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Database: UniProt
Entry: A0A1V6TX68_9EURO
LinkDB: A0A1V6TX68_9EURO
Original site: A0A1V6TX68_9EURO 
ID   A0A1V6TX68_9EURO        Unreviewed;      1007 AA.
AC   A0A1V6TX68;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN   ORFNames=PENFLA_c003G09425 {ECO:0000313|EMBL:OQE30540.1};
OS   Penicillium flavigenum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE30540.1, ECO:0000313|Proteomes:UP000191342};
RN   [1] {ECO:0000313|Proteomes:UP000191342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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   -!- 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:OQE30540.1}.
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DR   EMBL; MLQL01000003; OQE30540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6TX68; -.
DR   STRING; 254877.A0A1V6TX68; -.
DR   OrthoDB; 239968at2759; -.
DR   Proteomes; UP000191342; Unassembled WGS sequence.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; cd01370; KISc_KIP3_like; 1.
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:SF13; KINESIN-LIKE 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191342}.
FT   DOMAIN          9..381
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          640..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          396..423
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        645..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..750
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..872
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         135..142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1007 AA;  110786 MW;  ECB5604C34147F23 CRC64;
     MAASDGASSI SVAVRVRPFT IREAAQITRC DEGPLFLGDG SLAGAPTPKL NQKGIRSIVK
     VIDDRCLVFD PPEDNPVQKF SRSVVPNGKR VKDQTFAFDR VFDQNTSQGE VYESTTRSLL
     DNVLDGYNAT VFAYGATGCG KTHTITGTAQ QPGIIFLTMQ ELFERIDERA GEKSTEISLS
     YLEIYNETIR DLLVPSGSSG KGGLMLREDS NQSVSVAGLS SYHPQNVGEV MDMIMRGNER
     RTMSPTAANA TSSRSHAVLQ INIAQKDRNA DVNEPHTMAT FSIIDLAGSE RASATQNRGE
     RLFEGANINK SLLSLGSCIN ALCDPRKRNH IPYRNSKLTR LLKFALGGNC KTVMIVCVSP
     SSQHFDETQN TLRYANRAKN IQTKVTRNVF NVNRHVKDFL VKIDEQMNLI NELKAQAKDY
     EKVAFAKFRK QGEKKDAVLR EGVARIRNAY EHTLPERQEK TNNMLKLRQI GRRIGILSSW
     IAAFDNVCAA RENEEGLSNL YAVRKSAQGI LLELEGSRHH YNQKLSKNTW DRAVTSAVEN
     SAKQLREFDI TDNSDYANLN REAELLRSNA EREALTAVVE QDKAGEAAAV QLLLQAQFEM
     MSSIGDIMQL NASDAIKKGR VILTKMLEDC SDVATNLVKP DGTMPSVPNV SSARPPSPTK
     TKKRFSLVSL PPVSNANPPV TLTPAAPASP TKGSPRRRKG TAGRKSVSFT PKKVQVKVPK
     RSVRWKDDEE DGTLTEFQKT PKKVDSADES SFEDSLLPPR SGSPIPRNIP RVVSPSGSIS
     PTSDEPAEFA GPALNVQKNN SRFKAGFLTK RTGSSPLAPP PSSSLPLSRR ESSPLRDIEG
     SSFMNRTSTE RPSRIAVRSP SGNFSSSPVS ENRDNWKSDK EEAIKINSAM RRMSSGRIAS
     GQFGTQSSNA LRVHRRRSPT SNTYGTPPAD NHMFTASQAR RMVKSEREHD TKPRVLSPHT
     LPVMKHTGRR TTLGGDGRPR NISLSSRDAI RLSAMAAPPT DHNSQAW
//
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