ID W9IB90_FUSOX Unreviewed; 1774 AA.
AC W9IB90;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Kinesin family member 1/13/14 {ECO:0000313|EMBL:EWY90535.1};
GN ORFNames=FOYG_08021 {ECO:0000313|EMBL:EWY90535.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY90535.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWY90535.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) 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}.
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DR EMBL; JH717843; EWY90535.1; -; Genomic_DNA.
DR HOGENOM; CLU_001485_20_2_1; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000030753; 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:UP000030753}.
FT DOMAIN 8..355
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1603..1754
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 619..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1657..1686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 753..826
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 705..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1532
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1774 AA; 197316 MW; 55D9CA7B252C62DB CRC64;
MPPAGGGNIK VVVRCRPFNS REIERGAKCI VEMKGNQTVI TAPEGKGVKD GGPKAFAFDR
SYWSFNKDDP NYAGQSNLFD DLGQPLLDNA FQGYNNCIFA YGQTGSGKSY SMMGYGKEIG
IVPLICQDMF KRIDELKKDK TTKCTVEVSY LEIYNERVRD LLNPSTKGNL KVREHPSTGP
YVEDLAKLAV NEFQEIEHLM DEGNKARTVA ATNMNQTSSR SHAVFTLMLT QKKYDTDTKM
EMEKVAKISL VDLAGSERAT STGATGARLK EGAEINRSLS TLGRVIAALA DLSTGGKKKK
GTGQVPYRDS VLTWLLKDSL GGNSMTAMIA AVSPADINFD ETLSTLRYAD SAKRIKNHAV
VNEDANARMI RELKEELSLL RSKLGNGPVP GGAAGGGLVS GETYPEGTPL DQQMVSITGS
DGVLKKVSKA EIAEQLSQSE KLLTDLNQTW EEKLLKTEEI HKEREAALEE LGVSIEKGFV
GLHTPKKMPH LVNLSDDPLL AECLVYNLKP GTTTVGNVDT NADHQANIRL NGSRILHDHC
TFENAPDGTV TLTPSEGASV MINGKRITEP SQLHSGYRVI LGDFHIFRFN HPMEARAERA
EVPERPQSLL RHSITASQLQ ALDRGSPSPS PRPGHERSFS RVSEFGDISR PESPSIFQRS
GRESDWSLAR REAAGAILGS DQNLTSLTDE ELNALFEDVQ RARAERVNGR EDGDDSESSY
PIRDKYLSNG TMDNFSLDTA LTMPSTPKQG EPDDRLKEVR EELQSKLEKQ KEEYQDQLKS
AEAANVEIEE IKQEKVKMEA ALKELKEDMQ KQLNQQRKQF EEKIEKMDPL KMPKKSPTLS
EEEIEMAKKT VKTWRGRHFV KMAEAVLQNA SILKEAQVMS HELDEHVVFQ FAAVDVGHVL
CSSYDMVLNG LTGEGDDVAL EEAHKPCIGI RVVDYKHSVV HLWSLEKLHD RVRQMRQMHQ
YLDQPEYAQH LSLDNPFVET CMPSYTLVGE VDVPLKAVFE CRVQDSTLDV LSPYTSHVVG
IIKLSLEPSH ARAPTNTLKF NVVMHELVGF AEREGTEVHA QLFIPGISEE DGITTTQMIK
DFDEGPIRFE SVHSMSIPLF APQDVTLRVA IFAKVSTMHL DKLLSWDDMR DAVPVREDKA
KASRINESQF YTQEKHDLLS RIQIMELNEN GEYGAVEVTQ TSELDTGTFQ LHQGLQRRIG
INISHSSGDA LPWSGVTAVR VGKIRLVDSA GKTPDMGANE PDISLKLSQS PIFRENANGT
KSLTIYAQWD SSLHNSLLLD RVTQDKYRVQ MTISWEISSE KLAEPMKFSQ KVCVQILSRT
FVRQTSMFSA LWQNVRFVRS STGIFTLAMR PAPVKKVGDL WRLNSQHDYV KGEENLTSWT
PRGVSLVSDF LMARKKKRRA ADMSVTESVL AKLGLDGANT LPEKKEPEPE PSPELKPIIP
SDDDLLNDTP ETSQTPSLDD EEQPPADEPQ LQLFIEAQQP ETDLSNLEQR EIREPHVDEQ
DQPVKEEPKK EDTEEPSSET PEATEVEEEE TITVEEPLLK PEYDEDQTYL LTKCLKLWKK
YPDPSNNILS PTNMAPPADG LMTDGPAQPT LIATVIRVPK NPKVLKGGYL MIPNSDSTRW
VKRFVELRRP YLHLHSATDG DEVGLISLRN SRIDSQPGVL GLLQGPDDSG AQGQDGGTDF
TPGHRRTASG RVISTIWTGS GPGASSGGPG LQRLPERMQS AVFAIYGTDN TWLFAARSER
DKMDWIFRID QTYMSSNDSV PGSGIASPYP GSDF
//
