ID A0A194VU62_9PEZI Unreviewed; 953 AA.
AC A0A194VU62;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=VM1G_02736 {ECO:0000313|EMBL:KUI67345.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI67345.1};
RN [1] {ECO:0000313|EMBL:KUI67345.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI67345.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) 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}.
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DR EMBL; CM003100; KUI67345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VU62; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000078559; Chromosome 3.
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}; 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}.
FT DOMAIN 214..568
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 816..843
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 294..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 953 AA; 102511 MW; 008343DED907721E CRC64;
MTTALPKPSR SSSNGPPSMA LPALPVTKTR MSSGLQAPST PVRSLASTPK SGLRAPSSAI
GPPPSTPAPM SALTQPRAMS AAVNGSPKSL RKTVSINSFP QPPRGNTRIG SLPPSPLSGN
RKAKASNSTD NHASGTASLL NNSAEGKSVT RASARFSDGL ISVSSPPQSR SSSAQDSYST
SATTYDEPID ATTAKTSTDV ASKRQSKGDN SKGNVVVSVR VRPDAGSQDQ RPDGEWLVDG
RKALIGYRGK EGGDYYYDNV FATHDDNSRV YDHIAKRLVR RVMEGYHGTV FAYGMTGTGK
TFSMQGTASS PGVIPLAITD IFSYIRETPS REFLLRVSYL EIYNEKIHDL LSMPTNGGVG
GAAVQEEIKL REDSKRGVYA SPLKEEIVQS PTQLLRVIAR GDQARRTAST QFNSRSSRSH
AVVQIVVESR ERIPGGPAAP GDKRSGLLPG GVRVSTLSLI DLAGSEKAAE TKERRQEGSH
INKSLLTLGT VIAKISEHKD SKSDKDGKHL PYRDSKLTRL LQGALSGDSL VSILCTIQTG
SSGSAAAVTT HTNETLNTLK FASRAKNNLV SHAKRAEEAL GAGGEGGARV LLERYRMEIQ
ELKAQLETQA KKDKKDKKED DTEMTKDAEE ELAREREAAA RHEEQMLEMQ LARTALKERI
DHLNRLILSS KSIGVNASGT WSSLSINQRF SQASMRSSLT PSQASKPMLE RSSSLASSAS
TIGQRPSLEH RISTSGDRSL GDEDDSVGEF GDGTASLQAQ NRALQADLAD KNRYITTLEK
RLLQARRASS SRASSGTVSG SKGIMVGEDH SVSAALKEKD AEIAELRAQL EDKDRMLIAL
RSAARRGENA ERSIESRASL LFESGSHPGS PASSSRPSFR NSIRSSPKDH RKSGDDVSRI
LDEMLQDRVE AGHIVRSTRG SVRVVNREKT IGEHTQTSRQ SSESNRRPVV VEV
//
