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
//