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Database: UniProt
Entry: A0A026VY99_OOCBI
LinkDB: A0A026VY99_OOCBI
Original site: A0A026VY99_OOCBI 
ID   A0A026VY99_OOCBI        Unreviewed;      1840 AA.
AC   A0A026VY99;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Kinesin-like protein KIF13A {ECO:0000313|EMBL:EZA47844.1};
GN   ORFNames=X777_15163 {ECO:0000313|EMBL:EZA47844.1};
OS   Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Dorylinae; Ooceraea.
OX   NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA47844.1, ECO:0000313|Proteomes:UP000053097};
RN   [1] {ECO:0000313|EMBL:EZA47844.1, ECO:0000313|Proteomes:UP000053097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA   Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA   Zhang G., Kronauer D.J.;
RT   "The genome of the clonal raider ant Cerapachys biroi.";
RL   Curr. Biol. 24:451-458(2014).
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; KK107770; EZA47844.1; -; Genomic_DNA.
DR   STRING; 2015173.A0A026VY99; -.
DR   OMA; YPTHTPH; -.
DR   Proteomes; UP000053097; 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   CDD; cd01365; KISc_KIF1A_KIF1B; 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; IPR027640; Kinesin-like_fam.
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; PTHR24115:SF997; KINESIN HEAVY CHAIN 73, ISOFORM E; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 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; 1.
DR   Pfam; PF16183; Kinesin_assoc; 2.
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; 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   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:UP000053097}.
FT   DOMAIN          1..312
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1757..1799
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          805..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1366..1395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1419..1460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1476..1499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1556..1716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1816..1840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          556..583
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        807..826
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1559..1574
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1578..1597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1598..1620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1621..1638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1655..1671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1682..1702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1819..1840
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         59..66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1840 AA;  205567 MW;  2EF41C9C4612989C CRC64;
     MNSLCCRNKP KTFAFDHCFY SLDPIVGNYA SQEIVFDALG LDILDNAFQG YNACIFAYGQ
     TGSGKSYTMM GSGDNKGIIP RLCDNLFDMI AKQQSSELTY KVEVSYMEIY NEKVHDLLDP
     KPNKQSLKVR EHNVLGPYVD GLSQLAVTSF QVDIDNLMAE GNKSRTVAAT NMNSESSRSH
     AVFSVILTQT LTDSKSGVSG EKVSRMSLVD LAGSERAVKT GAVGDRLKEG SNINKSLTTL
     GLVISKLADQ NSGNNKKKDN FVPYRDSVLT WLLKDNLGGN SKTVMVATIS PAADNYEETL
     STLRYADRAK RIVNHAVVNE DPNARIIREL RQEVETLKEM LLQATVQGSI GQQRTDITEK
     LSESERLMKE MSQTWEEKLV KTERLQHERQ QALEKMGISV QASGIQVEKN KYYLVNLNDD
     PSLNELLVYY LKQRTLVGGR SAKTEQDIQL HGLGILPEHC VITIEESGLY MTPLNGARCF
     VNGTQVVDKS LLQHGDRIVW GNHHFFRVNC PRSATAINSE PQTPAQNIDY NFAREELMLN
     ELSNDPIQRA IARLEKQHEE DKQVALEKQR LEYERQFQQL RNILSPSTPY SPYVPYDPLR
     GSQSGKLPAC TPTTQMRVEK WAQERDEMFK RSLGQLKTDI LKANALVQEA NFLAEEMGKQ
     TKFSVTLQIP PNNLSPNRKR GAFVSEPAIL VKRTNMGSQV WSMEKLENKL VDMRDMYEER
     KDPHNGQRLP AIKDEVPGKT QDPFYESQEN HNLIGVANIF LEVLFHDVRL DYHTPIISQQ
     GEVAGRLQVE ISRISGQFPQ DRICEAASES SADSTSSEPD DYSGGSSHIT CRVTIKQATG
     LPLSLSHFVF CQYMFWGHPE PIVVPPMVNA ELPNSNCVAG QRDSLTFKFD HTKDFTVPIT
     EEFMEHAAEG ALSIEVWGHR SAGFSRSKPG WEVEQQQLAK ARSLADRWSE LTRKIELWVE
     IQELNEQGEY SPVEVALKQD TCTGGIHQLR QGQQRRIQVR VKPVQNSGTL PIICQSILNI
     AVGSVSVRNR LQIPLDSYQD EDLSILREKW SDALMRRRQY LDQQIQKLIN KQDKTEQDME
     REQSLVDQWV SLTEERNAVL VPAAGSGIPG APADWTPPAG MEPHIPVLFL DLNADDLSTH
     QSGEEVSVTG LNSILPKEHG NKFYNLPIIR HLEKDVCAIA AWDSSIHDNV HLNRVTDANE
     RVFLILKTTV RLSHPAPMDL VLRKRLALNI YKRQSITDRI FKRIVRTDCL AQTGVTYEVV
     SNIPKASEEL EDRESLAQIA ASGEDNSLCD GETYIEKYTR GVSAVESILT LDRLRQNVAV
     KELLQAQGQP LMRKTASVPN FSQIMRFDTS MDALNVTRSE SVTDLNTEIN GLPHPRRAST
     GHARNDENFI SAPPKSFGIA SPNMVSSKLG LRMTTLHEET SNVGNQASTP VNDDDEEKSD
     ADYSEYEAYQ APPKPIKPLT SSRTLDSLVE LQSTKINTPS MSSSGYGSQA VSTTNLTSED
     SISIKSISVD ETPDLEYRNL LDSKKPEKMD SSLVEETPEE YLGEINSALD NLSVSQRTCT
     EEHTRKHLEE TGAYADTDMD SPVSSTKSES ESNSNAIHNE TLRKDAHDQV SHDRRKSETE
     TNQLSNSGDD SSMDGSSVVH TKLPPGKVVR RRKTSNGTGR PTSSQHRASF PMVRPQVSES
     KAAARLEQTL QPSMSYENGD NSSSERIDAD DVSDKSSAFG SRYDLTRVET PLPDWVVVGE
     SVLVRPYSYS GVIAYVGPTE FASGNWIGVE LDAPTGKNDG AVNGHRYFTC RPKCGIFVKV
     DKLIQDRRGR ALRSYTKQEL APAPSTSMRR SVSKGNFSSR
//
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