ID A0A2T4GHU0_FUSCU Unreviewed; 1796 AA.
AC A0A2T4GHU0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Kinesin-like protein unc-104 {ECO:0000313|EMBL:PTD03112.1};
GN ORFNames=FCULG_00009508 {ECO:0000313|EMBL:PTD03112.1};
OS Fusarium culmorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD03112.1, ECO:0000313|Proteomes:UP000241587};
RN [1] {ECO:0000313|EMBL:PTD03112.1, ECO:0000313|Proteomes:UP000241587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV {ECO:0000313|EMBL:PTD03112.1,
RC ECO:0000313|Proteomes:UP000241587};
RA Schmidt R.;
RT "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT interactions.";
RL Submitted (FEB-2018) 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:PTD03112.1}.
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DR EMBL; PVEM01000016; PTD03112.1; -; Genomic_DNA.
DR OMA; RIDKPKR; -.
DR Proteomes; UP000241587; 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 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:SF3; KINESIN FAMILY MEMBER 14-LIKE; 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 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:UP000241587}.
FT DOMAIN 8..358
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1623..1776
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 617..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1682..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 752..825
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1466..1500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1796 AA; 198977 MW; 3E1DB835626CCB8E CRC64;
MPPAGGGNIK VVKRQRRAVL KQRAEIERNA QCIVEMKGNQ TVITAPEGKG VKDSGPKAFA
FDRSYWSFNK DDPNYAGQSN LFDDLGQPLL DNAFEGYNNC IFAYGQTGSG KSYSMMGYGK
EIGIVPMICQ EIFKRADEIQ KDGKTKCTVE VSYLEIYNER VRDLLNPSTK GNLKVREHPS
TGPYVEDLAK LAVNTFQEIE HLMDEGNKAR TVAATNMNQT SSRSHAVFTL MLTQKKIDTD
TKMALEKVAK ISLVDLAGSE RANSTGATGA RLKEGAEINR SLSTLGRVIA ALADLSTPGK
KKKGSGQVPY RDSVLTWLLK DSLGGNSMTA MIAAVSPADI NFDETLSTLR YADSAKRIKN
HAVVNEDANA RMIRELKEEL SLLRGKLGGG GGPGGAVVAG ETYAEGTPLD QQMVSITGPD
GVLKKVSKAE IAEQLSQSEK LLTDLNQTWE EKLLKTEEIH KEREAALEEL GVSIEKGFVG
LHTPKKMPHL VNLSDDPLLA ECLVYNLKPG TTTVGNVDTN ADHQANIRLN GSRILHDHCS
FENAADGTVT LTPSEGASVM INGKRITEPS QLHSGYRVIL GDFHIFRFNH PMEARAERAE
VPDRPQSLLR HSITASQLQA LDRGSPSPSP RPGHERSFSR VSEFGDISRP ETPSIFQRNG
RESDWSLARR EAAGAILGSD QNLTSLSDEE LNALFEDVQK ARAERVNVRE DGDDSDSSYP
IREKYLSNGT MDNFSLDTAL TMPSTPKQGE PDDRLREVRE ELQNKLEKQK EEYQDQLKSA
EAANVEIEEI KQEKVKMEAA LQELKEDMQK QLNQQRKQFE EKMEKMDPLK MPKKSPTLSD
EEIETAKSIV KAWRGRHFVK MAEAVLQNAS ILKEAQVMSH ELDEHVVFQF AAVDVGHILC
SSYDMVLNGL TGEGDDVALE EAHKPCIGIR VVDFKHSVVH LWSLEKLHDR VRQMRQMHQY
LDQPEYAQHL SLDNPFIETC MPSYTLVGEV DVPLKAVFER RVQDSTLDVL SPYTSHLVGI
IKLSLEPSHA RAPTNTVKFN VVMHELVGFA EREGTEVHAQ LFIPGISEED GITTTQMIKD
FDEGPIRFES VHSMSIPLFA PKDVTLRVAI FAKVSAMHLD KLLSWDDMRD AVPIREDKAK
ASRINESQFF TQEKHDLLSR IQIMELNENG EYSPVEVTQT SELDTGTYQL HQGLQRRIGI
NISHSSGDAL PWGGVTAVRV GKVRLVDSAG KTPDMGANEP DISLKLSQSP IFRDNANGTK
SLTIYAQWDS SLHNSLLLDR VTQDKYRVQM TICWEISSEK LAEPMKFSQK VCVQILSRSF
VRQTSMFSAL WQNVRFVRSS TGIFTLAMRP APVKKVGDLW RLNSQHDYVK GEESLTSWTP
RGVSLVSDFL MARKKKKRAA DMEVTEAVLA KLGFDGASMI SDKKEPSPEP SPELKPIIPS
DDDLLNDTPE TSQTLLDDDD EQPAEDAPQA EHSEETPQLE AGESETETER QEEARSEIDA
AEQNGSDVPE SEGLEDQEGQ EGHPEENGVE EVASEKSDAV DAEEDETVQV EEPPPPPPPK
PEYDEEQTDL LNKCLKLWKK YPDPSDNILS LTNMAPPTDG LTTDAPAQPT LVATVIRVPK
NPKVLKGGYL MIPNSDSTRW VKRFVELRRP YLHLHSATDG DEVGLISLRN SRVDSQPGVM
GLLQGPTDSG SQGQNGQEGP DFTPGHRRTG SGRVISTIWT GSGGNASAGG SGLQRLPDRM
QSAVFAIYGT DNTWLFAARS ERDKMDWIFR IDQTYLAGND SIPGSGISSP YPGSDF
//
