ID A0A3P8SU89_AMPPE Unreviewed; 3133 AA.
AC A0A3P8SU89;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000015286.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000015286.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000015286.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR STRING; 161767.ENSAPEP00000015286; -.
DR Ensembl; ENSAPET00000015683.1; ENSAPEP00000015286.1; ENSAPEG00000010810.1.
DR GeneTree; ENSGT00940000163117; -.
DR OMA; CVCLLND; -.
DR Proteomes; UP000265080; Chromosome 18.
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 GO; GO:0048731; P:system development; IEA:UniProt.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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 InterPro; IPR023393; START-like_dom_sf.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR PANTHER; PTHR47117:SF1; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 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 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:UP000265080}.
FT DOMAIN 1..348
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 265..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1759..1781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1802..1835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1918..1939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1956..2036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2055..2102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2214..2236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2418..2440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2487..2604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2846..2876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 356..383
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 588..629
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2912..2951
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 265..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1971..1985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1986..2000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2064..2080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2088..2102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2420..2440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2519..2604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 3133 AA; 349421 MW; 424DCA9E3014C32A CRC64;
GRLTVKVEDK FVRIRNMKVS VSVDSREKLL EFCFDYCYWS VDPAEPHYAS QEEVFQDLGV
SVLSGASEGY NVCLFAYGQT GSGKTYTMMG TPESIGLTPR ICQDVVSSFC PCSFLEIYNE
RVRDLLRGGE QKKRASLKVR EHPDKGPYVQ DLSQHVVSDC KQAMDLLEEG IANRITAATH
NHDASSRSHA IFTIQYTQAI LENNLPSETV SKINLVDLAG SERADPHYCR DRLTEGSNIN
KSLVTLGIVI SALAQNSQMS NSCQSINSVA SEGDGSTVGS HSSSLSGGGG GGRRHCFIPY
RDSVLTWLLK DSLGGNSKTI MIATVSPSAN SYNETLSTLR YAAHARNIVN KPRVNEDANV
RLIRELREEI DRLKNMLLSF EMVEQLTKDW SESWRDKKEL LEQYSVDINR DRAGFLISSL
QPHLVALDGD VLSTGVVFYH LRRSSLNQNV AFISSFLSVV LQGSASCEIE NHRGVVTLRP
