ID A0A163TGQ6_ABSGL Unreviewed; 883 AA.
AC A0A163TGQ6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN Name=ABSGL_10508.1 scaffold 12026 {ECO:0000313|EMBL:SAM04642.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM04642.1};
RN [1] {ECO:0000313|EMBL:SAM04642.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM04642.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-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}.
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DR EMBL; LT554414; SAM04642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163TGQ6; -.
DR STRING; 4829.A0A163TGQ6; -.
DR InParanoid; A0A163TGQ6; -.
DR OMA; AYMEIYM; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000078561; 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:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 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:UP000078561}.
FT DOMAIN 5..328
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 561..596
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 394..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 425..466
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 607..641
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 668..748
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 790..835
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 527..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 883 AA; 98947 MW; 792CA5F42FF2E666 CRC64;
MSGNNIKVVC RFRPQNSLEI REGGQPIIDI NDEGTQVGLK GDFSGSFAFD KVFGMETPQK
DVFDYSIKSI VDDVTAGYNG TVFAYGQTGS GKTFTMMGAD IGDEKTKGII PRIISQIFDS
IMAAPSNVEF TVKVSYMEIY MEKVRDLLNP SNDNLAIHED KTKGVYVKDL LEIYVGSSDE
VYEVMRRGSN NRVVASTNMN AESSRSHSIV VITITQKNVD SGAAKSGKLY LVDLAGSEKV
GKTGATGQTL EEAKKINKSL TALGMVIYSL TDGKSSHVPY RDSKLTRILQ ESLGGNSRTT
LIINCSPSSY NEAETLSTLR FGMRAKSITN KAKVNSDLSP AELKALLKRV KSETITFQTY
ITALEGEVNV WRTGGSVPED KWVTMDKINK GDFNALPPAP GFKSPTSDDS SRPTTPAIIL
EKDERDELLK RENELMDQIA EKETELANRE KLLESLKEEM TYYKDQEQLV TKENQQMTTE
LTDLRLQLQK ISYESKENAI TVDSLKESNQ ELMAELEELK RNLSEMRISS KDAASDEKEK
KKAEKMAEMM SGFDPSSEIN EKERQIRGAL HKLDGDNNGS LTIEELVTLR RELAESKVLL
EQHGKSIDDL TYEKDALNKK KLDLEGRLGS LEAEYEELLD KTIADEEAQV QKNVDMADTI
SGLKGKLEAQ YTSKRKAQQQ EIDELKKEMD RKNDSHQKLS NALTDLKSAN DQLQTALAEQ
PNEAQSELSE REKDLERMRK TMANQLAEFE VMKKALMRDL QQRCEKVVDL EMSLDETREQ
YNSVLRASNN KAQQKKMAFL ERNLEQLTNV QKQFEAQLQA VRERLEQARS QKSQNSMAAL
SFGRIAKPLR GGGSAVEPSE MPTSPTDKRD KRGSWIAGFI NGR
//
