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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//