ID M3K5A4_CANMX Unreviewed; 848 AA.
AC M3K5A4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=G210_4111 {ECO:0000313|EMBL:EMG50460.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG50460.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG50460.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) 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:EMG50460.1}.
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DR EMBL; AOGT01000257; EMG50460.1; -; Genomic_DNA.
DR AlphaFoldDB; M3K5A4; -.
DR STRING; 1245528.M3K5A4; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_001485_21_2_1; -.
DR OMA; MQRNAFP; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; IEA:UniProt.
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 GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd01370; KISc_KIP3_like; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF13; 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};
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:UP000011777}.
FT DOMAIN 30..417
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 173..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 848 AA; 95714 MW; 258F386B2E797DF7 CRC64;
MSHPTSLESS STSARPTTIA SSIPTAKQSS ISVAVRVRPF TAAESDKLIK IDNDEIFLGD
GCLSSDRNGS TSAASSGTNR RSHIGVYGGL RKIINVVDDR MLIFDPSETN PLTKMQKNAF
PNSFKGSRIR EHRFVFDRLF DEDSSQDQVY KNTTQPLLDS ILDGYNATVF AYGATGCGKT
HTISGTPDDP GVIFLTMKEL YQKIEELSDR KIIDVSLSYL EIYNETIRDL LHPETRCQSL
VIREDANNKI SVANLSSHRP NSVEEVMELI IHGNRNRTSS PTEANATSSR SHAVLQINVV
QKDRTADTSQ EHTFATLSII DLAGSERAAA TKNRGARLNE GANINKSLLA LGNCINALCD
PRRKNHVPYR DSKLTRLLKF SLGGNCKTVM IVCVSPSSQH YDETLNTLKY ADRAKEIKTK
IIRNQHNLDR HVGSYLKMIT EQKQEIEELR ARETKVVNTA LARRQDLETK VFKLLLDSLD
STRQALAKQN QDKWKKYFIL AKRKLLLLQK IDTETILNEK TDDDDNTNGN TTIGKIYDLC
EQLIMKIKNQ LPQLEDQYSQ RTDTDYILEE SALLTLKRLE GEDGWTEYHS KMYTNAIEAM
KRDVHTDLLM YSSILYDNLI HDLATFGYIP SAIGQILGQT PQDTVLQEIV IGLENLVNGD
FDFAMEQHAM EFMKTKLTND HGGNSHEESF MMIDDNDDDD SEEFGMPTKK QRLDSPPRAL
RKPKRMSRIT SKLKKPSHWE STNNNLMYDT SMEENSIIQT ENKFDDLPDT SPKVNNILHD
INDLDLPFDP MLDSPPQQEK TSKKLLADLK RNRSPPSLPN RKISGTNIPD TRMPLLNKQA
ASRITSDS
//