ID A0A0L8GGT8_OCTBM Unreviewed; 1411 AA.
AC A0A0L8GGT8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=OCBIM_22034264mg {ECO:0000313|EMBL:KOF75760.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF75760.1};
RN [1] {ECO:0000313|EMBL:KOF75760.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF75760.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF75760.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) 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}.
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DR EMBL; KQ422015; KOF75760.1; -; Genomic_DNA.
DR RefSeq; XP_014781486.1; XM_014926000.1.
DR EnsemblMetazoa; Ocbimv22034265m; Ocbimv22034265m.p; Ocbimv22034264m.g.
DR EnsemblMetazoa; XM_014926000.1; XP_014781486.1; LOC106877171.
DR GeneID; 106877171; -.
DR OrthoDB; 126886at2759; -.
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:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd22708; FHA_KIF16; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR CDD; cd06874; PX_KIF16B_SNX23; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR000253; FHA_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 InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00787; PX; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, 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 3..353
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1278..1411
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT COILED 584..790
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 863..920
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 979..1013
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1119..1205
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 104..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1411 AA; 164449 MW; B699B9EE5AB1AE7E CRC64;
MTSVKVAVRV RPINQREEEL DSKFIISMED NKTTIINNKI PETVSEGDCG RESMRVKEFT
FDFSFWSASK ATNFASQDHV FQSLGLDVVR SAYDGYNACV FAYGQTGSGK SYTMMGNQDD
HGLIPRICKE LFSRMVDGNS SYRTEVSFLE IYNEKVRDLL QKTHADDKGL HTLRVREHPK
DGPYVQELSK HYVHNYDDIK SLMDYGNINR TTAATNMNDV SSRSHAIFTI LFTQAKFVKD
MPSEIHSKIH LVDLAGSERA DATGATGQRL KEGASINKSL VTLGNVISVL AEMSEKKVKS
IFIPYRNSVL TWLLKDSLGG NSRTIMVATI SPADVNYGET LSTLRYANRA KNIINRPTIN
EDPNVRLIRE LRAEIARLRA MLGGNIDNIT TPKVQEKLHE NEARVKVLTD EWAGKWKETA
CILQEQTTLA LRKEGLGVVL DSELPHLIGI DDDILSTGIM LYHLKAGKTT IGRGDAEVEQ
DIVLAGVDVQ SEHCVIENDD SVVTLYPINN ALCTINGANI QGSAKLTQGA VILLGKTNMF
RFNHPAEAAK MREELKSCNL TFSRTSLLSQ SMNDLYRSTD SLNIVGMRQE IENMEEKHRQ
AEMDRLCKQA ELEKELQIKR SQLNSLQLEM EKAQDETKKV QLQVRQEQAK LKRKSQEIEK
QFKDYLEEKE KFQLEKEMER IKRQKETEEE IAKRLAERSA SCCTEVENEL KKLTQEETVL
RNNLMKTKEL LEKEIHDLEL KQEAKLNLEQ QIEDIEMEKL NKETKLEAMT QQYDQQKADL
EYQKQKMRRE LEGDKRIIEG LTYELQEAGK KFSEFTVAHD GWIESQGEEV KKKWYQIENK
EIELIQEYEN SMKDFEIQHK KDFEDINFEK QEIEDAKQEL EKHQQQKQEE YTKAKNAEDR
EKINVEIEEL EAAVKELLLH EEEHIKGEKS YLQRYNDKKD LFTKSFNEQK DQIDQEKNAL
RQSEKFRIEK QVYEKSLILE ERENSVKMQE EILQDMEKNL KISTEKLVSE INELSVKQEQ
MMKQSEEQDG NLQASIIELK KRQDQVEKQE RLELERIAKE KRRLLALLEQ SSPTKQKIKN
GSPSFSIEYN GEIHEVPKRV SSSKQRQNSI EENTSNLSLQ EIKQQYKIAE SQLEEKIRIF
EEERDAELER IEYEKYKLQE LENQERINSL VEQEVRRRLF EEKVQREKQR RIEKEQEKKE
RDEEISRLKV MHSRELRQLK AKYERSEGLH SSVIPTKSNP YATVMSPDSY TSSRLEHRRM
KYPSSPDIFT GANQNQTSAI RIYIPTYLYR GHGSDTHYEY EVKICVKDEA WSVFRRYSRF
RQLHTDMKIQ YAEVGSLIFP PKKLFSRSEK VVSERRYQLE FYLRSLLEIL MKIPSCPINP
SNNEFLSKQT LCDFDPFYKK GLFEATKHGT T
//
