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Database: UniProt
Entry: A0A0N0DEF0_FUSLA
LinkDB: A0A0N0DEF0_FUSLA
Original site: A0A0N0DEF0_FUSLA 
ID   A0A0N0DEF0_FUSLA        Unreviewed;      1723 AA.
AC   A0A0N0DEF0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Kinesin kif21b {ECO:0000313|EMBL:KPA41065.1};
GN   ORFNames=FLAG1_06042 {ECO:0000313|EMBL:KPA41065.1};
OS   Fusarium langsethiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA41065.1, ECO:0000313|Proteomes:UP000037904};
RN   [1] {ECO:0000313|EMBL:KPA41065.1, ECO:0000313|Proteomes:UP000037904}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fl201059 {ECO:0000313|EMBL:KPA41065.1,
RC   ECO:0000313|Proteomes:UP000037904};
RA   Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA   Frandsen R.J., Nielsen K., Thrane U.;
RT   "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT   producer.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KPA41065.1}.
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DR   EMBL; JXCE01000109; KPA41065.1; -; Genomic_DNA.
DR   OrthoDB; 1430657at2759; -.
DR   Proteomes; UP000037904; Unassembled WGS sequence.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
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   PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF15; ZGC:66125; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Coiled coil {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:UP000037904}.
FT   DOMAIN          51..437
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          740..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1212..1238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1552..1605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          556..590
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          668..702
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          833..860
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          951..996
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1065..1137
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1265..1409
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1465..1538
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1622..1713
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        22..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..796
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..946
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1565..1581
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         138..145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1723 AA;  191574 MW;  4769668350F7596E CRC64;
     MASSPPASPG GIQRPMSAIA ARAQPRSTSR LSMSSKAGGG SRASDDDSRT AVKVVVRVRP
     PLKPEDPGYD LIPQRFQKAM VHTTSETSLA IDSPQGRKLF VFDRVFNPDV TQEGIWDYVS
     DCINSFVQGY NVSLLAYGQS GAGKSYTMGT SGPGEQYDQE LMGVIPRAAT ALFEKLETPK
     SAAKANRSSL SHLRSPRGYS QQNALGDREW SLKATYVEIY NEQLRDLLVP DTTPLNERVN
     VAIREDTKGN IILTGLRQVE INSADDLMNA LNFGSSIRQT DATAINAKSS RSHAVFSLNL
     IQRKSKAGSG QTSDKRHSMP AEGLASQDVS VTTDSKLHFV DLAGSERLKN TGAQGDRAKE
     GISINAGLAA LGKVISQLSA RNAGAHVSYR DSRLTRLLQD SLGGNAITYM IACVTPAEFH
     LSETLNTVQY AQRARAIQSK PRIQQMEEGD SKAIIDRLKA EVAFLREQIR NAESGPSPRR
     TAPLTNERSD RQNEREAELQ NQLLDTQESY TALSQRHARL IAELARAREN ESGANQLDEF
     SGDTADDRIN RSNSFAQAVE QVVMEYEKTI QSLEQSLSST RSTLSNVETN LLEKETKCAY
     VETINNQLQT RLTKLVDREN NTENYLHDLE AKLDGHTSGE EKNATIIMEL RKEISRVREN
     EASCEDYIST LEERLAEADQ DAELMQREID RLEQVVERQR SLGKLDSLLH ELDQIQDGKE
     PGAENGIENH ADSANGVVSR RATAEHSRNL SHVSRHSQME DPIPEGDEEQ DHSRTRIGTV
     TEVDEDPLRL EKPSEHEPPP SPAQSKFVAD KLENMTQELF DLRVEHESTL NDYDSLHAKY
     ESAMRRLAEM QDAVDEARHS QAQRQSVISV ATPTRTTRPE SFLSDTRTND LKTGPRSSFT
     RSLSSELSSA MDSPATAASS NGDILSDDET ATTKPAAAST ENLPNEENVE LAAELQRLKF
     MAQEREAAEQ ELAERYAQLE SKHNETLDIV EELKTDLSRA RIIEATSPRS STPVIRRKSS
     QNLLVVDRAQ RSFSSLRNIA VENFGTHPEA MQSFEINLNA AIHELHVRSE RIQELEADVA
     AAKKEMETKM TIISGLTRER SSLKASPVEM TMVATLRDQL EQNERQLTET RNAHMAREHA
     LTTELEALRQ ALGTKSSTQA PDNFDPKYEQ RVAELQTEVA TWERKHKEAL DSMENTEFQM
     RGTIGQLEAQ VASNHVQLSS SRSESNGDKD EPTKEAEQRQ QNLIGFLRHE IDEYKAIINS
     NATKVVELEQ AHSAARAELD ELHKAHEAVK QDNSRQLQLL ANLQEQIAAH DQTSQTNQSS
     LDELKIQHSK ALAELKTTEQ KGYEEQVEVL LSEHAESALR LETELAEARD ELHSVSTHVA
     NALGLDANVD KLAERIDELA ASKKALDAEQ AKRSEIESSV AELTTINEQI MKDFEDAKTV
     LADMLDGGAA SGPLVEQIRL AKRRMTDLDD RSKKNSRLVE ELEEQLQNNF DEVQITNNRL
     STLQTERNTR LDEANAATAR LTAELEVLKH DYAALQNKMD EVAAGIHRSN SNSTIRKSAS
     HVSLPSPPPA IPLPPLPNGA QSPVSGAPGS PTAGRPISKD NINISQITED QEARIRTIEK
     HLTAERQLTQ TLEEALTDLE RQTKQVKADC DAWKKRAGEL EAEVKELKDR PPPEPVQDNR
     WSLQAVEEER KKRQAAEAAR RQLEERMNAI NKGKKKKGSL NCF
//
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