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Database: UniProt
Entry: A0A229X1A1_9EURO
LinkDB: A0A229X1A1_9EURO
Original site: A0A229X1A1_9EURO 
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
//
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