ID A0A2I2GFI0_9EURO Unreviewed; 1186 AA.
AC A0A2I2GFI0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative kinesin family protein {ECO:0000313|EMBL:PLB51587.1};
GN ORFNames=P170DRAFT_453254 {ECO:0000313|EMBL:PLB51587.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB51587.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB51587.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB51587.1,
RC ECO:0000313|Proteomes:UP000234275};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-5/BimC subfamily.
CC {ECO:0000256|ARBA:ARBA00034704}.
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:PLB51587.1}.
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DR EMBL; MSFO01000002; PLB51587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2GFI0; -.
DR STRING; 1392250.A0A2I2GFI0; -.
DR VEuPathDB; FungiDB:P170DRAFT_453254; -.
DR OrthoDB; 536293at2759; -.
DR Proteomes; UP000234275; 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:0051301; P:cell division; IEA:UniProtKB-KW.
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; IPR025901; Kinesin-assoc_MT-bd_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 Pfam; PF13931; Microtub_bind; 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 Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000234275}.
FT DOMAIN 82..418
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 477..525
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 668..695
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 744..797
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1186 AA; 132511 MW; 920621BFB24317D1 CRC64;
MAGPQRPTSG LPTRRTTTTR SQPTTRRFGS AVGEKPPSKS PAIPTRASTA TSRALKSPGE
PTSITAKKRE RDYEREINED TSIHVVVRCR GRNDRELKEN SGVVVSTEGV KCKNVELSMG
PNALSDKTYT FDKVFSAAAD QVTVYEDIVL PIVNEMLAGY NCTIFAYGQT GTGKTYTMSG
DMTDTLGILS DHAGIIPRVF YSLFNKLEET ESTVKCSFIE LYNEELRDLL SAEENPKLKI
FENETKKGQN SSTLVQGMEE TFIHSATSGI ELLQLGSHKR QVAATKCNDL SSRSHTVFTI
TVQTKRTSES GEEYISSGKL NLVDLAGSEN IQRSGAENKR AAEAGLINKS LLTLGRVINA
LVDKSPHIPY RESKLTRLLQ DSLGGRTKTC IIATVSPSRS NLEETISTLD YAFRAKNIRN
KPQINYMSKK TLLREFTLEI EKLKGELIAT RHRNGVYMTV DAYENLTMEN DSRRIVNEEQ
RAKIESMEAN LRHKVQELFT LTSNFNNLKK DNEETRVSLQ ETEDVLDKTE IVLKDTKTLL
EEEEMLRKAH QETEEQLYDA GTGLLSTLDS TVGDVDGLHA KIQRKADLEN ANMATWQTST
SEVSDVTQKV DMSVQNFQSQ HSELLKTMAE KINGFVADEL SNIQQNQSEL LQRTSSFEKA
EEEARSQTHG AHDEMNEVLE EIKDLREEVK SKVGEGLNGL SAAAARISKE VIGEFTDFHA
QLHGSYSTLG QEFKAMFENM VGHLNGQKTE INRLRLEIQE ANLRTVEANR RASSQLAHTL
EEEQATAEAE RDVLLSQIKT LIEDSRQRQQ GRLKGKVEDV RKEISSSGDT LEHTTAHYDR
QVDEWVFKSE QFAKDVNASR DEIKTKMQND WEVFDQRNIS IQKATESVHE ETVRIVDAQM
NNMDKQMEAL DDFVDKARSQ NGQFRDAHIT SLENMASNVH DSYSSMHDQI SGLGDRVNQL
QEDATQQHLD LEESTAPLSE EVRRPLQTLR ANILQRPLED YVPTGVTPQK RQYEYPSVLP
RTEAHDTLRS RMRMATDLTV LPFNGEEPLS PDVSTGISSS KGFVYNDAAD EVGTQPPPTT
VTPSNTGLRE VDANVAVKPR VSSIDENSPS DPPSGKRKSS SMADSSDIDD LDDQPTKRRR
SSHAPTEAKL PHKMLSKKMA GMMEGRENVP PAGISGSRRL RGSPST
//
