ID A0A091DZ90_FUKDA Unreviewed; 979 AA.
AC A0A091DZ90;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
DE Flags: Fragment;
GN ORFNames=H920_02207 {ECO:0000313|EMBL:KFO36402.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO36402.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO36402.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO36402.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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}.
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DR EMBL; KN121439; KFO36402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DZ90; -.
DR STRING; 885580.ENSFDAP00000001503; -.
DR eggNOG; KOG0239; Eukaryota.
DR Proteomes; UP000028990; 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; 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 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:UP000028990}.
FT DOMAIN 547..870
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 160..263
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 300..334
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 367..447
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 502..533
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 34..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 630..637
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO36402.1"
SQ SEQUENCE 979 AA; 109491 MW; 707D8884A839E99C CRC64;
PEKATKPRAM VPSPRTRNLG ATPSLPSLRR VGRAGELPEP KMARRGKDTV VGSDEDSSAR
IAARPALGQC RTLSGDWAGP GSPRRLYLTV RQALQDKGCE SKSQGTKEDN LSKRQALVPR
RDREALKAGA ATNVEKTGGR LFGRGRCSNL PGSPGAAPEV HRMVEAMSQL QKEKAQLQEE
LVVLRERLAL HNSDQQATTT QLQNQVENLK EKLVSQAQEV TRLRSELRGT ELEKHRDPLM
VENERLRQEL GRYEAELQEL RVQPAAAAPC SGCKHSQEST QLRHKVSQLQ LEVAENKGML
SELNVEVQQK TDRLAEVELR LKDCLAEKAQ EEERLSRRLR DSHETIASLR AQSPPVKYVT
KTVEVESSRT RQALSESQAQ NQHLQEQVAM QRQVLKEMEQ QLHSSNQLTT QLRAQISMYE
AELERAHGQM LEEMQSMEED KNRAIEEAFA RAQVEMKAVH ENLAGVRTNL LMLQPALRTL
TNDYNGLKRQ VRNFPMLLDE ALQSARAEID EIIEEVNSNN QDLLRKYRRE LQLRKKCHNE
LVRLKGNIRV IARVRPITKE DGEGPEATNV VSFDPDDDAI IHLLHKGKPV SFELDKVFSP
QASQQDVFQE VQALITSCID GFNVCIFAYG QTGAGKTYTM EGTPENPGIN QRALQLLFSE
VREKASDWEY TITVSAAEIY NEILRDLLGT EPQEKLEIRL CPDGSGQLYV PGLTRFRVQS
VADINKVFEF GYANRTTEFT NLNEHSSRSH ALLIVTVQGR DCSTGIRTMG KLNLVDLAGS
ERVGKSGAEG SRLREAQHIN KSLSALGDVI AALRSRQGHV PFRNSKLTYL LQDSLSGDSK
TLMVVQVSPV EKNTSETLYS LRFAERVRSV ELGPGSRRTE LGSWSSQEHL ELEPNCQTPQ
PTARAHSAPG SGPSSRPGSI RRKLQPSGEL SAHDCHNHCF PYLEGPFLSF FLKKNPSLSL
RSSQGGQHCV HFIDGKTRP
//
