ID   A0A0M4EVC7_DROBS        Unreviewed;       613 AA.
AC   A0A0M4EVC7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Sub {ECO:0000313|EMBL:ALC41557.1};
GN   ORFNames=Dbus_chr2Rg1136 {ECO:0000313|EMBL:ALC41557.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC41557.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC41557.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC41557.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   EMBL; CP012524; ALC41557.1; -; Genomic_DNA.
DR   RefSeq; XP_017835425.1; XM_017979936.1.
DR   AlphaFoldDB; A0A0M4EVC7; -.
DR   SMR; A0A0M4EVC7; -.
DR   STRING; 30019.A0A0M4EVC7; -.
DR   GeneID; 108594798; -.
DR   OMA; IDGDHTF; -.
DR   OrthoDB; 3109027at2759; -.
DR   Proteomes; UP000494163; Chromosome 2r sequence.
DR   GO; GO:0015630; C:microtubule cytoskeleton; 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   CDD; cd00106; KISc; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24115:SF1014; KINESIN-LIKE PROTEIN SUBITO; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 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; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000494163}.
FT   DOMAIN          81..474
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          565..610
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         164..171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   613 AA;  70341 MW;  E56F381B1873C637 CRC64;
     MDKCQENTNK RDARSFLCAR EPSIDRRYRP RPNKQKRLFN EAIPESEDSL DYSDTESENT
     EATPNFTDDG TTADIKEIES GPQVFLRLRP VDLDSSSYVV SECGNTLIVN PPANENTSNN
     VNRMEKHYSF SGIFDSYVDQ KEIYEKCVAP KILEEECLTL MTYGTSGSGK TYTLLGDCVR
     PGVIPRALEN IFRMYGTRIY NTPSLKLVNS ELNILGDSAI AKELQIHLAM LAQCPDISSL
     HQRQQKVIED DYEFQPKPLG DVSVMIWVSF AEIYNEQVYD LLTLSSKQSS KCETRRKNLK
     IVGNNGKAFI KGLTSVFVKR SEEAFKLLRL GQQRLTYAST AVNANSSRSH CIFTLDVLKY
     YRSGNTTQCS YKFCDLAGSE RVDKTGTKGF RLKEAQSINT SLMVLGRCLD AASSSQKKNN
     TDLIPYRESK LTMLLQAPLL GRERLAMIVT VTPLDKYYEE NLNVVNFASI AKDIIFKQPM
     IMRHKKRYSV FAESNGIDTQ YVERLEEENH SLLAEIERLR YENVLQMQLQ EEKLRKELTD
     RFQDSIQTNL DANQERMDKM KVLLNREHEA KMAAQKRKYE EEIEDLREEI EDLKEELQEL
     KSSNSDIEII DDD
//