ID H0EX27_GLAL7 Unreviewed; 761 AA.
AC H0EX27;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 22-FEB-2023, entry version 54.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=M7I_7352 {ECO:0000313|EMBL:EHK96952.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK96952.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHK96952.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(2012).
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 ECO:0000256|RuleBase:RU000394}.
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:EHK96952.1}.
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DR EMBL; AGUE01000215; EHK96952.1; -; Genomic_DNA.
DR AlphaFoldDB; H0EX27; -.
DR HOGENOM; CLU_001485_24_2_1; -.
DR InParanoid; H0EX27; -.
DR Proteomes; UP000005446; Unassembled WGS sequence.
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 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 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 ECO:0000256|RuleBase:RU000394};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000005446}.
FT DOMAIN 15..369
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 761 AA; 82370 MW; 8175D5C97F40D343 CRC64;
MAASLPRPSR PSFGPPTTAL PALPSKKTRK STGGIQTTPE LLSDSIPSLP KSALHNVFST
EDNNAKVYDS SAKRLVRRVM EGYHGTVFAY GMTGTGKTFS MQGTATSPGV IPLAITDIFS
YIRETPSREF LLRVSYLEIY NEKIHDLLSA PAAGGIGPNA GQQEEIKLRE DAKRGVYASP
LKEEIVQSPT QLLRVIARGD QARRTSSTQF NARSSRSHAV VQIVVESRER IPGNVAMGND
KRSGMLPGGV RVSTLSLIDL AGSERAAETK ERRTEGSHIN KSLLTLGTVI ARLSGDKDKD
GKPTDKDGKH LPYRDSKLTR LLQGALSGDS LVSILCTIQT GATGSAAAAN THTGETLNTL
KFAARAKNNI VSHAKKAEEA LGAGGDGGAR VLLERYRMEI LDLRSQLDGQ AKSKHDDDEE
QREKEAEQRH EEQMLEMQLA RTALKERIEH LNRLILSSKS TGVNASGSYS SLSMHPRLSA
MTSNGHLSQM STRSSMAPSQ KSRRSMDRTS SVNSVSTIGQ LPGAHRLSGG DHSMEDEDSI
GENGDGTATL QAQNRALQAD LADKNRYCQT LEKRLLQARR SSHSRTSVNF GMPGKSGVMV
GEDHGVAALL KEKDSEIADL RARLDDKDRM LTALRSAARS RDTADRDPRT PSAIQLLEDG
PLSPVSARAS QLLENETSPI GSRPHLGPVP KKRTKSVDEM SKMLDEMIQD RVETGQLVKS
VKGSIRLPAE RKPRSSEPPI AVEKSLPAVP DEASALVSEV Q
//
