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
//