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Database: UniProt
Entry: U7PUM0_SPOS1
LinkDB: U7PUM0_SPOS1
Original site: U7PUM0_SPOS1 
ID   U7PUM0_SPOS1            Unreviewed;      1925 AA.
AC   U7PUM0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1624_05428 {ECO:0000313|EMBL:ERS98641.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS98641.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(2014).
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; KI440846; ERS98641.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7PUM0; -.
DR   STRING; 1391915.U7PUM0; -.
DR   eggNOG; KOG0245; Eukaryota.
DR   HOGENOM; CLU_001485_20_2_1; -.
DR   OrthoDB; 126886at2759; -.
DR   Proteomes; UP000018087; 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   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR027640; Kinesin-like_fam.
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; 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; 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|PROSITE-ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018087}.
FT   DOMAIN          12..365
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1640..1880
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          626..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1452..1476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1517..1585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1708..1816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          772..845
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1460..1476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1550..1567
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1708..1724
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1725..1784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1796..1816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         111..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1925 AA;  211423 MW;  3DCE3313582473AC CRC64;
     MAPGAPAGAG GNIKVVVRVR PFNGREMDRN AACIVEMRDN QTVLTPPPDH AGPAKGNKDT
     SQKVFAFDRS YWSFNKDDPN YAGQSNLHED LGLPLLDNAF QGYNNCIFAY GQTGSGKSYS
     MMGYGKEIGI IPQICQDMFK RIGEMQSDPN LKCTVEVSYL EIYNERVRDL LNPATKGNLK
     VREHPSTGPY VEDLAKLVVG SFQEIEHLMD EGNKARTVAA TNMNETSSRS HAVFTLMLTQ
     KKFDVETKME MEKVAKISLV DLAGSERATS TGATGARLKE GAEINRSLST LGRVIAALAD
     LSTGKKKKGG ASTQVPYRDS VLTWLLKDSL GGNSMTAMIA AISPADINYD ETLSTLRYAD
     SAKRIKNHAV INEDANARMI RELKEELALL RSKLGGGGPG GAGGANVPPD EVYAEGTPLE
     KQLVSITQAD GTVKRVSKAE IAEQLSQSEK LLTDLNQTWE QKLAKTEEIH KEREAALEEL
     GISIEKGFIG LSTPKKMPHL VNLSDDPLLA ECLVYNLKPG TTTVGNVDSP TEHQANIQLN
     GSRILQDHCT FENAPDGTVT VVPMPDAAVM VNGKRITEPK QLHSGYRVIL GDFHIFRFNH
     PMEARAERAE IRAEQGQSLL RQSITASQLQ SLDRMSPSPS PRGMGHGHDR SISKAGSDFG
     GFSDSRPESP APFSRSGRDS DWSFARREAA GAILGTDRNV ASLTDDELNT LFEEVQRARA
     ERVTTGREGD EDMESMSSYP IREKYMSTGT IDNFSLDTAL TMPSTPKQGE VDDKLREVRE
     ELQIQLEKQK EEYQDQLKTA EAANVEVEEI KKEKERMVDA LQTLKVEMQK QLDVQRQQFE
     EKMEKMDPLK RPKAKPKLSP EEIELAKKVT KHWRSRHYVQ MAEEVLQHAA TLKEAQIMSH
     ELGENVFFQF AVVDVGHSIF SSYDMVLNDL EEGEDPALEQ AQKPCVGVRL IDYKYNVVRL
     WSLEKLYERI RQMRLLHQCL DQPEYGDPVD MASPFIESHM PAYTLIGDVD VPLKTVFESR
     VQDFSLDVIS PYTGHAIGIM KLALEPSSAR APPSMLKFNV VMHEMIGFPE REGTEVHAQL
     FIPGISEDDG ITTTQMINDF DEDPIRFESV HSMSVPIAGP QDATLRVAVF AKVSSMHLDK
     LLSWDDMRDA ALPTRESGPQ AARIAESHFF TEERHDVLSR IQILEMNEEG AYVPVEVAQL
     NELDPGTFQL HQGIQRRIAI NVSHSSGDML PWDGVSALRV GKIQLLDASG KQPDPNSVPP
     PDVTLKLSSA PSFRNNANGT RSITLTGQWD SSQHNSALMD RVTADNFRVQ MTVWWDITSE
     KLAEPMKFSA TFCCQILSRS FVRQPSMLST LWQSVRFVRS STAMFTIATR PAPIKRVGDL
     WRMNSQHDYV KGEENLGAWA PRGVTLVSDY ISGRKKRQRI LEIGAAQNAL KRIGLPAPKF
     TPEHEARLLA ESGIHSADTS DDVAVDEAAR ERNGEMESIE ELLRDTADAS QILAAPAEPA
     PEAALEAVPE IEPGADDEVA TPRAEPSTEP FAESNEVEPG ETPTTGTETV AADEEDKALE
     EHRTQAGAEP EVPGPPASGY TDEEERVLHK SLKLWKKYPD PLAQLLAPEN TAPPVNGVTS
     DSAEPPSLIT TVIRVPKNPK VMKGGYLLVP SNDATRWIKR FVELRRPYLH IHNVTDGDEV
     ALVSLRNARV ESEPGILGLL ESRHPDYRHN GFDIQDHHDY SQDESQSEQN GGYTNGGSSN
     GDESASEAES HRTNGTNGTS GTNGTTGTNG TDGNNGTNGS NGLSSPPPSL PPTPASKSTT
     PYRAGHRRTS SGRMISTIWT GSGGSVGHVG AKRRPGLQRL SDRLQAGVFA IYGTDNTWLF
     AARSERDKME WIARIDQSFL MPASSVSSSM ANTRSASPNI AAGVVAAVGA FIGSKMGPTG
     QNADG
//
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