ID A0A163JC83_ABSGL Unreviewed; 673 AA.
AC A0A163JC83;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 34.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN Name=ABSGL_03902.1 scaffold 4693 {ECO:0000313|EMBL:SAL98373.1};
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:SAL98373.1};
RN [1] {ECO:0000313|EMBL:SAL98373.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL98373.1};
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; LT552071; SAL98373.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163JC83; -.
DR STRING; 4829.A0A163JC83; -.
DR InParanoid; A0A163JC83; -.
DR OMA; VEACQIA; -.
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: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; SSF90257; Myosin rod fragments; 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:UP000078561}.
FT DOMAIN 79..424
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 28..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 432..596
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 34..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 673 AA; 76171 MW; A96530555B53ED1C CRC64;
MPGSRIPVSN HHQQQQLASL TSSFLQSMAD KQPPVSPPST PLLYSPAPLT PSPSSSYPLI
ASKSLRPRQT KSTTIARENI QVMVRCRPPS ETELRNHEED CWLLTPEQGS VKLNDPDGIV
FEYDKVFKGT NNGDIYQAGI QKLVRSTMDG YNGTVFAYGQ TASGKTYTMV IQNQDTYTWN
RLTRSHVHLF IVDLAYFCCT SEEPGVIPKA VQDVFAYIEE EAIDREFLLQ VSYMEIYNEK
INDLLSAKHS PTGLLIRTAN GQDYVENLTA IAVTTPEEVM AFIKLGEERR HTGETDFNEN
SSRSHTIFQL IIESKSRVSS LASVRTSRLN LIDLAGSEKV ATNTERRQEG AFINKSLLTL
GKVITHLNAG AKHIPYRDSK LTRILSASLS GNDRVSVICT INPAWKSKDE STNTLRFAQG
VKKVEINPKI TQVAQHSRLQ NYKEQIVDLE NQMMKKTKQE AETKEKLSHL LGLILTSSKM
MPTATHQDEI NQKEEDLKQL DDRLSQSQQN LEEKTVVIDE LQRAVQDYQR MNDQLQTQLN
KYSDSFAEVS KRWNALEASI NRYKDRVFAS ERRVAILEAQ QQADDYSKRL MGQQLEECQA
RLDQKIQDDF LLAGIESLYE EPIDDENSKD DESIKDGGGG GGDETRTALF LRFLYLNEGS
WLLLFAFAVW LFL
//