ID A0A8M9PLX5_DANRE Unreviewed; 982 AA. AC A0A8M9PLX5; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 12-OCT-2022, entry version 2. DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394}; GN Name=kif23 {ECO:0000313|RefSeq:XP_021323261.1}; GN Synonyms=cb738 {ECO:0000313|RefSeq:XP_021323261.1}, knsl5 GN {ECO:0000313|RefSeq:XP_021323261.1}, mklp1 GN {ECO:0000313|RefSeq:XP_021323261.1}, wu:fi30e02 GN {ECO:0000313|RefSeq:XP_021323261.1}, wu:fi39f08 GN {ECO:0000313|RefSeq:XP_021323261.1}, zMKLP1 GN {ECO:0000313|RefSeq:XP_021323261.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_021323261.1}; RN [1] {ECO:0000313|RefSeq:XP_021323261.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_021323261.1}; RG RefSeq; RL Submitted (APR-2022) to UniProtKB. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283, CC ECO:0000256|RuleBase:RU000394}. 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 RefSeq; XP_021323261.1; XM_021467586.1. DR Proteomes; UP000000437; Chromosome 18. DR Gene3D; 2.60.40.4330; -; 1. DR Gene3D; 3.40.850.10; -; 1. DR InterPro; IPR032384; Kif23_Arf-bd. DR InterPro; IPR038105; Kif23_Arf-bd_sf. DR InterPro; IPR027640; Kinesin-like_fam. 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 PANTHER; PTHR24115; PTHR24115; 1. DR Pfam; PF00225; Kinesin; 1. DR Pfam; PF16540; MKLP1_Arf_bdg; 1. DR PRINTS; PR00380; KINESINHEAVY. DR SMART; SM00129; KISc; 1. DR SUPFAM; SSF52540; SSF52540; 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}; Coiled coil {ECO:0000256|SAM:Coils}; KW Microtubule {ECO:0000256|RuleBase:RU000394}; KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283, KW ECO:0000256|RuleBase:RU000394}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000000437}. FT DOMAIN 25..451 FT /note="Kinesin motor" FT /evidence="ECO:0000259|PROSITE:PS50067" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 173..192 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 689..731 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 767..797 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 826..845 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 914..982 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 568..644 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 697..712 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 767..790 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 925..939 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 112..119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283" SQ SEQUENCE 982 AA; 111492 MW; 386E13C227FA7428 CRC64; MIRQAKGKTP RRPPPKKPSN NQKDPVGVYC RVRPLGAEDE ECCIEVISNT TIQLHAPDGL KANRNGEFKE TQYSFKKVFG IKTTQRELFE DVAKPLAQDL IHGKNGLLFT YGVTGSGKTH TMTGSPGQGG LLPRSLDMIF NSIGPYQAKR YVFKPDDKNG MEVQNQVDAL LDRQKRDSQT SVPKTPNTRR VDPEFADMIS PEEACKAEGV DEDSSYSVFV SYIEIYNNYI YDLLEETPFD PIKPKWNGAG TPVRNITEFI PPQSKILRED QNHNMYVAGC TEVEVKSTEE AFEVFWRGQK KRRIANTQLN RESSRSHSVF IVKLAQAPLD ADGDNVLQDK NQVNVSQLCL VDLAGSERTS RTRAEGNRLR EAGNINQSLM TLRTCIEVLR ENQMCGTNKM VPYRDSKVTH LFKNYFDGEG KVRMVVCVNP KADDYEETLL VMRFAEMTQE VEVARPVDRP ICGFAAGRRQ RNQAFKEELT RRLEERGGPV DGDCPTVLNQ LLQAFPPLPP CEISGPNDDV TLPRLIEALE KRHKIRQMMI EEYNKTATML KSVLQEQDGN ILSKENVIQE QRGKLGEKDK MLQNQKNEID RLEKKSKMLE YKIDILQKTT NIYEEDKRSL QNELESREQR LQREMSEKRR IEARMQGMVS DTKLKWEKEC ERRVNAKQLE MQNKLWVKDE KLKQLKAIVT EGKTENRQPQ RPSREKDKVP PKRSASPSPA PSSYNGSQSS LSSLEPIYNF SQTVRPDTHF PRAGSVSVAS CISEWEQGVP QSRRQGSQSP PDCRNRTQGL PDSLSRRRGR CWAREVPVQP ADVDLEETVH WTGPPVRPLH RRSHSAGGER WVDHKPTTNV DLDTVMQPNI PNAIKVNAPN EKALSKCDKY VLTHQEVASD GEIQTKLIKG EVFKTRGGGQ SVQFTDIETL KQETPVAASR KRRSSESGPD SEPMEGNWTD VETRCSVAVE MRAGSNLGPG YQHHGYTKRR KP //