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Database: UniProt
Entry: W6QWJ8_PENRF
LinkDB: W6QWJ8_PENRF
Original site: W6QWJ8_PENRF 
ID   W6QWJ8_PENRF            Unreviewed;       717 AA.
AC   W6QWJ8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Kinesin, motor domain {ECO:0000313|EMBL:CDM33897.1};
GN   ORFNames=PROQFM164_S03g000621 {ECO:0000313|EMBL:CDM33897.1};
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM33897.1};
RN   [1] {ECO:0000313|EMBL:CDM33897.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164 {ECO:0000313|EMBL:CDM33897.1};
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA   Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in cheese
RT   making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
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}.
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DR   EMBL; HG792017; CDM33897.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6QWJ8; -.
DR   STRING; 1365484.W6QWJ8; -.
DR   OMA; NRHPQKA; -.
DR   OrthoDB; 47485at2759; -.
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   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24115:SF1014; KINESIN-LIKE PROTEIN SUBITO; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 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; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283}.
FT   DOMAIN          10..479
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          187..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..717
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         111..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   717 AA;  79886 MW;  93480DC0116EE26A CRC64;
     MPPKQPQTSL FQVYLRLRPP MTPNPNECDR FLNVEAPEAS QEETEIVSPA STHVTLQPPN
     DTRKRAVERF GFTKVFEETA SQLDVFHDTG MEPIIRGVLK ENRDGLVATL GVTGSGKSHT
     ILGSKTQRGM TQMALDVIFR SLESTNKTDH GSITPVMLAS LAVADASEAQ LFSAQTFLEA
     VYGEPNGRTS RAQTPMSPSR ANTPLTEPTP ALNFPRRHIR ERPCALPRLP DMSHLTVDMD
     SNADYVVLVS MYEVYNDRIF DLLSPSIASG QGNMSRGNNQ KDRRRPLLFK STEGSPDRKL
     VAGLRKIACS SYEEALAILD VGLTERKVTG TGMNSVSSRS HGFFSLEVKK RTYSKRTGEQ
     NWAGNALTVV DLAGSERART AKTAGATLAE AGKINESLMY LGQCLQMQSN IQDGMKTALV
     PYRQCKLTEL LFSNSFPSSH QMSRGQYPQK AIMIVTADPV GDFNATSQIL RYSALAREVT
     VPRIPSICES ILSAASGSHR SISGSTSPNF DSAEELERAA AEITRLTRDC HGLAVKLAEE
     EIARADVEMR LSAAEERCLM IEQDVREECW AEMDEKMEEE RRRWQRAWDE QIGRNDEHID
     KKVELVSRGF QIFEDSASNE RVEELEQEND QLRRKLAAFE REMHNQSPTR KNRPKNATSA
     RSNPLGRGSD VENALQRMDQ LKLADTMFAP PSPGSSPIKK TRKMGTRKWD LAPEDQI
//
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