GenomeNet

Database: UniProt
Entry: S7PSY6_MYOBR
LinkDB: S7PSY6_MYOBR
Original site: S7PSY6_MYOBR 
ID   S7PSY6_MYOBR            Unreviewed;       675 AA.
AC   S7PSY6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=D623_10020721 {ECO:0000313|EMBL:EPQ11652.1};
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:EPQ11652.1, 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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
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; KE163350; EPQ11652.1; -; Genomic_DNA.
DR   RefSeq; XP_005872620.1; XM_005872558.1.
DR   AlphaFoldDB; S7PSY6; -.
DR   GeneID; 102249344; -.
DR   KEGG; myb:102249344; -.
DR   CTD; 84643; -.
DR   eggNOG; KOG0246; Eukaryota.
DR   OrthoDB; 239968at2759; -.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd01367; KISc_KIF2_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; PTHR47971:SF22; KINESIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR47971; KINESIN-RELATED PROTEIN 6; 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|PROSITE-
KW   ProRule:PRU00283}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000052978}.
FT   DOMAIN          213..543
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          583..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..602
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         303..310
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   675 AA;  75526 MW;  B35E93C648BE3790 CRC64;
     MASQLCLPAA RRLSSLKPLL APSRDVQVGV CVAIQRSDGR IHLAVVTEFK RENTWVTVEW
     VEEGVKKGKK IDLETIFLLN PSLASAEQAT RSRSLSSLSL APSSAIGDRV STRWIARIPP
     KNETPSGDSL SVTVPGSPCL VKWKKSPCLR SIEKLQKQRE TRRQLQVAIR AQRALDVHAG
     NPHHEIMRMI EEYRRRLDRS EVSRLGPPRG DRRICVCVRK RPLNQHEAAM KDLDIITIPS
     DHVVLVHESK QKVDLTRYLE NQTFCFDHAF DDTASNELVY KFTAQPLVES VFRQGMATCF
     AYGQTGSGKT HTMGGAFLGK AQSCSKGIYA LAAQDVFFLL NSPAYEKLGL KVYGTFFEIY
     GGKVFDLLNC KKQLQVLEDG SQQVHVVGLQ EREVCCVEDL LNLVERGNSC RTSGQTSVNA
     HSSRSHAVLQ IILKSRGALH GKFSLVDLAG NERGADTAKA NRKRQLEGAD INKSLLALKE
     CIRALGQNKS HTPFRASKLT QVLRDSFIGQ NSSTCMIATI SPGMSSCENT LNTLRYANRV
     KELTLDFRPP QGCLSRVGHE VPRLLENHIR NPEMSLQREE LMKTPPPMQT EKEEETREME
     TLSTPLMEKT LTSRKEPSQW PGNNIQETAD GVNYDVHFCI VQLLSTLEQK IGILTGIQKK
     LKLLRADLQQ KRKVE
//
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