ID A0A2T9YT97_9FUNG Unreviewed; 2175 AA.
AC A0A2T9YT97;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=BB561_001763 {ECO:0000313|EMBL:PVU95551.1};
OS Smittium simulii.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133385 {ECO:0000313|EMBL:PVU95551.1, ECO:0000313|Proteomes:UP000245383};
RN [1] {ECO:0000313|EMBL:PVU95551.1, ECO:0000313|Proteomes:UP000245383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWE-8-4 {ECO:0000313|EMBL:PVU95551.1,
RC ECO:0000313|Proteomes:UP000245383};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
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:PVU95551.1}.
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DR EMBL; MBFR01000053; PVU95551.1; -; Genomic_DNA.
DR STRING; 133385.A0A2T9YT97; -.
DR Proteomes; UP000245383; 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:UP000245383}.
FT DOMAIN 21..367
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 646..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 668..772
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 826..864
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2035..2139
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 646..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2175 AA; 248351 MW; C3C751CD8C976378 CRC64;
MLNSDIDNSS ADNMARPVSM KVQVVVRIKP NHSEQISTSL QRKASKSNAL DVTSENEIRI
LEDHNIAGNG PRVFKYDHVF DVDTNQQQVY NVAVADLTDR FFEGYNVTVM AYGQTSSGKT
YTMGTGVDSN TKGVVNFALE HIFTQTQASL LKNDDTRREF AVSFIEIYND DLIDLTLDHN
SASIIQIRED NNGRIIWSGV NEKKIYSAQE ALEILKRGAS NRQTGSTKMN SQSSRSHAIF
SVIQTQTKIN SGVEMRSVSK FNFVDLAGSE RLKKTQSVGN RAKEGISINS GLLALGNVIS
ALSTAQNRST AKNGFFIPYR VSKLTRLLQD SLGGTAYTIM IACVSMSSTD VVETIDTLKY
ASKASSISNK GTNNWESIDA SLHTQILTLK QDISRLQDKL KDKDLIIKTH TVDSTNAGTL
NNNLLYQLDY QNQIQDMQLE LETSNKAYSE LLTKFNELCQ DFENSSIYPS KNSKSYTNNH
LSNPLSLKYD NMSSQSKLNY SHNLIDSDES KRHSNFGDSA LLNNFTSKNN FTDTIDSFNS
PYRLSSEVSD VKLNAIISNN KAMAFIDSIG SDKRFSRIPR IKNKHKTPSK AVHSGIDFDY
NTSSNLDFIR KKDLQGESDL DSDSRNSSLY QLSEENQLPQ DYYSEDLYSA NNSGDQKSMK
YDSGNDFDND YKQVIRELKI ELSELQDELK FKNSQLEINQ TKLEFAEQTN EMLSLKQKSI
GKNLEISEQN SSVEILVYND LKQKCDDIQQ KYDQLQKINS QQQQEIEAQR QKTYTSIGTI
TNNELENGLD TINILHSKEI EDIVSVNEKL KQDYDKEIQE LSMFNLIKSK KNIQEHSKEI
ERLIQDNQAQ NEKIKQEHAN EIKELSLINQ TRYEKTIQDH AKEIDELSLL NQSQHKKIID
HAKEIEELSL INQARFEKIA QEHSKEIDRI MLDNRAQNEK IEQEYSKEIE DLIIINQTQY
ATIKQKHAVE IDHTMLNNQA QNEKIEQEHT KEIEELSLFN QTRYEKIIQD HAKEIEELSL
MNQAQNEKIK QDHAKKMEKL SLLNQTECEK IKQDHAKEIE ELLLLNQAHN EAIRNDHAKE
IERIMLDNQT QHEKNIQYHE QELFQRELDF KNYILDVDTK YTNEINALKQ EHAASLLEMN
QAHREIKTYS SSVQTSDSSF ESSCSEFAES MSLNLNDNLV TTNNRDLTTK QNTYSNEDLK
VYKKKITLIL QFLQNQVFER TSSLKKLQDI VQKNISLDYM SDNQSLLLRS SVFSDDMAVI
DYNKYKQRIE NIKQMSIGEK KHMLTRESHS YQTLICSEDN NIKSGLLKTP LLASSIPCLY
TDNFKYCYTD KKRTELSKLY SPRYKNNLSL YSYKFNPNSA SYNKFTQNTD SINQILLSPL
GIYANQEIEY SPDYRRSKAT TSDMINSPRL SVNAFIDSEI PLVSVENIFT ANVIYGTDSN
KYKAIQGSPT LVNNFVFDDA VNTLDKLTNL IKESIDNSKK IKAKSADLHK KSISYKELIS
FSHIVDCEQT DFELIFSSYK ELLSQLERAN ISKQNLMLVN ERLCTALETL EAQSVLLIGY
FNSLPLNLQG KRNSLEAISL SKKDNESQKP SDNNEFTIKN FDKKTEFNKS TNSLGSKTPI
SIRKKSKLSL YNIIDGDSST EMINKNLEIL ENSGKTNDQK LSTVPIHLYE NILTERNELL
QKISSYQILI NEQHLRLRRQ DKTLAAIPGS HKIASLKSIS VNNFKDKNIV HRILSTGNIN
LPKSKISFDS SLSELFDSQR HGLSIKVSEK NLNKSIECLR KKSTLQKSIS EYSLVGNKDN
GSCPIHESSV FLVSNKEKDF KNGDLHKPTN DDAGNLIINQ NPITNASKPA DCAVINSSID
IIDNNNRDIN SSNQNNSSLF LSFDSSPDIG KNNLVFSGLD VNSFLDSDKL NILNGSFDSA
GIKDFESNYA ETNMSDMKLN VLDNIIEDKS DIIHSSELEI SEFKSIDNFN IYNQKNSSNV
ETKLTKDKNV IIKQDFSEEN RDSLIKGISN EKRMEDILEG SYSFGESCSD PGVNLQHIDE
EMMKLQVRLQ DAMGQLHDSE NNLEKQNEVI QKLESDLKTH TLLITALETN LTNCEQQIIE
YKEDSTKYAN ELLRSKSECK TLNEQIKQLT FRLEESKTAA TQITHDRDIW KIRYQDLRNE
TEGADQKKKS SFFCF
//
