ID A0A1Y2DUJ0_9PEZI Unreviewed; 926 AA.
AC A0A1Y2DUJ0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=BCR38DRAFT_345294 {ECO:0000313|EMBL:ORY62907.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY62907.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY62907.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY62907.1,
RC ECO:0000313|Proteomes:UP000193689};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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}.
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:ORY62907.1}.
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DR EMBL; MCFJ01000008; ORY62907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2DUJ0; -.
DR STRING; 1141098.A0A1Y2DUJ0; -.
DR InParanoid; A0A1Y2DUJ0; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000193689; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; cd01369; KISc_KHC_KIF5; 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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF29; 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 ECO:0000256|RuleBase:RU000394}; Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:ORY62907.1};
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:UP000193689}.
FT DOMAIN 6..329
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 395..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..533
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 639..708
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 757..849
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 406..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 926 AA; 102578 MW; E97C4198FDC77E77 CRC64;
MSGANSIKVV ARFRPQNKVE LASGGQPIVK FDGDDTCAIT SAEAQGSFTF DRVFDMKTAQ
SDIFDYSIKP TVDDILNGYN GTVFAYGQTG AGKSYTMMGT SIEDDEGKGV TPRIVEQIFS
SIMSSPGTIE YTVRVSYMEI YMERIRDLLQ PQNDNLPVHE EKNRGVYVKG LLEIYVSSVQ
EVFEVMRRGG NARAVAATNM NQESSRSHSI FVITITQKNV ETGSAKSGQL FLVDLAGSEK
VGKTGASGQT LEEAKKINKS LSALGMVINA LTDGRSSHIP YRDSKLTRIL QESLGGNSRT
TLIINCSPSS YNDAETLSTL RFGMRAKSIK NKAKVNAELS PAELKAMLKK AQTSMSTFEN
YISNLEGEIQ LWRAGEAVPK ERWTPAMSEG VVATKADARP ARPSTPSRLI TDSRSETPAL
TERAGTPGIP LDKDEREEFL RRENELQDQL SEKESQVVAA EKSLAESKDE LSFLKEHDSK
LGKENEKLTT EVNEAKMQLE RIAFESKEAQ ITMDALKEAN SELTTELDEV KQQLLDVKMS
AKETSAVLDE KEKKKAEKMA KMMAGFDLGG DVFSENERTI AQAIQHVEAL YEQSSAGDPI
PPDDISDLKA RLVETQGIIR QAELSLYSGI SSDSDARRRQ ELETRLEVMQ RDYEELLTRN
LSDADVEEVK ERLKEAYANK QTTQMELVDE LKADIAQKAA ENARMKTLID DLQIRIKSGA
VAAPGLANGK TIQQQIAEFD VMKKSLMRDL QNRCERVVEL EISLDETREQ YNNVLRSSNN
RAQQKKMAFL ERNLEQLTQV QRQLVEQNGA LKKEVAIAER KLIARNERIQ SLESLLQDSQ
EKLTAANHRF ESQLTAVKER LEAAKAGSTR GLNSPTGNGG FSFGSRIAKP LRGGGEAAPA
QVPTITNLQN ESGAGNKRSS WFFQKS
//
