ID A0A096LZ58_POEFO Unreviewed; 636 AA.
AC A0A096LZ58;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000024449.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000024449.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AYCK01014904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096LZ58; -.
DR Ensembl; ENSPFOT00000024592.1; ENSPFOP00000024449.1; ENSPFOG00000005596.2.
DR GeneTree; ENSGT00940000159632; -.
DR Proteomes; UP000028760; 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 GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd01376; KISc_KID_like; 1.
DR Gene3D; 1.10.150.280; AF1531-like domain; 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 InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR24115:SF1000; KINESIN-LIKE PROTEIN KIF22; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR Pfam; PF12836; HHH_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 SUPFAM; SSF47781; RuvA domain 2-like; 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:UP000028760};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 30..355
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 375..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..476
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 375..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 636 AA; 71396 MW; 35386B9C803499D9 CRC64;
LLCVAQAFGE ISKMAQRLTV SDGVSKKTSR VRVAVRLRPY MSRQDEKDEG PCVRGLDSQN
LEIINWRNAT ETVKYHFSIF YGEQTTQQEV FLSSVKPILP HILNGQNASV FAYGPTGAGK
THTMLGTAEQ PGVIPRAVRE VFNLVSAKDE DEGWDYSIGM SYLEIYNEKV LDLLSPNSQD
LPIRENKDKN ILIPGLTHTA ISSFSDFDKH FIPATLNRTT ASTKLNQRSS RSHAILLIKV
VRTQRALPHR QQTGKLYLVD LAGSEDNRRT GNQGIRLKES GAINLSLFTL SKVVDALNSG
TAARIPYRDS KLTRLLQDSL GGSAHSVMIT NIAPEYRYYF DTFSALNFAA KSKLIVNKPF
TRETVAVPVL PAPVKRSREE HEAVGSGAEP HKKKQKEEKK SEQDGSSPSA HYHSLSEPSV
MERLIALEKL MMSCQDRNRQ SVLKDVAQSR KEIQELKEKQ REFERKAMLL SQLAKEKSSS
KDEAAFKNTL APLQRKQPNV TKPNKQQAVV QPMQGQNDGN RFVMEEEGGE SRNRKDENKI
KPPDGKENVE SSWESQLDKS VLNESKQKIL HILNTGCLKE LKGLQQIGDK KAKLILGWRE
IQGHFTKLED LINIEGMTQK RFSSFMKANI LSALGK
//
