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Database: UniProt
Entry: A0A3M0IIF5_HIRRU
LinkDB: A0A3M0IIF5_HIRRU
Original site: A0A3M0IIF5_HIRRU 
ID   A0A3M0IIF5_HIRRU        Unreviewed;       885 AA.
AC   A0A3M0IIF5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=DUI87_35484 {ECO:0000313|EMBL:RMB88148.1};
OS   Hirundo rustica rustica.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC   Hirundo.
OX   NCBI_TaxID=333673 {ECO:0000313|EMBL:RMB88148.1, ECO:0000313|Proteomes:UP000269221};
RN   [1] {ECO:0000313|EMBL:RMB88148.1, ECO:0000313|Proteomes:UP000269221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chelidonia {ECO:0000313|EMBL:RMB88148.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:RMB88148.1};
RA   Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA   Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT   "A high quality draft genome assembly of the barn swallow (H. rustica
RT   rustica).";
RL   Submitted (JUL-2018) 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,
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:RMB88148.1}.
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DR   EMBL; QRBI01000350; RMB88148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0IIF5; -.
DR   STRING; 333673.A0A3M0IIF5; -.
DR   Proteomes; UP000269221; 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   CDD; cd01369; KISc_KHC_KIF5; 1.
DR   Gene3D; 6.10.250.1590; -; 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:SF56; KINESIN MOTOR DOMAIN-CONTAINING 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|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   Microtubule {ECO:0000256|RuleBase:RU000394};
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:UP000269221}.
FT   DOMAIN          1..293
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          336..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          815..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          381..482
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          565..648
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          675..809
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        655..669
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         54..61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   885 AA;  99325 MW;  9E2F688FB6B55899 CRC64;
     MAEPSSECSI KGKPYVFDRV FPPNTTQEQV YHACAMQIVK DVLAGYNGTI FAYGQTSSGK
     THTMELHDPQ QMGIIPRIAR DIFNHIYSMD ENLEFHIKVS YFEIYLDKIR DLLDMTKTNL
     SVHEDKNRVP YVKGCTERFV SSPEEILDVI DEGKSNRHVA VTNMNEHSSR SHSIFLIHIK
     QENVETEQKL SGKLYLVDLA GSEKVSKTGA EGAVLDEAKN INKSLSALGN VISALAEGTK
     AYVPYRDSKM TRILQDSLGG NCRTTMFICC SPSSYNDAET KSTLMFGQRA KTIKNTASVN
     LELTAEQWKK KFEKEKEKNK ALRETLARLE AELSRWRSGE AVPETEQLNE AEPGPGEGPG
     EGQGGVPEEP PLNDNSSSIV IHISDEERRK YEEEIRKLYK QLDDKDDEIN QQSQIMEKLK
     QQMLDQEEVL AAARGGGEAA RRELAALRAE HGAARAEVTE VLAALEELAR SYDRKAQEAE
     DTGRHNRRLA DELARTEATT LSLESELSRA RELGGQQRRR AAEVLNGLLR DLSELSALVG
     SGDIKLPVEV SGAIEEEFAV ARLYISKIKS EVKSVVKRCR QLENLQVECH RKLEVTGREL
     SSCQLLISQH EAKIRSLTEY AQSLELRKRH LEEAHDALGE ELARLQAQEA AQGAARKQRE
     QDESQDTDEV KAALELQLES QREAQHKQLA RLRDEVNERQ KTIDELRELL YERHEQSKQD
     LKGLEETVAR ELQTLHNLRK LFVQDVTTRV KKLVRDNADL RCELPKLEKR LRATAGRVQA
     LEGALRAAKE GARLDKRRYQ QEVERIREAV RARGARRGPG AHIAKPVRPG QVPSPTGLSY
     TNSLFQGYPG GSPLPGPHGL SDLSCACEAE EAARLLPLRQ ETAAS
//
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