GenomeNet

Database: UniProt
Entry: S7MVA1_MYOBR
LinkDB: S7MVA1_MYOBR
Original site: S7MVA1_MYOBR 
ID   S7MVA1_MYOBR            Unreviewed;       594 AA.
AC   S7MVA1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=D623_10006868 {ECO:0000313|EMBL:EPQ08399.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ08399.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA   Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA   Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA   Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   EMBL; KE162470; EPQ08399.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7MVA1; -.
DR   eggNOG; KOG4280; Eukaryota.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000394};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000394};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052978}.
FT   DOMAIN          1..215
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          357..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          224..251
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        394..409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..441
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   594 AA;  66838 MW;  6FF095223D4D090E CRC64;
     MIEERPTHAI TVRVSYLEIY NESLFDLLST LPYVGPSATP VAIVENPHGV FIKGLSVHLT
     SQEEDAFSLL FEGETNRIIA SHTMNKNSSR SHCIFTIYVE ARSRTLSDEK YITSKINLVD
     LAGSERLGKS GSEGRVLKEA TYINKSLSFL EQAIVALGDQ KRDHIPFRQC KLTHALKDSL
     GGNCNMVLVT NIYGEAAQLD ETLSSLRFAS RMKLVTTEPA VNEKYDAERM VKNLEKELVL
     LKQELAIHDS LANRSHVNYD PMDEVQIAEI NSQVRRYLDG ALDEIDIINL RQIQEVFNQF
     RVVLTQQEQE VEAALRRKYT LIDKNDFAAI SAVQKAGLMD ADGHLVGESD GQGFGLGVAS
     YSSKPGKKTK SRRTLKEQLS SPAKKEGGSS PVSGKDMDVS TSKTQLTPLS KEGDVKDVIV
     RDRETSNIET LPSDSPKEEP RPPRPSTPPS KPVAFEDFKN ERGSEINRIF KENKSILNER
     RKRASETTQR INVIKREIDV TKEGLSAQKS LREKQGEYEK KGLIIIDEEE FLLILKLKDL
     KKQYRAEYQD LRDLRAEIQY CQHLVDQCRH RLLTGVRSGK GGGRRSSGTR RPGF
//
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