ID A0A0N0RTK2_9HYPO Unreviewed; 1756 AA.
AC A0A0N0RTK2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Kinesin-like protein unc-104 {ECO:0000313|EMBL:KOS20129.1};
GN ORFNames=ESCO_006302 {ECO:0000313|EMBL:KOS20129.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS20129.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS20129.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) 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}.
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:KOS20129.1}.
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DR EMBL; LGSR01000018; KOS20129.1; -; Genomic_DNA.
DR STRING; 150374.A0A0N0RTK2; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000053831; 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; 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:UP000053831}.
FT DOMAIN 8..357
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1574..1738
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 626..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 754..820
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1451..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1542..1559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1756 AA; 194370 MW; 72DFD4BAFB8ED681 CRC64;
MAPAGGGNIK VVVRVRPFNG REIDRGSKCI VEMQGNQTVI TPPEGNSVKG AKDTAPKAFA
FDRSYWSFNK DDPNYAGQSN LFDDLGKPLL DNAFQGYNNC IFAYGQTGSG KSYSMMGYGK
DVGIIPNICQ EMFRRIDAVQ ADNTSKCTVE VSYLEIYNER VRDLLNPSTK GNLKVREHPS
TGPYVEDLAK LVVTSFQEIE NLMDEGNKAR TVAATNMNET SSRSHAVFTL MLTQKKYDAD
TKMEMEKVAK ISLVDLAGSE RATSTGATGQ RLKEGAEINR SLSTLGRVIA SLADLSTGKK
KKGGSQVPYR DSVLTWLLKD SLGGNSMTAM IAAISPADIN YDETISTLRY ADSAKRIKNH
AVVNEDANAR MIRELKEELA VLRSKLGGGG GGGGGGAGGA GVTPDEIYDD GTPLEKQIVS
ITAPDGTVKK VSKAEIAEQL SQSEKLLTDL NQTWEQKLAK TEEIHKEREA ALEELGISIE
KGFVGLHTPK KMPHLVNLSD DPLLAECLVY NLKPGTTTVG NVESNADNQV NIRLNGTRIL
HHHCTFENAP DGTVTVIPTE GASVMINGKR ITEPKQLHSG YRVILGDFHI FRFNHPMEAR
AERAEGSAQS TSLLRQSITA SQMQILDRAT SSPSRSHERS FSKASDYGVD GSARSESPFS
RHGKDSDWSF ARREAAGAIL GTDHNFASLT DEELNSLFEE VQRARAERVN GREDGDGDSE
SAASYAFREK YMSTGTIDNF SLDTALTMPS TPKQGDAEDR LREVREELQS QLERQKEEYQ
DQLKSAEAAN VEFEEIKREK ARMEAALVQL KNDMQKQLHL QRRQFEAKIE KMDPLKRPKA
SPRLSEDELE RARQTIKVWR GRHFVKMAES VLQSASILKE AQIMSNELDE NVVFQFTTVD
VGQNLCSSYD MVLNGLTGEG DDAALEEAYK PCVGIRVVDY RHSVARLWSL EKLSDRVRQM
RQMHQYLDQP EYAQHLSLDN PFVETCMPSY TLIGEVDIPL KAVFQSRVQD YQLDVVSPFT
SQEVGIIKLS LEPSHARAPS NTLKFNVVMH ELVGFAEREG TDVHAQLFIP GVSEDDGITT
TQMIRDFDEG PIRFESVHSM SVPLFAPEDV TLRAAIFAKV STMHLDKLLS WDDIRDACPN
NADNAKGARI NESQFFTQEK HDLLSRIQIM ELNEVGQYAA VEVTQTSELD TGTFQLHQGL
QRRICIDICH SSGDALPWGD VTSVRVGQVR LLDSAGKTPD LAPTDADIPL KLASNLVFRE
NPNGTRSITM HAQWDSSLHN SLLLDRVTAE KYRVQMTVSW DISSDKLAEP MKFSQKVCVQ
ILSRTFVRQS SIISSLWQNI RFVRTSTGIF TLTMKPAPIK RVGDLWRMNS QHDYVKGEEN
LHSWTPRGVS LVSDFIVARK KKRRNMEMSL TQTTLARLGL DSWPASEISE DPEPEPSPVI
KPIIPNDDDL LNDTPETSQS DVSAEEAGEA TKPGKRQQQE EEEERGEGEG VAEGSKEQEE
EQEEEGSSAP KSEYDEHHTD VLEKCLKLWR KYPDPLARML SPENTTAPSN GLASETPEPP
SLITTIIRVP KNPKVQKGGY LLVPNNESTR WVKRFVELRR PYLHIHSATD GDEVGLVSLR
NSRCDSQPGV LGLLHGPDDY DMPPGHGPNH AGPDFTPGHR RTGSGRVIST IWTAAAGGAP
GLAGAGGANG GHPGLTRLSE RMQSAVFAIY GTDNTWLFAA RSERDKMDWL FRIDQTFSAE
SASGSGAISP RVAHDY
//
