GenomeNet

Database: UniProt
Entry: G3TX86_LOXAF
LinkDB: G3TX86_LOXAF
Original site: G3TX86_LOXAF 
ID   G3TX86_LOXAF            Unreviewed;      1473 AA.
AC   G3TX86;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Kinesin family member 13B {ECO:0000313|Ensembl:ENSLAFP00000020194.1};
GN   Name=KIF13B {ECO:0000313|Ensembl:ENSLAFP00000020194.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000020194.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000020194.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000020194.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000020194.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000020194.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   Ensembl; ENSLAFT00000026461.1; ENSLAFP00000020194.1; ENSLAFG00000004531.4.
DR   GeneTree; ENSGT00940000155500; -.
DR   HOGENOM; CLU_001485_29_2_1; -.
DR   Proteomes; UP000007646; 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-KW.
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; cd22730; FHA_KIF13B; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR   InterPro; IPR032405; Kinesin_assoc.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF5; -; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12473; DUF3694; 2.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT   DOMAIN          1..38
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1358..1400
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          231..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1060..1094
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1146..1175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1251..1271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1289..1317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1094
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1290..1316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1473 AA;  164546 MW;  E0EAE0DDF29C758A CRC64;
     DSLGGNSKTA MVATVSPAAD NYDETLSTLR YADRAKNIVN HAVVNEDPNA RIIRDLREEV
     EKLREQLTKA EAMKSPELKE RLEESEKLIQ EMTVTWEEKL RKTEEIAQER QKQLESLGIS
     LQSSGIKVGD DKCFLVNLNA DPALNELLVY YLKEHTLIGS ANSQDIQLCG MGILPEHCII
     DITTEGQVML TPQKNTRTFV NGSCVSSPIQ LHHGDRILWG NNHFFRLNLP KKKKKAQSED
     EEHDNSMKND NSSEQLDVDG DSSSEVSSEI NFNYEYAQME VTMKALGNND PMQSILKSLE
     QQHEEEKRSA LERQRLMYEH ELEQLRRRLS PEKQNYRSSM DRFPFHSPSA QQRLRQWAEE
     RREATLNNSL MRLREQIVKA NLLVREASYI AEELDKRTEY KVTLQIPASS LDANKKRGSV
     LSEPAIQVRR KGKGKQIWSL EKLDNRLLDM RDLYQEWKEC EEDSPVIRSY FKRADPFYDE
     QENHSLIGVA NVFLESLFYD VKLQYAVPIV NQKGEVAGRL HVEVMRISGE IGERIAGGDD
     AVDISFDRET QENKLVCMVK ILQATGLPQH LSHFVFCKYN FWDQQEPMIV APEVDTSSSP
     VSKEPQCMVV FDHCNEFSVN ITEDFIEHLS EGALAIEVYG HKMTDPRKNP AVWDLGIIQA
     KTRSLRDRWS EVTRKVEFWV QILEQNENGD YCPVEVISAK DVPTGGIFQL RQGQSRRIQV
     EVKSVQESGT LPLMEECILS VGVGCIKIRP LRSPKTHETF HEERHDSTSI QDRDLERLRR
     KWLNALTKRQ EYLDQQLQKL VSKHDKTEDD ADREAQLLEM RLTLTEERNA VMVPSAGSGI
     PGAPAEWTPV PGMETHIPVI FLDLNADDFS SQDNLDDPEA GGWDATLTGE EEEEFFELQI
     VKQHDAEVKA EASWDSAVHN CPQLSKGTPS DERVFLIVRV TVQLSHPAEM QLVLRKRICV
     TVHGRQGFAQ SLLKKMSHRS SIPGCGVTFE IVSNIPEFDA QGVEEREALA RMAANVENPA
     SADSEAYIEK YLRSVLAVEN LLTLDRLRQE VAVKEQLTGK GKLSRRSISS PNVNRLSGSR
     QDLTPSYSLG SNKPVPRIMV QSTLLDVAVT RMEEAHQENM GISETPEVTV QIPPVVKIYD
     KPAKVPSQQP LPANAQAQEV PEGPPSPLSE TSSGYFSHSV STATLSDALV TGLDAASQAA
     PSSPPTPICQ VPLETDLSFP SVVSCAESHL SAPLENQTSL PSLPIQPNLE LDISKPQFPP
     DLLSQSSAPT SPFRIQKVRT SELKSFTRML GGDSCSSSTE EEQLASGGSG DSNSGGQALE
     KLEVVSDSEE ASEVPEWLKE GEYVTIGTNK MGIVRYIGPT DFQEGTWIGV ELDLPSGKND
     GSIGGKQYFK CNPGYGLLVK PSRVRKAMGA ARRRSTGLRL QGAAASEARR SATLSGSATN
     LASLTALAKA EVGAALRAER NQKSTENRKS WAS
//
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