ID A0A229X1A1_9EURO Unreviewed; 956 AA.
AC A0A229X1A1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=CDV55_102494 {ECO:0000313|EMBL:RHZ58495.1}, CFD26_103157
GN {ECO:0000313|EMBL:RLL93657.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL93657.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL93657.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ58495.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RLL93657.1}.
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DR EMBL; NKHV02000123; RHZ58495.1; -; Genomic_DNA.
DR EMBL; NIDN02000281; RLL93657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229X1A1; -.
DR STRING; 1245748.A0A229X1A1; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; 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:SF33; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000215289}.
FT DOMAIN 214..571
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 596..654
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 751..778
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 810..837
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 296..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 956 AA; 103164 MW; 640B2D92B39513B7 CRC64;
MSTIPEPSRP AASPPAGALP PLPAPKVRKS LPLATDIQRA SSPSHSPSKL RTPSSPRSNF
NRSPLSGSIS NQSILRSASG GRRPASPEKS LRRTISIAAF PQPPKVNGRS SVASASSVPH
NIPLGSVRVK SGSRLSSGTT SSYRSSRPPS LLSGHGDGRN GPVLDPREQE ASPTQSRSSS
AQGSYSTSAT TCEDADDATG IAKSNSKNKQ AKGNVIVSVR VRPNLTGADG SASDGDWVVD
GRRGLISYKG KEGGVDYLYD NVFPPHEHNA RVYDAAAKRL VRRVMEGYHG TVFAYGMTGT
GKTFSMQGTA TSPGVIPLAI TDIFSFIRET PHREFLLRVS YLEIYNEKIH DLLSTSGSPG
LAGSQQEDIK LREDSKRGVY ATPLKEEIVQ SPTQLLRVIA RGDLARRTGS TQFNARSSRS
HAVVQIVVES RERAPTSNPS QERRSGMAPG GVRVSTLSLI DLAGSERAAE DKERRTEGAH
INKSLLTLGT IIAKLSENKD KGGTAADREG RHLPYRDSKL TRLLQPALSG NSLVSILCTI
QIDGSGSSAT AGSLSTETLN TLKFAARAKN SIVSHAKRAE EAFGSGGGDA GSRVLLERYR
MEIQTLRSQL ESQAKDQAEK ELKLEEQQLE KEAKMRHEEQ MLEMQLARTA LKERIEHLNR
LILCSKSTGV NSHNGIAAFG RLSRMSTTDS ISRSLRSSVS QSTLGAGGFS SARPVSFLST
NSTEFSVNLP YQNAHLEHEE DEIMGEFADG RASAQRQIAA LQADLNDKNR YISTLERRLL
QARRSSHSRI SMGVKSVNAP SEEPDLRALL REKDMEINEL RLQLDDKDRM LAALRSAARH
RDLAHVTTDP FPADPKIKRA SLNSNGGIMP SYDRAAGSLS SPESDEKGPD GKSMDDVSRI
LDEMIQDRVE SGHLVKGSRG SVRVADEKQR TLEPAAGIPG LNTASTISEK DGTNVM
//