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Database: UniProt
Entry: A0A2C9M9P9_BIOGL
LinkDB: A0A2C9M9P9_BIOGL
Original site: A0A2C9M9P9_BIOGL 
ID   A0A2C9M9P9_BIOGL        Unreviewed;      1722 AA.
AC   A0A2C9M9P9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Kinesin-like protein unc-104 {ECO:0008006|Google:ProtNLM};
GN   Name=106057456 {ECO:0000313|EnsemblMetazoa:BGLB040161-PJ};
OS   Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB040161-PJ, ECO:0000313|Proteomes:UP000076420};
RN   [1] {ECO:0000313|EnsemblMetazoa:BGLB040161-PJ}
RP   IDENTIFICATION.
RC   STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB040161-PJ};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000256|ARBA:ARBA00004489}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   RefSeq; XP_013070106.1; XM_013214652.1.
DR   EnsemblMetazoa; BGLB040161-RJ; BGLB040161-PJ; BGLB040161.
DR   VEuPathDB; VectorBase:BGLB040161; -.
DR   OrthoDB; 126886at2759; -.
DR   Proteomes; UP000076420; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; cd22705; FHA_KIF1; 1.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR   InterPro; IPR032405; Kinesin_assoc.
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; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR049780; PH_KIFIA_KIFIB.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF2; KINESIN-LIKE PROTEIN KIF1A ISOFORM X1; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 2.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   DOMAIN          3..355
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1608..1706
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1085..1147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1513..1542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1562..1581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          625..674
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1095..1109
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1121..1146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1518..1542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1562..1577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1722 AA;  196038 MW;  0C80DBA2E91CA74E CRC64;
     MSSVKVAVRV RPFNNREMSR EAECIIDMSG NTTTITNPKA GPKEAQNKSF NFDYSYWSHT
     TPEDPNFADQ KKVYDDIGLE MLDHAFEGYN VCIFAYGQTG SGKSYTMMGK NEPGQEGIIP
     QLCEDLFRRI SGQKNNDTTF SVEVSYFEIY CERVRDLLNP SNKNALRVRE HPLLGPYVED
     LSKLAVQSFE DINNLIDEGN KARTVAATNM NETSSRSHAV FTIIFSQRRY DPDTKIVGEK
     VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEISS MDPKAKNKKK
     KADFIPYRDS VLTWLLRENL GGNSKTAMVA ALSPADINYD ETLSTLRYAD RAKQIMCKAV
     VNEDPNAKLI RELKEEVARL KDILTSEGIE LGEGQSMQEY LEQRGRSRSR KESVTLEGGD
     DALERLKETE KLIAELNLSW EEKLHKTESI RKEREALLAE MGVALKEDGG TIGVFSPKKS
     PHLVNLNEDP LMSECLLYYI KEGTTRVGLH DAEKPNDVQL SGSNILEEHC LFENIDGNVT
     LIPCEGALCY VNGRQVTEPV KMKTGARVIL GKHHVFRFNH PQQARASRAL MSESMIESTD
     NPITEPVDWT FAQLELLEKQ GIDLRKEMES RLMLLEEQYR KEKEEADLLF EQQRQDYENR
     IQSLQEQVER HSMISSVATT NIFEEEEEEE EVHWSDREKD LAAWAFRKWK YHQFTSLRDD
     LWGNAIFLKE ANAISVELNK KVQFQFVLLT DTLYSPLPAD LLPAEERDDS RPFPKTIVAV
     EVQDTKNGAT HYWSLEKLRQ RLELMREMYH NEAELSPTSP EPNIDSMTGG DPFYDRFPWF
     RLVGRAFVYL SNLFYPVPLV HRVAVVNDKG DVKGYLRVAV QAITDKDDPQ EYSAGVKQSG
     NAKITFSDEE YFNKKQIQAT SFPLPPGMEK PVDTMVSSLE ELRIVEGEGQ TMDNSMLISE
     NHLIESDNKT KGQYGKFDYC PEMNASDLPE HLTIGSQFQF RVTILQASNI SPEYADIFCQ
     FNFLHRHDEA FSTEPLKNTG KGPPLGFYHV QNFTVTVTKS FIDYIKTQPL VFEVLGHYQQ
     HPLHEQSKDC PYVRPPPSRS FPTMPVSKPV PSPKYGIIAP SSKSEEDEKD KNDDLERKKK
     RKAQDSSSPV HSQCDLLVWF EICELAPNGE YVPVVVDHSE DLPTKGIFML HQGIQRRLRI
     TIVHEKRTHF AWKDVRELVV GRIRNTQEFY DYDIETTVLS LGLFPAHFLQ YQNDDRVFFQ
     FEAAWDSSLH NSPMLNRVTA YGEKVYMTLS AYLEVENCAQ PACITKDLCM VVHSRDTKIS
     APSPRFRALK SLFGVARYPD CGKVSGIYEL LLRQYSDSGS PGVERRQRRV LDTSLTYVRG
     EENLNGWRPR GDSLLGDHQW ELEKLARLQL VEKTRHVILL REKLAEQNKS HELSKLDKEI
     VNRQAKNQKI QGYEHTEIKS DENPKDVDIK EKNVQILCRG ESFDLKTDGD PEKELAARCV
     RLMLQGRLPL KPPPVKLDSM LSSTTTVTSE ESETSSDSLG TSLSSSMVSD IVKAVPIQSS
     KSCDSLLTSS PSPSGESADR KLSLPIKTIN LDTPMFVPDI EEVRPSPVVS RRGYLNFLED
     NTNGWIKKWV VVRRPYVYIF NNEKDPVVRG IINLATANIE YSEDQQALLK TQNAFSVMTK
     HRCFLLQTLD DKDFHDWLYA INPLLAGQIR SKLSRRKQPM KI
//
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