ID A0A2C9M9R1_BIOGL Unreviewed; 1769 AA.
AC A0A2C9M9R1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Kinesin-like protein unc-104 {ECO:0008006|Google:ProtNLM};
GN Name=106057456 {ECO:0000313|EnsemblMetazoa:BGLB040161-PC};
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-PC, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB040161-PC}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB040161-PC};
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_013070098.1; XM_013214644.1.
DR EnsemblMetazoa; BGLB040161-RC; BGLB040161-PC; BGLB040161.
DR GeneID; 106057456; -.
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 1655..1753
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1132..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 625..674
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1142..1156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1624
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 1769 AA; 201526 MW; D0ADB34765BD9326 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 HYWSLEKLRH RLTLMREIYN EDLSPDTPEA KQDIFHCLSA CGQQNVFNFR
TLIPSRQRLE LMREMYHNEA ELSPTSPEPN IDSMTGGDPF YDRFPWFRLV GRAFVYLSNL
FYPVPLVHRV AVVNDKGDVK GYLRVAVQAI TDKDDPQEYS AGVKQSGNAK ITFSDEEYFN
KKQIQATSFP LPPGMEKPVD TMVSSLEELR IVEGEGQTMD NSMLISENHL IESDNKTKGQ
YGKFDYCPEM NASDLPEHLT IGSQFQFRVT ILQASNISPE YADIFCQFNF LHRHDEAFST
EPLKNTGKGP PLGFYHVQNF TVTVTKSFID YIKTQPLVFE VLGHYQQHPL HEQSKDCPYV
RPPPSRSFPT MPVSKPVPSP KYGIIAPSSK SEEDEKDKND DLERKKKRKA QDSSSPVHSQ
CDLLVWFEIC ELAPNGEYVP VVVDHSEDLP TKGIFMLHQG IQRRLRITIV HEKRTHFAWK
DVRELVVGRI RNTQEFYDYD IETTVLSLGL FPAHFLQYQN DDRVFFQFEA AWDSSLHNSP
MLNRVTAYGE KVYMTLSAYL EVENCAQPAC ITKDLCMVVH SRDTKISAPS PRFRALKSLF
GVARYPDCGK VSGIYELLLR QYSDSGSPGV ERRQRRVLDT SLTYVRGEEN LNGWRPRGDS
LLGDHQWELE KLARLQLVEK TRHVILLREK LAEQNKSHEL SKLDKEIVNR QAKNQKIQGY
EHTEIKSDEN PKDVDIKEKN VQILCRGESF DLKTDGDPEK ELAARCVRLM LQGRLPLKPP
PVKLDSMLSS TTTVTSEESE TSSDSLGTSL SSSMVSDIVK AVPIQSSKSC DSLLTSSPSP
SGESADRKLS LPIKTINLDT PMFVPDIEEV RPSPVVSRRG YLNFLEDNTN GWIKKWVVVR
RPYVYIFNNE KDPVVRGIIN LATANIEYSE DQQALLKTQN AFSVMTKHRC FLLQTLDDKD
FHDWLYAINP LLAGQIRSKL SRRKQPMKI
//