LPDCVCLLND REVTEPCRLA QGTVITLGGV HKFRFNHPAE AAVLRERRRV GKNDCFTLCD
CLFSLVSSWF LSLSFILDHV PYFHSVEEVK LPQQQGACLT PSEEPSARQR VEEQKRYVES
LRQEIQAEQR RVERELEREQ AHLRQQHTES QFRQWILQEK HHLTTVDQRI TQESGVQADL
LPAPLLERLT SQVSRDQEDP TVDCPSQVVR ARKKSVQDEL LKHHALCRAE SRIRRKRLHY
QLERIASKRR LLEAKRELQQ LEKALPAGPD SPESPELGSP SKLEGRPLVS RRHSFSADLL
SRLYPQHTPI YRYVPRVIKP GELIAWDYEA TFQSLSRFYL AVFVSACELD QRTPSENIRQ
RRWHSTEALM NQTSQWIDRQ QELAGWAEEQ EDRDEGASDC ESIFSLDSLS SAYAAALAEQ
LRHEDTGQSE AESEDSQMSK DSLTMESSCK FSTVKRLKQT PSYSLVKDSP HSVMQHNRTT
ETSSDWDCCQ KPLVIPTEAY WSQQGSPKTR EIDTARNPPP QSSLIAKSRG RDTVHKLTEE
FENMQTTSTS SPRSLSSCSV MESENLLVLT DAWSSTDAAD SPRIHRDSLP FQRTIMFRHA
ESSSSSPSPT SMNLSDSQGG SRSYSSTSTN NGGVNVTVLE HRLEGSKDCL ATPEDTLMSS
IQKDVGYCVE QLRQSNEVKK AVTDTPDFSY NEHPASLSTS DPNAFEPTET PQTIQATSNL
LQVFTDTPDK VAANITMSSD TELCTSAHQT ILHFSTNPTN QGQVVEAMPG AAKIFKSSTE
TEVLCNVDDA AATLRGVQQY HFRNTKDASF TGDETKGADQ SIALQQEVVK STCKNSRKRN
KDQQDAFIGS LKIPKRSNSG ELVTSCCVTA DSQDDIRPDD NNNTNDSKGE QSTIETDSTQ
FDCGCFGGSI REDTVTSFVS DLTSTKLEPS CQIFEFSESG LKHGDRNSRS GTSVGRYPVV
ENGSVTIKAV SVETIGGEYQ IAKHKTHQES RKHISKSGAI CSAIDLRISE VVKEHVKLSL
IGSDNARKNK SQSLKALSSS ACYLSCNDDE HRWMEKCLRD ESGNQAKEGT NLSVERVICK
NTVDESEHLA SNMAADLKTS NKNVTLKYSE VTQKIVDAQN FSDEISNRPV FSPCVLQNSS
AEKANIQSIL SLNSQGGCEQ SESPTINLSM VSDASSAGKY IDYQGITEET NAFAQEMTDE
GKHRVASHLN LAIDDICSKK VDSQTCSDVV LNTDLIFDRI AEHPKPQLHQ IPHETVPTTG
HTKLKCDCTV EDVSMEAASS VENKDHYSSK QTSQKLTEHF QNSPETAGAI KLLADGRLHQ
FKPDKRHSNK NIVPSCHNEN VETDTTTGGN ASSTAQDQFS CRQTHLDNLA QTCVVNLNYN
NKYQSLSNSQ CKFDKDTQVD CKGDRVMKSD KQAWTRQIMQ RHQALSTQST SKNILSSAQE
HKMPKENGIR NPSSTGSVLS KEARLNTVAG TLGNSAVMSN KAKTKRLRKS NMKTYPTSSS
DSSLKSSDEG EGDNRAVKMH HNRLTSKWVK LGTQNNVKQE ARHARSSDAD NSTLVSVRNS
KLKTSCNVNS VKSEVKCSED YTQKRRSLPP QAMSQKTDSE RVSPYAKRNE PQHTQKSQDS
SIHFASSDIN PFVHQWQDDD SNQHCYKNPA FGSAADLACK SPLLNSSEKR ITSSIEDYKE
RATRTSELSH PASVDIRSRL ANLTFSSTSS SNSVPGGFGN NSSQVDEIMF VYSSEQESQA
SNTQTQRRKT CEHSTQTELQ TVNNANSSVD IKESPTWASM ESMSAQLSKL IDSTSDLLGD
VQGMRTGEAR RPSSRKNLSG VSFSYNESKD CVKTDCSTQT AADVAIQTEK LLTEKEVAIL
QTPRETSKSH EVNVIVKVIG SEVVSVSQDK NMHCVVKTKA NTDEKMKSTP DLRVNTAAAS
QSENDPLKTP HLKTAADCQR RVRSASSRVS KQSTSEELGH RSIPEITCRS SKNCYQENHS
PSKTNHTSAF IKKHATYTDR ASSPILTVGT RLRMRHKGKQ SAPLCPPKYR DRKTNNPSEE
DSLTIPSVSG DNQLTTQNHD VSSSKSESVS LENVSEMSCS GPKGSDQGPS SLNSSLDRYT
GTDGRNVNYK DDQPSSKWQT TSPPWRTSAL TNGFILQNHS SPITRLQASN FPTPALSSGD
FCVDSYNASL LDDKTDQLQE DDMVSLAPSE CNTDVLVNIE PVTSVFPRED PERVPEDLPM
HNKFTNWSGV NRQQSKCSNK MTTLRTNDHM RSRNCAEWGE MESFGSNVES VVPSDRRARE
IVKLRQEREH VMATVNLNMN PTPLTVELTE AKLHYGLGET DALLKVLSPI VNCNESPLMP
SQQVYHSRKS VTLCCLRQER EERLQTYRRA RSPSKHPRSG PQEAVSSSKV PAAMPSRRKE
YLQRLRQEVI DITTCHRVPD PPRGEGQCPS DIEQLLRDYS RAREEARTEI AKARERLRER
TELEKRRLQQ QALSQEFKVT SDLKIHFPNI IYVLMYGGLC LFRYQGEDRG IRAYYKPSSS
PSVHGFLGVG ELNRPLDSLW NTICQLSKSH MYNHSIRSVW TRPLDDSTQL GEQTSQPRLY
IFIYVDAIRG EMMPSCWVLQ PVRHNGQETT RVIYLLQLDL GTPSFPHRLL NAVARRQAAV
IADLDAFVSS KTH
//
