ID A0A067TRM7_GALM3 Unreviewed; 1134 AA.
AC A0A067TRM7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=GALMADRAFT_239701 {ECO:0000313|EMBL:KDR81633.1};
OS Galerina marginata (strain CBS 339.88).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR81633.1, ECO:0000313|Proteomes:UP000027222};
RN [1] {ECO:0000313|Proteomes:UP000027222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-5/BimC subfamily.
CC {ECO:0000256|ARBA:ARBA00034704}.
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DR EMBL; KL142370; KDR81633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067TRM7; -.
DR STRING; 685588.A0A067TRM7; -.
DR HOGENOM; CLU_001485_33_2_1; -.
DR OrthoDB; 536293at2759; -.
DR Proteomes; UP000027222; Unassembled WGS sequence.
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 GO; GO:0007051; P:spindle organization; IEA:UniProt.
DR CDD; cd01364; KISc_BimC_Eg5; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR047149; KIF11-like.
DR InterPro; IPR047241; KIF11-like_kin_motor_dom.
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; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 1.
DR PANTHER; PTHR47970:SF12; KINESIN-LIKE PROTEIN KIF11; 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:UP000027222}.
FT DOMAIN 67..427
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 443..553
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1134 AA; 127121 MW; 60712588FA99644A CRC64;
MATRRPASSR ARINNNTNPM PPPSQQQRPK SVMSRPPSSQ RTGDEQDSTS APGAPRIQRG
QEDSETHIQV IIRCRGRSDR EMQANSPSIV QIEGAKCRDL KIETTTPVSS LGVLTLPPTR
TYPFDLVFGP EATQSMIYHD VVGPMLSEVM TGYNCTLFAY GQTGTGKTYT MQGDLYPTPM
GNPSAHAGII PRVLFRLFHE LEKAHTDFVV KISFIELYNE ELRDLLAIDL SAPTTLTQPM
GKDAKGSEEK LKIFDDATKR GVFIQGLEEI AVKDSKDALA LLMKGSERRQ IAATKFNDHS
SRSHSVFSIT VHIKETNTMG DDLLKVGKLN LVDLAGSENI GRSGAENKRA REAGIINQSL
LTLGRVINAL VDKAQHVPYR ESKLTRLLQD SLGGRTKTCI IATISPARAN LEETLSTLDY
ALRAKSIRNK PELNQRMTRN SLLKEYVAEI ERLKSDLLAA REKNGIYFSE ETWNQMNAEN
ELKETELVEA KKQVEIIENQ MRSVRDEYDQ SIAVLKRREE ELQQTKRQLE ETQKILGQRE
EELQQAKDAY QEEVLVRQAH QATEVVLDGV AADLKTVAAE SLLGISGLFD KLERKNKVFL
SNKRVVSENE KLIHSLADSL TKRLFEFDSS SSKIRTNLQD ETTQFRSSQK DAMANHLQEV
NDHFDKAQEL FQQIETHQVV EDCALSTIKQ EIEKAHKSLN QEVTSWAENL TTSCSQLCNK
STELAIAQIN TLEDSTTVLH TLVETISREI HSYLDGERNA LAEMQSLSKT ASAQEIAHLQ
SQNKLLAQMV VNEKEDAEKA KNELLQRVSG LLGDFMHKRD DTLRASIGSL QRSNKEAEQL
LTATYHQQSK VHGDMGLRNE EVAKQMEVVK DQGAREKNKT TQNVGQAREL ISTRITEIQS
KVATSATGHS AWVHQQAQAM EKSTRDASEE QTKAKRARIE STDVIYARYE AHHSVQHQFL
ASASRQGEKH ATQTLSWISE QAQSTKDYEE ATAKNLESIQ QAASNLAKKG VKDDVPTGST
PRKRKWQYRD EWSLTKGRAE LLSDWKQQIS PAIEDDNALA GPVTDSHGSS QNKFGFNHRR
IESCESENAG SALHAPETDR RSEAMKVVAP LTEPLIDSRK KNNVLTTRAS RRLR
//
