ID A0A151XD30_9HYME Unreviewed; 1791 AA.
AC A0A151XD30;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Kinesin-like protein KIF13A {ECO:0000313|EMBL:KYQ58267.1};
DE Flags: Fragment;
GN ORFNames=ALC60_02687 {ECO:0000313|EMBL:KYQ58267.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ58267.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ58267.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ58267.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ58267.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; KQ982294; KYQ58267.1; -; Genomic_DNA.
DR STRING; 64791.A0A151XD30; -.
DR Proteomes; UP000075809; 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; cd22706; FHA_KIF13; 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; 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; 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; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 2.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 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; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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}; Reference proteome {ECO:0000313|Proteomes:UP000075809}.
FT DOMAIN 1..235
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 245..282
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1685..1727
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 802..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1622..1646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1740..1791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 536..568
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 804..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1631..1646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KYQ58267.1"
SQ SEQUENCE 1791 AA; 201358 MW; C2A2F11A30692426 CRC64;
IIFYPCYRNK PKTFAFDHCF YSLDPGADSF ASQDIVFNAL GRDILDNAFQ GYNACIFAYG
QTGSGKSYTM MGSGDNKGII PRLCDNLFDM IAKQQSSELS YKVEVSYMEI YNEKVHDLLD
PKPNKQSLKV REHNVLGPYV DGLSQLAVTS FQDIDNLMAE GNKSRTVAAT NMNSESSRSH
AVFSVILTQT LTDLKSGVSG EKVSRMSLVD LAGSERAVKT GAVGDRLKEG SNINKIYKFI
DIKIDNLGGN SKTVMVATIS PAADNYEETL STLRYADRAK RIVNHAVVNE DPNARIIREL
RQEVETLKEM LLHATGSIVG QQRTDITEKL SESERLMKEM SQTWEEKLVK TERLQHERQQ
ALEKMGISVQ ASGIQVEKSK YYLVNLNDDP SLNELLVYYL KHIFVFQERT LVGGRSAKRE
QDIQLHGLGI LPEHCVITIE ESGLYMTPLN GARCFVNGTQ VVNKTLLQHG DRIVWGNHHF
FRVNCPRSAT VCNDIFREII GSNVILSVPT QNIDYNFARE ELMLNELSND PIQRAIARLE
KQHEEDKQVA LEKQRQEYER QFQQLRNILS PSTPYSPYVP YDPLRGSQSG KLPACTPTTQ
MRVEKWAQER DEMFKRSLGQ LKTDILKANA LVQEANVLAE EMGKQTKFSV TLQIPPNNLS
PNRKSVFFQR GAFVSEPAIL VKRANMGSQV WSMEKLENKL VDMRDMYEER KDFEMYMYYL
NIVYEIIFLQ DEVPGKTQDP FYESQENHNL IGVANIFLEV LFHDVRLDYH TPIISQQGEV
AGRLQVEISR ISGQFPQDRI CEAASESSAD STSSEAEDYS GGSSHITCRI TIKQATGLPL
SLSHFVFCQY MFWNHPEPIV VPPMINAELP NSNCITGQRD SLTFKFDDTK DFTVPITEEF
MEHAAEGALS IEVWGHRSAG FSRSKPGWEV EQQQLAKARS LADRWSELTR KIELWVEIQE
LNEQGEYSPV EVAIKQDTCT GGIYQLRQGQ QRRIQVRVKP VQNSGTLPII CQSILNIAVG
SVSVRNRLQI PLDSYQDEDL SILRDKWSDA LMRRRQYLDQ QIQKLINKQD KTEQDMEREQ
SLVDQWVSLT EERNAVLVPA AGSGIPGAPA DWTPPAGMEP HIPVLFLDLN VTLTKYYLAD
DLSTHQSGEE VSVTGLNSIL PKEHGNKFYS LPIIRHLEKD VCAIAAWDSS IHDNVHLNRV
TDTGNYPLRF SKKLVKYFLK SIIVLIFPII YIEKYTRGVS AVESILTLDR LRQSVAIKEL
LQAQGQPLMR KTASVPNFSQ IMRFDMSMDS LNVTRSESVT DLNMENGLPH PRRASTGHAR
NDENFISVPP KPFGIASPNM VSSKLGPRMT TLHEETSNMG NQACTPINDD DEEKSDADYS
EYEAYQAPPK PVKPLTSSRT LDSLVELQST KINTPSMSSS GYGSQAVSTT NLTSEDSISI
KSISVDETPD LEYRNLLDSK KPEKMDSSLV EETPEEYLSE VNISQSAGTE EHTKKNLEEM
GTYIDTDIDS PVSSTRSESE TNSNMFHVET QRKSTSNQIL SDRKNEMEIS QMSNSGDDSP
MEGTSVVHTK LPPGKVVRRK KTSNGSGRPT SSQHRASFPM VRPQLSESKA AVHLEQTLQP
TMTYENGDNS SSERIDADDV SDKSSAFGSR HDLTRVETPL PDWIVVGESV LVRPYSYSGV
IAYVGPTEFA SGIWIGVELD APTGKNDGAV NGHRYFTCRP KCGIFVKMDK LIQDRRGRAL
RSYTKQESTP APSTSMRRSI SKGEGLHSLH RSRSRGEGLS TTGTRSFPRG K
//
