ID A0A074WJZ8_9PEZI Unreviewed; 919 AA.
AC A0A074WJZ8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 37.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=M436DRAFT_66517 {ECO:0000313|EMBL:KEQ70107.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ70107.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ70107.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ70107.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(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,
CC ECO:0000256|RuleBase:RU000394}.
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DR EMBL; KL584718; KEQ70107.1; -; Genomic_DNA.
DR RefSeq; XP_013424369.1; XM_013568915.1.
DR AlphaFoldDB; A0A074WJZ8; -.
DR STRING; 1043004.A0A074WJZ8; -.
DR GeneID; 25414062; -.
DR HOGENOM; CLU_001485_3_1_1; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000027730; 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 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:SF15; KINESIN-LIKE PROTEIN KIN-4A; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000027730}.
FT DOMAIN 5..329
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 371..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 516..550
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 679..706
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 765..834
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 371..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..919
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 919 AA; 101808 MW; F803F16A6C8AF1E2 CRC64;
MASNSIKVVA RFRPQNKVEL ASGGTPIVQF ESPDTCNVQS RDGGGGAFTF DRVFDMGCRQ
SDVFDFSIRP TVDDILNGYN GTVFAYGQTG AGKSYTMMGS DIGSNDHKGV IPRITEQIFA
SIMASESNIE YTVRVSYMEI YMERIRDLLV PQNDNLPIHE EKNRGVYVKG LMEVYVSSVD
EVYQILERGG MSRAVAATNM NQESSRSHSI FVITVGQKNV ETGSVKSGQL FLVDLAGSEK
VGKTGASGQT LEEAKKINKS LSALGMVINA LTDGKSSHVP YRDSKLTRIL QESLGGNSRT
TLIINCSPSS YNDAETVSTL RFGMRAKSIK NKAKVNQELS PAELKALLRK AQSQVSDFET
YISTLESEVG NWRKGQSVPK EQWTPTLKNG PARSAPRPAT PSLLSEQRKG AETPSSRPDS
RLDLERAGTP TTALEKDERE EFLRRENELQ DQLAEKESVI ATNEKALQDT RQELRDLRET
HSRVNKDNEK LAGDVESLKM QVERITFETK EESIMMDSLK EANNDLSNEL DELRKELLEA
KMNARETSAV IDEKEKLKKE RMAQMMAGFD LGDEVFSENE RNVQEAIKQL DVLLESASNG
DALGLEPLTK LRERLVATQG AIRQVDHSNQ GGALEHKLLT VQKQYEELLQ TNLSEADVED
VKRRLQESLE SHTGGQAGSS DLNAALARQQ EENSRMRNEV ESLRRQTVNG ANGAKSLHQQ
LADFDAMKKS LMRDLQNRCE RVVELEISLD STREQYNSVL RSANSKQQQK KLAFLERNLE
QLTQVQRQLV EQNAQLKKEV AIADRKLAAR GERIHGLEQL LGESQEKLMQ ANHRFEAQLT
AVKERLEAAK VSAASRNGMV AGGGGAAPNG FGSELGSRIA KPLRGGGGAG PMVPTLAGLQ
QQSQQDGPKR SSWFFNQRT
//