGSQGRLAET ELIGEERHDV LASLCICELD AQGEYKPVSL
     HRPRSKAAGA AGSVVSELRQ GLQRRISIQL IHDSGRQLEW RKIARLTVGN VRLVDAQGRT
     HESSSSNALS LPVRGQSVDF HSNGTSTLRA WAAWDSSAHD SLFLNRVSTS EEQRVLVDVS
     VDLDVEKPVC ASPPKFVQTM AVRVGARDAK TRPSMAVGSS SAAGRLLSFM SGGNDSASSN
     TSTVTAATCQ SASRRISTIF TLTLAPPSRR SIKTRDDLWR LDTASKYVRG QEALGAWRAK
     GPEEVEKHRK WLDRQVRRVD VEGWRVVLAR EDKAGRRGKE LSASAQTEVL ARAVELWQAA
     MPAKAAAQTG VDPVSGEDDD RETVIDLRAS SSNNGSTSPQ PASSSSSTPA ESSVASTQAS
     STSASASIPT PPLIPEVSAT DVTALCAKPT RQGILYLPSD SSAWQARLFV LSRPYLLVYP
     AGGSNADEPG ISLAIFIGAG GVRVEAVDTV MEDALLGGSE GERGVTLALY TASNSYMLRA
     KSRVERDEWI GAIGGGVGGN RR
//
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