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Database: UniProt
Entry: A0A163JC83_ABSGL
LinkDB: A0A163JC83_ABSGL
Original site: A0A163JC83_ABSGL 
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
//
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