ID   A0A3B4WX97_SERLL        Unreviewed;      1178 AA.
AC   A0A3B4WX97;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Kinesin family member 1C {ECO:0000313|Ensembl:ENSSLDP00000007682.1};
GN   Name=KIF1C {ECO:0000313|Ensembl:ENSSLDP00000007682.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000007682.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000007682.1}
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   AlphaFoldDB; A0A3B4WX97; -.
DR   STRING; 1841481.ENSSLDP00000007682; -.
DR   Ensembl; ENSSLDT00000007929.1; ENSSLDP00000007682.1; ENSSLDG00000005987.1.
DR   GeneTree; ENSGT00940000159295; -.
DR   Proteomes; UP000261360; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2530; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR000253; FHA_dom.
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:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 2.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 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}.
FT   DOMAIN          5..348
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          942..1178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          599..626
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          785..812
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        960..991
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1017
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1032..1050
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1116..1145
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1178 AA;  131529 MW;  2A6599EDB13F69BA CRC64;
     MAGASVKVAV RVRPFNSRET GRNAKCVIQM QGNTTCISNP KQPKDGAKNF TFDYSYWSHT
     TIDDPSFASQ RQVYKDIGEE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGK QEPGQEGIIP
     QLCEDLFQRT GENTDPDLTY SVEVSYMEIY CERVRDLLNP KSQGTLRVRE HPILGPYVED
     LSKLAVTGFT DIRDLMDAGN KARTVAATNM NETSSRSHAV FTIVFTQKRR DQMTSLDTEK
     VSKISLVDLA GSERADSSGA KGTRLKEGAN INKSLTTLGK VISALAEMSS KKRKSDFIPY
     RDSVLTWLLK ENLGGNSRTA MIAALSPADI NYEETLSTLR YADRAKQIRC NAVINEDPNA
     KLIRELKAEV ERLRNLLFSQ GLQELLDNAG IYTLYCQTSW TDPRLCVCVC VCVCVCVCVC
     ACVLKTESIR LEREALLAEM GVSIKEDGGT LGVFSPKGTP HLVNLNEDPL MSECLLYYIK
     EGFTRVGQQD VDIKLSGHFI KEIHCVFVSE TNDQGEVVVT LEPLVGAETY VNGKQITDAV
     VLKQGNRIVM GKNHVFRFNH PEQARLERER SVTADQQAEP EDWNYAQREL LEKQGIDIKL
     EMEKRLQDME TQYRKEKEEA DLLLEQHRLY ADSDSGDDSD KRSCEESWRL ISSLREKLPA
     NKVQSIVKRC GLPSSGKRRE PLRVYQIPQR RRISKDPKRV TMEDLRMQAV KEICYEVALG
     DFRHSRQEIE ALSIVKMKEL CRMYAKKDAN EKESWRAVAQ DVCDTVGIGE ERIQKGKVYD
     LKAHIDKLTD ILEEVKLQNN MKDEEIKALR DRMIKMESII PVQVRSLVTS YGGMGCGDGG
     GVGPDHPEVR VQRLMDEDPA FRRGRLRWLK QEQQRILNLQ QQNITKKLRG QNQSLTAPIV
     PVHLPGTGRF IPPQECKLKF PFKSNPAHRL SWGPASAALQ ALGFGEGGEG GEEGGSEGKG
     SPSPPPPHGQ SPALLPLPFQ VPPPPPRMRT PSPHRAWQQR NQGNQGNQSG FHYHHQGNNQ
     NHQHRYRRNS LDSSTHGNIN YDNNQHHSGG GGGGHQGRPR QRRGVSPGPG GERGGGRGGG
     GGGGGGGGGR DRDGGFHYNQ RQHHQYHHHP YYNPHNAPFQ PGPHPNYHSL PRSGAPPPPA
     DMLLGAGPPP GGWGFTTPPR MRRQFSAPDL KNNKETPI
//