ID A0A3B4WC49_SERLL Unreviewed; 1240 AA.
AC A0A3B4WC49;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Kinesin-like protein KIF16B {ECO:0000313|Ensembl:ENSSLDP00000001330.1};
GN Name=KIF16B {ECO:0000313|Ensembl:ENSSLDP00000001330.1};
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:ENSSLDP00000001330.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000001330.1}
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; A0A3B4WC49; -.
DR Ensembl; ENSSLDT00000001411.1; ENSSLDP00000001330.1; ENSSLDG00000001098.1.
DR GeneTree; ENSGT00940000162838; -.
DR Proteomes; UP000261360; Unplaced.
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:0035091; F:phosphatidylinositol binding; 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 CDD; cd06874; PX_KIF16B_SNX23; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR000253; FHA_dom.
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; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
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; PF00787; PX; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50195; PX; 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 3..358
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1104..1240
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 648..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 807..834
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 648..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1240 AA; 142029 MW; B2A7E0C56989EE6B CRC64;
MASVRVAVRV RPMNRREKDL TAKSIIKMEG TKTSITNLKI PDGVAGDTTR DRTKTFTYDF
SYDSTDCKSC AFVSQERVFR DLGTDVLKAA FEGYNACVFA YGQTGSGKSY TMMGNPGDAG
LIPRICEGLF SRISDATRWD VASFRTEVSY LEIYNERVRD LLRRKSTQTY NLRVREHPKD
GPYVEDLSKH LVQNYSDVEE LMEAGNINRT TASTGMNDVS SRSHAIFTIN FTQAKFDAEM
PSETVSKIHL VDLAGSERAD ATGATGVRLK EGGNINKSLV TLGNVISALA DMTQDGVNTN
LKKKSVFVPY RDSVLTWLLK DSLGGNAKTI MIATVSPADV NYGETLSTLR YANRAKNIIN
KPTINEDANV RLIRELRAEI ARLKLNTATL FRSASSPAAL RSAVLELTKE WTNKWNETQN
ILKEETLALR KEGIGVVLDS ELPHLIGIDD DLLSTGIILY HLKEGRTYVG REDASTEQDI
ILHGLDLESE HCKFENQNGT VTLVPLGGAQ CSVNGVQVTE PSQLNQGAVI LLGRTNMFRF
NHPKEAAKLR EKRKSGLLST FSLSMTDLSK SCENLSTVML YNPGRLINDM EAKQQSEKVE
LERLQQEVES QRKESEEVQQ RILRQEESLR RRSQDIESRL RDFLAEKERF EEERRSEPPG
EELQRRQRQN QQQEGEAEEE QDEEQRLQQE AAEQTEIYRE LERLKREREE QKVRLEAERR
RLEEQEREQL SLVGRLEEQL REKHEAATTL LTREDARRLE EERRALAEIR GELLRAKETG
ERPDVEDSGE EARSAQARYT DFKAAQVKEL GQLEEGLRQQ RERLEKEVTA ERSTVLLLAH
GLRERQQQLK ETQEKGAQDA TAVCQEEQLV KQAEHRLQFK ERQLVSLADG LLPALAEEKQ
RAVEMLERSS GGSNGNCDSP PGLDNTLFQV EKELEDKEDK LNLHWHSAQQ LQQLQETYEF
TANVARQEEK VRRKEKEILE SKEKQQREAM EQAVARLERR HSALRRSVSL EPDTEEQRHK
SSVQRNLRGT DLDQQRSEHI QYIQCILYVH HIEHVEHIEH EVQRRLRKMN LLNGGSSMDL
SLSCESLRHL VSRPLGTSAD GLQEPVKISI PRYVLRGQGK DEHFEFEVKI TVMDETWTVF
RRYSRFREMH KSLKLKYPEL AALEFPPKKL FGNRDERMVA ERRNHLERYL RNLFRVMLSS
SGSPLRTDAD GGFHLSKHAI CEFSPFFKKG VFEYGSHGTG
//
