ID A0A0A2KTM6_PENIT Unreviewed; 954 AA.
AC A0A0A2KTM6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 03-MAY-2023, entry version 35.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=PITC_064630 {ECO:0000313|EMBL:KGO67700.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO67700.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO67700.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO67700.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO67700.1}.
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DR EMBL; JQGA01001270; KGO67700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KTM6; -.
DR STRING; 40296.A0A0A2KTM6; -.
DR HOGENOM; CLU_001485_24_0_1; -.
DR OMA; LNTMKFA; -.
DR OrthoDB; 5476186at2759; -.
DR PhylomeDB; A0A0A2KTM6; -.
DR Proteomes; UP000030104; 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:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 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};
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:UP000030104}.
FT DOMAIN 214..565
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..954
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 954 AA; 102942 MW; 80D3E06580A374A9 CRC64;
MASMSTLQQS SQLSRLSNPP AGSLPPLPNP KPRKSTGSDT PRAASPYQTS KLRTPSSPKP
SLKSPLSTSN STSNLNTARS TSGGRTPGSP DKSLRRTISI ASFPQPPKAS SRPSTASSLS
GIQGATSSVR PQRSSRLSTG TTSSYRSSKT PSLFTGGGEG KFISSGDARD PDASPTHSRS
SSAQGSCSTS ATTFEDADDA TGKSNSKPKE IKGNVLVSVR VRPDNNNGGE TSRNHGEWSV
DSRQSLISYR GKEGGDYFYD NVFNPQENNA KVYDSAAKRL VRRVMEGYHG TVFAYGMTGT
GKTFSMQGTA TSPGVIPLAI TDIFSFIRET PHREFLLRVS YLEIYNEKIN DLLSASAANA
PAGAQQEEIK LREDSKRGVY ATPLKEEIVQ SPTQLLRVIA RGDHARRTSS TQFNARSSRS
HAVVQIVVES RERVPSGSAQ DKRSGIAPGG VRVSTLSLID LAGSERAAED KERRTEGAHI
NKSLLTLGTI ISRLSENKDK QGNPADGDGR HLPYRDSKLT RLLQPALSGG SLVSILCTIQ
LTSAINSHTG ETLNTMKFAA RAKNNIVSHA KKAEEAYGSG GGDSGSRVLL ERYRMEIQAL
RGQLDTQAKS QAEKELRWDE QQYEKEAQAR HEEQMLEMQL ARTALKERIE HLNRLILSSK
STGVNRHNSL SAFGRFSRMS ATDSGTRSLR SSASQSTLGA GHSSIRPISF ASVNSNDPSS
PMIYPGGSFG NEEEYDLGEF GDGKACLQRQ VTALQADLGD KNRYISTLER RLLQARRSSH
SRMSGGIKPA NPTIAEHPDI SALVREKDIE INELRLQLDD KDRMLAALRS ATRHRDLAAV
TNDSQSPELK SKNGSTAGDR DSFAGTNGFI AQSESPGKRP LSGESEKGDA GKNMDEVSRM
LEEMIQGRAE SGHNPKNRRS IDSDSRRVSS SAEVPSLNPT APSGDPNLSS PFRG
//