ID A0A395T0H9_9HYPO Unreviewed; 1754 AA.
AC A0A395T0H9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Kinesin family member 1 13 14 {ECO:0000313|EMBL:RGP77822.1};
GN ORFNames=FLONG3_4056 {ECO:0000313|EMBL:RGP77822.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP77822.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP77822.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP77822.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP77822.1}.
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DR EMBL; PXOG01000085; RGP77822.1; -; Genomic_DNA.
DR STRING; 694270.A0A395T0H9; -.
DR Proteomes; UP000266234; 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; cd06503; ATP-synt_Fo_b; 1.
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:UP000266234}.
FT DOMAIN 1..323
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1580..1734
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 584..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1384..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1640..1667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 718..791
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1412..1442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1459
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1754 AA; 194500 MW; 8B3B487544BED158 CRC64;
MKGNQTVITA PEGKGVKDGG PKAFAFDRSY WSFNKDDPNY AGQSNLFDDL GQPLLDNAFQ
GYNNCIFAYG QTGSGKSYSM MGYGKEIGIV PMICQEIFKR IDEIQKDGKT KCTVEVSYLE
IYNERVRDLL NPSTKGNLKV REHPSTGPYV EDLAKLAVNG FQEIEHLMDE GNKARTVAAT
NMNQTSSRSH AVFTLMLTQK KIDTDTKMAL EKVAKISLVD LAGSERANST GATGARLKEG
AEINRSLSTL GRVIAALADL STPGKKKKGA GQVPYRDSVL TWLLKDSLGG NSMTAMIAAV
SPADINFDET LSTLRYADSA KRIKNHAVVN EDANARMIRE LKEELSLLRG KLGGGGGVGG
AGVVAGETYA EGTPLDQQMV SITGPDGVLK KVSKAEIAEQ LSQSEKLLTD LNQTWEEKLL
KTEEIHKERE AALEELGVSI EKGFVGLHTP KKMPHLVNLS DDPLLAECLV YNLKPGTTTV
GNVDTNADHQ ANIRLNGSRI LHDHCSFENA ADGTVTLIPS EGASVMINGK RITEPSQLHS
GYRVILGDFH IFRFNHPMEA RAERAEVPER PQSLLRHSIT ASQFQALDRG SPSPSPRPGH
ERSFSRVSEF GDISRPETPS IFQRNGRESD WSLARREAAG AILGSDQNLT SLSDEELNAL
FEDVQKARAE RVNVREDGDD SESSYPIREK YLSNGTMDNF SLDTALTMPS TPKQGEPDDR
LKEVREELQN KLEKQKEEYQ DQLKNAEAAN VEIEEIKQEK VKMEAALKEL KEDMQKQLNQ
QRKQFEEKME KMDPLKMPKK SPTLSDEEIE TAKKVIKAWR GRHFVKMAEA VLQNASILKE
AQVMSHELDE HVVFQFAAVD VGHVLCSSYD MVLNGLTGEG DDVALEEAHK PCIGVRVVDF
KHSVVHLWSL EKLHDRVRQM RQMHQYLDQP EYAQHLSLDN PFIETCMPSY TLVGEVDVPL
KAVFECRVQD SVLDVLSPYT SHVVGIIKLS LEPSHARAPT NTLKFNVVMH ELVGFAEREG
TEVHAQLFIP GISEEDGITT TQMIKDFDEG PIRFESVHSM SIPLFAPQDV TLRVAIFAKV
STMHLDKLLS WDDMRDAVPI REDKAKASRI NESQFFTQEK HDLLSRIQIM ELNENGEYGA
VEVTQTSELD TGTFQLHQGL QRRIGINVSH SSGDSLPWGG VTSVRVGRIR LVDSAGKTPD
MGANEPDISL KLSQSPIFRD NANGTKSLTI YAQWDSSLHN SLLLDRVTQD KYRIQMTISW
EISSEKLAEP IKFSQKVCVQ ILSRSFVRQT SMFSALWQNV RFVRSSTGIF TLAMRPAPVK
KVGDLWRLNS QHDYVKGEEN LTSWTPRGVS LVSDFLMARK KKKRAADMEV TEAVLSKLGL
DAVSTTSEKK ELEPEPSPEL KPIIPSDDDL LNDTPEPSQT PLDDDEQPST DVPQADASEE
SQQLVADESE DEVEQQEEAQ FEADATKQEE VDVSEAEEPE EQPKENGIEE VALETPEATD
AEEDETIKVE EPLPPPKPEY DEEQTDLLTK CLKLWKKYPD PSDKILSLTN MAPPTDGLIS
DAPAQPTLVA TVIRVPKNPK VLKGGYLMVP NSDSTRWVKR FVELRRPYLH LHSANDGDEV
GLISLRNSRI DSQPGVLDLL QGSGDSGVQG QNGQDGGPDF TPGHRRTSSG RVISTIWTGS
GGGATAGGSG LQRLPERMQS AVFAIYGTDN TWLFAARSER DKMDWIFRID QTYLSGNDSI
PGSGMASPYP GSDF
//
