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Database: UniProt
Entry: A0A1S3EY40_DIPOR
LinkDB: A0A1S3EY40_DIPOR
Original site: A0A1S3EY40_DIPOR 
ID   A0A1S3EY40_DIPOR        Unreviewed;       932 AA.
AC   A0A1S3EY40;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   Name=Kifc3 {ECO:0000313|RefSeq:XP_012868357.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012868357.1};
RN   [1] {ECO:0000313|RefSeq:XP_012868357.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012868357.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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   RefSeq; XP_012868357.1; XM_013012903.1.
DR   AlphaFoldDB; A0A1S3EY40; -.
DR   GeneID; 105983124; -.
DR   CTD; 3801; -.
DR   OrthoDB; 453489at2759; -.
DR   Proteomes; UP000081671; Unplaced.
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; cd01366; KISc_C_terminal; 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; PTHR47972:SF5; KINESIN-LIKE PROTEIN KIFC3; 1.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 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   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:UP000081671}.
FT   DOMAIN          551..874
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          28..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          173..338
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          385..451
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          506..537
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        113..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..897
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..932
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         634..641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   932 AA;  103761 MW;  42C6D3A031250820 CRC64;
     MVPSRRTWNL GATPSLRGLW RVGRAPEPEL GMARPAPASP AARPFPHTGP GRLRTGRGKD
     TPVSGDEDPS TRIAARPALA QCRALSVDWA GPGSPHRLYL TVQQALQDKG CESKSQGTKE
     DKLLKRPAPR RDREAPEAGG RMNIEKTGKG GGRLFGSGRC SSLSGSPGAA PVVHRMVEAM
     SQLQEEKSQL QEELVVLRER LALHDSDQHA TSTQLQNQVE NLKEKLISQA QEVSRLRSEL
     GGTDLEKHRD RLMVENERLR QELQELRAQP AAPCPGCEHS QESTQLRDKL SQLQLEVAEN
     KGMLSELNLE VQQKTDRLAE VELRLKDCLA EKAQEEERLS RRLRDSHETI ASLRAQSPPV
     KYVIKTVEVE SSKTKQALSE SQARNQHLQE QVAMQRQVLK EMEQQLHSSH QLTAQLRAQI
     AMYEAELERA HGQMLEEMQS LEEDKNRAIE EAFARAQVEM KAVHENLAGV RTNLLTLQPA
     LRTLTNDYNG LKRQVRGFPM LLQEALRSVK AEIGQAIEEV NNNNQELLRK YRRELQLRKK
     CHNELVRLKG NIRVIARVRP VTKEDGEGPE ATNAVTFDPD DDSIIHLLHK GKPVSFELDK
     VFSPGASQQD VFQEVQALIT SCIDGFNVCI FAYGQTGAGK TYTMEGTPEN PGINQRALQL
     LFSEVQEKAS DWQYTITVSA AEIYNEVLRD LLGREPQEKL EIRLCPDGSG QLYVPGLTEF
     QVQSVEDINK VFEFGHTNRT TEFTNLNEHS SRSHALLIVT VRGVDCSTGL RTIGKLNLVD
     LAGSERVGKS GAEGHRLREA QHINKSLSAL GDVIAALRSR QGHVPFRNSK LTYLLQDSLS
     GDSKTLMVVQ VSPVEKNASE TLYSLKFAER VRSVELGPGS RRTELGSWSS QEHLEWEPAC
     QTPQPSARAH SAPTSGTSSR PGSIRRKLQP SA
//
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