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Database: UniProt
Entry: A0A2N6NGH4_BEABA
LinkDB: A0A2N6NGH4_BEABA
Original site: A0A2N6NGH4_BEABA 
ID   A0A2N6NGH4_BEABA        Unreviewed;      1746 AA.
AC   A0A2N6NGH4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Kinesin-like protein {ECO:0000313|EMBL:PMB66378.1};
GN   Name=unc-104 {ECO:0000313|EMBL:PMB66378.1};
GN   ORFNames=BM221_007366 {ECO:0000313|EMBL:PMB66378.1};
OS   Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS   shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB66378.1, ECO:0000313|Proteomes:UP000235728};
RN   [1] {ECO:0000313|EMBL:PMB66378.1, ECO:0000313|Proteomes:UP000235728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEF-007 {ECO:0000313|EMBL:PMB66378.1,
RC   ECO:0000313|Proteomes:UP000235728};
RX   PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA   Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT   "Characterization of T-DNA insertion mutants with decreased virulence in
RT   the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL   Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
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:PMB66378.1}.
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DR   EMBL; MRVG01000008; PMB66378.1; -; Genomic_DNA.
DR   OMA; RIDKPKR; -.
DR   Proteomes; UP000235728; 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:UP000235728}.
FT   DOMAIN          8..358
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1561..1725
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          619..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1423..1490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1655..1684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          751..828
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1427..1450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1462..1490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1655..1679
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   1746 AA;  193607 MW;  4A2B683D89DAAFAB CRC64;
     MAPAGGGNIK VVVRVRPFNS REIDRGSKCI VEMKDNQTVI STPDGHGGKS AKAEAPKSFA
     FDRSYWSFDK NDSNYAAQSN LFDDLGKPLL DNAFQGYNNC IFAYGQTGSG KSYSMMGYGK
     EIGIIPNICQ DMFSRINQIQ ADATTKCTVE VSYLEIYNER VRDLLNPSTK GNLKVREHPS
     TGPYVEDLAK LVVGSFQEIE NLMDEGNKAR TVAATNMNET SSRSHAVFTL MLTQKKYDAE
     TKMEMEKVAK ISLVDLAGSE RATSTGATGA RLKEGAEINR SLSTLGRVIA ALADLSTGAK
     KKKGGSQVPY RDSVLTWLLK DSLGGNSMTA MIAAISPADI NYDETLSTLR YADSAKRIKN
     HAVINEDANA RMIRELKEEL ALLRSKLGGG TVGAGGAPIP ADEIYDENTP LEKQMVSITG
     ADGLPKKVSK AEIAEQLSQS EKLLTDLNQT WEQKLQKTEE IHKEREAALE ELGISIEKGF
     IGLHTPKKMP HLVNLSDDPL LAECLVYNLK PGTTTVGNVD TNADHQANIR LNGTRILHDH
     CTFENAAADG TVTVIPSEGA SVMVNGKRIT EATQLHSGYR VILGDFHIFR FNHPMEARAE
     RAEVGNSLLR QSVTASHIQA WERSTSSPTP GSRPGHERAY SKASDFGDLS RPESPSLRNN
     RDTDWSAARR EAAGAILGSD QTNFTSLTDE ELNALFEEVQ RARAERVIVR EDGEDTESVT
     SYQLREKYMS NGTIDNFSLD TALTMPSTPK QGEAEDRLRE VREELQSQLE KQKEEFQDQL
     KSAEAANVEV EEIKREKVKM EAALQELKED MQKQLKMQKK QFEDKIEKMD PLKRPKASSK
     LSEGELERAK KVIGIWRDRH YVKMAETVLQ NAAVLKEAQI MSNELDESVV FQFAVVDVGH
     VMCSSYDMVL NGLTSEGEDV ALEETPKPCI GIRVIDYRNN VVRLWSLEKL HDRVRQMRQM
     HQYLDQPEYA QHLSLDNPFI EHCMPSYTLI GEVDVPLKAV FESRVQDFSL DVLSPYTSHA
     IGIVKLSLEP SHARAPTNTL KFNVVMHEFI GFAEREGTEV HAQLFIPGVS EEDGVTTTQM
     ITEFDEGPIR FESVHNMSVP LFAPQDVMLR ASIYAKVQPM HLDKLLSWDD MRDAAPSRDG
     TKASRINEAQ FYTQEKHDML SRIQILELNE MGEYAPVEVT QVSELDTGTF QLHQGLQRRI
     AINIAHSSGD ALPWGDVTAV RVGKVRLVDS GGKTPDMGAS EPDIQLRLTS HPIFRQNPNG
     TRSITVFAQW DSSLHNSLLL DRVTADKYKV QMSISWEISS EKLAEPMKFS QKVCIQVLSR
     TFVRQTSMFS ALWQNMRFIR SSTGIFTITM RPAPIKRVGD LWRMNSRHDY VKGEENLDSW
     NPRGVSLVSD FILARKKRRR IAEIGAVHMM LHVLGIDPSG QLVKEASEPE PEPEIQKPVL
     PDDDDLLHDT PEASQVPCLE EEAEARAADA GIEDEAKGEG EADGEETVKV EVSATSEKPI
     YNEQQVELLQ QCLSLWLKYP DPLAKILSPA NTAPPTNGVT SEPPELPSLI TTVVRVSKNP
     KVLKGGYLLV PNSDSTRWVK RFVELRRPYL HIHSASDGDE VALVSLRNSR VDSQPGVLAL
     LNGPDDYDNA PGQNGGADFI PGHRRTASGR VISTIWTGNN NGGSSSSSSS GTRANNGGGP
     GLQRLSERMQ AGVFAIYGTD NTWLFAARSE RDKMDWIFRI DQTYMSAAGE SQPGSGFASP
     HPGSDY
//
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