ID A0A3B3THE9_9TELE Unreviewed; 1051 AA.
AC A0A3B3THE9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Kinesin family member 11 {ECO:0000313|Ensembl:ENSPLAP00000000665.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000000665.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000000665.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000256|ARBA:ARBA00004647}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-5/BimC subfamily.
CC {ECO:0000256|ARBA:ARBA00034704}.
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DR RefSeq; XP_014908362.1; XM_015052876.1.
DR RefSeq; XP_014908363.1; XM_015052877.1.
DR AlphaFoldDB; A0A3B3THE9; -.
DR STRING; 48699.ENSPLAP00000000665; -.
DR Ensembl; ENSPLAT00000016048.1; ENSPLAP00000000665.1; ENSPLAG00000001549.1.
DR GeneID; 106959980; -.
DR KEGG; plai:106959980; -.
DR CTD; 3832; -.
DR GeneTree; ENSGT00940000155921; -.
DR OrthoDB; 536293at2759; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0000922; C:spindle pole; 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:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0007051; P:spindle organization; IEA:UniProt.
DR CDD; cd01364; KISc_BimC_Eg5; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR047149; KIF11-like.
DR InterPro; IPR047241; KIF11-like_kin_motor_dom.
DR InterPro; IPR025901; Kinesin-assoc_MT-bd_dom.
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; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 1.
DR PANTHER; PTHR47970:SF12; KINESIN-LIKE PROTEIN KIF11; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF13931; Microtub_bind; 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 Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}.
FT DOMAIN 17..357
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 954..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 366..469
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 598..629
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 681..715
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 883..910
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 957..971
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1051 AA; 118062 MW; 689E77836AF94F73 CRC64;
MASTNGTGGR REEKGRNIQV VVRCRPFNTM EHRASYGVID CDQSRKEVLV RTGGVNDKSS
RKTYTFDMVF GPAAKQIDVY RSVVCPILDE VIMGYNCTVF AYGQTGTGKT FTMEGERTPN
AQFTWEEDPL AGIIPRTLHQ IFEKLSENGT EFSVKVSLLE IYNEELFDLL SPTEDVNERL
QLFDDPRNKR GVVVKGLEEV VVHNKDEVYQ ILERGAAKRR TASTLMNAYS SRSHSVFSVT
IHMKEITLDG EELVKIGKLN LVDLAGSENI GRSGAVDKRA REAGNINQSL LTLGRVITAL
VEKRPHVPYR ESKLTRILQD SLGGRTKTSI IATVSPSSSN LEETLSTLEY ASRAKNIMNK
PEVNQKLTKR TLIKEYTEEI ERLKRDLAAT RDKNGVYLSS ENYESMMTQI TAQEEQIAMM
EEELKKVNDL FLDSKSRLEQ CSMDLDEKQQ RLEETSRHLE KTKEKLVEEE FICSELSSVH
ESLYSAAGQL LSAVGESTSD VSGLHAKLDR KTKVEQHNMQ MQQSFSQRMD GAFSSMQRSV
QQHGAAQARM LTGYAHAVDG LLVGNEATLR GALVAVETLV GGVQALVADG AARCREKVER
HEALTREQRE ALLQLLEEHQ QEVQDVLAVR TLPGLTAIRE LGDTLQVSME TQRDLANQQV
EAMKETGVFL SGLVLDLAAL RQEARTGLSA LQEEQERLQQ QIQRAQQQHQ QGMNRAIQFL
QDQLNLVAME TQQHYSELQA ASRTLQGPVE ALQQNLSSRC DAVEQRSSSQ AERLLSSSSS
LASSLHQAAQ QNRVLLEEMS GRCSDLHGAV SGLVDRDAEW TSRTREQAAH RAQDQLVLME
QLAEEAQSLH QGVETRGAER LRAAEADLSG RQEENRRVLT ALQEQTGSDR AVLERQRAEL
QEQVEAGRQL VRSFLRDELQ QDVPTGLTPQ RREFVYPRVL KKSGSRSELL EALRMRQEEE
EEEDEGPEDD KQSQVDQDSL EDDFSSCSES LAAEPPFVDE NLVFNESKRL PFFKQKKGSR
KETKVLSRSK MADSEGQASP MKSRLPLRCQ N
//
